(data stored in ACNUC7421 zone)

SWISSPROT: NADE_BACSU

ID   NADE_BACSU              Reviewed;         272 AA.
AC   P08164;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 5.
DT   11-DEC-2019, entry version 152.
DE   RecName: Full=NH(3)-dependent NAD(+) synthetase {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000303|PubMed:7890752};
DE            EC=6.3.1.5 {ECO:0000255|HAMAP-Rule:MF_00193, ECO:0000269|PubMed:7890752};
DE   AltName: Full=General stress protein 38;
DE            Short=GSP38;
DE   AltName: Full=Spore outgrowth factor B;
DE   AltName: Full=Sporulation protein OutB;
GN   Name=nadE {ECO:0000255|HAMAP-Rule:MF_00193};
GN   Synonyms=outB {ECO:0000303|PubMed:2435704}; OrderedLocusNames=BSU03130;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2435704; DOI=10.1128/jb.169.4.1480-1484.1987;
RA   Albertini A.M., Caramori T., Henner D.J., Ferrari E., Galizzi A.;
RT   "Nucleotide sequence of the outB locus of Bacillus subtilis and regulation
RT   of its expression.";
RL   J. Bacteriol. 169:1480-1484(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-19.
RC   STRAIN=168 / IS58;
RX   PubMed=9298659; DOI=10.1002/elps.1150180820;
RA   Antelmann H., Bernhardt J., Schmid R., Mach H., Voelker U., Hecker M.;
RT   "First steps from a two-dimensional protein index towards a response-
RT   regulation map for Bacillus subtilis.";
RL   Electrophoresis 18:1451-1463(1997).
RN   [5]
RP   PROTEIN SEQUENCE OF 2-11, AND PHOSPHORYLATION.
RX   PubMed=1556067; DOI=10.1128/jb.174.8.2474-2477.1992;
RA   Mitchell C., Morris P.W., Vary J.C.;
RT   "Identification of proteins phosphorylated by ATP during sporulation of
RT   Bacillus subtilis.";
RL   J. Bacteriol. 174:2474-2477(1992).
RN   [6]
RP   SIMILARITY TO E.COLI NADE.
RX   PubMed=2118513; DOI=10.1128/jb.172.9.5482-5485.1990;
RA   Albertini A.M., Galizzi A.;
RT   "The Bacillus subtilis outB gene is highly homologous to an Escherichia
RT   coli ntr-like gene.";
RL   J. Bacteriol. 172:5482-5485(1990).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY,
RP   SUBUNIT, AND DEVELOPMENTAL STAGE.
RX   PubMed=7890752; DOI=10.1074/jbc.270.11.6181;
RA   Nessi C., Albertini A.M., Speranza M.L., Galizzi A.;
RT   "The outB gene of Bacillus subtilis codes for NAD synthetase.";
RL   J. Biol. Chem. 270:6181-6185(1995).
RN   [8] {ECO:0000244|PDB:1NSY}
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH AMP; ATP AND
RP   DIPHOSPHATE, AND SUBUNIT.
RX   PubMed=8895556; DOI=10.1002/j.1460-2075.1996.tb00896.x;
RA   Rizzi M., Nessi C., Mattevi A., Coda A., Bolognesi M., Galizzi A.;
RT   "Crystal structure of NH3-dependent NAD+ synthetase from Bacillus
RT   subtilis.";
RL   EMBO J. 15:5125-5134(1996).
RN   [9] {ECO:0000244|PDB:2NSY}
RP   X-RAY CRYSTALLOGRAPHY (1.3 ANGSTROMS) IN COMPLEX WITH AMP; NAD AND
RP   DIPHOSPHATE, AND SUBUNIT.
RX   PubMed=9753692; DOI=10.1016/s0969-2126(98)00114-2;
RA   Rizzi M., Bolognesi M., Coda A.;
RT   "A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate
RT   intermediate in the NAD+ synthetase structure.";
RL   Structure 6:1129-1140(1998).
RN   [10] {ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1FYD, ECO:0000244|PDB:1IFX, ECO:0000244|PDB:1IH8}
RP   X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH AMP; ATP; NAD AND
RP   DIPHOSPHATE, AND SUBUNIT.
RX   PubMed=11375500; DOI=10.1107/s0907444901003523;
RA   Devedjiev Y., Symersky J., Singh R., Jedrzejas M., Brouillette C.,
RA   Brouillette W., Muccio D., Chattopadhyay D., DeLucas L.;
RT   "Stabilization of active-site loops in NH3-dependent NAD+ synthetase from
RT   Bacillus subtilis.";
RL   Acta Crystallogr. D 57:806-812(2001).
RN   [11] {ECO:0000244|PDB:1KQP}
RP   X-RAY CRYSTALLOGRAPHY (1.0 ANGSTROMS) IN COMPLEX WITH
RP   NICOTINAMIDE-ADENINE-DINUCLEOTIDE-ADENYLATE INTERMEDIATE AND DIPHOSPHATE,
RP   AND SUBUNIT.
