ID BETB_VIBVU Reviewed; 486 AA. AC Q8D3K3; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 27-MAR-2024, entry version 125. 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=VV2_1687; OS Vibrio vulnificus (strain CMCP6). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Vibrio. OX NCBI_TaxID=216895; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases. 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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; AE016796; AAO08543.1; -; Genomic_DNA. DR RefSeq; WP_011082525.1; NC_004460.2. DR AlphaFoldDB; Q8D3K3; -. DR SMR; Q8D3K3; -. DR GeneID; 66967033; -. DR KEGG; vvu:VV2_1687; -. DR HOGENOM; CLU_005391_0_0_6; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000002275; Chromosome 2. 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; IPR029510; Ald_DH_CS_GLU. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR InterPro; IPR011264; BADH. 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; PS00687; ALDEHYDE_DEHYDR_GLU; 1. PE 3: Inferred from homology; KW Metal-binding; NAD; NADP; Oxidation; Oxidoreductase; Potassium. FT CHAIN 1..486 FT /note="Betaine aldehyde dehydrogenase" FT /id="PRO_0000056556" FT ACT_SITE 159 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 247 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 281 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 459 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 23 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 90 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 147..149 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 173..176 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 226..229 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 241 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 249 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 281 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /note="covalent" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 382 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 452 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 455 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT MOD_RES 281 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" SQ SEQUENCE 486 AA; 52281 MW; 26B432CE203BD763 CRC64; MEVTAHYIGG KPFVGDTGES FATLNPATGE VLAHIEQADE RVLGHAIESA KLGFSVWSSM SAAERSRCLL KAAQLIRDHN DELAELEVRD TGKPIQEASV VDIATGADVI EYFAGLVNGL GGEQQSLGSN QFFYTRREPL GICAGIGAWN YPIQIAMWKA APALAAGNAM IFKPSEETPL SALKLAELFT QAGVPDGVFN VVQGDYRVGQ MLTAHPEIDK VSFTGESGTG KKVMADSAAT LKPVTMELGG KSPLIIFDDA DLDDAVSAAM VANFYTQGEV CTHGTRVYVQ RAMYDAFVEQ LKERTEKLIV GDPMNMETQI GSLISKSHLE KVLGAISSAK ESGATLLTGG FQVTERGLEK GCFVAPTVFV DCRDEMPHVQ NEIFGPVMSV LVFDDEDEVI ARANNTQYGL AAGVFTQNLS KAHRVIHQLQ AGICWINTWG NSPAEMPVGG YKLSGIGREN GQETLLHYTQ TKSVFVELGA FDSPYA //