ID C7LAL6_BRUMC Unreviewed; 487 AA. AC C7LAL6; DT 13-OCT-2009, integrated into UniProtKB/TrEMBL. DT 13-OCT-2009, sequence version 1. DT 04-NOV-2026, entry version 101. 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:ACU47551.1}; GN OrderedLocusNames=BMI_I551 {ECO:0000313|EMBL:ACU47551.1}; OS Brucella microti (strain BCCN 7-01 / CAPM 6434 / CCM 4915). OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria; OC Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella; OC Brucella melitensis group. OX NCBI_TaxID=568815 {ECO:0000313|EMBL:ACU47551.1, ECO:0000313|Proteomes:UP000002188}; RN [1] {ECO:0000313|EMBL:ACU47551.1, ECO:0000313|Proteomes:UP000002188} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CCM 4915 {ECO:0000313|EMBL:ACU47551.1, RC ECO:0000313|Proteomes:UP000002188}; RX PubMed=19653890; DOI=10.1186/1471-2164-10-352; RA Audic S., Lescot M., Claverie J.-M., Scholz H.C.; RT "Brucella microti: the genome sequence of an emerging pathogen."; RL BMC Genomics 10:352-352(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: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; CP001578; ACU47551.1; -; Genomic_DNA. DR RefSeq; WP_002963701.1; NC_013119.1. DR AlphaFoldDB; C7LAL6; -. DR SMR; C7LAL6; -. DR GeneID; 93017027; -. DR GeneID; 99644234; -. DR KEGG; bmr:BMI_I551; -. DR PATRIC; fig|359391.4.peg.602; -. DR HOGENOM; CLU_005391_0_1_5; -. DR OMA; AAFLNWS; -. DR PhylomeDB; C7LAL6; -. DR UniPathway; UPA00529; UER00386. DR Proteomes; UP000002188; Chromosome 1. 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:UP000002188}. FT DOMAIN 16..476 FT /note="Aldehyde dehydrogenase" FT /evidence="ECO:0000259|Pfam:PF00171" FT ACT_SITE 161 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT ACT_SITE 249 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10007" FT ACT_SITE 249 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT ACT_SITE 283 FT /note="Nucleophile" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804, FT ECO:0000256|PROSITE-ProRule:PRU10008" FT ACT_SITE 461 FT /note="Charge relay system" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 27 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 93 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="1" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 149..151 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 175..178 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 243 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 251 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 283 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /note="covalent" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 384 FT /ligand="NAD(+)" FT /ligand_id="ChEBI:CHEBI:57540" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 454 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT BINDING 457 FT /ligand="K(+)" FT /ligand_id="ChEBI:CHEBI:29103" FT /ligand_label="2" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" FT MOD_RES 283 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00804" SQ SEQUENCE 487 AA; 52035 MW; E4B8F2DFC983A654 CRC64; MKAQPKASHF IGGAFVEDKA GKPLPVIYPA TGEEIASLYS ATPGIIEAAY AAALKAQGEW AALKPVERGR ILRRTAEILR EKNRKLSKLE TLDTGKALQE TLVADAASAA DALEFFGGII SGFNGEFVEL GGSFAYTRRE ALGICVGIGA WNYPIQIAAW KSAPALAMGN AFIFKPSENT PLSALALAEA YKEAGLPDGL FNVVQGYGDV GAALVNHRLT AKVSLTGSVP TGRRIMAQAG EQLKHVTMEL GGKSPLIVFD DADLESAIGG AMLGNFYSTG QVCSNGTRVF VHKNIRERFI ERLVERTRKI RIGDPFDEAT QMGPLISAAQ RDKVLSYIKK GKAEGATLAC GGGVPKLQGF DKGFFIEPTV FADVTDTMTI AREEIFGPVM SVLEFSDEDE VIARANDSEF GLAAGVFTAD LSRGHHVIGQ IKAGTCWINA YNLTPVEVPF GGYKQSGIGR ENGIAALAHY SQIKTVYVEM GKVDSPY //