ID BETB_SINFN Reviewed; 487 AA. AC C3MIE5; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 91. 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=NGR_c07000; OS Sinorhizobium fredii (strain NBRC 101917 / NGR234). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium. OX NCBI_TaxID=394; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NBRC 101917 / NGR234; RX PubMed=19376903; DOI=10.1128/aem.00515-09; RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A., RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A., RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A., RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.; RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion RT systems."; RL Appl. Environ. Microbiol. 75:4035-4045(2009). 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; CP001389; ACP24493.1; -; Genomic_DNA. DR RefSeq; WP_012707278.1; NC_012587.1. DR RefSeq; YP_002825246.1; NC_012587.1. DR AlphaFoldDB; C3MIE5; -. DR SMR; C3MIE5; -. DR STRING; 394.NGR_c07000; -. DR KEGG; rhi:NGR_c07000; -. DR PATRIC; fig|394.7.peg.3515; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_0_5; -. DR OrthoDB; 9772584at2; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000001054; 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 CDD; cd07090; ALDH_F9_TMBADH; 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 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..487 FT /note="Betaine aldehyde dehydrogenase" FT /id="PRO_1000148557" FT ACT_SITE 162 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 250 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 284 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 26 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" 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 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 229..232 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 244 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 252 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 284 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 284 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" SQ SEQUENCE 487 AA; 51748 MW; 97ACA1FADD8BB118 CRC64; MKAQPKASHF IDGEYVEDTA GTVIESIYPA TGEVIARLHA ATPDIVEKAI AAAKRAQPEW AAMSPTARGR ILKRAAEIMR ERNRELSELE TLDTGKPIQE TIVADPTSGA DSFEFFGGIA AAALNGDYIP LGGDFAYTKR VPLGVCVGIG AWNYPQQIAC WKGAPALAAG NSMVFKPSEN TPLGALKIAE ILIEAGLPKG LYNVIQGDRS TGPLLVNHPD VAKVSLTGSV PTGKKVAAAA AAELKHVTME LGGKSPLIVF DDADLESAIG GAMLGNFYST GQVCSNGTRV FVQRKIKDAF LARLKERTEA IVIGDPMDEA TQLGPMVSKA QRDKVLSYIE QGKAEGARLV TGGGIPNAVN TEGTYIQPTV FADVTDEMTI AREEIFGPVM CVLDFDDEAE VVARANATEF GLSAGVFTAD LTRAHRVVDQ LEAGTLWINT YNLAPVEIPF GGSKQSGFGR ENSVAALNHY TELKTVYVGM GKVEAPY //