ID Q65EH9_BACLD Unreviewed; 323 AA.
AC Q65EH9; Q62PZ6;
DT 25-OCT-2004, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Probable 2-ketogluconate reductase YvcT {ECO:0000313|EMBL:AAU25165.1};
GN Name=yvcT {ECO:0000313|EMBL:AAU25165.1};
GN OrderedLocusNames=BL03603 {ECO:0000313|EMBL:AAU25165.1};
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010 {ECO:0000313|EMBL:AAU25165.1, ECO:0000313|Proteomes:UP000000606};
RN [1] {ECO:0000313|EMBL:AAU25165.1, ECO:0000313|Proteomes:UP000000606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB
RC 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46
RC {ECO:0000313|Proteomes:UP000000606};
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Jorgensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000256|ARBA:ARBA00005854,
CC ECO:0000256|RuleBase:RU003719}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000002; AAU25165.1; -; Genomic_DNA.
DR RefSeq; WP_009329636.1; NC_006322.1.
DR AlphaFoldDB; Q65EH9; -.
DR STRING; 279010.BL03603; -.
DR KEGG; bli:BL03603; -.
DR PATRIC; fig|279010.13.peg.3782; -.
DR eggNOG; COG1052; Bacteria.
DR HOGENOM; CLU_019796_1_2_9; -.
DR Proteomes; UP000000606; Chromosome.
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; IPR029752; D-isomer_DH_CS1.
DR InterPro; IPR006140; D-isomer_DH_NAD-bd.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR10996:SF178; 2-HYDROXYACID DEHYDROGENASE YGL185C-RELATED; 1.
DR PANTHER; PTHR10996; 2-HYDROXYACID DEHYDROGENASE-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.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|RuleBase:RU003719};
KW Reference proteome {ECO:0000313|Proteomes:UP000000606}.
FT DOMAIN 5..319
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase
FT catalytic"
FT /evidence="ECO:0000259|Pfam:PF00389"
FT DOMAIN 108..288
FT /note="D-isomer specific 2-hydroxyacid dehydrogenase NAD-
FT binding"
FT /evidence="ECO:0000259|Pfam:PF02826"
SQ SEQUENCE 323 AA; 36404 MW; 33191A41E716E6E1 CRC64;
MKPFVYVTKP VPKEIEEMLA EHCEYEIWTS RERIPRTTLL EKIKEADGLL TSGTKIDREL
LSNALKLKIV SNNSVGYDNF DIEAMKEKSV IGTHTPYILD DTVADLAFGL ILSSARRIAE
LDRYVREGKW TKSEDDESLF GSDVHHRTLG IIGMGRIGEQ VAKRAALGFD MEVLYYSRSR
KPDTEKKTGA VYTGFHELLE RSDFIVLVTP LTDETYRLIG EAEFKKMKPS SIFINISRGK
TVDEQALIQA LKEGWIKGAG LDVFEKEPIE KDNPLLSLSN VTLVPHIGSS THVTHVNMLK
SAVQNLIDGL QGKRPKDIVK ELR
//
