(data stored in SCRATCH zone)

SWISSPROT: GGAP1_ARATH

ID   GGAP1_ARATH             Reviewed;         442 AA.
AC   Q8RWE8; Q8LKQ7; Q940B4; Q9SZ25;
DT   30-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   11-DEC-2019, entry version 97.
DE   RecName: Full=GDP-L-galactose phosphorylase 1;
DE            EC=2.7.7.69;
DE   AltName: Full=Protein VITAMIN C DEFECTIVE 2;
GN   Name=VTC2; OrderedLocusNames=At4g26850; ORFNames=F10M23.190;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF GLY-224 AND SER-290.
RX   PubMed=12068090; DOI=10.1104/pp.003533;
RA   Jander G., Norris S.R., Rounsley S.D., Bush D.F., Levin I.M., Last R.L.;
RT   "Arabidopsis map-based cloning in the post-genome era.";
RL   Plant Physiol. 129:440-450(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617198; DOI=10.1038/47134;
RA   Mayer K.F.X., Schueller C., Wambutt R., Murphy G., Volckaert G., Pohl T.,
RA   Duesterhoeft A., Stiekema W., Entian K.-D., Terryn N., Harris B.,
RA   Ansorge W., Brandt P., Grivell L.A., Rieger M., Weichselgartner M.,
RA   de Simone V., Obermaier B., Mache R., Mueller M., Kreis M., Delseny M.,
RA   Puigdomenech P., Watson M., Schmidtheini T., Reichert B., Portetelle D.,
RA   Perez-Alonso M., Boutry M., Bancroft I., Vos P., Hoheisel J.,
RA   Zimmermann W., Wedler H., Ridley P., Langham S.-A., McCullagh B.,
RA   Bilham L., Robben J., van der Schueren J., Grymonprez B., Chuang Y.-J.,
RA   Vandenbussche F., Braeken M., Weltjens I., Voet M., Bastiaens I., Aert R.,
RA   Defoor E., Weitzenegger T., Bothe G., Ramsperger U., Hilbert H., Braun M.,
RA   Holzer E., Brandt A., Peters S., van Staveren M., Dirkse W., Mooijman P.,
RA   Klein Lankhorst R., Rose M., Hauf J., Koetter P., Berneiser S., Hempel S.,
RA   Feldpausch M., Lamberth S., Van den Daele H., De Keyser A., Buysshaert C.,
RA   Gielen J., Villarroel R., De Clercq R., van Montagu M., Rogers J.,
RA   Cronin A., Quail M.A., Bray-Allen S., Clark L., Doggett J., Hall S.,
RA   Kay M., Lennard N., McLay K., Mayes R., Pettett A., Rajandream M.A.,
RA   Lyne M., Benes V., Rechmann S., Borkova D., Bloecker H., Scharfe M.,
RA   Grimm M., Loehnert T.-H., Dose S., de Haan M., Maarse A.C., Schaefer M.,
RA   Mueller-Auer S., Gabel C., Fuchs M., Fartmann B., Granderath K., Dauner D.,
RA   Herzl A., Neumann S., Argiriou A., Vitale D., Liguori R., Piravandi E.,
RA   Massenet O., Quigley F., Clabauld G., Muendlein A., Felber R., Schnabl S.,
RA   Hiller R., Schmidt W., Lecharny A., Aubourg S., Chefdor F., Cooke R.,
RA   Berger C., Monfort A., Casacuberta E., Gibbons T., Weber N., Vandenbol M.,
RA   Bargues M., Terol J., Torres A., Perez-Perez A., Purnelle B., Bent E.,
RA   Johnson S., Tacon D., Jesse T., Heijnen L., Schwarz S., Scholler P.,
RA   Heber S., Francs P., Bielke C., Frishman D., Haase D., Lemcke K.,
RA   Mewes H.-W., Stocker S., Zaccaria P., Bevan M., Wilson R.K.,
RA   de la Bastide M., Habermann K., Parnell L., Dedhia N., Gnoj L., Schutz K.,
RA   Huang E., Spiegel L., Sekhon M., Murray J., Sheet P., Cordes M.,
RA   Abu-Threideh J., Stoneking T., Kalicki J., Graves T., Harmon G.,
RA   Edwards J., Latreille P., Courtney L., Cloud J., Abbott A., Scott K.,
RA   Johnson D., Minx P., Bentley D., Fulton B., Miller N., Greco T., Kemp K.,
