GBSA_BACSU
ID GBSA_BACSU Reviewed; 490 AA.
AC P71016;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000305};
DE Short=BADH {ECO:0000305};
DE EC=1.2.1.8 {ECO:0000269|PubMed:9297465};
DE AltName: Full=Glycine betaine aldehyde dehydrogenase {ECO:0000303|PubMed:8752328};
GN Name=gbsA {ECO:0000303|PubMed:8752328}; OrderedLocusNames=BSU31060;
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 1-25, FUNCTION,
RP PATHWAY, INDUCTION, AND DISRUPTION PHENOTYPE.
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 FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND SUBUNIT.
RX PubMed=9297465; DOI=10.1007/s002030050500;
RA Boch J., Nau-Wagner G., Kneip S., Bremer E.;
RT "Glycine betaine aldehyde dehydrogenase from Bacillus subtilis:
RT characterization of an enzyme required for the synthesis of the
RT osmoprotectant glycine betaine.";
RL Arch. Microbiol. 168:282-289(1997).
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).
RN [5]
RP DISRUPTION PHENOTYPE.
RC STRAIN=168 / 3NA;
RX PubMed=26658822; DOI=10.1007/s00253-015-7197-6;
RA Graf N., Wenzel M., Altenbuchner J.;
RT "Identification and characterization of the vanillin dehydrogenase YfmT in
RT Bacillus subtilis 3NA.";
RL Appl. Microbiol. Biotechnol. 100:3511-3521(2016).
CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC betaine from choline (PubMed:8752328, PubMed:9297465). Catalyzes the
CC oxidation of betaine aldehyde to betaine (PubMed:9297465). Shows
CC specificity for betaine aldehyde as substrate. Can use both NAD(+) and
CC NADP(+), but NAD(+) is strongly preferred (PubMed:9297465).
CC {ECO:0000269|PubMed:8752328, ECO:0000269|PubMed:9297465}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=betaine aldehyde + H2O + NAD(+) = glycine betaine + 2 H(+) +
CC NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.8; Evidence={ECO:0000269|PubMed:9297465};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC Evidence={ECO:0000269|PubMed:9297465};
CC -!- ACTIVITY REGULATION: Activity is stimulated by low concentrations of
CC salts and by moderate concentrations of glycine betaine. Highly
CC tolerant to high ionic conditions. In vitro, activity is highly
CC stimulated in the presence of proline. {ECO:0000269|PubMed:9297465}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=125 uM for betaine aldehyde {ECO:0000269|PubMed:9297465};
CC KM=143 uM for NAD(+) {ECO:0000269|PubMed:9297465};
CC pH dependence:
CC Optimum pH is 8.0. {ECO:0000269|PubMed:9297465};
CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC choline pathway; betaine from betaine aldehyde: step 1/1.
CC {ECO:0000269|PubMed:8752328}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9297465}.
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 (PubMed:8752328). No effect on
CC vanillin degradation (PubMed:26658822). {ECO:0000269|PubMed:26658822,
CC ECO:0000269|PubMed:8752328}.
CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC {ECO:0000305}.
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; U47861; AAC44364.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15084.1; -; Genomic_DNA.
DR PIR; A69629; A69629.
DR RefSeq; NP_390984.1; NC_000964.3.
DR RefSeq; WP_003243430.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P71016; -.
DR SMR; P71016; -.
DR STRING; 224308.BSU31060; -.
DR PaxDb; P71016; -.
DR PRIDE; P71016; -.
DR EnsemblBacteria; CAB15084; CAB15084; BSU_31060.
DR GeneID; 938829; -.
DR KEGG; bsu:BSU31060; -.
DR PATRIC; fig|224308.179.peg.3366; -.
DR eggNOG; COG1012; Bacteria.
DR InParanoid; P71016; -.
DR OMA; GMKYVTM; -.
DR PhylomeDB; P71016; -.
DR BioCyc; BSUB:BSU31060-MON; -.
DR BioCyc; MetaCyc:MON-8602; -.
DR UniPathway; UPA00529; UER00386.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
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 Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016160; Ald_DH_CS_CYS.
DR InterPro; IPR029510; Ald_DH_CS_GLU.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR011264; BADH.
DR Pfam; PF00171; Aldedh; 1.
DR SUPFAM; SSF53720; SSF53720; 1.
DR TIGRFAMs; TIGR01804; BADH; 1.
DR PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS; 1.
DR PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; NAD; Oxidoreductase; Reference proteome.
FT CHAIN 1..490
FT /note="Betaine aldehyde dehydrogenase"
FT /id="PRO_0000056533"
FT ACT_SITE 249
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10007"
FT ACT_SITE 283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10008"
FT BINDING 174
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 177
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 227..232
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
FT BINDING 384
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250|UniProtKB:P47895"
SQ SEQUENCE 490 AA; 53666 MW; 67F44C5818B4AD55 CRC64;
MSQTLFIDGE WISAEKEQIR SIINPFNQEE IATVSEGGRE DAIKAIAAAR RAFDKGEWSS
LSGLERGKIV LKIAELIRRD LEELAELESL DTGKTLEESK ADMDDIANVF QYYAGLADKD
GGEIISSPIP DSESKIIREP IGVCGQITPW NYPLLQASWK IAPALAAGNT IVMKPSEITP
LTTIKVFKLM EEAGVPKGVA NLVLGPGATV GDELAVNKDV DLISFTGGIE TGKKIMRAAS
GNVKKIALEL GGKNPNIVFK DADLEVAVDQ ALNAVFFHAG QVCSAGSRLL VEDAIHDQFL
AELVKRAKRI KLGNGFHAET ESGPLISAEH RAKVEKYVEI GIEEGAKLET GGKRPEDPEL
QNGFFYEPTI FSNCNSDMRI VQEEVFGPVL TVETFSSEEE VIELANDTIY GLAGAVWSKD
IEKCERVAAR LRMGTVWIND FHPYFAQAPW GGYKQSGFGR ELGKIGLEEY TEVKHVYRNT
KPAAVNWFNS
