(data stored in ACNUC7421 zone)

SWISSPROT: PDXS_BACSU

ID   PDXS_BACSU              Reviewed;         294 AA.
AC   P37527; P27877;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   11-DEC-2019, entry version 150.
DE   RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824};
DE            Short=PLP synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824};
DE            EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01824, ECO:0000269|PubMed:16030023, ECO:0000269|PubMed:17189272, ECO:0000269|PubMed:18260082, ECO:0000269|PubMed:18271580, ECO:0000269|PubMed:18516049};
DE   AltName: Full=Pdx1 {ECO:0000255|HAMAP-Rule:MF_01824};
DE   AltName: Full=Superoxide-inducible protein 7;
DE            Short=SOI7;
GN   Name=pdxS {ECO:0000255|HAMAP-Rule:MF_01824}; Synonyms=yaaD;
GN   OrderedLocusNames=BSU00110;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA   Ogasawara N., Nakai S., Yoshikawa H.;
RT   "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT   chromosome containing the replication origin.";
RL   DNA Res. 1:1-14(1994).
RN   [2]
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   [3]
RP   PROTEIN SEQUENCE OF 2-16.
RC   STRAIN=168 / DB100;
RX   PubMed=1495386; DOI=10.1111/j.1365-2958.1992.tb00882.x;
RA   Mitchell C., Morris P.W., Vary J.C.;
RT   "Amino acid sequences of several Bacillus subtilis proteins modified by
RT   apparent guanylylation.";
RL   Mol. Microbiol. 6:1579-1581(1992).
RN   [4]
RP   PROTEIN SEQUENCE OF 2-32.
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   CHARACTERIZATION.
RC   STRAIN=168 / SMY;
RX   PubMed=14762015; DOI=10.1128/jb.186.4.1191-1196.2004;
RA   Belitsky B.R.;
RT   "Physical and enzymological interaction of Bacillus subtilis proteins
RT   required for de novo pyridoxal 5'-phosphate biosynthesis.";
RL   J. Bacteriol. 186:1191-1196(2004).
RN   [6]
RP   MUTAGENESIS OF LYS-149, IDENTIFICATION OF REACTION SUBSTRATES, AND PH
RP   DEPENDENCE.
RX   PubMed=15771487; DOI=10.1021/ja042792t;
RA   Burns K.E., Xiang Y., Kinsland C.L., McLafferty F.W., Begley T.P.;
RT   "Reconstitution and biochemical characterization of a new pyridoxal-5'-
RT   phosphate biosynthetic pathway.";
RL   J. Am. Chem. Soc. 127:3682-3683(2005).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   IDENTIFICATION OF REACTION PRODUCT.
RC   STRAIN=168;
RX   PubMed=16030023; DOI=10.1074/jbc.m501356200;
RA   Raschle T., Amrhein N., Fitzpatrick T.B.;
RT   "On the two components of pyridoxal 5'-phosphate synthase from Bacillus
RT   subtilis.";
RL   J. Biol. Chem. 280:32291-32300(2005).
RN   [8]
RP   COMPLEX FORMATION OF PDXS AND PDXT.
RX   PubMed=17408246; DOI=10.1021/bi602602x;
RA   Neuwirth M., Flicker K., Strohmeier M., Tews I., Macheroux P.;
RT   "Thermodynamic characterization of the protein-protein interaction in the
RT   heteromeric Bacillus subtilis pyridoxalphosphate synthase.";
RL   Biochemistry 46:5131-5139(2007).
RN   [9]
RP   CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-81 AND LYS-149, ACTIVE SITE,
RP   REACTION MECHANISM, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=168;
RX   PubMed=17189272; DOI=10.1074/jbc.m610614200;
RA   Raschle T., Arigoni D., Brunisholz R., Rechsteiner H., Amrhein N.,
RA   Fitzpatrick T.B.;
RT   "Reaction mechanism of pyridoxal 5'-phosphate synthase. Detection of an
RT   enzyme-bound chromophoric intermediate.";
RL   J. Biol. Chem. 282:6098-6105(2007).
