ID A0A0L0GRK7_9ENTR Unreviewed; 312 AA.
AC A0A0L0GRK7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=Glyoxylate/hydroxypyruvate reductase A {ECO:0000256|HAMAP-Rule:MF_01666};
DE EC=1.1.1.79 {ECO:0000256|HAMAP-Rule:MF_01666};
DE EC=1.1.1.81 {ECO:0000256|HAMAP-Rule:MF_01666};
DE AltName: Full=2-ketoacid reductase {ECO:0000256|HAMAP-Rule:MF_01666};
GN Name=ghrA {ECO:0000256|HAMAP-Rule:MF_01666,
GN ECO:0000313|EMBL:KNC91567.1};
GN ORFNames=GM31_01755 {ECO:0000313|EMBL:KNC91567.1};
OS Trabulsiella odontotermitis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Trabulsiella.
OX NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC91567.1, ECO:0000313|Proteomes:UP000037393};
RN [1] {ECO:0000313|EMBL:KNC91567.1, ECO:0000313|Proteomes:UP000037393}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12 {ECO:0000313|EMBL:KNC91567.1,
RC ECO:0000313|Proteomes:UP000037393};
RX PubMed=26162887;
RA Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA Plunkett G.3rd., Perna N.T., Poulsen M.;
RT "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT Related to Its Association with Fungus-Growing Termites.";
RL Appl. Environ. Microbiol. 81:6577-6588(2015).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glyoxylate and
CC hydroxypyruvate into glycolate and glycerate, respectively.
CC {ECO:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01666};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01666}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. GhrA subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_01666}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KNC91567.1}.
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DR EMBL; JNGI01000126; KNC91567.1; -; Genomic_DNA.
DR RefSeq; WP_049857530.1; NZ_JNGI01000126.1.
DR AlphaFoldDB; A0A0L0GRK7; -.
DR STRING; 379893.GCA_001297775_02701; -.
DR PATRIC; fig|379893.4.peg.358; -.
DR OrthoDB; 9787219at2; -.
DR Proteomes; UP000037393; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0008465; F:glycerate dehydrogenase activity; IEA:RHEA.
DR GO; GO:0030267; F:glyoxylate reductase (NADP+) activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd12164; GDH_like_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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 PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01666};
KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_01666};
KW NADP {ECO:0000256|HAMAP-Rule:MF_01666};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01666}; Pyruvate {ECO:0000313|EMBL:KNC91567.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037393}.
FT DOMAIN 105..277
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT ACT_SITE 227
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01666"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01666"
SQ SEQUENCE 312 AA; 35196 MW; FCC30BE44EC83FA4 CRC64;
MDIIFYHPTF DIPFWIAELE KHIPGAKVRE WKSGDKGPAD YALVWHPPVE MLQGRTLKAV
FALGAGVDSI LSQLKAHPEM LPETTPLFRL EDTGMAEQMQ EYAVSQVLHW FRRFDDYQQQ
KNAVNWQPLP EYHREDFTIG ILGAGVLGSK VAESLLAWGF PVRCWSRSRK NWPNVTSFAG
KDALPDFLRE TRVLINLLPN TPETVGIINA SLLNQLRDAC YVLNLARGVH VIEADLLQAL
ERGKVKGAML DVFSQEPLPA ESPLWKHPRV AITPHVAAVT RPAQAIEVIS RTILQLERGE
PVRGQVDRQL GY
//
