ID A0A0G1KVP1_9BACT Unreviewed; 371 AA.
AC A0A0G1KVP1;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=D-isomer specific 2-hydroxyacid dehydrogenase NAD-binding protein {ECO:0000313|EMBL:KKT87648.1};
GN ORFNames=UW89_C0021G0005 {ECO:0000313|EMBL:KKT87648.1};
OS Parcubacteria group bacterium GW2011_GWB1_45_10.
OC Bacteria.
OX NCBI_TaxID=1618877 {ECO:0000313|EMBL:KKT87648.1, ECO:0000313|Proteomes:UP000033817};
RN [1] {ECO:0000313|EMBL:KKT87648.1, ECO:0000313|Proteomes:UP000033817}
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:KKT87648.1}.
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DR EMBL; LCKC01000021; KKT87648.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1KVP1; -.
DR STRING; 1618877.UW89_C0021G0005; -.
DR Proteomes; UP000033817; 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 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; PTHR43026; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-RELATED; 1.
DR PANTHER; PTHR43026:SF1; 2-HYDROXYACID DEHYDROGENASE HOMOLOG 1-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.
DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 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 12..335
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..305
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
FT REGION 345..371
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 371 AA; 40324 MW; 4E7EA2F5AB37A265 CRC64;
MPKIAFFEVK DWEKDYLKQS FSDKPEFELV FFAEKFDKNI CPKDAQAISI FVGSTVNAAD
LAEFIGLKLV TTRSTGFDHL ETQAISEKGI KLGYVPGYGD NTVAEFAFGL LLAVVRKIFS
AFDRIQEKRD FSIEGFEGFD LAGKTIGIIG TGRIGLQSIK IANGFSMKVI AFDKFPKPDL
ETQHNFKYVS FDELLQDSDV ITLHVPYLPE NHHLINADAI AKMKQGAVII NTARGGLIET
KALLAGLESG KISGAGLDVF EGEKSVFDEQ KAVLYGNPGI EDLALLAENN LLFNHARVVA
TPHIAFFTRE ALQRILNTDT ENIKSFFATG EPKSSIATSA RFPSTALGAS SSTNPQASST
SSSGAPSAKT T
//