RA   Kramer J., Fulton L., Mardis E., Dante M., Pepin K., Hillier L.W.,
RA   Nelson J., Spieth J., Ryan E., Andrews S., Geisel C., Layman D., Du H.,
RA   Ali J., Berghoff A., Jones K., Drone K., Cotton M., Joshu C., Antonoiu B.,
RA   Zidanic M., Strong C., Sun H., Lamar B., Yordan C., Ma P., Zhong J.,
RA   Preston R., Vil D., Shekher M., Matero A., Shah R., Swaby I.K.,
RA   O'Shaughnessy A., Rodriguez M., Hoffman J., Till S., Granat S., Shohdy N.,
RA   Hasegawa A., Hameed A., Lodhi M., Johnson A., Chen E., Marra M.A.,
RA   Martienssen R., McCombie W.R.;
RT   "Sequence and analysis of chromosome 4 of the plant Arabidopsis thaliana.";
RL   Nature 402:769-777(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RA   Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Morosawa T.,
RA   Kamiya A., Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K.,
RA   Kohara Y., Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K.,
RA   Akiyama K., Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J.,
RA   Hayashizaki Y., Shinozaki K.;
RT   "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
RL   Submitted (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   IDENTIFICATION.
RX   PubMed=12119013; DOI=10.1021/bi025942q;
RA   Brenner C.;
RT   "Hint, Fhit, and GalT: function, structure, evolution, and mechanism of
RT   three branches of the histidine triad superfamily of nucleotide hydrolases
RT   and transferases.";
RL   Biochemistry 41:9003-9014(2002).
RN   [7]
RP   INDUCTION BY JASMONATE AND OZONE.
RX   PubMed=16262714; DOI=10.1111/j.1365-313x.2005.02560.x;
RA   Sasaki-Sekimoto Y., Taki N., Obayashi T., Aono M., Matsumoto F.,
RA   Sakurai N., Suzuki H., Hirai M.Y., Noji M., Saito K., Masuda T.,
RA   Takamiya K., Shibata D., Ohta H.;
RT   "Coordinated activation of metabolic pathways for antioxidants and defence
RT   compounds by jasmonates and their roles in stress tolerance in
RT   Arabidopsis.";
RL   Plant J. 44:653-668(2005).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=17462988; DOI=10.1074/jbc.m702094200;
RA   Linster C.L., Gomez T.A., Christensen K.C., Adler L.N., Young B.D.,
RA   Brenner C., Clarke S.G.;
RT   "Arabidopsis VTC2 encodes a GDP-L-galactose phosphorylase, the last unknown
RT   enzyme in the Smirnoff-Wheeler pathway to ascorbic acid in plants.";
RL   J. Biol. Chem. 282:18879-18885(2007).
RN   [9]
RP   FUNCTION, INDUCTION BY LIGHT, MUTAGENESIS OF GLY-224 AND SER-290, CATALYTIC
RP   ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, TISSUE SPECIFICITY, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=17877701; DOI=10.1111/j.1365-313x.2007.03266.x;
RA   Dowdle J., Ishikawa T., Gatzek S., Rolinski S., Smirnoff N.;
RT   "Two genes in Arabidopsis thaliana encoding GDP-L-galactose phosphorylase
RT   are required for ascorbate biosynthesis and seedling viability.";
RL   Plant J. 52:673-689(2007).
RN   [10]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=17485667; DOI=10.1073/pnas.0701625104;
RA   Laing W.A., Wright M.A., Cooney J., Bulley S.M.;
RT   "The missing step of the L-galactose pathway of ascorbate biosynthesis in
RT   plants, an L-galactose guanyltransferase, increases leaf ascorbate
RT   content.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:9534-9539(2007).
