ID A0A0G1E2E0_9BACT Unreviewed; 335 AA.
AC A0A0G1E2E0;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Hydroxyacid dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=UV50_C0007G0006 {ECO:0000313|EMBL:KKS77286.1};
OS Parcubacteria group bacterium GW2011_GWB1_42_9.
OC Bacteria.
OX NCBI_TaxID=1618871 {ECO:0000313|EMBL:KKS77286.1, ECO:0000313|Proteomes:UP000034249};
RN [1] {ECO:0000313|EMBL:KKS77286.1, ECO:0000313|Proteomes:UP000034249}
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:KKS77286.1}.
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DR EMBL; LCES01000007; KKS77286.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1E2E0; -.
DR PATRIC; fig|1618871.3.peg.343; -.
DR Proteomes; UP000034249; 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; cd12187; LDH_like_1; 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; 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|RuleBase:RU003719}.
FT DOMAIN 13..335
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 107..304
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 335 AA; 36823 MW; BE0C01478D43ADC3 CRC64;
MKIGFFELEQ WEKDYLADKM SALGEVAMID SILTAENLPT ENDFEIISVF VNSIIDARVL
DHLPNLKLVV TRSTGFDHID LDLCKSRGVA VANVPSYGED TVAEYTFALL LNLSRKVHLS
FDRIRETGSF SLDGLRGFDL KGKTLGVIGT GRIGRNVIEI ATGFNMNVIA YDPKPNAEYA
AKMNYQYLEL NDVLAQADIV TLHVPYTEAS HHLIDAESFQ RMKKGVYFLN TARGPLVDTM
ALVGALRSGQ VAGAGLDVLE EEGVIKDELN VLTSGKLEGH DLKAVLADHL LVDMPNVIVT
PHNAFNTWEA LKRILDTSAD NIKNFVAGSL SNLVN
//