ID BETB_XANCP Reviewed; 490 AA. AC Q8P5D8; DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2002, sequence version 1. DT 27-MAR-2024, entry version 117. 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=XCC3403; OS Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB OS 528 / LMG 568 / P 25). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=190485; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25; RX PubMed=12024217; DOI=10.1038/417459a; RA da Silva A.C.R., Ferro J.A., Reinach F.C., Farah C.S., Furlan L.R., RA Quaggio R.B., Monteiro-Vitorello C.B., Van Sluys M.A., Almeida N.F. Jr., RA Alves L.M.C., do Amaral A.M., Bertolini M.C., Camargo L.E.A., Camarotte G., RA Cannavan F., Cardozo J., Chambergo F., Ciapina L.P., Cicarelli R.M.B., RA Coutinho L.L., Cursino-Santos J.R., El-Dorry H., Faria J.B., RA Ferreira A.J.S., Ferreira R.C.C., Ferro M.I.T., Formighieri E.F., RA Franco M.C., Greggio C.C., Gruber A., Katsuyama A.M., Kishi L.T., RA Leite R.P., Lemos E.G.M., Lemos M.V.F., Locali E.C., Machado M.A., RA Madeira A.M.B.N., Martinez-Rossi N.M., Martins E.C., Meidanis J., RA Menck C.F.M., Miyaki C.Y., Moon D.H., Moreira L.M., Novo M.T.M., RA Okura V.K., Oliveira M.C., Oliveira V.R., Pereira H.A., Rossi A., RA Sena J.A.D., Silva C., de Souza R.F., Spinola L.A.F., Takita M.A., RA Tamura R.E., Teixeira E.C., Tezza R.I.D., Trindade dos Santos M., RA Truffi D., Tsai S.M., White F.F., Setubal J.C., Kitajima J.P.; RT "Comparison of the genomes of two Xanthomonas pathogens with differing host RT specificities."; RL Nature 417:459-463(2002). 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; AE008922; AAM42673.1; -; Genomic_DNA. DR RefSeq; NP_638749.1; NC_003902.1. DR RefSeq; WP_011038501.1; NC_003902.1. DR AlphaFoldDB; Q8P5D8; -. DR SMR; Q8P5D8; -. DR STRING; 190485.XCC3403; -. DR EnsemblBacteria; AAM42673; AAM42673; XCC3403. DR KEGG; xcc:XCC3403; -. DR PATRIC; fig|190485.4.peg.3640; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_0_6; -. DR OrthoDB; 9812625at2; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000001010; Chromosome. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IBA:GO_Central. 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; KW Reference proteome. FT CHAIN 1..490 FT /note="Betaine aldehyde dehydrogenase" FT /id="PRO_0000056559" 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; 52542 MW; 53CBBE9697CA4782 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 LLFGGERLRD GALAQGCYVA PTIFSDCTDV MTIVREEIFG PVLSLLTYDD EDEAITRANA TSYGLAAGVV TPDLSRAHRL IHRLEAGICW INTWGESPAP MPVGGYKQSG VGRENGLATL QAYTRTKSVQ VELERYASVF //