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Database: UniProt
Entry: C1DM66
LinkDB: C1DM66
Original site: C1DM66 
ID   PDXB_AZOVD              Reviewed;         380 AA.
AC   C1DM66;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 1.
DT   16-JAN-2019, entry version 63.
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=Avin_29870;
OS   Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=322710;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ / ATCC BAA-1303;
RX   PubMed=19429624; DOI=10.1128/JB.00504-09;
RA   Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA   Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA   Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K.,
RA   Hernandez J.A., Houmiel K., Imperial J., Kennedy C., Larson T.J.,
RA   Latreille P., Ligon L.S., Lu J., Maerk M., Miller N.M., Norton S.,
RA   O'Carroll I.P., Paulsen I., Raulfs E.C., Roemer R., Rosser J.,
RA   Segura D., Slater S., Stricklin S.L., Studholme D.J., Sun J.,
RA   Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H., Dean D.R.,
RA   Dixon R., Wood D.;
RT   "Genome sequence of Azotobacter vinelandii, an obligate aerobe
RT   specialized to support diverse anaerobic metabolic processes.";
RL   J. Bacteriol. 191:4534-4545(2009).
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; CP001157; ACO79153.1; -; Genomic_DNA.
DR   RefSeq; WP_012701540.1; NC_012560.1.
DR   ProteinModelPortal; C1DM66; -.
DR   SMR; C1DM66; -.
DR   STRING; 322710.Avin_29870; -.
DR   PRIDE; C1DM66; -.
DR   EnsemblBacteria; ACO79153; ACO79153; Avin_29870.
DR   KEGG; avn:Avin_29870; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   BioCyc; AVIN322710:G1GCS-2854-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002424; 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:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; IEA:UniProtKB-UniRule.
DR   CDD; cd12158; ErythrP_dh; 1.
DR   Gene3D; 3.30.1370.170; -; 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; IPR024531; Erythronate-4-P_DHase_dimer.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR038251; PdxB_dimer_sf.
DR   PANTHER; PTHR42938:SF3; PTHR42938:SF3; 1.
DR   Pfam; PF00389; 2-Hacid_dh; 1.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   Pfam; PF11890; DUF3410; 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.
FT   CHAIN         1    380       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_1000216068.
FT   NP_BIND     126    127       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   NP_BIND     205    207       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    207    207       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    236    236       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    253    253       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      66     66       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     231    231       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     256    256       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     257    257       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   380 AA;  41469 MW;  FD50B4D555C5D469 CRC64;
     MRILADENIP LVHAFFSAFG EIRQLPGRAI VSGSLGDADV LLVRSVTRVD AALLEGSRVR
     FVGTCTIGTD HLDLDYLRRR GIAWASAPGC NARGVVDYVL GSLLSLAERQ GVDLASRCYG
     VVGAGQVGGR LVEVLRGLGW RVLVCDPPRQ ALERGDFVDL PTLLRECDVL SVHTPLTHEG
     AHPTRHLFGR EQLARLRPGT WLINASRGAV VDNRALREAL AGRTDLQAVL DVWEGEPLVD
     VALAGLCHIA TPHIAGYSLD GKLRGTAQVY RAFCEQQGVP PGVLLDELLP PPWLGELGLD
     GRADPAWALA TLCRAVYDPR RDDADFRRSL EGDEQARRSA FDALRKHYPP RREIDGLRVR
     LSGEAPRLRQ LVRALGAEPV
//
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