ID BETB_PARPJ Reviewed; 489 AA. AC B2TCJ9; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 27-MAR-2024, entry version 90. 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=Bphyt_5059; OS Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN) OS (Burkholderia phytofirmans). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=398527; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17436 / LMG 22146 / PsJN; RX PubMed=21551308; DOI=10.1128/jb.05055-11; RA Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J., Sessitsch A.; RT "Complete genome sequence of the plant growth-promoting endophyte RT Burkholderia phytofirmans strain PsJN."; RL J. Bacteriol. 193:3383-3384(2011). 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; CP001053; ACD19423.1; -; Genomic_DNA. DR RefSeq; WP_012426934.1; NC_010676.1. DR AlphaFoldDB; B2TCJ9; -. DR SMR; B2TCJ9; -. DR STRING; 398527.Bphyt_5059; -. DR KEGG; bpy:Bphyt_5059; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_0_4; -. DR OrthoDB; 6187633at2; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000001739; 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 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. FT CHAIN 1..489 FT /note="Betaine aldehyde dehydrogenase" FT /id="PRO_1000133945" FT ACT_SITE 162 FT /note="Charge relay system" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 251 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 285 FT /note="Nucleophile" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT ACT_SITE 463 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 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 229..232 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 245 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 253 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 285 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /note="covalent" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 386 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 456 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT BINDING 459 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT SITE 247 FT /note="Seems to be a necessary countercharge to the FT potassium cations" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" FT MOD_RES 285 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00804" SQ SEQUENCE 489 AA; 52478 MW; 131E1FA2DF8266CE CRC64; MAVFATQRLY IGGGYVDATS GETFDTLDPA TGETLASVQQ ASAADVDRAV RSAKQGQREW AALTAMQRSR ILRRAVDLLR ERNDELAALE TRDTGKPIAE TLAVDIVTGA DVIEYYAGLA TAIEGQQIPL RPTSFVYTRR EPLGVCAGIG AWNYPIQIAC WKSAPALAAG NAMIFKPSEI TPLSALKLAE IFTEAGVPAG VFNVVQGDGR VGAMLAAHPD IEKISFTGGV ETGKKVMSMA GASSLKEVTM ELGGKSPLLV FDDANLERAA DIATSANFFS SGQVCTNGTR VFVQRGVLDR FEALVLERVK RIRVGKPTDA ATNFGPLVSA AQLHKVLGYI ESGKQEGARL VAGGKRLTEG HFAGGQYVEP TVFADCRDDM RIVREEIFGP VMSILVFDDE DEAIARANHT AYGLAAGVVT ENLARAHRVI HRLEAGICWI NTWGESPAEM PVGGYKQSGV GRENGITTLE HYTRIKSVQV ELGPYQPVF //