ID YOAD_BACSU Reviewed; 344 AA.
AC O34815; Q796G0;
DT 13-OCT-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 27-MAR-2024, entry version 132.
DE RecName: Full=Putative 2-hydroxyacid dehydrogenase YoaD;
DE EC=1.1.1.-;
GN Name=yoaD; OrderedLocusNames=BSU18560;
OS Bacillus subtilis (strain 168).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Lapidus A., Galleron N., Sorokin A., Ehrlich D.;
RT "Sequence analysis of the Bacillus subtilis chromosome region between the
RT terC and odhAB loci cloned in a yeast artificial chromosome.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION, AND OPERON STRUCTURE.
RC STRAIN=168;
RX PubMed=12193636; DOI=10.1128/jb.184.18.5179-5186.2002;
RA Auger S., Danchin A., Martin-Verstraete I.;
RT "Global expression profile of Bacillus subtilis grown in the presence of
RT sulfate or methionine.";
RL J. Bacteriol. 184:5179-5186(2002).
CC -!- INDUCTION: Induced by sulfate, part of the yoaDCB operon.
CC {ECO:0000269|PubMed:12193636}.
CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid
CC dehydrogenase family. {ECO:0000305}.
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DR EMBL; AF027868; AAB84446.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13749.1; -; Genomic_DNA.
DR PIR; F69895; F69895.
DR RefSeq; NP_389738.1; NC_000964.3.
DR RefSeq; WP_009967372.1; NZ_JNCM01000036.1.
DR AlphaFoldDB; O34815; -.
DR SMR; O34815; -.
DR STRING; 224308.BSU18560; -.
DR PaxDb; 224308-BSU18560; -.
DR EnsemblBacteria; CAB13749; CAB13749; BSU_18560.
DR GeneID; 940109; -.
DR KEGG; bsu:BSU18560; -.
DR PATRIC; fig|224308.179.peg.2023; -.
DR eggNOG; COG0111; Bacteria.
DR InParanoid; O34815; -.
DR OrthoDB; 9805416at2; -.
DR PhylomeDB; O34815; -.
DR BioCyc; BSUB:BSU18560-MONOMER; -.
DR Proteomes; UP000001570; 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; cd12171; 2-Hacid_dh_10; 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; PTHR42789; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 1.
DR PANTHER; PTHR42789:SF1; D-ISOMER SPECIFIC 2-HYDROXYACID DEHYDROGENASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_6G10090); 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.
PE 2: Evidence at transcript level;
KW NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..344
FT /note="Putative 2-hydroxyacid dehydrogenase YoaD"
FT /id="PRO_0000386538"
FT ACT_SITE 251
FT /evidence="ECO:0000255"
FT ACT_SITE 280
FT /evidence="ECO:0000255"
FT ACT_SITE 300
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 193
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
FT BINDING 275
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000255"
SQ SEQUENCE 344 AA; 38630 MW; 4FE6916A4CA224F8 CRC64;
MKNTMKRMFC SMTVLVTAPY NEEGRKELEN LFGSVAYQSW KEQGRAYRED ELIQLLKATN
ATGLITELDQ VTDSVFASVP ELSFVGVCRG MPSNVDVAAA SKRGIPVFYT PGRNAQAVAE
MFIGNVISFL RHTSASNQWL KDGEWDSDYL QAYVKFKGNE LTGKTVGMIG FGAVGQRIAK
LLTAFDCKIK YYDPYIQDDH PLYEKASLKT VFSDSDIVSV HLPRTEETLG LIDRQYFDLM
KESAIFVNTS RAVVVNREDL LFVLKEHKIS GAILDVFYHE PPEESDYELI SLPNVLATPH
LAGATFEVED HHVTILNKAL KKWKGEKTLN IQTMYNKDAL KTGG
//
