ID A0A0P9AHE1_9CLOT Unreviewed; 320 AA.
AC A0A0P9AHE1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Hydroxypyruvate reductase {ECO:0000313|EMBL:KPU44887.1};
DE EC=1.1.1.81 {ECO:0000313|EMBL:KPU44887.1};
GN ORFNames=OXPF_13650 {ECO:0000313|EMBL:KPU44887.1};
OS Oxobacter pfennigii.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Oxobacter.
OX NCBI_TaxID=36849 {ECO:0000313|EMBL:KPU44887.1, ECO:0000313|Proteomes:UP000050326};
RN [1] {ECO:0000313|EMBL:KPU44887.1, ECO:0000313|Proteomes:UP000050326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 3222 {ECO:0000313|EMBL:KPU44887.1,
RC ECO:0000313|Proteomes:UP000050326};
RA Poehlein A., Bengelsdorf F.R., Schiel-Bengelsdorf B., Duerre P., Daniel R.;
RT "Genome sequence of Oxobacter pfennigii DSM 3222.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:KPU44887.1}.
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DR EMBL; LKET01000028; KPU44887.1; -; Genomic_DNA.
DR RefSeq; WP_054874443.1; NZ_LKET01000028.1.
DR AlphaFoldDB; A0A0P9AHE1; -.
DR STRING; 36849.OXPF_13650; -.
DR PATRIC; fig|36849.3.peg.1451; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000050326; Unassembled WGS sequence.
DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0008652; P:amino acid biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd12173; PGDH_4; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}; Pyruvate {ECO:0000313|EMBL:KPU44887.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000050326}.
FT DOMAIN 5..312
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..283
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 320 AA; 35374 MW; 5DF9D58AF8B3324A CRC64;
MSFTVLIPQN ISKNGINYLM ECGYKIKMGN GCDEKAITED VVDCDAILVR NVRITPKIID
AGNKLKVIAR HGVGLDTIDV DYAEKKGVWV TNAPLSNTNA VAEHTMFLLL SCSKNAKVID
EEFRNGNFDI RNTVTNIELK GKTLGIIGLG RIGQSVAKKA FYGFSMNVIG YKPRAKREDI
FHEIVLKDNI QEVLECSDFV TLHLPLLPAT KKSIGMEQFV AMKKESYFIN TSRGAIIKEG
ELIEALEKKV IAGAAIDVFE EEPPNANDKL LHMNNVIVTP HNAAFTYESY ENMAMDAALG
VHEVLSGKIP TWAGNRPQNT
//
