ID V6F8Q1_MAGGM Unreviewed; 328 AA.
AC V6F8Q1;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glyoxylate reductase {ECO:0000313|EMBL:CDL01153.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:CDL01153.1};
GN Name=gyaR {ECO:0000313|EMBL:CDL01153.1};
GN OrderedLocusNames=MGMSRv2__3938 {ECO:0000313|EMBL:CDL01153.1};
OS Magnetospirillum gryphiswaldense (strain DSM 6361 / JCM 21280 / NBRC 15271
OS / MSR-1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Magnetospirillum.
OX NCBI_TaxID=431944 {ECO:0000313|EMBL:CDL01153.1, ECO:0000313|Proteomes:UP000018922};
RN [1] {ECO:0000313|EMBL:CDL01153.1, ECO:0000313|Proteomes:UP000018922}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6361 / JCM 21280 / NBRC 15271 / MSR-1
RC {ECO:0000313|Proteomes:UP000018922};
RX PubMed=24625872; DOI=10.1128/genomeA.00171-14;
RA Wang X., Wang Q., Zhang W., Wang Y., Li L., Wen T., Zhang T., Zhang Y.,
RA Xu J., Hu J., Li S., Liu L., Liu J., Jiang W., Tian J., Li Y., Schuler D.,
RA Wang L., Li J.;
RT "Complete genome sequence of Magnetospirillum gryphiswaldense MSR-1.";
RL Genome Announc. 2:e00171-e00114(2014).
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; HG794546; CDL01153.1; -; Genomic_DNA.
DR AlphaFoldDB; V6F8Q1; -.
DR STRING; 1430440.MGMSRv2__3938; -.
DR KEGG; mgy:MGMSRv2__3938; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_5; -.
DR Proteomes; UP000018922; Chromosome I.
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; 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:CDL01153.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000018922}.
FT DOMAIN 17..323
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 113..292
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 328 AA; 36289 MW; 6543F453DC7C7CDE CRC64;
MPQKKPLVVV TRKLPDAIET RMMELFDTRL NLDDKPMSKA DLIEAVKTAD VLVPTITDRI
DAAILSQAGP NLKLIANFGT GVDHIDLASA RQRSVTVTNT PGVLTEDTAD MTMALILAVP
RRLAEGERLL RSEKWNGWSP THMLGHRIWG KRLGIIGMGR IGQAVARRAK AFGMSIHYHN
RKRLHPELEA ELEATYWESL DQMLARMDVV TVHCPHTPAT FHLLSARRLA LLQPHAYVIN
TSRGEIVDEN ALTRMLGRGE LAGAGLDVFE HEPAVNPKLL GLDNVVLLPH LGSATIEGRM
DMGEKVIINI KTFADGHNPP DRVLASMF
//
