BETA_STAA8
ID BETA_STAA8 Reviewed; 569 AA.
AC Q2FV11;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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};
GN OrderedLocusNames=SAOUHSC_02932;
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47;
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL D.C. (2006).
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; CP000253; ABD31927.1; -; Genomic_DNA.
DR RefSeq; WP_000066521.1; NZ_LS483365.1.
DR RefSeq; YP_501385.1; NC_007795.1.
DR AlphaFoldDB; Q2FV11; -.
DR SMR; Q2FV11; -.
DR STRING; 1280.SAXN108_2881; -.
DR EnsemblBacteria; ABD31927; ABD31927; SAOUHSC_02932.
DR GeneID; 3921639; -.
DR KEGG; sao:SAOUHSC_02932; -.
DR PATRIC; fig|93061.5.peg.2651; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_9; -.
DR OMA; NHFESCA; -.
DR UniPathway; UPA00529; UER00385.
DR PRO; PR:Q2FV11; -.
DR Proteomes; UP000008816; Chromosome.
DR GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniRule.
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..569
FT /note="Oxygen-dependent choline dehydrogenase"
FT /id="PRO_0000258935"
FT ACT_SITE 475
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
FT BINDING 9..38
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00750"
SQ SEQUENCE 569 AA; 63610 MW; A6E35293AADDDFA6 CRC64;
MSNKNKSYDY VIIGGGSAGS VLGNRLSEDK DKEVLVLEAG RSDYFWDLFI QMPAALMFPS
GNKFYDWIYS TDEEPHMGGR KVAHARGKVL GGSSSINGMI YQRGNPMDYE GWAEPEGMET
WDFAHCLPYF KKLEKTYGAA PYDKFRGHDG PIKLKRGPAT NPLFQSFFDA GVEAGYHKTP
DVNGFRQEGF GPFDSQVHRG RRMSASRAYL HPAMKRKNLT VETRAFVTEI HYEGRRATGV
TYKKNGKLHT IDANEVILSG GAFNTPQLLQ LSGIGDSEFL KSKGIEPRVH LPGVGENFED
HLEVYIQHKC KEPVSLQPSL DIKRMPFIGL QWIFTRTGAA ASNHFEGGGF VRSNNEVDYP
NLMFHFLPIA VRYDGQKAAV AHGYQVHVGP MYSNSRGSLK IKSKDPFEKP SIRFNYLSTE
EDKKEWVEAI RVARNILSQK AMDPFNGGEI SPGPEVQTDE EILDWVRRDG ETALHPSCSA
KMGPASDPMA VVDPLTMKVH GMENLRVVDA SAMPRTTNGN IHAPVLMLAE KAADIIRGRK
PLEPQYIDYY KHGVHDENEG AIEVKPYAK