RX   PubMed=12077433; DOI=10.1107/s0907444902006698;
RA   Symersky J., Devedjiev Y., Moore K., Brouillette C., DeLucas L.;
RT   "NH3-dependent NAD+ synthetase from Bacillus subtilis at 1 A resolution.";
RL   Acta Crystallogr. D 58:1138-1146(2002).
CC   -!- FUNCTION: Catalyzes the ATP-dependent amidation of deamido-NAD to form
CC       NAD. Uses ammonia as a nitrogen source. {ECO:0000255|HAMAP-
CC       Rule:MF_00193, ECO:0000269|PubMed:7890752}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + deamido-NAD(+) + NH4(+) = AMP + diphosphate + H(+) +
CC         NAD(+); Xref=Rhea:RHEA:21188, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57540,
CC         ChEBI:CHEBI:58437, ChEBI:CHEBI:456215; EC=6.3.1.5;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00193,
CC         ECO:0000269|PubMed:7890752};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.62 mM for NH(4)(+) {ECO:0000269|PubMed:7890752};
CC         KM=0.28 mM for deamido-NAD {ECO:0000269|PubMed:7890752};
CC         KM=0.21 mM for ATP {ECO:0000269|PubMed:7890752};
CC       pH dependence:
CC         Optimum pH is 8.2-8.7. {ECO:0000269|PubMed:7890752};
CC       Temperature dependence:
CC         Optimum temperature is 40-45 degrees Celsius.
CC         {ECO:0000269|PubMed:7890752};
CC   -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from
CC       deamido-NAD(+) (ammonia route): step 1/1. {ECO:0000255|HAMAP-
CC       Rule:MF_00193, ECO:0000269|PubMed:7890752}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00193,
CC       ECO:0000269|PubMed:11375500, ECO:0000269|PubMed:12077433,
CC       ECO:0000269|PubMed:7890752, ECO:0000269|PubMed:8895556,
CC       ECO:0000269|PubMed:9753692}.
CC   -!- DEVELOPMENTAL STAGE: Synthesis starts during germination and outgrowth,
CC       and is highest at the end of exponential growth. Present in dormant
CC       spores. {ECO:0000269|PubMed:7890752}.
CC   -!- INDUCTION: By heat shock, salt stress, oxidative stress, glucose
CC       limitation and oxygen limitation.
CC   -!- PTM: Phosphorylated. {ECO:0000269|PubMed:1556067}.
CC   -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00193, ECO:0000305}.
DR   EMBL; M15811; AAA22635.1; -; Genomic_DNA.
DR   EMBL; D50453; BAA08947.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12107.1; -; Genomic_DNA.
DR   PIR; A26936; A26936.
DR   RefSeq; NP_388195.1; NC_000964.3.
DR   RefSeq; WP_003246440.1; NZ_JNCM01000030.1.
DR   PDB; 1EE1; X-ray; 2.06 A; A/B=2-272.
DR   PDB; 1FYD; X-ray; 2.25 A; A/B=2-272.
DR   PDB; 1IFX; X-ray; 2.25 A; A/B=2-272.
DR   PDB; 1IH8; X-ray; 1.90 A; A/B=2-272.
DR   PDB; 1KQP; X-ray; 1.03 A; A/B=2-272.
DR   PDB; 1NSY; X-ray; 2.00 A; A/B=2-272.
DR   PDB; 2NSY; X-ray; 2.00 A; A/B=2-272.
DR   PDBsum; 1EE1; -.
DR   PDBsum; 1FYD; -.
DR   PDBsum; 1IFX; -.
DR   PDBsum; 1IH8; -.
DR   PDBsum; 1KQP; -.
DR   PDBsum; 1NSY; -.
DR   PDBsum; 2NSY; -.
DR   SMR; P08164; -.
DR   STRING; 224308.BSU03130; -.
DR   BindingDB; P08164; -.
DR   ChEMBL; CHEMBL4615; -.
DR   DrugBank; DB02596; Alpha,Beta-Methyleneadenosine-5'-Triphosphate.
DR   DrugBank; DB04099; Deamido-Nad+.
DR   DrugBank; DB00798; Gentamicin.
DR   jPOST; P08164; -.
DR   PaxDb; P08164; -.
DR   PRIDE; P08164; -.
DR   EnsemblBacteria; CAB12107; CAB12107; BSU03130.
DR   GeneID; 938339; -.
DR   KEGG; bsu:BSU03130; -.
DR   PATRIC; fig|224308.179.peg.327; -.
DR   eggNOG; ENOG4107RA1; Bacteria.
DR   eggNOG; COG0171; LUCA.
DR   HOGENOM; HOG000238070; -.
DR   InParanoid; P08164; -.
DR   KO; K01916; -.
DR   OMA; CAINPIG; -.
DR   PhylomeDB; P08164; -.
DR   BioCyc; BSUB:BSU03130-MONOMER; -.
DR   BRENDA; 6.3.1.5; 658.
DR   SABIO-RK; P08164; -.
DR   UniPathway; UPA00253; UER00333.
DR   EvolutionaryTrace; P08164; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004359; F:glutaminase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro.
DR   GO; GO:0008795; F:NAD+ synthase activity; IBA:GO_Central.
