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Database: UniProt
Entry: A4SNU1
LinkDB: A4SNU1
Original site: A4SNU1 
ID   PDXB_AERS4              Reviewed;         377 AA.
AC   A4SNU1;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   16-JAN-2019, entry version 78.
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=ASA_2534;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A.,
RA   Kimball J., Munholland J., Murphy C., Sarty D., Williams J.,
RA   Nash J.H., Johnson S.C., Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights
RT   into the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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; CP000644; ABO90563.1; -; Genomic_DNA.
DR   RefSeq; WP_005310562.1; NC_009348.1.
DR   ProteinModelPortal; A4SNU1; -.
DR   SMR; A4SNU1; -.
DR   STRING; 382245.ASA_2534; -.
DR   PRIDE; A4SNU1; -.
DR   EnsemblBacteria; ABO90563; ABO90563; ASA_2534.
DR   GeneID; 4997223; -.
DR   KEGG; asa:ASA_2534; -.
DR   PATRIC; fig|382245.13.peg.2499; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   OrthoDB; 1638924at2; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000225; 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.
FT   CHAIN         1    377       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297431.
FT   NP_BIND     210    212       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    212    212       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    241    241       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    258    258       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     236    236       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     261    261       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     262    262       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   377 AA;  41462 MW;  48EA1F0D46D4F93E CRC64;
     MKIVVDENMP HALELFAEFG EVIPLPGRQM QAVDLQDADV LLVRSVTRVD AELLATSPRL
     RFVGTATIGT DHVDKALLAV RNIPFFSAPG CNKYSVGDYV LSTLLVLAER HELNLREMSL
     AVIGAGNTGE CVACKAEALG MRVLRCDPPR ARVAGQAGET DAFVDYQTAL GADIVSFHVP
     ITREGPDATF HLLDEQVIAA RPAGQILVNA SRGEVWDNQA LLARQQGLEP LRLVMDVWEG
     EPEPLRALVP HTEIATPHIA GYSLEGKARG TWMLYQALCQ QLGRAARQDL QSLLPAPEVR
     ALTPGQPVDQ ALIKQLVHLI YDVRRDDARF RNRIELPGSF DEQRKHYPER RELSSLHVNG
     PFASDTLARL GFTVQPG
//
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