ID A0A151AVJ4_9CLOT Unreviewed; 303 AA.
AC A0A151AVJ4;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Hydroxypyruvate reductase {ECO:0000313|EMBL:KYH31675.1};
DE EC=1.1.1.81 {ECO:0000313|EMBL:KYH31675.1};
GN ORFNames=CLTEP_23380 {ECO:0000313|EMBL:KYH31675.1};
OS Clostridium tepidiprofundi DSM 19306.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1121338 {ECO:0000313|EMBL:KYH31675.1, ECO:0000313|Proteomes:UP000075531};
RN [1] {ECO:0000313|EMBL:KYH31675.1, ECO:0000313|Proteomes:UP000075531}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19306 {ECO:0000313|EMBL:KYH31675.1,
RC ECO:0000313|Proteomes:UP000075531};
RA Poehlein A., Daniel R.;
RT "Genome sequence of Clostridium tepidiprofundi DSM 19306.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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:KYH31675.1}.
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DR EMBL; LTBA01000044; KYH31675.1; -; Genomic_DNA.
DR RefSeq; WP_066826860.1; NZ_LTBA01000044.1.
DR AlphaFoldDB; A0A151AVJ4; -.
DR STRING; 1121338.CLTEP_23380; -.
DR PATRIC; fig|1121338.3.peg.2417; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000075531; Unassembled WGS sequence.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05303; PGDH_2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 2.
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; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43761:SF1; 2-HACID_DH DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR PANTHER; PTHR43761; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_1G13630); 1.
DR Pfam; PF00389; 2-Hacid_dh; 1.
DR Pfam; PF02826; 2-Hacid_dh_C; 1.
DR SUPFAM; SSF52283; Formate/glycerate dehydrogenase catalytic domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:KYH31675.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000075531}.
FT DOMAIN 4..302
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..280
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 303 AA; 33464 MW; AEBBE47BF499059E CRC64;
MYRVLVTDGM DKGAVEQLKQ KGYEVVEQHF EPDALGEELK NFDVMVVRSA TKVRQPIIDK
AAEAGRLKLI IRGGVGLDNI DVAYAMEKGI KVSNTPKASS SSVAELAIGH MFAISRFINI
SNVTMREGKW EKKKYKGVEL AGKTLGLIGF GRISREVAKR AEALGMKVIY TDIIGKAEGY
DQYKFCELNE LLKEADYVSL HIPFIKEQGP TIRKEQIEMM KDGAFLINCA RGGVVEEDAL
YEALKSGKLA GAAIDVFEEE PTKNEALINL SNVSVTPHIG ASTKEAQKRI GEEVVSIIEE
FFK
//