RN   [10]
RP   CATALYTIC ACTIVITY, IDENTIFICATION OF REACTION INTERMEDIATE, AND REACTION
RP   MECHANISM.
RX   PubMed=18260082; DOI=10.1002/anie.200704390;
RA   Hanes J.W., Keresztes I., Begley T.P.;
RT   "Trapping of a chromophoric intermediate in the Pdx1-catalyzed biosynthesis
RT   of pyridoxal 5'-phosphate.";
RL   Angew. Chem. Int. Ed. Engl. 47:2102-2105(2008).
RN   [11]
RP   FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION OF GLYCERALDEHAYDE-3-PHOSPHATE
RP   AS SUBSTRATE, CHARACTERIZATION OF REACTION INTERMEDIATE, AND REACTION
RP   MECHANISM.
RC   STRAIN=168;
RX   PubMed=18271580; DOI=10.1021/ja076604l;
RA   Hanes J.W., Burns K.E., Hilmey D.G., Chatterjee A., Dorrestein P.C.,
RA   Begley T.P.;
RT   "Mechanistic studies on pyridoxal phosphate synthase: the reaction pathway
RT   leading to a chromophoric intermediate.";
RL   J. Am. Chem. Soc. 130:3043-3052(2008).
RN   [12]
RP   CATALYTIC ACTIVITY, CHARACTERIZATION OF REACTION INTERMEDIATES, AND
RP   REACTION MECHANISM.
RX   PubMed=18516049; DOI=10.1038/nchembio.93;
RA   Hanes J.W., Keresztes I., Begley T.P.;
RT   "13C NMR snapshots of the complex reaction coordinate of pyridoxal
RT   phosphate synthase.";
RL   Nat. Chem. Biol. 4:425-430(2008).
RN   [13]
RP   MUTAGENESIS OF LYS-18; SER-75 AND ASP-99.
RX   PubMed=19152323; DOI=10.1021/bi801887r;
RA   Wallner S., Neuwirth M., Flicker K., Tews I., Macheroux P.;
RT   "Dissection of contributions from invariant amino acids to complex
RT   formation and catalysis in the heteromeric pyridoxal 5-phosphate synthase
RT   complex from Bacillus subtilis.";
RL   Biochemistry 48:1928-1935(2009).
RN   [14]
RP   FLUORESCENCE SPECTROSCOPY, AND CROSS LINKING.
RX   PubMed=19074821; DOI=10.1074/jbc.m804728200;
RA   Raschle T., Speziga D., Kress W., Moccand C., Gehrig P., Amrhein N.,
RA   Weber-Ban E., Fitzpatrick T.B.;
RT   "Intersubunit cross-talk in pyridoxal 5'-phosphate synthase, coordinated by
RT   the C terminus of the synthase subunit.";
RL   J. Biol. Chem. 284:7706-7718(2009).
RN   [15]
RP   X-RAY CRYSTALLOGRAPHY (2.08 ANGSTROMS) OF APOENZYME AND COMPLEX WITH
RP   SUBUNIT PDXS, AND SUBUNIT.
RX   PubMed=17159152; DOI=10.1073/pnas.0604950103;
RA   Strohmeier M., Raschle T., Mazurkiewicz J., Rippe K., Sinning I.,
RA   Fitzpatrick T.B., Tews I.;
RT   "Structure of a bacterial pyridoxal 5'-phosphate synthase complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:19284-19289(2006).
CC   -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from ribose
CC       5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and ammonia. The
CC       ammonia is provided by the PdxT subunit. Can also use ribulose 5-
CC       phosphate and dihydroxyacetone phosphate as substrates, resulting from
CC       enzyme-catalyzed isomerization of RBP and G3P, respectively.
