GBSB_BACSU
ID GBSB_BACSU Reviewed; 402 AA.
AC P71017;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Choline dehydrogenase {ECO:0000305};
DE EC=1.1.1.- {ECO:0000305|PubMed:8752328};
DE AltName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:8752328};
GN Name=gbsB {ECO:0000303|PubMed:8752328}; OrderedLocusNames=BSU31050;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF N-TERMINUS,
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, INDUCTION, DISRUPTION PHENOTYPE, AND
RP ALTERNATIVE INITIATION.
RC STRAIN=168 / JH642;
RX PubMed=8752328; DOI=10.1128/jb.178.17.5121-5129.1996;
RA Boch J., Kempf B., Schmid R., Bremer E.;
RT "Synthesis of the osmoprotectant glycine betaine in Bacillus subtilis:
RT characterization of the gbsAB genes.";
RL J. Bacteriol. 178:5121-5129(1996).
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 SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP INDUCTION.
RC STRAIN=168 / JH642;
RX PubMed=22408163; DOI=10.1128/jb.06642-11;
RA Nau-Wagner G., Opper D., Rolbetzki A., Boch J., Kempf B., Hoffmann T.,
RA Bremer E.;
RT "Genetic control of osmoadaptive glycine betaine synthesis in Bacillus
RT subtilis through the choline-sensing and glycine betaine-responsive GbsR
RT repressor.";
RL J. Bacteriol. 194:2703-2714(2012).
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine from choline. {ECO:0000269|PubMed:8752328}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=choline + NAD(+) = betaine aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:33051, ChEBI:CHEBI:15354, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945;
CC Evidence={ECO:0000305|PubMed:8752328};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:33052;
CC Evidence={ECO:0000305|PubMed:8752328};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine aldehyde from choline (dehydrogenase route):
CC step 1/1. {ECO:0000269|PubMed:8752328}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Comment=Appears to be translated from two alternative initiation
CC sites, at least when overexpressed in E.coli.
CC {ECO:0000269|PubMed:8752328};
CC Name=Long;
CC IsoId=P71017-1; Sequence=Displayed;
CC Name=Short;
CC IsoId=P71017-2; Sequence=VSP_018637;
CC -!- INDUCTION: By choline and by high osmolarity in the presence of choline
CC (PubMed:8752328, PubMed:22408163). Repressed by GbsR (PubMed:22408163).
CC {ECO:0000269|PubMed:22408163, ECO:0000269|PubMed:8752328}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gbsAB genes abolishes the
CC choline-glycine betaine synthesis pathway and the ability of B.subtilis
CC to deal effectively with high-osmolarity stress in choline- or glycine
CC betaine aldehyde-containing medium. {ECO:0000269|PubMed:8752328}.
CC -!- SIMILARITY: Belongs to the iron-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC44365.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U47861; AAC44365.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB15083.2; -; Genomic_DNA.
DR PIR; B69629; B69629.
DR RefSeq; NP_390983.2; NC_000964.3. [P71017-1]
DR RefSeq; WP_003243227.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P71017; -.
DR SMR; P71017; -.
DR STRING; 224308.BSU31050; -.
DR PaxDb; P71017; -.
DR EnsemblBacteria; CAB15083; CAB15083; BSU_31050.
DR GeneID; 938832; -.
DR KEGG; bsu:BSU31050; -.
DR PATRIC; fig|224308.179.peg.3365; -.
DR eggNOG; COG1454; Bacteria.
DR InParanoid; P71017; -.
DR OMA; IRFGPGC; -.
DR PhylomeDB; P71017; -.
DR BioCyc; BSUB:BSU31050-MON; -.
DR BioCyc; MetaCyc:MON-8601; -.
DR UniPathway; UPA00529; UER00587.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
DR PANTHER; PTHR11496; PTHR11496; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW Alternative initiation; Direct protein sequencing; NAD; Oxidoreductase;
KW Reference proteome.
FT CHAIN 1..402
FT /note="Choline dehydrogenase"
FT /id="PRO_0000000875"
FT VAR_SEQ 1..9
FT /note="Missing (in isoform Short)"
FT /evidence="ECO:0000305|PubMed:8752328"
FT /id="VSP_018637"
SQ SEQUENCE 402 AA; 43421 MW; 98B1F3B3FC75748B CRC64;
MTLNMKVESM QKFHTFEIPT VIKHGIGAIK HTGEEVAALG VSKALLVTDP GIYKAGVADP
VIESLKEAGI EVVLFNKVEP NPPVRLVNEG SELYKKENCN GLVAVGGGSS MDTAKAIGVE
ATHEGSVLDY EAADGKKPLE NRIPPLTTIP TTAGTGSEVT QWAVITDEER EFKFNTGGPL
IAAHLTIIDP ELHVSMPPHV TAMTGIDALA HAIECYTMKF AQPITDAVAL MAIEYAAHYI
KRAFADGEDL EARYGMAQAA MLAGLSYGSE SAGAAHAMSQ TLGGIIPVAH GQCVAAMMGP
VMEYNWKGYP EKFARIAKAF GIDTSKMTTE EAAKASVNWM YDLVEDLEVP TLEEQGVSPD
MIERLSKEAM KDPQTFGNPR DLNEKAYNWI YKRCFNLTPK TV
