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   02-SEP-2026, entry version 154.
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; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   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 + NAD(+) + H2O = glycine betaine + NADH + 2
CC         H(+); 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:22408163, PubMed:8752328). 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}.
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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; NC_000964.3.
DR   AlphaFoldDB; P71016; -.
DR   SMR; P71016; -.
DR   FunCoup; P71016; 115.
DR   STRING; 224308.BSU31060; -.
DR   PaxDb; 224308-BSU31060; -.
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   OrthoDB; 9762913at2; -.
DR   PhylomeDB; P71016; -.
DR   BioCyc; BSUB:BSU31060-MONOMER; -.
DR   BioCyc; MetaCyc:MONOMER-8602; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000001570; Chromosome.
DR   AbasyAtlas; P71016; -.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase (NAD+) activity; EXP:UniProtKB.
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   CDD; cd07119; ALDH_BADH-GbsA; 1.
DR   FunFam; 3.40.605.10:FF:000026; Aldehyde dehydrogenase, putative; 1.
DR   FunFam; 3.40.309.10:FF:000012; Betaine aldehyde dehydrogenase; 1.
DR   FunFam; 3.40.605.10:FF:000007; NAD/NADP-dependent betaine aldehyde dehydrogenase; 1.
DR   Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1.
DR   Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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   NCBIfam; TIGR01804; BADH; 1.
DR   PANTHER; PTHR43860; BETAINE ALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR43860:SF2; BETAINE ALDEHYDE DEHYDROGENASE-RELATED; 1.
DR   Pfam; PF00171; Aldedh; 1.
DR   SUPFAM; SSF53720; ALDH-like; 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
//