ID W1Q3T2_ABIDE Unreviewed; 331 AA.
AC W1Q3T2;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative (R)-2-hydroxyisocaproate dehydrogenase {ECO:0000313|EMBL:ESK65821.1};
GN ORFNames=GCWU000182_000887 {ECO:0000313|EMBL:ESK65821.1};
OS Abiotrophia defectiva ATCC 49176.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Abiotrophia.
OX NCBI_TaxID=592010 {ECO:0000313|EMBL:ESK65821.1, ECO:0000313|Proteomes:UP000019050};
RN [1] {ECO:0000313|EMBL:ESK65821.1, ECO:0000313|Proteomes:UP000019050}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49176 {ECO:0000313|EMBL:ESK65821.1,
RC ECO:0000313|Proteomes:UP000019050};
RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA Hall O., Minx P., Tomlinson C., Mitreva M., Nelson J., Hou S., Wollam A.,
RA Pepin K.H., Johnson M., Bhonagiri V., Nash W.E., Warren W., Chinwalla A.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (JUN-2013) 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:ESK65821.1}.
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DR EMBL; ACIN03000005; ESK65821.1; -; Genomic_DNA.
DR RefSeq; WP_023391537.1; NZ_KI535340.1.
DR AlphaFoldDB; W1Q3T2; -.
DR STRING; 592010.GCWU000182_000887; -.
DR GeneID; 84816964; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_1_9; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000019050; Unassembled WGS sequence.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR CDD; cd12184; HGDH_like; 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 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 Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000019050}.
FT DOMAIN 9..328
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 112..299
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 331 AA; 36341 MW; DF454145324E2D95 CRC64;
MKVLAYGVRD VELPIFEAVN QKFGYDLVCV ANYLNGPEEA RQAAGCQAVI LRGNCWANKE
VLDIYKELGV EYVLTRTVGV NHIDVAYAKE LGFKLAYVPF YSPNAISELA LTLAMTLLRN
VAYTTNRTSQ QDFRVDNQMF AKEIRNCTVG VVGIGRIGLT TATLFKGLGA NVLAYDAFPK
EGVDHICTQV ELDELLAKSD VISIHAPYIP ANGKVITKEF ISKMKPGAIL VNTARGELQD
VDAIIEAIES GHLAGAGLDV LENESQFFFK DLRGQKISDP AVKKLVDLYP KVLLTPHMGS
YTDEAVENMV ETSFNNLKSY LETGQCSNDI A
//
