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BETB_BRUA2
ID   BETB_BRUA2              Reviewed;         487 AA.
AC   Q2YMP8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00804};
DE            Short=BADH {ECO:0000255|HAMAP-Rule:MF_00804};
DE            EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00804};
GN   Name=betB {ECO:0000255|HAMAP-Rule:MF_00804}; OrderedLocusNames=BAB1_0576;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine
CC       betaine. Catalyzes the irreversible oxidation of betaine aldehyde to
CC       the corresponding acid. {ECO:0000255|HAMAP-Rule:MF_00804}.
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:0000255|HAMAP-
CC         Rule:MF_00804};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC   -!- COFACTOR:
CC       Name=K(+); Xref=ChEBI:CHEBI:29103;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00804};
CC       Note=Binds 2 potassium ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00804};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via
CC       choline pathway; betaine from betaine aldehyde: step 1/1.
CC       {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SUBUNIT: Dimer of dimers. {ECO:0000255|HAMAP-Rule:MF_00804}.
CC   -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00804}.
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DR   EMBL; AM040264; CAJ10532.1; -; Genomic_DNA.
DR   RefSeq; WP_002963701.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YMP8; -.
DR   SMR; Q2YMP8; -.
DR   STRING; 359391.BAB1_0576; -.
DR   EnsemblBacteria; CAJ10532; CAJ10532; BAB1_0576.
DR   GeneID; 45124015; -.
DR   KEGG; bmf:BAB1_0576; -.
DR   PATRIC; fig|359391.11.peg.2886; -.
DR   HOGENOM; CLU_005391_0_1_5; -.
DR   OMA; GMKYVTM; -.
DR   PhylomeDB; Q2YMP8; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000002719; Chromosome I.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.309.10; -; 1.
DR   Gene3D; 3.40.605.10; -; 1.
DR   HAMAP; MF_00804; BADH; 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   3: Inferred from homology;
KW   Metal-binding; NAD; NADP; Oxidation; Oxidoreductase; Potassium;
KW   Reference proteome.
FT   CHAIN           1..487
FT                   /note="Betaine aldehyde dehydrogenase"
FT                   /id="PRO_1000047029"
FT   ACT_SITE        161
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        249
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        283
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        461
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         27
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         93
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         149..151
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         175..178
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         228..231
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         243
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         251
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         283
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         384
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         454
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         457
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   MOD_RES         283
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
SQ   SEQUENCE   487 AA;  52035 MW;  E4B8F2DFC983A654 CRC64;
     MKAQPKASHF IGGAFVEDKA GKPLPVIYPA TGEEIASLYS ATPGIIEAAY AAALKAQGEW
     AALKPVERGR ILRRTAEILR EKNRKLSKLE TLDTGKALQE TLVADAASAA DALEFFGGII
     SGFNGEFVEL GGSFAYTRRE ALGICVGIGA WNYPIQIAAW KSAPALAMGN AFIFKPSENT
     PLSALALAEA YKEAGLPDGL FNVVQGYGDV GAALVNHRLT AKVSLTGSVP TGRRIMAQAG
     EQLKHVTMEL GGKSPLIVFD DADLESAIGG AMLGNFYSTG QVCSNGTRVF VHKNIRERFI
     ERLVERTRKI RIGDPFDEAT QMGPLISAAQ RDKVLSYIKK GKAEGATLAC GGGVPKLQGF
     DKGFFIEPTV FADVTDTMTI AREEIFGPVM SVLEFSDEDE VIARANDSEF GLAAGVFTAD
     LSRGHHVIGQ IKAGTCWINA YNLTPVEVPF GGYKQSGIGR ENGIAALAHY SQIKTVYVEM
     GKVDSPY
 
 
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