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Database: UniProt
Entry: K7RQN7_ACIA4
LinkDB: K7RQN7_ACIA4
Original site: K7RQN7_ACIA4 
ID   K7RQN7_ACIA4            Unreviewed;       575 AA.
AC   K7RQN7;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   08-MAY-2019, entry version 45.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   Name=betA {ECO:0000313|EMBL:AFV88611.1};
GN   OrderedLocusNames=PACID_07730 {ECO:0000313|EMBL:AFV88611.1};
OS   Acidipropionibacterium acidipropionici (strain ATCC 4875 / DSM 20272 /
OS   JCM 6432 / NBRC 12425 / NCIMB 8070) (Propionibacterium
OS   acidipropionici).
OC   Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC   Acidipropionibacterium.
OX   NCBI_TaxID=1171373 {ECO:0000313|EMBL:AFV88611.1, ECO:0000313|Proteomes:UP000000214};
RN   [1] {ECO:0000313|EMBL:AFV88611.1, ECO:0000313|Proteomes:UP000000214}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 4875 / DSM 20272 / JCM 6432 / NBRC 12425 / NCIMB 8070
RC   {ECO:0000313|Proteomes:UP000000214};
RX   PubMed=23083487; DOI=10.1186/1471-2164-13-562;
RA   Parizzi L.P., Grassi M.C., Llerena L.A., Carazzolle M.F.,
RA   Queiroz V.L., Lunardi I., Zeidler A.F., Teixeira P.J., Mieczkowski P.,
RA   Rincones J., Pereira G.A.;
RT   "The genome sequence of Propionibacterium acidipropionici provides
RT   insights into its biotechnological and industrial potential.";
RL   BMC Genomics 13:562-562(2012).
CC   -!- FUNCTION: Involved in the biosynthesis of the osmoprotectant
CC       glycine betaine. Catalyzes the oxidation of choline to betaine
CC       aldehyde and betaine aldehyde to glycine betaine at the same rate.
CC       {ECO:0000256|SAAS:SAAS00321133}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=A + choline = AH2 + betaine aldehyde;
CC         Xref=Rhea:RHEA:17433, ChEBI:CHEBI:13193, ChEBI:CHEBI:15354,
CC         ChEBI:CHEBI:15710, ChEBI:CHEBI:17499; EC=1.1.99.1;
CC         Evidence={ECO:0000256|RuleBase:RU003969,
CC         ECO:0000256|SAAS:SAAS01117340};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=betaine aldehyde + H2O + NAD(+) = betaine + 2 H(+) +
CC         NADH; Xref=Rhea:RHEA:15305, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:15710, ChEBI:CHEBI:17750,
CC         ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.8;
CC         Evidence={ECO:0000256|SAAS:SAAS01117337};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2,
CC         ECO:0000256|SAAS:SAAS01080756};
CC   -!- PATHWAY: Amine and polyamine biosynthesis; betaine biosynthesis
CC       via choline pathway; betaine aldehyde from choline (cytochrome c
CC       reductase route): step 1/1. {ECO:0000256|RuleBase:RU003969,
CC       ECO:0000256|SAAS:SAAS00321105}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|RuleBase:RU003968, ECO:0000256|SAAS:SAAS01080758}.
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DR   EMBL; CP003493; AFV88611.1; -; Genomic_DNA.
DR   RefSeq; WP_015069524.1; NC_019395.1.
DR   STRING; 1171373.PACID_07730; -.
DR   EnsemblBacteria; AFV88611; AFV88611; PACID_07730.
DR   KEGG; pbo:PACID_07730; -.
DR   PATRIC; fig|1171373.8.peg.781; -.
DR   KO; K00108; -.
DR   OMA; LSWKIHM; -.
DR   BioCyc; PACI1171373:G1HC8-760-MONOMER; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000000214; Chromosome.
DR   GO; GO:0008802; F:betaine-aldehyde dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008812; F:choline dehydrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0019285; P:glycine betaine biosynthetic process from choline; IEA:UniProtKB-UniPathway.
DR   Gene3D; 3.50.50.60; -; 1.
DR   Gene3D; 4.10.450.10; -; 1.
DR   InterPro; IPR011533; BetA.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR027424; Glucose_Oxidase_domain_2.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
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.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000000214};
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080750};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968,
KW   ECO:0000256|SAAS:SAAS01080744}; NAD {ECO:0000256|SAAS:SAAS00321145};
KW   Oxidoreductase {ECO:0000256|SAAS:SAAS01080751,
KW   ECO:0000313|EMBL:AFV88611.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000214}.
FT   DOMAIN       84    107       GMC_OxRdtase_N. {ECO:0000259|PROSITE:
FT                                PS00623}.
FT   BINDING      86     86       FAD; via carbonyl oxygen.
FT                                {ECO:0000256|PIRSR:PIRSR000137-2}.
FT   BINDING     222    222       FAD; via amide nitrogen and carbonyl
FT                                oxygen. {ECO:0000256|PIRSR:PIRSR000137-
FT                                2}.
SQ   SEQUENCE   575 AA;  63128 MW;  D2F076DB1B36DD3D CRC64;
     MGKHYDYVIV GGGSAGSVLA NRLSADPGTS VLVLEAGRSD FRIDPFVHMP AALSFPIGSR
     FYDWRYETEP EPYMGGRRVY HARGKVLGGS SSINGMIFQR GNAMDYQRWA ADPGMEHWDY
     AHCLPYFKRM EDCTAGADAW RGGSGPLRLE RGPADKPIFG AFFEAAQQAG YPLTDDINGY
     RQEGFAPFDK NVVNGRRLSA ARAYLHPVMN RHNLTVHTLS TVTRLRTRTS GGRTSRVTGV
     DYLHGRRKAS ADAGEVILCG GAFNTPQLLQ LTGIGNPDDL RAVGVSPIAE VPGVGRNMQD
     HLEVYLQHEA KQPVSIGPWM KYRHYPRIGA EWLFLRRGMG ATNHFEAGGF VRTNDEVDHP
     NLMFHFLPIA IRYDGGAPVV EEGYQVHIGP MYSDARGTLR IKSQDPLQHP AIRFNYLSTE
     QDRREWVEVV NTARTILAQP AFSAIDAGEI SPGPAVSSDS EILDWVARDA ETALHPSCTA
     RMGTGQDAVV DPETMKVNGV EGLRAADASV MPYVTNGNIY APVMMIAEKA ADLIAGNTPL
     DPLTDVPYYR AGEGMPLFWP PADPRNSDQT LAAHN
//
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