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Database: UniProt
Entry: Q9KQ92
LinkDB: Q9KQ92
Original site: Q9KQ92 
ID   PDXB_VIBCH              Reviewed;         381 AA.
AC   Q9KQ92;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   13-APR-2004, sequence version 2.
DT   16-JAN-2019, entry version 113.
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=VC_2108;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A.,
RA   Gill S.R., Nelson K.E., Read T.D., Tettelin H., Richardson D.L.,
RA   Ermolaeva M.D., Vamathevan J.J., Bass S., Qin H., Dragoi I.,
RA   Sellers P., McDonald L.A., Utterback T.R., Fleischmann R.D.,
RA   Nierman W.C., White O., Salzberg S.L., Smith H.O., Colwell R.R.,
RA   Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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=AAF95254.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; AE003852; AAF95254.1; ALT_INIT; Genomic_DNA.
DR   PIR; C82118; C82118.
DR   RefSeq; NP_231740.1; NC_002505.1.
DR   PDB; 5DT9; X-ray; 2.66 A; A=1-381.
DR   PDBsum; 5DT9; -.
DR   ProteinModelPortal; Q9KQ92; -.
DR   SMR; Q9KQ92; -.
DR   STRING; 243277.VC2108; -.
DR   DNASU; 2613364; -.
DR   EnsemblBacteria; AAF95254; AAF95254; VC_2108.
DR   GeneID; 2613364; -.
DR   KEGG; vch:VC2108; -.
DR   PATRIC; fig|243277.26.peg.2014; -.
DR   eggNOG; ENOG4105CJ0; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   KO; K03473; -.
DR   OMA; SAPGCNA; -.
DR   UniPathway; UPA00244; UER00310.
DR   Proteomes; UP000000584; Chromosome 1.
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   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; NAD; Oxidoreductase;
KW   Pyridoxine biosynthesis; Reference proteome.
FT   CHAIN         1    381       Erythronate-4-phosphate dehydrogenase.
FT                                /FTId=PRO_0000075991.
FT   NP_BIND     127    128       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
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      67     67       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   BINDING     147    147       NAD. {ECO:0000255|HAMAP-Rule:MF_01825}.
FT   BINDING     176    176       NAD; via carbonyl oxygen.
FT                                {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}.
FT   BINDING     259    259       Substrate. {ECO:0000255|HAMAP-
FT                                Rule:MF_01825}.
FT   STRAND        1      6       {ECO:0000244|PDB:5DT9}.
FT   HELIX        12     16       {ECO:0000244|PDB:5DT9}.
FT   TURN         17     19       {ECO:0000244|PDB:5DT9}.
FT   STRAND       20     25       {ECO:0000244|PDB:5DT9}.
FT   HELIX        27     29       {ECO:0000244|PDB:5DT9}.
FT   HELIX        32     35       {ECO:0000244|PDB:5DT9}.
FT   STRAND       39     43       {ECO:0000244|PDB:5DT9}.
FT   STRAND       45     47       {ECO:0000244|PDB:5DT9}.
FT   TURN         51     56       {ECO:0000244|PDB:5DT9}.
FT   STRAND       62     68       {ECO:0000244|PDB:5DT9}.
FT   HELIX        75     80       {ECO:0000244|PDB:5DT9}.
FT   STRAND       84     86       {ECO:0000244|PDB:5DT9}.
FT   TURN         89     92       {ECO:0000244|PDB:5DT9}.
FT   HELIX        93    111       {ECO:0000244|PDB:5DT9}.
FT   HELIX       115    117       {ECO:0000244|PDB:5DT9}.
FT   STRAND      120    123       {ECO:0000244|PDB:5DT9}.
FT   HELIX       127    138       {ECO:0000244|PDB:5DT9}.
FT   STRAND      143    146       {ECO:0000244|PDB:5DT9}.
FT   HELIX       148    153       {ECO:0000244|PDB:5DT9}.
FT   HELIX       162    168       {ECO:0000244|PDB:5DT9}.
FT   STRAND      170    174       {ECO:0000244|PDB:5DT9}.
FT   STRAND      180    184       {ECO:0000244|PDB:5DT9}.
FT   HELIX       192    195       {ECO:0000244|PDB:5DT9}.
FT   STRAND      203    206       {ECO:0000244|PDB:5DT9}.
FT   HELIX       210    212       {ECO:0000244|PDB:5DT9}.
FT   HELIX       215    222       {ECO:0000244|PDB:5DT9}.
FT   STRAND      229    234       {ECO:0000244|PDB:5DT9}.
FT   TURN        243    245       {ECO:0000244|PDB:5DT9}.
FT   HELIX       246    248       {ECO:0000244|PDB:5DT9}.
FT   STRAND      249    252       {ECO:0000244|PDB:5DT9}.
FT   HELIX       261    279       {ECO:0000244|PDB:5DT9}.
FT   HELIX       287    290       {ECO:0000244|PDB:5DT9}.
FT   STRAND      298    300       {ECO:0000244|PDB:5DT9}.
FT   HELIX       307    317       {ECO:0000244|PDB:5DT9}.
FT   HELIX       320    330       {ECO:0000244|PDB:5DT9}.
FT   HELIX       336    342       {ECO:0000244|PDB:5DT9}.
FT   HELIX       350    352       {ECO:0000244|PDB:5DT9}.
FT   STRAND      353    357       {ECO:0000244|PDB:5DT9}.
FT   HELIX       364    369       {ECO:0000244|PDB:5DT9}.
FT   STRAND      372    375       {ECO:0000244|PDB:5DT9}.
SQ   SEQUENCE   381 AA;  41865 MW;  CC900794B7B81360 CRC64;
     MKILIDENMP YAQALFSQLG EVILKPGRTL TADDLIDVDA LMIRSVTKVN DALLAKANRL
     KFVGTATAGM DHVDQALLRE RGIFFTAAPG CNKVGVAEYV FSVLMVLAQQ QGFSVFDKTV
     GIIGAGQVGS YLAKCLSGIG MKVLLNDPPK QAQGDEREFT ELETLLKQAD VITLHTPITR
     GGEWPTHHLI DAAILEQLRS DQILINAARG PVVDNAALKA RLQQGDGFTA VLDVFEFEPQ
     VDMELLPLLA FATPHIAGYG LEGKARGTTM IFNSYCEFLG SAHCANPASL LPKAPVPKVY
     LERAWDEETL RTLTQIIYDV RKDDAQFRRE IHQPGAFDLM RKHYWDRREY SAVTLAGGAD
     CHLAPLAKLG FQVEVCDEPT I
//
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