DR   GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central.
DR   GO; GO:0030435; P:sporulation resulting in formation of a cellular spore; IEA:UniProtKB-KW.
DR   CDD; cd00553; NAD_synthase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00193; NadE_ammonia_dep; 1.
DR   InterPro; IPR022310; NAD/GMP_synthase.
DR   InterPro; IPR003694; NAD_synthase.
DR   InterPro; IPR022926; NH(3)-dep_NAD(+)_synth.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR23090; PTHR23090; 1.
DR   Pfam; PF02540; NAD_synthase; 1.
DR   TIGRFAMs; TIGR00552; nadE; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P08164.
DR   SWISS-2DPAGE; P08164.
KW   3D-structure; ATP-binding; Direct protein sequencing; Ligase; Magnesium;
KW   Metal-binding; NAD; Nucleotide-binding; Phosphoprotein; Reference proteome;
KW   Sporulation; Stress response.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1556067,
FT                   ECO:0000269|PubMed:9298659"
FT   CHAIN           2..272
FT                   /note="NH(3)-dependent NAD(+) synthetase"
FT                   /id="PRO_0000152159"
FT   NP_BIND         45..52
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1FYD,
FT                   ECO:0000244|PDB:1IH8, ECO:0000244|PDB:1KQP,
FT                   ECO:0000244|PDB:1NSY, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   NP_BIND         258..259
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1IFX,
FT                   ECO:0000244|PDB:1KQP, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   METAL           51
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000244|PDB:1KQP, ECO:0000244|PDB:1NSY,
FT                   ECO:0000244|PDB:2NSY, ECO:0000255|HAMAP-Rule:MF_00193"
FT   METAL           163
FT                   /note="Magnesium"
FT                   /evidence="ECO:0000244|PDB:1KQP, ECO:0000244|PDB:1NSY,
FT                   ECO:0000244|PDB:2NSY, ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         33
FT                   /note="Deamido-NAD; shared with neighboring subunit"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1IFX,
FT                   ECO:0000244|PDB:1KQP, ECO:0000244|PDB:2NSY"
FT   BINDING         79
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1FYD,
FT                   ECO:0000244|PDB:1IH8, ECO:0000244|PDB:1KQP,
FT                   ECO:0000244|PDB:1NSY, ECO:0000244|PDB:2NSY"
FT   BINDING         85
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1FYD,
FT                   ECO:0000244|PDB:1IH8, ECO:0000244|PDB:1KQP,
FT                   ECO:0000244|PDB:1NSY, ECO:0000244|PDB:2NSY"
FT   BINDING         138
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1IFX,
FT                   ECO:0000244|PDB:1KQP, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         158
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1KQP,
FT                   ECO:0000244|PDB:1NSY, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         171
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1IFX,
FT                   ECO:0000244|PDB:1KQP, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         178
FT                   /note="Deamido-NAD; shared with neighboring subunit"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1IFX,
FT                   ECO:0000244|PDB:1KQP, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         187
FT                   /note="ATP"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1FYD,
FT                   ECO:0000244|PDB:1IH8, ECO:0000244|PDB:1KQP,
FT                   ECO:0000244|PDB:1NSY, ECO:0000244|PDB:2NSY,
FT                   ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         209
FT                   /note="ATP; via amide nitrogen and carbonyl oxygen"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1FYD,
FT                   ECO:0000244|PDB:1IH8, ECO:0000244|PDB:1NSY,
FT                   ECO:0000244|PDB:2NSY, ECO:0000255|HAMAP-Rule:MF_00193"
FT   BINDING         224
FT                   /note="Deamido-NAD"
FT                   /evidence="ECO:0000244|PDB:1EE1, ECO:0000244|PDB:1KQP,
FT                   ECO:0000244|PDB:2NSY"
FT   HELIX           3..11
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           19..37
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          41..45
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           50..68
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          74..79
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          82..84
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           88..98
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          101..105
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           109..123
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           129..151
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          154..156
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           161..164
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   TURN            165..167
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   TURN            171..175
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   TURN            181..184
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           187..196
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           202..205
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          214..216
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           221..225
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           229..236
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           243..255
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   HELIX           257..260
FT                   /evidence="ECO:0000244|PDB:1KQP"
FT   STRAND          261..264
FT                   /evidence="ECO:0000244|PDB:1IH8"
SQ   SEQUENCE   272 AA;  30395 MW;  8021E88B5946C2E0 CRC64;
     MSMQEKIMRE LHVKPSIDPK QEIEDRVNFL KQYVKKTGAK GFVLGISGGQ DSTLAGRLAQ
     LAVESIREEG GDAQFIAVRL PHGTQQDEDD AQLALKFIKP DKSWKFDIKS TVSAFSDQYQ
     QETGDQLTDF NKGNVKARTR MIAQYAIGGQ EGLLVLGTDH AAEAVTGFFT KYGDGGADLL
     PLTGLTKRQG RTLLKELGAP ERLYLKEPTA DLLDEKPQQS DETELGISYD EIDDYLEGKE
     VSAKVSEALE KRYSMTEHKR QVPASMFDDW WK
//

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