RN   [11]
RP   FUNCTION, AND MUTAGENESIS OF HIS-238.
RX   PubMed=18463094; DOI=10.1074/jbc.m802594200;
RA   Linster C.L., Adler L.N., Webb K., Christensen K.C., Brenner C.,
RA   Clarke S.G.;
RT   "A second GDP-L-galactose phosphorylase in arabidopsis en route to vitamin
RT   C. Covalent intermediate and substrate requirements for the conserved
RT   reaction.";
RL   J. Biol. Chem. 283:18483-18492(2008).
RN   [12]
RP   INTERACTION WITH TLP1.
RX   PubMed=17982713; DOI=10.1007/s10265-007-0118-8;
RA   Ogura Y., Komatsu A., Zikihara K., Nanjo T., Tokutomi S., Wada M.,
RA   Kiyosue T.;
RT   "Blue light diminishes interaction of PAS/LOV proteins, putative blue light
RT   receptors in Arabidopsis thaliana, with their interacting partners.";
RL   J. Plant Res. 121:97-105(2008).
RN   [13]
RP   TISSUE SPECIFICITY, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND
RP   INDUCTION BY LIGHT.
RX   PubMed=18516687; DOI=10.1007/s11103-008-9350-4;
RA   Muller-Moule P.;
RT   "An expression analysis of the ascorbate biosynthesis enzyme VTC2.";
RL   Plant Mol. Biol. 68:31-41(2008).
CC   -!- FUNCTION: Catalyzes a reaction of the Smirnoff-Wheeler pathway, the
CC       major route to ascorbate biosynthesis in plants. Acts as a
CC       phosphorylase rather than as a transferase. Uses preferentially GDP-L-
CC       galactose and GDP-D-glucose as substrates. Lower activity with GDP-L-
CC       fucose, very low activity with GDP-D-mannose, and no activity with UDP-
CC       D-glucose, UDP-D-galactose or ADP-D-glucose. Highly specific for
CC       inorganic phosphate as the guanylyl acceptor.
CC       {ECO:0000269|PubMed:17462988, ECO:0000269|PubMed:17485667,
CC       ECO:0000269|PubMed:17877701, ECO:0000269|PubMed:18463094}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP-beta-L-galactose + phosphate = beta-L-galactose 1-
CC         phosphate + GDP + H(+); Xref=Rhea:RHEA:27698, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189, ChEBI:CHEBI:61454,
CC         ChEBI:CHEBI:75522; EC=2.7.7.69;
CC         Evidence={ECO:0000269|PubMed:17462988, ECO:0000269|PubMed:17485667,
CC         ECO:0000269|PubMed:17877701};
CC   -!- ACTIVITY REGULATION: Not inhibited by dithiothreitol, N-ethylmaleimide,
CC       phenylmethane sulfonyl fluoride, ascorbate, L-galactose and L-
CC       galactonolactone.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.01 mM for GDP-L-galactose {ECO:0000269|PubMed:17462988};
CC         KM=0.25 mM for GDP-L-galactose {ECO:0000269|PubMed:17877701};
CC         KM=0.0079 mM for GDP-L-galactose {ECO:0000269|PubMed:18463094};
CC         KM=0.0044 mM for GDP-D-glucose {ECO:0000269|PubMed:17462988};
CC         KM=0.52 mM for GDP-D-mannose {ECO:0000269|PubMed:17462988};
CC         KM=2.4 mM for phosphate (in the presence of GDP-L-galactose)
CC         {ECO:0000269|PubMed:18463094};
CC         KM=0.76 mM for phosphate (in the presence of GDP-D-glucose)
CC         {ECO:0000269|PubMed:18463094};
CC         KM=0.25 mM for phosphate {ECO:0000269|PubMed:17877701};
CC         KM=45 mM for L-galactose 1-phosphate {ECO:0000269|PubMed:17462988};
CC         KM=29 mM for D-glucose 1-phosphate {ECO:0000269|PubMed:17462988};
CC         KM=54 mM for D-mannose 1-phosphate {ECO:0000269|PubMed:17462988};
CC         KM=67 mM for D-galactose 1-phosphate {ECO:0000269|PubMed:17462988};
CC       pH dependence:
CC         Optimum pH is 7.5. {ECO:0000269|PubMed:17877701};
CC   -!- PATHWAY: Cofactor biosynthesis; L-ascorbate biosynthesis via GDP-alpha-
CC       D-mannose pathway; L-ascorbate from GDP-alpha-D-mannose: step 2/5.
