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Database: UniProt
Entry: B0RNV0
LinkDB: B0RNV0
Original site: B0RNV0 
ID   BETB_XANCB              Reviewed;         490 AA.
AC   B0RNV0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 85.
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};
GN   OrderedLocusNames=xcc-b100_0794;
OS   Xanthomonas campestris pv. campestris (strain B100).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=509169;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B100;
RX   PubMed=18304669; DOI=10.1016/j.jbiotec.2007.12.013;
RA   Vorhoelter F.-J., Schneiker S., Goesmann A., Krause L., Bekel T.,
RA   Kaiser O., Linke B., Patschkowski T., Rueckert C., Schmid J., Sidhu V.K.,
RA   Sieber V., Tauch A., Watt S.A., Weisshaar B., Becker A., Niehaus K.,
RA   Puehler A.;
RT   "The genome of Xanthomonas campestris pv. campestris B100 and its use for
RT   the reconstruction of metabolic pathways involved in xanthan
RT   biosynthesis.";
RL   J. Biotechnol. 134:33-45(2008).
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; AM920689; CAP50135.1; -; Genomic_DNA.
DR   AlphaFoldDB; B0RNV0; -.
DR   SMR; B0RNV0; -.
DR   KEGG; xca:xcc-b100_0794; -.
DR   HOGENOM; CLU_005391_0_2_6; -.
DR   UniPathway; UPA00529; UER00386.
DR   Proteomes; UP000001188; Chromosome.
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   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   NCBIfam; TIGR01804; BADH; 1.
DR   PANTHER; PTHR11699:SF228; 4-TRIMETHYLAMINOBUTYRALDEHYDE DEHYDROGENASE; 1.
DR   PANTHER; PTHR11699; 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   3: Inferred from homology;
KW   Metal-binding; NAD; NADP; Oxidation; Oxidoreductase; Potassium.
FT   CHAIN           1..490
FT                   /note="Betaine aldehyde dehydrogenase"
FT                   /id="PRO_1000133961"
FT   ACT_SITE        162
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        252
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        286
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   ACT_SITE        464
FT                   /note="Charge relay system"
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         150..152
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         176..179
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         180
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         230..233
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         246
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         254
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         286
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /note="covalent"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   BINDING         387
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
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   BINDING         460
FT                   /ligand="K(+)"
FT                   /ligand_id="ChEBI:CHEBI:29103"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   SITE            248
FT                   /note="Seems to be a necessary countercharge to the
FT                   potassium cations"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
FT   MOD_RES         286
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00804"
SQ   SEQUENCE   490 AA;  52498 MW;  25795922C6CA4786 CRC64;
     MPRFPDQLLY IGGRYVPARG GHTFEVVNPA TGEVLANVHN ADADDLDAAV DSAKAGQRHW
     AALTVVERSR ILLRAVALLR ERNDALAELE TLNTGKPLSE TRSVDIVTGA DVLEYYAGVA
     QALQGVQVPL REGSFFYTRH EPLGVVGAIG AWNYPIQIAL WKAAPALAAG NAMIFKPSEV
     TPLTALKLAE IFTEAGLPDG VFNVLPGDGA SVGHALTEHP EIEKISFTGG TATGRKVMAS
     ASSSSLKDVT MELGGKSPLI VCADADLDLA ADIAMMANFY SSGQVCTNGT RVFVPRALRT
     AFEARLLARV QRIHIGDPLD ERTTFGPMVS AAHMQRVLEH IEQGKAEGAR LLCGGERLRD
     GALAQGCYVA PTIFSDCTDV MTIVREEIFG PVLSLLTYDD EDEAITRANA TSYGLAAGVV
     TPDLSRAHRL IHRLEAGICW INTWGESPAP MPVGGYKQSG VGRENGLATL QAYTRTKSVQ
     VELERYASVF
//
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