ID A0A0T6A629_9BACT Unreviewed; 325 AA.
AC A0A0T6A629;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=NAD-binding D-isomer specific 2-hydroxyacid dehydrogenase, glyoxylate reductase {ECO:0000313|EMBL:KRT70540.1};
DE EC=1.1.1.26 {ECO:0000313|EMBL:KRT70540.1};
GN ORFNames=XU15_C0004G0116 {ECO:0000313|EMBL:KRT70540.1};
OS candidate division NC10 bacterium CSP1-5.
OC Bacteria; candidate division NC10.
OX NCBI_TaxID=1640516 {ECO:0000313|EMBL:KRT70540.1, ECO:0000313|Proteomes:UP000051123};
RN [1] {ECO:0000313|EMBL:KRT70540.1, ECO:0000313|Proteomes:UP000051123}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-5 {ECO:0000313|EMBL:KRT70540.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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:KRT70540.1}.
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DR EMBL; LDXR01000004; KRT70540.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T6A629; -.
DR STRING; 1640516.XU15_C0004G0116; -.
DR Proteomes; UP000051123; Unassembled WGS sequence.
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}.
FT DOMAIN 5..318
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 110..286
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 325 AA; 36287 MW; 2EFCA3D6B0B98C2C CRC64;
MKPKVLITRM LPQPALDIAL KQCNVDLNRR DVRYAKKQLI WRLKGKAGMI CLLTDTVDAE
VLRKSPRLKV VSNVAAGLDN IDVQAATRHG IMVTNTPGVL TETTAEFAWA LLLATARRVV
EADRFVRAGK WKEWMLMGFL GRDLYGKTLG ICGLGRIGSA VARRARGFNM RIRYTQRYRN
EAKERELNAT YMDKMTLLKE SDFLVLVLPL TSETRHYIGP KELKAMKDTA ILVNVARGPI
VDEKALLHAL KKKTIAAAGL DVFEREPKVL RGLLRLQNLI LAPHIASASM ETRTRMACMA
AENCVAAVTG HRPPNLVNPE VLVRA
//
