GenomeNet

Database: UniProt
Entry: Q5ZX15
LinkDB: Q5ZX15
Original site: Q5ZX15 
ID   PDXB_LEGPH              Reviewed;         350 AA.
AC   Q5ZX15;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   05-DEC-2018, entry version 84.
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=lpg0918;
OS   Legionella pneumophila subsp. pneumophila (strain Philadelphia 1 /
OS   ATCC 33152 / DSM 7513).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=272624;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Philadelphia 1 / ATCC 33152 / DSM 7513;
RX   PubMed=15448271; DOI=10.1126/science.1099776;
RA   Chien M., Morozova I., Shi S., Sheng H., Chen J., Gomez S.M.,
RA   Asamani G., Hill K., Nuara J., Feder M., Rineer J., Greenberg J.J.,
RA   Steshenko V., Park S.H., Zhao B., Teplitskaya E., Edwards J.R.,
RA   Pampou S., Georghiou A., Chou I.-C., Iannuccilli W., Ulz M.E.,
RA   Kim D.H., Geringer-Sameth A., Goldsberry C., Morozov P., Fischer S.G.,
RA   Segal G., Qu X., Rzhetsky A., Zhang P., Cayanis E., De Jong P.J.,
RA   Ju J., Kalachikov S., Shuman H.A., Russo J.J.;
RT   "The genomic sequence of the accidental pathogen Legionella
RT   pneumophila.";
RL   Science 305:1966-1968(2004).
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; AE017354; AAU27005.1; -; Genomic_DNA.
DR   RefSeq; WP_010946653.1; NC_002942.5.
DR   RefSeq; YP_094952.1; NC_002942.5.
DR   ProteinModelPortal; Q5ZX15; -.
DR   SMR; Q5ZX15; -.
DR   STRING; 272624.lpg0918; -.
DR   PaxDb; Q5ZX15; -.
DR   EnsemblBacteria; AAU27005; AAU27005; lpg0918.
DR   GeneID; 19832484; -.
DR   KEGG; lpn:lpg0918; -.
DR   PATRIC; fig|272624.6.peg.950; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000278825; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000609; 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; IPR029753; D-isomer_DH_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
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; PS00065; D_2_HYDROXYACID_DH_1; 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    350       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000297446.
FT   NP_BIND     124    125       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   NP_BIND     203    205       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    205    205       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    231    231       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    248    248       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     144    144       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     226    226       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     251    251       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
SQ   SEQUENCE   350 AA;  38952 MW;  C164CDBAB117A9D1 CRC64;
     MNILADALLP GLDSAFPPPF TVTLYHKADE IPELLHYKDV LLCRSTLKIN GDLLKNHQIK
     FVATATSGTD HIDFPFLESQ NISIIDAKGC NAISVADYVV ACLAYLDKQQ LIQGKTAGII
     GLGQVGTKVY ERLNAAEFQL CLYDPPKATR DTSFQSCSLE DLFECDLLCV HAELHSDAPY
     PSLNLINRDF LKELKPGCII INASRGGIVN EEALLHLGSA ILYCTDVYNN EPHIDSRIVS
     KATLCTPHIA GHSLEAKFAA VAIVSRKLHQ MLGLPYPQFA TPEKPYRLNE NSDWRELALS
     IYNPIHETLE LKHAGNLSSA FLTLRKNHHH RHDFTTYFDS DSIKKYPLLG
//
DBGET integrated database retrieval system