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Database: UniProt
Entry: Q8A2E4
LinkDB: Q8A2E4
Original site: Q8A2E4 
ID   PDXB_BACTN              Reviewed;         348 AA.
AC   Q8A2E4;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JAN-2019, entry version 106.
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=BT_3361;
OS   Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / NCTC
OS   10582 / E50 / VPI-5482).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC   Bacteroides.
OX   NCBI_TaxID=226186;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482;
RX   PubMed=12663928; DOI=10.1126/science.1080029;
RA   Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K.,
RA   Chiang H.C., Hooper L.V., Gordon J.I.;
RT   "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL   Science 299:2074-2076(2003).
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; AE015928; AAO78467.1; -; Genomic_DNA.
DR   RefSeq; NP_812273.1; NC_004663.1.
DR   RefSeq; WP_011108789.1; NC_004663.1.
DR   ProteinModelPortal; Q8A2E4; -.
DR   SMR; Q8A2E4; -.
DR   STRING; 226186.BT_3361; -.
DR   PaxDb; Q8A2E4; -.
DR   PRIDE; Q8A2E4; -.
DR   EnsemblBacteria; AAO78467; AAO78467; BT_3361.
DR   GeneID; 1072463; -.
DR   GeneID; 31619332; -.
DR   KEGG; bth:BT_3361; -.
DR   PATRIC; fig|226186.12.peg.3429; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   InParanoid; Q8A2E4; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; BTHE:G13PU-8328-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000001414; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IBA:GO_Central.
DR   CDD; cd12158; ErythrP_dh; 1.
DR   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
DR   InterPro; IPR029753; D-isomer_DH_CS.
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.
DR   PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    348       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075972.
FT   ACT_SITE    209    209       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    238    238       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    255    255       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      46     46       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      67     67       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     147    147       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     233    233       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     258    258       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     259    259       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   348 AA;  39077 MW;  B6178E1AEA3C0E2A CRC64;
     MKIIIDDKIP YIKEAAEKIA DEAIYAPGKD FTRELVQDAD ALIIRTRTHC NRELLEGSKV
     KFIATATIGF DHIDTEYCKQ AGIEWANAPG CNSASVAQYI QSSLLIWKSL RNKKPDELTI
     GIIGVGNVGS KVAKVAQDFG MRVLLNDLPR EEKEGNITFT SLEKIAEECD IITFHVPLYK
     EGKYKTYHLA DGNFFRSLQR KPVVINTSRG EVIETNALLE AINNGIISDA VIDVWEHEPE
     INRELLEKVL IGTPHIAGYS ADGKANATRM SLDSICRFFH LSATYEITPP APSSPLIEAK
     DREEALLKMY NPIEDSNRLK SHPELFETLR GDYPLRREEK AYNIIGIK
//
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