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Database: UniProt
Entry: A0KLP0
LinkDB: A0KLP0
Original site: A0KLP0 
ID   PDXB_AERHH              Reviewed;         376 AA.
AC   A0KLP0;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   13-FEB-2019, entry version 79.
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=AHA_2683;
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 /
OS   JCM 1027 / KCTC 2358 / NCIMB 9240).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / JCM 1027 / KCTC 2358 / NCIMB 9240;
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J.,
RA   Haft D.H., Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M.,
RA   Jin S., Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all
RT   trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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; CP000462; ABK37289.1; -; Genomic_DNA.
DR   RefSeq; WP_011706497.1; NC_008570.1.
DR   RefSeq; YP_857191.1; NC_008570.1.
DR   ProteinModelPortal; A0KLP0; -.
DR   SMR; A0KLP0; -.
DR   STRING; 380703.AHA_2683; -.
DR   EnsemblBacteria; ABK37289; ABK37289; AHA_2683.
DR   GeneID; 4490660; -.
DR   KEGG; aha:AHA_2683; -.
DR   PATRIC; fig|380703.7.peg.2689; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   BioCyc; AHYD380703:G1G7B-2681-MONOMER; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000756; 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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    376       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297430.
FT   NP_BIND     209    211       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    211    211       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    240    240       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    257    257       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      45     45       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     235    235       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     260    260       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     261    261       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   376 AA;  41143 MW;  033AF98319DB2E03 CRC64;
     MKIVVDENMP HARELFAEFG EVIPLPGRQM LATDLQEADV LLVRSVTRVD AALLASCPRL
     SFVGTATIGT DHVDKGLLAE RGIPFFSAPG CNKYSVGDYV LSALLVLAER HELNLGAMSL
     AVIGAGNTGE CVAGKAEALG MRVLRCDPPR ARAAEANEAA QFVDYQQALE ADIVSFHVPI
     TRQGPDATFH LLDAAQIAAR PAGQILINAS RGEVWDNQAL LARQQSQAPL RLVMDVWEGE
     PEPLQALVPH TELATPHIAG YSLEGKARGT WMLYEALCRQ LRRTPRQDLQ SLLPIPEVRE
     VTPGQSADQA LIKQLVHLIY DVRRDDARFR NRLGVAGSFD EQRKHYPERR ELSSLQLKGP
     FAGAALARLG FVCQPD
//
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