ID BETB_PARP8 Reviewed; 489 AA. AC B2JS88; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-JUN-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=Bphy_3309; OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / OS STM815) (Burkholderia phymatum). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=391038; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815; RX PubMed=25197461; DOI=10.4056/sigs.4861021; RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R., RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D., RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M., RA Bristow J., Riley M.; RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host RT range and efficient nitrogen-fixing symbiont of Mimosa species."; RL Stand. Genomic Sci. 9:763-774(2014). 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; CP001044; ACC72465.1; -; Genomic_DNA. DR RefSeq; WP_012402638.1; NZ_CADFGH010000006.1. DR AlphaFoldDB; B2JS88; -. DR SMR; B2JS88; -. DR STRING; 391038.Bphy_3309; -. DR KEGG; bph:Bphy_3309; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_0_0_4; -. DR OrthoDB; 6187633at2; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000001192; 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; KW Reference proteome. FT CHAIN 1..489 FT /note="Betaine aldehyde dehydrogenase" FT /id="PRO_1000133944" 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; 52647 MW; D0EC8BB1F4E493A5 CRC64; MSAYGLQRLY IGGDYVDATS GVTFDTFDPA TGELLATVQQ ASEADIERAV QSAREGQRAW AAMTAMQRSR ILRRAVDLLR ERNDELAELE MRDTGKPIAE TRAVDIVTGA DVIEYYAGLA TAIEGQQIPL RAESFVYTRR EPLGVTAGIG AWNYPIQIAC WKSAPALAAG NAMIFKPSEV TPLSASKLAE IYLEAGVPAG VFNVVQGDGR VGAMLSAHPG IAKISFTGGV ETGKKVMSMA GGSSLKEVTM ELGGKSPLVV FEDADLDRAA DIAVTANFFS AGQVCTNGTR VFVHQSVQPA FEARVIERVK RIRVGKPSDP STNFGPLASA AQLDKVLGFI ESGKREGARL VAGGARIVEG DYARGQYVQP TVFSDCRDDM KIVREEIFGP VMSILSFVDE DDVIERANDT IYGLAAGVVT ENLARAHRAI HRLEAGICWI NTWGESPAEM PVGGYKQSGV GRENGITTLE HYTRIKSVQV ELGKYQPVF //