GHRA_SALTY
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 03-AUG-2022, entry version 108.
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}; 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., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC 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; EC=1.1.1.79;
CC 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; EC=1.1.1.81;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01666};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + NADP(+) = 3-hydroxypyruvate + H(+) + NADPH;
CC Xref=Rhea:RHEA:18657, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:17180, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.81;
CC Evidence={ECO:0000255|HAMAP-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}.
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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 AlphaFoldDB; Q8ZQ30; -.
DR SMR; Q8ZQ30; -.
DR STRING; 99287.STM1135; -.
DR PaxDb; Q8ZQ30; -.
DR DNASU; 1252653; -.
DR EnsemblBacteria; AAL20065; AAL20065; STM1135.
DR GeneID; 1252653; -.
DR KEGG; stm:STM1135; -.
DR PATRIC; fig|99287.12.peg.1202; -.
DR HOGENOM; CLU_019796_1_0_6; -.
DR OMA; VQMAEYV; -.
DR PhylomeDB; Q8ZQ30; -.
DR BioCyc; SENT99287:STM1135-MON; -.
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:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
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_Enterobacterales.
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; Cytoplasm; NAD; NADP; Oxidoreductase; Reference proteome.
FT CHAIN 1..312
FT /note="Glyoxylate/hydroxypyruvate reductase A"
FT /id="PRO_0000348372"
FT ACT_SITE 227
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01666"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01666"
FT STRAND 1..6
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 12..22
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 26..30
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 40..46
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 49..52
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 58..65
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 68..76
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 78..80
FT /evidence="ECO:0007829|PDB:3KBO"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 96..111
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 114..122
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 134..136
FT /evidence="ECO:0007829|PDB:3KBO"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 146..156
FT /evidence="ECO:0007829|PDB:3PP8"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 162..168
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 192..196
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 202..204
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 210..213
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 233..241
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 244..251
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 254..257
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 263..266
FT /evidence="ECO:0007829|PDB:3PP8"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:3PP8"
FT HELIX 282..298
FT /evidence="ECO:0007829|PDB:3PP8"
FT TURN 308..311
FT /evidence="ECO:0007829|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
