ID BETA_PSEAE Reviewed; 561 AA. AC Q9HTJ2; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 27-MAR-2024, entry version 127. DE RecName: Full=Oxygen-dependent choline dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750}; DE Short=CDH {ECO:0000255|HAMAP-Rule:MF_00750}; DE Short=CHD {ECO:0000255|HAMAP-Rule:MF_00750}; DE EC=1.1.99.1 {ECO:0000255|HAMAP-Rule:MF_00750}; DE AltName: Full=Betaine aldehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00750}; DE Short=BADH {ECO:0000255|HAMAP-Rule:MF_00750}; DE EC=1.2.1.8 {ECO:0000255|HAMAP-Rule:MF_00750}; GN Name=betA {ECO:0000255|HAMAP-Rule:MF_00750}; OrderedLocusNames=PA5372; OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208964; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / RC 1C / PRS 101 / PAO1; RX PubMed=10984043; DOI=10.1038/35023079; RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M., RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.; RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic RT pathogen."; RL Nature 406:959-964(2000). CC -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant glycine CC betaine. Catalyzes the oxidation of choline to betaine aldehyde and CC betaine aldehyde to glycine betaine at the same rate. CC {ECO:0000255|HAMAP-Rule:MF_00750}. CC -!- CATALYTIC ACTIVITY: CC Reaction=A + choline = AH2 + betaine aldehyde; Xref=Rhea:RHEA:17433, CC ChEBI:CHEBI:13193, ChEBI:CHEBI:15354, ChEBI:CHEBI:15710, CC ChEBI:CHEBI:17499; EC=1.1.99.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00750}; 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_00750}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00750}; CC -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis via CC choline pathway; betaine aldehyde from choline (cytochrome c reductase CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_00750}. CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family. CC {ECO:0000255|HAMAP-Rule:MF_00750}. 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; AE004091; AAG08757.1; -; Genomic_DNA. DR PIR; B82975; B82975. DR RefSeq; NP_254059.1; NC_002516.2. DR RefSeq; WP_003104848.1; NZ_QZGE01000031.1. DR AlphaFoldDB; Q9HTJ2; -. DR SMR; Q9HTJ2; -. DR STRING; 208964.PA5372; -. DR PaxDb; 208964-PA5372; -. DR GeneID; 881124; -. DR KEGG; pae:PA5372; -. DR PATRIC; fig|208964.12.peg.5629; -. DR PseudoCAP; PA5372; -. DR HOGENOM; CLU_002865_7_1_6; -. DR InParanoid; Q9HTJ2; -. DR OrthoDB; 9785276at2; -. DR PhylomeDB; Q9HTJ2; -. DR BioCyc; MetaCyc:MONOMER-8621; -. DR BioCyc; PAER208964:G1FZ6-5499-MONOMER; -. DR UniPathway; UPA00529; UER00385. DR Proteomes; UP000002438; Chromosome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0008812; F:choline dehydrogenase activity; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IBA:GO_Central. DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1. DR Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1. DR HAMAP; MF_00750; Choline_dehydrogen; 1. DR InterPro; IPR011533; BetA. DR InterPro; IPR036188; FAD/NAD-bd_sf. DR InterPro; IPR012132; GMC_OxRdtase. DR InterPro; IPR000172; GMC_OxRdtase_N. DR InterPro; IPR007867; GMC_OxRtase_C. DR NCBIfam; TIGR01810; betA; 1. DR PANTHER; PTHR11552:SF147; CHOLINE DEHYDROGENASE, MITOCHONDRIAL; 1. DR PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1. DR Pfam; PF05199; GMC_oxred_C; 1. DR Pfam; PF00732; GMC_oxred_N; 1. DR PIRSF; PIRSF000137; Alcohol_oxidase; 1. DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1. DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1. DR PROSITE; PS00623; GMC_OXRED_1; 1. DR PROSITE; PS00624; GMC_OXRED_2; 1. PE 3: Inferred from homology; KW FAD; Flavoprotein; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1..561 FT /note="Oxygen-dependent choline dehydrogenase" FT /id="PRO_0000205590" FT ACT_SITE 475 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750" FT BINDING 6..35 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750" SQ SEQUENCE 561 AA; 61837 MW; 57B6760D3F6F1F8F CRC64; MSQEFDYIII GAGSAGNVLA TRLTEDADVS VLLLEAGGPD YRFDFRTQMP AALAFPLQGR RYNWAYETDP EPYMNNRRME CGRGKGLGGS SLINGMCYIR GNALDFDGWA KEPGLEDWSY LDCLPYFRKA ETRDIGPNDY HGGDGPVSVT TPKAGNNPLF HAMVEAGVQA GYPRTDDLNG YQQEGFGPMD RTVTPEGRRA ATGRGYLDQA RGRPNLTIVT HALSDRILFS GKRAIGVSYL VGNGDNPVTA HARREVLVCS GAIASPQLLQ RSGVGPAALL RDLDIPVVHD LPGVGANLQD HLELYLQYAC KQPVSIYPAT KWWNQPAIGA QWLFLGKGLG ASNQFEAGGF IRTREAFEWP NIQFHFLPVA INYNGSKGVQ EHGFQAHMGS MRSPSRGRIH LKSRDPRQHP SILFNYMSHE QDWQEFRDGI RLTREIMNQP ALDPYRGREL SPGVSVQSDA ELDEFIRNHA ETAFHPSCSC KMGSDDMAVV DGQGRVHGME GLRVVDASIM PLIITGNLNA TTIMMAEKIA DRIRGRQPLP RSTAKYYVAG DAPVRGNPVR A //