CC   -!- SUBUNIT: Interacts with TLP1. {ECO:0000269|PubMed:17982713}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18516687}. Nucleus
CC       {ECO:0000269|PubMed:18516687}.
CC   -!- TISSUE SPECIFICITY: Expressed in leaves, stems, roots, flowers and
CC       siliques. Highest expression in green tissues.
CC       {ECO:0000269|PubMed:17877701, ECO:0000269|PubMed:18516687}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in all developmental stages.
CC       {ECO:0000269|PubMed:18516687}.
CC   -!- INDUCTION: By jasmonate, ozone and high light. Circadian-regulation,
CC       with a peak in expression at the beginning of the light cycle.
CC       {ECO:0000269|PubMed:16262714, ECO:0000269|PubMed:17877701,
CC       ECO:0000269|PubMed:18516687}.
CC   -!- DISRUPTION PHENOTYPE: Dwarf. 20% of the wild-type ascorbate level, due
CC       to the partial redundancy with VTC5. Vtc2 and vtc5 double mutants show
CC       growth arrest immediately upon germination and are not viable.
CC       {ECO:0000269|PubMed:17877701}.
CC   -!- SIMILARITY: Belongs to the GDPGP1 family. {ECO:0000305}.
CC   -!- CAUTION: According to publications, it is related to the galactose-1-
CC       phosphate uridylyltransferase type 1 family and histidine triad
CC       superfamily (PubMed:12119013). However, such families are not detected
CC       by prediction tools such as Pfam or SUPFAM.
CC       {ECO:0000305|PubMed:12119013}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAM34266.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB36531.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=CAB79540.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
DR   EMBL; AF508793; AAM34266.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL035440; CAB36531.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AL161565; CAB79540.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002687; AEE85260.1; -; Genomic_DNA.
DR   EMBL; AY056134; AAL07213.1; -; mRNA.
DR   EMBL; AY093138; AAM13137.1; -; mRNA.
DR   EMBL; BT006589; AAP31933.1; -; mRNA.
DR   EMBL; AK226394; BAE98540.1; -; mRNA.
DR   PIR; T04808; T04808.
DR   RefSeq; NP_567759.1; NM_118819.3.
DR   BioGrid; 14079; 1.
DR   IntAct; Q8RWE8; 1.
DR   STRING; 3702.AT4G26850.1; -.
DR   iPTMnet; Q8RWE8; -.
DR   PaxDb; Q8RWE8; -.
DR   PRIDE; Q8RWE8; -.
DR   EnsemblPlants; AT4G26850.1; AT4G26850.1; AT4G26850.
DR   GeneID; 828792; -.
DR   Gramene; AT4G26850.1; AT4G26850.1; AT4G26850.
DR   KEGG; ath:AT4G26850; -.
DR   Araport; AT4G26850; -.
DR   TAIR; locus:2116342; AT4G26850.
DR   eggNOG; KOG2720; Eukaryota.
DR   eggNOG; ENOG4111FR6; LUCA.
DR   HOGENOM; HOG000006065; -.
DR   InParanoid; Q8RWE8; -.
DR   KO; K14190; -.
DR   OMA; WEDRMER; -.
DR   OrthoDB; 1178383at2759; -.
DR   PhylomeDB; Q8RWE8; -.
DR   BioCyc; MetaCyc:AT4G26850-MONOMER; -.
DR   BRENDA; 2.7.7.69; 399.
DR   SABIO-RK; Q8RWE8; -.
DR   UniPathway; UPA00990; UER00932.
DR   PRO; PR:Q8RWE8; -.
DR   Proteomes; UP000006548; Chromosome 4.
DR   ExpressionAtlas; Q8RWE8; baseline and differential.
