ID A0A0M2VBG3_9GAMM Unreviewed; 326 AA.
AC A0A0M2VBG3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=2-hydroxyacid dehydrogenase {ECO:0000313|EMBL:KKO47926.1};
GN ORFNames=VT06_14635 {ECO:0000313|EMBL:KKO47926.1};
OS Arsukibacterium sp. MJ3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Arsukibacterium.
OX NCBI_TaxID=1632859 {ECO:0000313|EMBL:KKO47926.1, ECO:0000313|Proteomes:UP000034895};
RN [1] {ECO:0000313|EMBL:KKO47926.1, ECO:0000313|Proteomes:UP000034895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MJ3 {ECO:0000313|EMBL:KKO47926.1,
RC ECO:0000313|Proteomes:UP000034895};
RA Lylloff J.E., Skov L.B., Jepsen M., Hallin P.F., Sorensen S.J.,
RA Stougaard P., Glaring M.A.;
RT "Draft genome sequences of two protease-producing strains of
RT Arsukibacterium isolated from two cold and alkaline environments.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KKO47926.1}.
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DR EMBL; LAHP01000023; KKO47926.1; -; Genomic_DNA.
DR RefSeq; WP_046555077.1; NZ_LAHP01000023.1.
DR AlphaFoldDB; A0A0M2VBG3; -.
DR STRING; 1632859.VT06_14635; -.
DR PATRIC; fig|1632859.4.peg.3023; -.
DR OrthoDB; 9805416at2; -.
DR Proteomes; UP000034895; 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; cd12183; LDH_like_2; 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; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000034895}.
FT DOMAIN 4..322
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 109..293
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 326 AA; 35769 MW; 78E2FAF23B03D033 CRC64;
MKVAVFSAKK YDQDGFSQWA DPSLQFSYFD SRLSTLNLKL AQGCHAICAF VNDDLSAPVL
QQMSAMGIEM VALRCAGFNN VDLDTAKALG IRVARVPAYS PEAVAEHTVA MMLTLNRKLH
KAYNRVRDNN FSLDGLMGFN MHGKTVGLIG TGRIGLATAR ILQGFGCKLV CYDIEPVAEL
AEHYVSLNEL YAQSDIISLH CPLNPATKHL INANSLAKMR DGVMLINTSR GGLINTKTVI
AGLKDRKIGY LGLDVYEQEA DIFFENLSEQ MIDDEVFERL LTFPNVLITS HQAFFTKEAL
QQISSITSDN LMAFAGGNAT GNELVT
//
