ID I7GG47_MYCS2 Unreviewed; 334 AA.
AC I7GG47;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:AFP42399.1};
DE EC=1.1.1.- {ECO:0000313|EMBL:AFP42399.1};
GN OrderedLocusNames=MSMEI_5966 {ECO:0000313|EMBL:AFP42399.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196 {ECO:0000313|EMBL:AFP42399.1, ECO:0000313|Proteomes:UP000006158};
RN [1] {ECO:0000313|EMBL:AFP42399.1, ECO:0000313|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000006158};
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [2] {ECO:0000313|EMBL:AFP42399.1, ECO:0000313|Proteomes:UP000006158}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000006158};
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP001663; AFP42399.1; -; Genomic_DNA.
DR AlphaFoldDB; I7GG47; -.
DR KEGG; msg:MSMEI_5966; -.
DR PATRIC; fig|246196.56.peg.6087; -.
DR Proteomes; UP000006158; Chromosome.
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; cd12156; HPPR; 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; 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; PS00065; D_2_HYDROXYACID_DH_1; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719,
KW ECO:0000313|EMBL:AFP42399.1}.
FT DOMAIN 49..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 117..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 334 AA; 34500 MW; 1B4187BD4635925F CRC64;
MSAQEETGRG AQGVLQVGPL KPSLNQTLVS TYGAYVLPDG PGRAAFLAEH GDRVTVAVTS
GRTGVDAELM SALPNLGAVV NFGVGYDTTD VDAAAARDIV VSNTPDVLSD CVADTAVGLL
IDVMRKFSAS DRYVRARRWV TEGNYPLAHK VSGSRVGIIG LGRIGTAIAT RLGAFGCTIS
YHNRREIEGS GYRYVGSAAD LAAQVDVLII AAAGGAGTRH LVDRAVLDAL GPDGYLVNIA
RGSVVDEDAL VEALADGRLA GAGLDVFTDE PNVPEALLGM ENVVLLPHVG SATVETRNAM
EALTLANLDA YLKTGELVTP VPMPAAAPAP TPVQ
//
