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Database: UniProt
Entry: Q83AR8
LinkDB: Q83AR8
Original site: Q83AR8 
ID   PDXB_COXBU              Reviewed;         366 AA.
AC   Q83AR8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   16-JAN-2019, 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=CBU_1812;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Coxiellaceae; Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E.,
RA   Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J.,
RA   DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J.,
RA   Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A.,
RA   Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella
RT   burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(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:
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO91305.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE016828; AAO91305.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_820791.1; NC_002971.3.
DR   ProteinModelPortal; Q83AR8; -.
DR   SMR; Q83AR8; -.
DR   STRING; 227377.CBU_1812; -.
DR   PRIDE; Q83AR8; -.
DR   EnsemblBacteria; AAO91305; AAO91305; CBU_1812.
DR   GeneID; 1209723; -.
DR   KEGG; cbu:CBU_1812; -.
DR   PATRIC; fig|227377.7.peg.1798; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000234432; -.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0033711; F:4-phosphoerythronate dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; ISS:TIGR.
DR   GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR   GO; GO:0036001; P:'de novo' pyridoxal 5'-phosphate biosynthetic process; IBA:GO_Central.
DR   GO; GO:0008615; P:pyridoxine biosynthetic process; ISS:TIGR.
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; Reference proteome.
FT   CHAIN         1    366       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075974.
FT   ACT_SITE    208    208       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    233    233       {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   ACT_SITE    250    250       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING      46     46       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     175    175       NAD; via carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     228    228       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     253    253       NAD; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     254    254       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
SQ   SEQUENCE   366 AA;  40969 MW;  FC5F34670DCF8C1F CRC64;
     MIKILADDRI PFVSELFGDF GELILKPGAH IQNRDLLAVN ALLTRSITSV DSALLEGTAV
     EFVGSATAGF DHIDSTWLKK QSIHWAYAPG ANATAVAEYV LHCVAYLHKK NLLPRKSATA
     AIIGVGHVGC VVSDRLRKIG FTVFHNDPPR AQLEKDFISV PLASLANVDL VCLHTPLVKT
     GNFPTYHLID NRFLKMLKPG SVLLNAGRGA VIDNNALLQC DHVITCLDVW ENEPTVNLQL
     LEKTTIATPH IAGYSKQAKL RATLMIYDAF LKYFHLSDTR RFSELQQLQE TMTLNIQDGR
     NAEDILLTLF DPGRESQRMR ETLAENPDQF EYLRRHFPLR NEFSAIQLTP TPSALLRKEL
     DDWGFK
//
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