GenomeNet

Database: UniProt
Entry: Q8ZQ30
LinkDB: Q8ZQ30
Original site: Q8ZQ30 
ID   GHRA_SALTY              Reviewed;         312 AA.
AC   Q8ZQ30;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-DEC-2018, entry version 95.
DE   RecName: Full=Glyoxylate/hydroxypyruvate reductase A {ECO:0000255|HAMAP-Rule:MF_01666};
DE            EC=1.1.1.79 {ECO:0000255|HAMAP-Rule:MF_01666};
DE            EC=1.1.1.81 {ECO:0000255|HAMAP-Rule:MF_01666};
DE   AltName: Full=2-ketoacid reductase {ECO:0000255|HAMAP-Rule:MF_01666};
GN   Name=ghrA {ECO:0000255|HAMAP-Rule:MF_01666};
GN   OrderedLocusNames=STM1135;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M.,
RA   Waterston R., Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium
RT   LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate
CC       and hydroxypyruvate into glycolate and glycerate, respectively.
CC       {ECO:0000255|HAMAP-Rule:MF_01666}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycolate + NADP(+) = glyoxylate + H(+) + NADPH;
CC         Xref=Rhea:RHEA:10992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29805,
CC         ChEBI:CHEBI:36655, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.79; Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NAD(+) = 3-hydroxypyruvate + H(+) + NADH;
CC         Xref=Rhea:RHEA:17905, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC         ChEBI:CHEBI:17180, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC         EC=1.1.1.81; Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) +
CC         NADPH; Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16659, ChEBI:CHEBI:17180, ChEBI:CHEBI:57783,
CC         ChEBI:CHEBI:58349; EC=1.1.1.81; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01666};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01666}.
CC   -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC       dehydrogenase family. GhrA subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01666}.
DR   EMBL; AE006468; AAL20065.1; -; Genomic_DNA.
DR   RefSeq; NP_460106.1; NC_003197.2.
DR   RefSeq; WP_000402556.1; NC_003197.2.
DR   PDB; 3KBO; X-ray; 2.14 A; A/B/C/D=1-312.
DR   PDB; 3PP8; X-ray; 2.10 A; A=1-312.
DR   PDBsum; 3KBO; -.
DR   PDBsum; 3PP8; -.
DR   ProteinModelPortal; Q8ZQ30; -.
DR   SMR; Q8ZQ30; -.
DR   STRING; 99287.STM1135; -.
DR   PaxDb; Q8ZQ30; -.
DR   PRIDE; Q8ZQ30; -.
DR   DNASU; 1252653; -.
DR   EnsemblBacteria; AAL20065; AAL20065; STM1135.
DR   GeneID; 1252653; -.
DR   KEGG; stm:STM1135; -.
DR   PATRIC; fig|99287.12.peg.1202; -.
DR   eggNOG; ENOG4105JPG; Bacteria.
DR   eggNOG; COG0111; LUCA.
DR   HOGENOM; HOG000136694; -.
DR   KO; K12972; -.
DR   OMA; VQMAEYV; -.
DR   PhylomeDB; Q8ZQ30; -.
DR   BioCyc; SENT99287:STM1135-MONOMER; -.
DR   EvolutionaryTrace; Q8ZQ30; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central.
DR   GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central.
DR   GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR   HAMAP; MF_01666; 2_Hacid_dh_C_GhrA; 1.
DR   InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR   InterPro; IPR023514; GhrA.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02826; 2-Hacid_dh_C; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    312       Glyoxylate/hydroxypyruvate reductase A.
FT                                /FTId=PRO_0000348372.
FT   ACT_SITE    227    227       {ECO:0000255|HAMAP-Rule:MF_01666}.
FT   ACT_SITE    275    275       Proton donor. {ECO:0000255|HAMAP-
FT                                Rule:MF_01666}.
FT   STRAND        1      6       {ECO:0000244|PDB:3PP8}.
FT   STRAND        8     10       {ECO:0000244|PDB:3PP8}.
FT   HELIX        12     22       {ECO:0000244|PDB:3PP8}.
FT   STRAND       26     30       {ECO:0000244|PDB:3PP8}.
FT   STRAND       40     46       {ECO:0000244|PDB:3PP8}.
FT   HELIX        49     52       {ECO:0000244|PDB:3PP8}.
FT   STRAND       58     65       {ECO:0000244|PDB:3PP8}.
FT   HELIX        68     76       {ECO:0000244|PDB:3PP8}.
FT   HELIX        78     80       {ECO:0000244|PDB:3KBO}.
FT   STRAND       87     89       {ECO:0000244|PDB:3PP8}.
FT   HELIX        96    111       {ECO:0000244|PDB:3PP8}.
FT   HELIX       114    122       {ECO:0000244|PDB:3PP8}.
FT   HELIX       134    136       {ECO:0000244|PDB:3KBO}.
FT   STRAND      139    142       {ECO:0000244|PDB:3PP8}.
FT   HELIX       146    156       {ECO:0000244|PDB:3PP8}.
FT   TURN        157    159       {ECO:0000244|PDB:3PP8}.
FT   STRAND      162    168       {ECO:0000244|PDB:3PP8}.
FT   STRAND      176    180       {ECO:0000244|PDB:3PP8}.
FT   HELIX       181    189       {ECO:0000244|PDB:3PP8}.
FT   STRAND      192    196       {ECO:0000244|PDB:3PP8}.
FT   HELIX       202    204       {ECO:0000244|PDB:3PP8}.
FT   HELIX       210    213       {ECO:0000244|PDB:3PP8}.
FT   STRAND      220    224       {ECO:0000244|PDB:3PP8}.
FT   HELIX       228    230       {ECO:0000244|PDB:3PP8}.
FT   HELIX       233    241       {ECO:0000244|PDB:3PP8}.
FT   STRAND      244    251       {ECO:0000244|PDB:3PP8}.
FT   STRAND      254    257       {ECO:0000244|PDB:3PP8}.
FT   HELIX       263    266       {ECO:0000244|PDB:3PP8}.
FT   STRAND      270    272       {ECO:0000244|PDB:3PP8}.
FT   HELIX       282    298       {ECO:0000244|PDB:3PP8}.
FT   TURN        308    311       {ECO:0000244|PDB:3KBO}.
SQ   SEQUENCE   312 AA;  35034 MW;  A46D708D25A7AD11 CRC64;
     MEIIFYHPTF NAAWWVNALE KALPHARVRE WKVGDNNPAD YALVWQPPVE MLAGRRLKAV
     FVLGAGVDAI LSKLNAHPEM LDASIPLFRL EDTGMGLQMQ EYAVSQVLHW FRRFDDYQAL
     KNQALWKPLP EYTREEFSVG IMGAGVLGAK VAESLQAWGF PLRCWSRSRK SWPGVESYVG
     REELRAFLNQ TRVLINLLPN TAQTVGIINS ELLDQLPDGA YVLNLARGVH VQEADLLAAL
     DSGKLKGAML DVFSQEPLPQ ESPLWRHPRV AMTPHIAAVT RPAEAIDYIS RTITQLEKGE
     PVTGQVDRAR GY
//
DBGET integrated database retrieval system