ID A0A0G1JVP5_9BACT Unreviewed; 323 AA.
AC A0A0G1JVP5;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase, NAD-binding protein {ECO:0000313|EMBL:KKT75408.1};
GN ORFNames=UW71_C0003G0002 {ECO:0000313|EMBL:KKT75408.1};
OS Parcubacteria group bacterium GW2011_GWB1_44_7.
OC Bacteria.
OX NCBI_TaxID=1618876 {ECO:0000313|EMBL:KKT75408.1, ECO:0000313|Proteomes:UP000033936};
RN [1] {ECO:0000313|EMBL:KKT75408.1, ECO:0000313|Proteomes:UP000033936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC 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:KKT75408.1}.
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DR EMBL; LCJJ01000003; KKT75408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1JVP5; -.
DR PATRIC; fig|1618876.3.peg.106; -.
DR Proteomes; UP000033936; 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; 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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1.
DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1.
PE 3: Inferred from homology;
KW NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719}.
FT DOMAIN 4..321
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 111..290
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 323 AA; 35359 MW; 1C06380BEAD8578D CRC64;
MAKIFITHKI PEICVKMLKD KGHDVEWRDK SELLPKTELL KILGGGSYDG VLCLLTDRID
IEVFTTTPAT KIFANYAVGF DNIDIIEAKK RGVAITNTPG ASTESVAEHT LALLLALTRR
VVEGDAFVRN EKYQGWDPML LWGVDLLGKT LGILGAGRIG AAVAKKSARG FGMKIIYHDI
VRNKKMEKET GANFLPSLNE VLKQADVISL HVPLLPTTKH LINAERLAMM KKTAYLINTS
RGSVIDEVAL VDGLKKDIIR GAALDVFENE PVLAEGLKNL PNVVLTPHIA SATAETRNDM
AKKAAENLIA FFDEQKPPNE VGI
//