CC       {ECO:0000255|HAMAP-Rule:MF_01824, ECO:0000269|PubMed:16030023,
CC       ECO:0000269|PubMed:18271580}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate +
CC         L-glutamine = H(+) + 3 H2O + L-glutamate + phosphate + pyridoxal 5'-
CC         phosphate; Xref=Rhea:RHEA:31507, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:58359, ChEBI:CHEBI:59776,
CC         ChEBI:CHEBI:597326; EC=4.3.3.6; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01824, ECO:0000269|PubMed:16030023,
CC         ECO:0000269|PubMed:17189272, ECO:0000269|PubMed:18260082,
CC         ECO:0000269|PubMed:18271580, ECO:0000269|PubMed:18516049};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=68 uM for ribose-5-phosphate {ECO:0000269|PubMed:16030023};
CC         KM=53 uM for ribose-5-phosphate {ECO:0000269|PubMed:17189272};
CC         KM=3.18 mM for ribulose-5-phosphate {ECO:0000269|PubMed:17189272};
CC         KM=77 uM for D-glyceraldehyde-3-phosphate
CC         {ECO:0000269|PubMed:16030023};
CC         Note=kcat is 0.040 min(-1) with ribose-5-phosphate as substrate. kcat
CC         is 0.042 min(-1) with ribulose-5-phosphate as substrate.
CC         {ECO:0000269|PubMed:17189272};
CC       pH dependence:
CC         Optimum pH is 6-6.5. {ECO:0000269|PubMed:15771487};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_01824}.
CC   -!- SUBUNIT: Homohexamer and homododecamer. In the presence of PdxT, forms
CC       a dodecamer of heterodimers. {ECO:0000255|HAMAP-Rule:MF_01824,
CC       ECO:0000269|PubMed:17159152}.
CC   -!- INTERACTION:
CC       Self; NbExp=2; IntAct=EBI-7828661, EBI-7828661;
CC       P37528:pdxT; NbExp=5; IntAct=EBI-7828661, EBI-7051766;
CC   -!- INDUCTION: By superoxide.
CC   -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000255|HAMAP-
CC       Rule:MF_01824}.
DR   EMBL; AL009126; CAB11787.1; -; Genomic_DNA.
DR   PIR; S66041; S66041.
DR   RefSeq; NP_387892.1; NC_000964.3.
DR   RefSeq; WP_003247145.1; NZ_JNCM01000024.1.
DR   PDB; 2NV1; X-ray; 2.08 A; A/B/C/D/E/F=1-294.
DR   PDB; 2NV2; X-ray; 2.12 A; A/C/E/G/I/K/M/O/Q/S/U/W=1-294.
DR   PDBsum; 2NV1; -.
DR   PDBsum; 2NV2; -.
DR   SMR; P37527; -.
DR   DIP; DIP-61325N; -.
DR   IntAct; P37527; 2.
DR   MINT; P37527; -.
DR   STRING; 224308.BSU00110; -.
DR   jPOST; P37527; -.
DR   PaxDb; P37527; -.
DR   PRIDE; P37527; -.
DR   EnsemblBacteria; CAB11787; CAB11787; BSU00110.
DR   GeneID; 939988; -.
DR   KEGG; bsu:BSU00110; -.
DR   PATRIC; fig|224308.179.peg.11; -.
DR   eggNOG; ENOG4105CD9; Bacteria.
DR   eggNOG; COG0214; LUCA.
DR   HOGENOM; HOG000227586; -.
DR   InParanoid; P37527; -.
DR   KO; K06215; -.
DR   OMA; IGVDMID; -.
DR   PhylomeDB; P37527; -.
DR   BioCyc; BSUB:BSU00110-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-15502; -.
DR   BRENDA; 4.3.3.6; 658.
DR   UniPathway; UPA00245; -.
DR   EvolutionaryTrace; P37527; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016843; F:amine-lyase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR   GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006520; P:cellular amino acid metabolic process; IBA:GO_Central.
DR   GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
DR   CDD; cd04727; pdxS; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_01824; PdxS; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001852; PdxS/SNZ.
DR   InterPro; IPR033755; PdxS/SNZ_N.
DR   InterPro; IPR011060; RibuloseP-bd_barrel.
DR   PANTHER; PTHR31829; PTHR31829; 1.
DR   Pfam; PF01680; SOR_SNZ; 1.
DR   PIRSF; PIRSF029271; Pdx1; 1.
DR   SUPFAM; SSF51366; SSF51366; 1.