DR   Genevisible; Q8RWE8; AT.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0010475; F:galactose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
DR   GO; GO:0080048; F:GDP-D-glucose phosphorylase activity; IDA:TAIR.
DR   GO; GO:0010472; F:GDP-galactose:glucose-1-phosphate guanylyltransferase activity; IDA:TAIR.
DR   GO; GO:0010471; F:GDP-galactose:mannose-1-phosphate guanylyltransferase activity; IDA:TAIR.
DR   GO; GO:0010473; F:GDP-galactose:myoinositol-1-phosphate guanylyltransferase activity; IDA:TAIR.
DR   GO; GO:0080047; F:GDP-L-galactose phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0010474; F:glucose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
DR   GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008928; F:mannose-1-phosphate guanylyltransferase (GDP) activity; IDA:TAIR.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0080046; F:quercetin 4'-O-glucosyltransferase activity; IDA:TAIR.
DR   GO; GO:0052544; P:defense response by callose deposition in cell wall; IMP:TAIR.
DR   GO; GO:0042742; P:defense response to bacterium; IMP:TAIR.
DR   GO; GO:0006006; P:glucose metabolic process; IBA:GO_Central.
DR   GO; GO:0019853; P:L-ascorbic acid biosynthetic process; IMP:TAIR.
DR   GO; GO:0009408; P:response to heat; IMP:TAIR.
DR   GO; GO:0009753; P:response to jasmonic acid; IEP:TAIR.
DR   InterPro; IPR026506; GDPGP.
DR   PANTHER; PTHR20884; PTHR20884; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8RWE8.
DR   SWISS-2DPAGE; Q8RWE8.
KW   Ascorbate biosynthesis; Cytoplasm; Guanine-nucleotide releasing factor;
KW   Hydrolase; Nucleotide-binding; Nucleotidyltransferase; Nucleus;
KW   Reference proteome; Transferase.
FT   CHAIN           1..442
FT                   /note="GDP-L-galactose phosphorylase 1"
FT                   /id="PRO_0000402541"
FT   ACT_SITE        238
FT                   /note="Tele-GMP-histidine intermediate"
FT                   /evidence="ECO:0000305"
FT   MUTAGEN         224
FT                   /note="G->D: In vtc2-2; loss of activity; dwarf."
FT                   /evidence="ECO:0000269|PubMed:12068090,
FT                   ECO:0000269|PubMed:17877701"
FT   MUTAGEN         238
FT                   /note="H->N: Strongly reduced activity."
FT                   /evidence="ECO:0000269|PubMed:18463094"
FT   MUTAGEN         290
FT                   /note="S->F: In vtc2-3; strongly reduced ascorbate levels."
FT                   /evidence="ECO:0000269|PubMed:12068090,
FT                   ECO:0000269|PubMed:17877701"
FT   CONFLICT        396
FT                   /note="G -> S (in Ref. 4; AAL07213)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   442 AA;  48970 MW;  84C389ED098BBA2D CRC64;
     MLKIKRVPTV VSNYQKDDGA EDPVGCGRNC LGACCLNGAR LPLYACKNLV KSGEKLVISH
     EAIEPPVAFL ESLVLGEWED RFQRGLFRYD VTACETKVIP GKYGFVAQLN EGRHLKKRPT
     EFRVDKVLQS FDGSKFNFTK VGQEELLFQF EAGEDAQVQF FPCMPIDPEN SPSVVAINVS
     PIEYGHVLLI PRVLDCLPQR IDHKSLLLAV HMAAEAANPY FRLGYNSLGA FATINHLHFQ
     AYYLAMPFPL EKAPTKKITT TVSGVKISEL LSYPVRSLLF EGGSSMQELS DTVSDCCVCL
     QNNNIPFNIL ISDCGRQIFL MPQCYAEKQA LGEVSPEVLE TQVNPAVWEI SGHMVLKRKE
     DYEGASEDNA WRLLAEASLS EERFKEVTAL AFEAIGCSNQ EEDLEGTIVH QQNSSGNVNQ
     KSNRTHGGPI TNGTAAECLV LQ
//

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