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Database: UniProt
Entry: Q7MV70
LinkDB: Q7MV70
Original site: Q7MV70 
ID   PDXB_PORGI              Reviewed;         369 AA.
AC   Q7MV70;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 2.
DT   25-OCT-2017, entry version 100.
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=PG_1220;
OS   Porphyromonas gingivalis (strain ATCC BAA-308 / W83).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales;
OC   Porphyromonadaceae; Porphyromonas.
OX   NCBI_TaxID=242619;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-308 / W83;
RX   PubMed=12949112; DOI=10.1128/JB.185.18.5591-5601.2003;
RA   Nelson K.E., Fleischmann R.D., DeBoy R.T., Paulsen I.T., Fouts D.E.,
RA   Eisen J.A., Daugherty S.C., Dodson R.J., Durkin A.S., Gwinn M.L.,
RA   Haft D.H., Kolonay J.F., Nelson W.C., Mason T.M., Tallon L., Gray J.,
RA   Granger D., Tettelin H., Dong H., Galvin J.L., Duncan M.J.,
RA   Dewhirst F.E., Fraser C.M.;
RT   "Complete genome sequence of the oral pathogenic bacterium
RT   Porphyromonas gingivalis strain W83.";
RL   J. Bacteriol. 185:5591-5601(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: 4-phospho-D-erythronate + NAD(+) = (3R)-3-
CC       hydroxy-2-oxo-4-phosphonooxybutanoate + NADH. {ECO:0000255|HAMAP-
CC       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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAQ66310.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE015924; AAQ66310.1; ALT_INIT; Genomic_DNA.
DR   ProteinModelPortal; Q7MV70; -.
DR   SMR; Q7MV70; -.
DR   STRING; 242619.PG1220; -.
DR   EnsemblBacteria; AAQ66310; AAQ66310; PG_1220.
DR   KEGG; pgi:PG_1220; -.
DR   PATRIC; fig|242619.8.peg.1133; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   KO; K03473; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000588; 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-KW.
DR   CDD; cd12158; ErythrP_dh; 1.
DR   HAMAP; MF_01825; PdxB; 1.
DR   InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom.
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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    369       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075981.
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      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     233    233       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     258    258       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
SQ   SEQUENCE   369 AA;  40669 MW;  9C7FF0957346B0FB CRC64;
     MKIVAEASVP YLRGIVDPVA DITYLHSDCF SPDTIRHARV LIVRSITKCT PALLQGTDVR
     LITTATAGFD HIDREYCESH GILWRNSPGC NATAVAQYVM CCLCRLALRE GFSLKEKVMG
     IVGVGHVGGE LKRLASAYGM EFLLCDPPRS EAEQDNSFLP LSRLVEQCDI ISFHVPLTHE
     DPHATYHLIG EAFLRSCADK RPILINACRG AVADTQALIR AVKSGWLQAL VIDCWEGEPD
     IDLSLLDLAD IATPHIAGFS ADGKANGARM CLEAITEVFG LEFPLLHTLA PPPPTHPIID
     LSLFPDHRIE RALLHTFDPL VPDRSLRASP KTFEEQRKAY PHPREMKAFT VVGATTEEAK
     ILRGMDFIS
//
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