BETA_PSEAE
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 03-AUG-2022, entry version 120.
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; Proteobacteria; 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 / 1C /
RC 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;
CC Evidence={ECO:0000255|HAMAP-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}.
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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; 287.DR97_2748; -.
DR PaxDb; Q9HTJ2; -.
DR PRIDE; Q9HTJ2; -.
DR EnsemblBacteria; AAG08757; AAG08757; 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 OMA; NHFESCA; -.
DR PhylomeDB; Q9HTJ2; -.
DR BioCyc; MetaCyc:MON-8621; -.
DR BioCyc; PAER208964:G1FZ6-5499-MON; -.
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:0016491; F:oxidoreductase activity; IBA:GO_Central.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IBA:GO_Central.
DR Gene3D; 3.50.50.60; -; 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 PANTHER; PTHR11552; PTHR11552; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR01810; betA; 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
