ID A0A0V8J7Q7_9BACI Unreviewed; 321 AA.
AC A0A0V8J7Q7;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Hydroxyacid dehydrogenase {ECO:0000313|EMBL:KSU83043.1};
GN ORFNames=AS030_10645 {ECO:0000313|EMBL:KSU83043.1};
OS Fictibacillus enclensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=1017270 {ECO:0000313|EMBL:KSU83043.1, ECO:0000313|Proteomes:UP000054099};
RN [1] {ECO:0000313|EMBL:KSU83043.1, ECO:0000313|Proteomes:UP000054099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NIO-1003 {ECO:0000313|EMBL:KSU83043.1,
RC ECO:0000313|Proteomes:UP000054099};
RX PubMed=24343101; DOI=10.1007/s10482-013-0097-9;
RA Dastager S.G., Mawlankar R., Srinivasan K., Tang S.K., Lee J.C.,
RA Ramana V.V., Shouche Y.S.;
RT "Fictibacillus enclensis sp. nov., isolated from marine sediment.";
RL Antonie Van Leeuwenhoek 105:461-469(2014).
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:KSU83043.1}.
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DR EMBL; LNQN01000002; KSU83043.1; -; Genomic_DNA.
DR RefSeq; WP_061971777.1; NZ_KQ758618.1.
DR AlphaFoldDB; A0A0V8J7Q7; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000054099; 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; cd05300; 2-Hacid_dh_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; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43333; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43333:SF1; 2-HACID_DH_C DOMAIN-CONTAINING PROTEIN; 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 NAD {ECO:0000256|ARBA:ARBA00023027};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000054099}.
FT DOMAIN 8..309
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..282
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 321 AA; 36353 MW; AE672D20AF36C685 CRC64;
MTARKLLIAQ NIDDSYVEKV QKIIPDWTIV TGKDKEIWQK EAPDAEIIAG WKKGMEEYTL
DRENAPLKWV QTWSAGVNNL PLDRLSSENI QLTSANGVHA FPISETIFAL MLGLTRKIHT
YVRNQQSKTW DHSNLKLEIH GKTLGILGTG AIGRETAKIA KAFGMKVLGM RHSGKPEQYI
DRMYTSEELH DLLPECDYVV VTLPLTKETN RMLGKKEFQH MKNTAFFINI GRGDIVVEED
LIQALNTGEI AGAGLDVFEK EPLDNNSPLW NMENVIITPH TAGSTEYYDQ RVIEDIFIPN
LKDYLDDKSL SINAVDYNKG Y
//
