ID A0QVC8_MYCS2 Unreviewed; 317 AA.
AC A0QVC8;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 122.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:ABK71418.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:ABK71418.1};
GN OrderedLocusNames=MSMEG_2529 {ECO:0000313|EMBL:ABK71418.1};
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:ABK71418.1, ECO:0000313|Proteomes:UP000000757};
RN [1] {ECO:0000313|EMBL:ABK71418.1, ECO:0000313|Proteomes:UP000000757}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155 {ECO:0000313|Proteomes:UP000000757};
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|RuleBase:RU003719}.
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DR EMBL; CP000480; ABK71418.1; -; Genomic_DNA.
DR RefSeq; WP_011728408.1; NZ_SIJM01000029.1.
DR RefSeq; YP_886866.1; NC_008596.1.
DR AlphaFoldDB; A0QVC8; -.
DR STRING; 246196.MSMEG_2529; -.
DR PaxDb; 246196-MSMEI_2469; -.
DR GeneID; 66733940; -.
DR KEGG; msm:MSMEG_2529; -.
DR PATRIC; fig|246196.19.peg.2495; -.
DR eggNOG; COG1052; Bacteria.
DR OrthoDB; 117809at2; -.
DR Proteomes; UP000000757; Chromosome.
DR GO; GO:0047964; F:glyoxylate reductase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0051287; F:NAD binding; IEA:InterPro.
DR CDD; cd05301; GDH; 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; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000000757}.
FT DOMAIN 30..316
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..285
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 317 AA; 33046 MW; DE01952B7F0F394C CRC64;
MTIYVSRLLT DRAMAHLESL GVPFRVGGGD PPSRADLEAG LAGADAAVIT LTERVDTALL
AAAGPQLKII ANVAVGYDNI DVDAAVSAGV TVTNTPGVLD RATADHTFAL ILAATRRVLD
GDRFLRSREP WVWGPRMLVG LDISASATLG ILGYGRIGKA VAQRAKGFDM KVLATARSRE
PGTSEDGVQF VDTDTLLAES DVLSVLTPLT PQTRHLIDAA ALAKMKPSAY LVNTARGGVV
DEAALMSALH NGALRGAALD VFENEPHIDP RLLDTPNLVL TPHIASAGES TRDAMGILAI
DNAAAVLAGK PALTPVR
//
