ID A0A117I5Z8_9MYCO Unreviewed; 321 AA.
AC A0A117I5Z8;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:GAS89300.1};
GN ORFNames=RMCB_3396 {ECO:0000313|EMBL:GAS89300.1};
OS Mycolicibacterium brisbanense.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=146020 {ECO:0000313|EMBL:GAS89300.1, ECO:0000313|Proteomes:UP000069620};
RN [1] {ECO:0000313|EMBL:GAS89300.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM15654 {ECO:0000313|EMBL:GAS89300.1};
RA Katahira K., Ogura Y., Gotoh Y., Hayashi T.;
RT "Draft Genome Sequences of Five Rapidly Growing Mycobacterium Species, M.
RT thermoresistibile, M. fortuitum subsp. acetamidolyticum, M. canariasense,
RT M. brisbanense, and M. novocastrense.";
RL Genome Announc. 4:e00322-16(2016).
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:GAS89300.1}.
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DR EMBL; BCSX01000028; GAS89300.1; -; Genomic_DNA.
DR RefSeq; WP_062829710.1; NZ_JACKTM010000068.1.
DR AlphaFoldDB; A0A117I5Z8; -.
DR STRING; 146020.RMCB_3396; -.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000069620; 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; cd12175; 2-Hacid_dh_11; 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; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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; PS00670; D_2_HYDROXYACID_DH_2; 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}.
FT DOMAIN 32..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 114..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 34858 MW; 73FA1465209BD815 CRC64;
MAVSPGPIRV LAHFEPGEKV LDFLAPQLDW LDVRFCAEDD DTTFYRELPE AEVLWHVLRP
ITGEDLHRAL RLRLVHKMGA GVNTIDVDTA TQLGILVANM PGANAASVAE GTVLLMLAAL
RRLIELDQYT REGDGWPTDP TLGETVRDIG GCTVGLIGYG NVAHRVERIV TAMDADVLHT
STRNTGHPRW RNLPELLSTS DIVSLHLPLT EATRGLLDRE ALASMKPGAV IVNTARGPII
DETALLEALG TGQISAAGLD VFPVEPIPAG HPLLALENVV LTPHVAWYTA DTMRRYLAAA
VDNCRRIHDG QPLVNVVNEV T
//
