GenomeNet

Database: UniProt
Entry: A5CWD1
LinkDB: A5CWD1
Original site: A5CWD1 
ID   PDXB_VESOH              Reviewed;         345 AA.
AC   A5CWD1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JAN-2019, entry version 75.
DE   RecName: Full=Erythronate-4-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01825};
DE            EC=1.1.1.290 {ECO:0000255|HAMAP-Rule:MF_01825};
GN   Name=pdxB {ECO:0000255|HAMAP-Rule:MF_01825};
GN   OrderedLocusNames=COSY_0635;
OS   Vesicomyosocius okutanii subsp. Calyptogena okutanii (strain HA).
OC   Bacteria; Proteobacteria; Gammaproteobacteria;
OC   sulfur-oxidizing symbionts.
OX   NCBI_TaxID=412965;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HA;
RX   PubMed=17493812; DOI=10.1016/j.cub.2007.04.039;
RA   Kuwahara H., Yoshida T., Takaki Y., Shimamura S., Nishi S., Harada M.,
RA   Matsuyama K., Takishita K., Kawato M., Uematsu K., Fujiwara Y.,
RA   Sato T., Kato C., Kitagawa M., Kato I., Maruyama T.;
RT   "Reduced genome of the thioautotrophic intracellular symbiont in a
RT   deep-sea clam, Calyptogena okutanii.";
RL   Curr. Biol. 17:881-886(2007).
CC   -!- FUNCTION: Catalyzes the oxidation of erythronate-4-phosphate to 3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=4-phospho-D-erythronate + NAD(+) = (R)-3-hydroxy-2-oxo-4-
CC         phosphooxybutanoate + H(+) + NADH; Xref=Rhea:RHEA:18829,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945,
CC         ChEBI:CHEBI:58538, ChEBI:CHEBI:58766; EC=1.1.1.290;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01825};
CC   -!- PATHWAY: Cofactor biosynthesis; pyridoxine 5'-phosphate
CC       biosynthesis; pyridoxine 5'-phosphate from D-erythrose 4-
CC       phosphate: step 2/5. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01825}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. PdxB subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01825}.
DR   EMBL; AP009247; BAF61748.1; -; Genomic_DNA.
DR   RefSeq; WP_011930018.1; NC_009465.1.
DR   ProteinModelPortal; A5CWD1; -.
DR   SMR; A5CWD1; -.
DR   STRING; 412965.COSY_0635; -.
DR   PRIDE; A5CWD1; -.
DR   EnsemblBacteria; BAF61748; BAF61748; COSY_0635.
DR   KEGG; vok:COSY_0635; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; CVES412965:G1G2Q-643-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12158; ErythrP_dh; 1.
DR   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR020921; Erythronate-4-P_DHase.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   PANTHER; PTHR42938:SF3; PTHR42938:SF3; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis.
FT   CHAIN         1    345       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297479.
FT   ACT_SITE    207    207       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    232    232       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    249    249       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     146    146       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     174    174       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     227    227       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     252    252       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
SQ   SEQUENCE   345 AA;  39077 MW;  5FB62A2484C3D208 CRC64;
     MKLVIDDACY AHKEIFSHFG NISTIAGRDI NSTSVKNADI LIVRSRTKVN HVLLDGSQVK
     FVGSTVTGLD HIDQDYLKSK GIKFFSAQGC NSMAVAEFVI SAIVNLADEL DFDYQKKTLG
     IIGIGNVGAR LAKKAKLMGI KTLLNDPPRQ MYENLPNFVD LKTTLSADIV TFHTPLTVNG
     KYPSYQLLNE NNFHYILDKT ILFNVARGGI IKETIWQEYK TLANIIDCWE DEPNINLKLQ
     NTAYLATPHI AGHSIDAKFI GSFMVYEALC DFLGKKQDSN IKNLINLDKL SINKDTLKNT
     LNKIYDFRQD AKAIQDINNF EDYRRNYPVR YEWHHFKSKT TLPIA
//
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