DR   TIGRFAMs; TIGR00343; TIGR00343; 1.
DR   PROSITE; PS01235; PDXS_SNZ_1; 1.
DR   PROSITE; PS51129; PDXS_SNZ_2; 1.
PE   1: Evidence at protein level;
DR   PRODOM; P37527.
DR   SWISS-2DPAGE; P37527.
KW   3D-structure; Direct protein sequencing; Lyase; Pyridoxal phosphate;
KW   Reference proteome; Schiff base.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1495386,
FT                   ECO:0000269|PubMed:9298659"
FT   CHAIN           2..294
FT                   /note="Pyridoxal 5'-phosphate synthase subunit PdxS"
FT                   /id="PRO_0000109383"
FT   REGION          235..236
FT                   /note="D-ribose 5-phosphate binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   ACT_SITE        81
FT                   /note="Schiff-base intermediate with D-ribose 5-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824,
FT                   ECO:0000269|PubMed:17189272"
FT   BINDING         24
FT                   /note="D-ribose 5-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         153
FT                   /note="D-ribose 5-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         165
FT                   /note="Glyceraldehyde 3-phosphate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   BINDING         214
FT                   /note="D-ribose 5-phosphate; via amide nitrogen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01824"
FT   MUTAGEN         18
FT                   /note="K->A: Almost no effect on activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         75
FT                   /note="S->A: Almost no effect on activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         81
FT                   /note="K->A,R: No activity, does not form covalent adduct
FT                   with ribose-5-phosphate."
FT                   /evidence="ECO:0000269|PubMed:17189272"
FT   MUTAGEN         99
FT                   /note="D->A: Results in 20-fold reduction of activity."
FT                   /evidence="ECO:0000269|PubMed:19152323"
FT   MUTAGEN         149
FT                   /note="K->A: No activity, does not form covalent adduct
FT                   with ribose-5-phosphate or ribulose 5-phosphate."
FT                   /evidence="ECO:0000269|PubMed:15771487,
FT                   ECO:0000269|PubMed:17189272"
FT   MUTAGEN         149
FT                   /note="K->R: No activity, but can, as the wild-type, form
FT                   covalent adduct with ribose-5-phosphate."
FT                   /evidence="ECO:0000269|PubMed:17189272"
FT   CONFLICT        30
FT                   /note="Q -> D (in Ref. 4; AA sequence)"
FT                   /evidence="ECO:0000305"
FT   STRAND          3..5
FT                   /evidence="ECO:0000244|PDB:2NV2"
FT   HELIX           7..15
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   TURN            16..19
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          21..27
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           28..36
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          40..44
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           49..54
FT                   /evidence="ECO:0000244|PDB:2NV2"
FT   HELIX           64..73
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          78..82
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           87..96
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          99..103
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           118..120
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          125..131
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           132..140
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          144..148
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   TURN            152..154
FT                   /evidence="ECO:0000244|PDB:2NV2"
FT   HELIX           158..176
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           179..181
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           182..189
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           193..202
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          209..211
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           218..226
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   STRAND          232..234
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           236..240
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           244..256
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   TURN            257..259
FT                   /evidence="ECO:0000244|PDB:2NV1"
FT   HELIX           261..267
FT                   /evidence="ECO:0000244|PDB:2NV1"
SQ   SEQUENCE   294 AA;  31612 MW;  1662DA1925DDA9B1 CRC64;
     MAQTGTERVK RGMAEMQKGG VIMDVINAEQ AKIAEEAGAV AVMALERVPA DIRAAGGVAR
     MADPTIVEEV MNAVSIPVMA KARIGHIVEA RVLEAMGVDY IDESEVLTPA DEEFHLNKNE
     YTVPFVCGCR DLGEATRRIA EGASMLRTKG EPGTGNIVEA VRHMRKVNAQ VRKVVAMSED
     ELMTEAKNLG APYELLLQIK KDGKLPVVNF AAGGVATPAD AALMMQLGAD GVFVGSGIFK
     SDNPAKFAKA IVEATTHFTD YKLIAELSKE LGTAMKGIEI SNLLPEQRMQ ERGW
//

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