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YJMD_BACSU
ID   YJMD_BACSU              Reviewed;         339 AA.
AC   O35045; Q796N1;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 135.
DE   RecName: Full=Uncharacterized zinc-type alcohol dehydrogenase-like protein YjmD;
DE            EC=1.-.-.-;
GN   Name=yjmD; OrderedLocusNames=BSU12330;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROBABLE OPERON STRUCTURE.
RC   STRAIN=168;
RX   PubMed=9579062; DOI=10.1099/00221287-144-4-877;
RA   Rivolta C., Soldo B., Lazarevic V., Joris B., Mauel C., Karamata D.;
RT   "A 35.7 kb DNA fragment from the Bacillus subtilis chromosome containing a
RT   putative 12.3 kb operon involved in hexuronate catabolism and a perfectly
RT   symmetrical hypothetical catabolite-responsive element.";
RL   Microbiology 144:877-884(1998).
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   PROBABLE OPERON STRUCTURE, AND INDUCTION.
RC   STRAIN=168 / MB24;
RX   PubMed=9882655; DOI=10.1128/jb.181.2.426-433.1999;
RA   Mekjian K.R., Bryan E.M., Beall B.W., Moran C.P. Jr.;
RT   "Regulation of hexuronate utilization in Bacillus subtilis.";
RL   J. Bacteriol. 181:426-433(1999).
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC   -!- INDUCTION: Induced by galacturonate, repressed by glucose.
CC       {ECO:0000305|PubMed:9882655}.
CC   -!- MISCELLANEOUS: Member of the exu locus which is required for
CC       galacturonate utilization.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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DR   EMBL; AF015825; AAC46329.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13090.1; -; Genomic_DNA.
DR   PIR; F69852; F69852.
DR   RefSeq; NP_389115.1; NC_000964.3.
DR   RefSeq; WP_003245542.1; NZ_JNCM01000035.1.
DR   AlphaFoldDB; O35045; -.
DR   SMR; O35045; -.
DR   STRING; 224308.BSU12330; -.
DR   PaxDb; O35045; -.
DR   PRIDE; O35045; -.
DR   EnsemblBacteria; CAB13090; CAB13090; BSU_12330.
DR   GeneID; 936463; -.
DR   KEGG; bsu:BSU12330; -.
DR   PATRIC; fig|224308.179.peg.1334; -.
DR   eggNOG; COG1063; Bacteria.
DR   InParanoid; O35045; -.
DR   OMA; ILGSHGM; -.
DR   PhylomeDB; O35045; -.
DR   BioCyc; BSUB:BSU12330-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004024; F:alcohol dehydrogenase activity, zinc-dependent; IBA:GO_Central.
DR   GO; GO:0051903; F:S-(hydroxymethyl)glutathione dehydrogenase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IBA:GO_Central.
DR   GO; GO:0046294; P:formaldehyde catabolic process; IBA:GO_Central.
DR   InterPro; IPR013149; ADH-like_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   2: Evidence at transcript level;
KW   Metal-binding; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN           1..339
FT                   /note="Uncharacterized zinc-type alcohol dehydrogenase-like
FT                   protein YjmD"
FT                   /id="PRO_0000360002"
FT   BINDING         38
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         60
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         90
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         104
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         145
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   339 AA;  36762 MW;  BD91891649037700 CRC64;
     MKAVQVRKAY DLVTAEVKKP VLSKDDEVLV KVKRVGICGS DMHIYHGTNP LATLPRVIGH
     EVTGQVEAVG ANVQSLKPGD HVVIEPISYC GSCYACRKGR PNVCAKLSVF GVHEDGGMRE
     YIVLPERQLH AVSKDLPWEE AVMAEPYTIG AQAVWRGQVE KGDTVLIQGA GPIGICVLKM
     AKLAGAAVMM TDLNNERLAF AKENGADAVV NVQAEHVAER VLEWTGNEGA NVVIDAVCLP
     ETFALSIEAV SPAGHVVVLG FDERAAQISQ LPITKKEVTI TGSRLQTNQF PKVVELLNGG
     RLMHNGLVTH TFSVDDVHHA FQFIKEHPDQ VRKAVITFD
 
 
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