ID B2VER1_ERWT9 Unreviewed; 485 AA. AC B2VER1; DT 01-JUL-2008, integrated into UniProtKB/TrEMBL. DT 01-JUL-2008, sequence version 1. DT 04-NOV-2026, entry version 114. DE RecName: Full=Betaine aldehyde dehydrogenase {ECO:0000256|HAMAP-Rule:MF_00804}; DE Short=BADH {ECO:0000256|HAMAP-Rule:MF_00804}; DE EC=1.2.1.8 {ECO:0000256|HAMAP-Rule:MF_00804}; GN Name=betB {ECO:0000256|HAMAP-Rule:MF_00804, GN ECO:0000313|EMBL:CAO96828.1}; GN OrderedLocusNames=ETA_17820 {ECO:0000313|EMBL:CAO96828.1}; OS Erwinia tasmaniensis (strain DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB OS 4357 / Et1/99). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Enterobacterales; Erwiniaceae; Erwinia. OX NCBI_TaxID=465817 {ECO:0000313|EMBL:CAO96828.1, ECO:0000313|Proteomes:UP000001726}; RN [1] {ECO:0000313|EMBL:CAO96828.1, ECO:0000313|Proteomes:UP000001726} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17950 / CFBP 7177 / CIP 109463 / NCPPB 4357 / Et1/99 RC {ECO:0000313|Proteomes:UP000001726}; RX PubMed=18462403; DOI=10.1111/j.1462-2920.2008.01639.x; RA Kube M., Migdoll A.M., Mueller I., Kuhl H., Beck A., Reinhardt R., RA Geider K.; RT "The genome of Erwinia tasmaniensis strain Et1/99, a non-pathogenic RT bacterium in the genus Erwinia."; RL Environ. Microbiol. 10:2211-2222(2008). 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:0000256|HAMAP-Rule:MF_00804}. CC -!- CATALYTIC ACTIVITY: CC Reaction=betaine aldehyde + NAD(+) + H2O = glycine betaine + NADH + 2 CC H(+); 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; CC Evidence={ECO:0000256|ARBA:ARBA00052192}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15306; CC Evidence={ECO:0000256|ARBA:ARBA00052192}; CC -!- CATALYTIC ACTIVITY: CC Reaction=betaine aldehyde + NADP(+) + H2O = glycine betaine + NADPH + 2 CC H(+); Xref=Rhea:RHEA:30067, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15710, ChEBI:CHEBI:17750, ChEBI:CHEBI:57783, CC ChEBI:CHEBI:58349; Evidence={ECO:0000256|ARBA:ARBA00051919}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:30068; CC Evidence={ECO:0000256|ARBA:ARBA00051919}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00804}; CC Note=Binds 2 potassium ions per subunit. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00804}. CC -!- SUBUNIT: Dimer of dimers. {ECO:0000256|ARBA:ARBA00065931, CC ECO:0000256|HAMAP-Rule:MF_00804}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000256|HAMAP-Rule:MF_00804, ECO:0000256|RuleBase:RU003345}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|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; CU468135; CAO96828.1; -; Genomic_DNA. DR RefSeq; WP_012441517.1; NC_010694.1. DR AlphaFoldDB; B2VER1; -. DR STRING; 465817.ETA_17820; -. DR KEGG; eta:ETA_17820; -. DR eggNOG; COG1012; Bacteria. DR HOGENOM; CLU_005391_1_0_6; -. DR OMA; AADKFTW; -. DR OrthoDB; 9812625at2; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000001726; Chromosome. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase (NAD+) activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006578; P:amino-acid betaine biosynthetic process; IEA:UniProtKB-UniRule. DR CDD; cd07090; ALDH_F9_TMBADH; 1. DR FunFam; 3.40.605.10:FF:000026; Aldehyde dehydrogenase, putative; 1. DR FunFam; 3.40.309.10:FF:000014; NAD/NADP-dependent betaine aldehyde dehydrogenase; 1. DR Gene3D; 3.40.605.10; Aldehyde Dehydrogenase, Chain A, domain 1; 1. DR Gene3D; 3.40.309.10; Aldehyde Dehydrogenase, Chain A, domain 2; 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 NCBIfam; NF009725; betB; 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 {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00804}; KW NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|HAMAP-Rule:MF_00804}; KW NADP {ECO:0000256|ARBA:ARBA00022857, ECO:0000256|HAMAP-Rule:MF_00804}; KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00804}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP- KW Rule:MF_00804}; KW Potassium {ECO:0000256|ARBA:ARBA00022958, ECO:0000256|HAMAP-Rule:MF_00804}; KW Reference proteome {ECO:0000313|Proteomes:UP000001726}. FT DOMAIN 18..474 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 158 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT ACT_SITE 247 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 247 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT ACT_SITE 281 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804, FT ECO:0000256|PROSITE-ProRule:PRU10008" FT ACT_SITE 459 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 22 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 23 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 89 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 146..148 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 172..175 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 241 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 249 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 281 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /note="covalent" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 382 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 452 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 455 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT MOD_RES 281 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" SQ SEQUENCE 485 AA; 52013 MW; 26411CFD527F79FA CRC64; MQRRGLFING REVSGNGDIF TTINPANGEV LAEITAASQQ DIDAAVASAH AGQRIWRGYT PVERSRVLLK AVALLRERNQ QLAELETADT GKPIAETSVV DIVTGADVLE YYAGLAVAVE GESIPLRDSA LVYTRREPLG VCAGIGAWNY PIQIALWKSA PALATGNAMI FKPSEVTPLS ALELAKIFSE AGLPDGVFNV VQGAGSVGQG LSQHPDIAKV SFTGEVNTGK RVTADAALAN LKSVTMELGG KSPLVVFDDA DLERAVDGAM AANFFSSGQV CTNGTRVFVQ RSLLPAFEKR LQEKMANIHC GDPTDPAVNF GPLVSEGHCQ KVVSYLELGQ QEGARLLAGG SRMTHGALAK GCYVEPTVFT DCRDDMRIVQ EEIFGPVMSI LVFDDEEEVI KRANDTHYGL AAGVFTNSLN RAHRVIHQLE AGICWVNTWG ESPAPMPVGG YKQSGLGREN GLETLHHYTR TKSILIEMGE FPSAF //