(data stored in ACNUC29543 zone)

SWISSPROT: BETA_PARP8

ID   BETA_PARP8              Reviewed;         572 AA.
AC   B2JS89;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   08-MAY-2019, entry version 76.
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=Bphy_3310;
OS   Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS   STM815) (Burkholderia phymatum).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=391038;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX   PubMed=25197461; DOI=10.4056/sigs.4861021;
RA   Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A.,
RA   Melkonian R., James E.K., Young J.P., Bena G., Hauser L., Land M.,
RA   Kyrpides N., Bruce D., Chain P., Copeland A., Pitluck S., Woyke T.,
RA   Lizotte-Waniewski M., Bristow J., Riley M.;
RT   "Complete genome sequence of Burkholderia phymatum STM815(T), a broad
RT   host range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL   Stand. Genomic Sci. 9:763-774(2014).
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:0000255|HAMAP-Rule:MF_00750}.
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:0000255|HAMAP-Rule:MF_00750};
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:0000255|HAMAP-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
CC       via choline pathway; betaine aldehyde from choline (cytochrome c
CC       reductase 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}.
DR   EMBL; CP001044; ACC72466.1; -; Genomic_DNA.
DR   RefSeq; WP_012402639.1; NC_010623.1.
DR   SMR; B2JS89; -.
DR   STRING; 391038.Bphy_3310; -.
DR   CAZy; AA3; Auxiliary Activities 3.
DR   EnsemblBacteria; ACC72466; ACC72466; Bphy_3310.
DR   GeneID; 27742996; -.
DR   KEGG; bph:Bphy_3310; -.
DR   eggNOG; ENOG4105CZ6; Bacteria.
DR   eggNOG; COG2303; LUCA.
DR   HOGENOM; HOG000139600; -.
DR   KO; K00108; -.
DR   OMA; LSWKIHM; -.
DR   OrthoDB; 543793at2; -.
DR   BioCyc; BPHY391038:G1GBS-3406-MONOMER; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000001192; Chromosome 2.
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   Gene3D; 4.10.450.10; -; 1.
DR   HAMAP; MF_00750; Choline_dehydrogen; 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   PANTHER; PTHR11552:SF157; PTHR11552:SF157; 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;
DR   PRODOM; B2JS89.
DR   SWISS-2DPAGE; B2JS89.
KW   Complete proteome; FAD; Flavoprotein; NAD; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN         1    572       Oxygen-dependent choline dehydrogenase.
FT                                /FTId=PRO_1000133324.
FT   NP_BIND       7     36       FAD. {ECO:0000255|HAMAP-Rule:MF_00750}.
FT   ACT_SITE    474    474       Proton acceptor. {ECO:0000255|HAMAP-
FT                                Rule:MF_00750}.
SQ   SEQUENCE   572 AA;  63110 MW;  8484418C99549861 CRC64;
     MAAKEYDYII IGAGSAGNVL ATRLTEDRDV TVLLLEAGGP DYRFDFRTQM PAALAYPLQG
     RRYNWAYETD PEPFMNNRRM ECGRGKGLGG SSLINGMCYI RGNALDYDGW AERKGLENWT
     YLDCLPYFRK AETRDAGAND YHGGDGPVHV TTSKRGVNPL FEAMVEAGVQ AGYPRTDDLN
     GYQQEGFGPM DRTVTANGRR ASTARGYLDQ ARPRPNLTIV TYATTDRILF SGKRAQGVVY
     LDGQAQITAH ARREVLLCSG AIASPQILQR SGVGPGGWLR DLDIPVVLDL PGVGQNLQDH
     LEMYMQYECK EPVSLYPALL LRNQPAIGIE WMLKGTGIGA SNHFEAGGFI RTRDDDPWPN
     IQYHFLPVAI NYNGTNAIKM HGFQAHVGSM RSPSRGRVKL RSRDPREHPS ILFNYMAEAL
     DWREFRDAIR ITREIIAQPA LDRFRGRELS PGAELQSDAQ IDAFVRARAE TAYHPSCSCA
     MGYDDMAVVD GEGRVHGLEG LRVVDASIMP RITTGNLNAP TIMLAEKIAD RIRGRAPLAR
     STAPYYVANG APARGAKHVE HAPAPSVAAH TH
//

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