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Database: UniProt
Entry: A0A0F6TAB0_9CORY
LinkDB: A0A0F6TAB0_9CORY
Original site: A0A0F6TAB0_9CORY 
ID   A0A0F6TAB0_9CORY        Unreviewed;       599 AA.
AC   A0A0F6TAB0;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 36.
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:AKE38086.1};
GN   ORFNames=UL81_00465 {ECO:0000313|EMBL:AKE38086.1};
OS   Corynebacterium camporealensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=161896 {ECO:0000313|EMBL:AKE38086.1, ECO:0000313|Proteomes:UP000033566};
RN   [1] {ECO:0000313|EMBL:AKE38086.1, ECO:0000313|Proteomes:UP000033566}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44610 {ECO:0000313|EMBL:AKE38086.1,
RC   ECO:0000313|Proteomes:UP000033566};
RX   PubMed=26021938;
RA   Ruckert C., Albersmeier A., Winkler A., Tauch A.;
RT   "Complete Genome Sequence of Corynebacterium camporealensis DSM 44610,
RT   Isolated from the Milk of a Manchega Sheep with Subclinical Mastitis.";
RL   Genome Announc. 3:e00572-15(2015).
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;
CC         Evidence={ECO:0000256|RuleBase:RU003969};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
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:0000256|RuleBase:RU003969}.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; CP011311; AKE38086.1; -; Genomic_DNA.
DR   RefSeq; WP_046453128.1; NZ_CP011311.1.
DR   AlphaFoldDB; A0A0F6TAB0; -.
DR   KEGG; ccj:UL81_00465; -.
DR   PATRIC; fig|161896.4.peg.92; -.
DR   HOGENOM; CLU_002865_7_1_11; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000033566; Chromosome.
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; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 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 {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:AKE38086.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000033566}.
FT   DOMAIN          108..131
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          282..296
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   599 AA;  67225 MW;  78304D78CC5B240B CRC64;
     MGVFDAVAQK VEKLTSGKKQ HKNVTDEVSD VVVVGGGSAG SVVAARLTEN PDTRVLVLEA
     GRPDSIWDLF IHMPSAFSFP IGAKNYDWMY ESEPEPEMNG RRVYHARGKL LGGSSSVNGM
     IFQRGNPMDY EKWGDNPGME HWDFAHCLPY FKKMETAAGS DESDPRRGHD GPLYLSRGPA
     ISPLFQALFK SVQEAGYNLT NDVNGYRQEG FAPFDRNIKH GRRWSAARAY LHPNLDRKNL
     DIRTRALTTK VLFDGQKAIG VEYEWEGETR RVFADKIVLS AGAINTPQLL QVSGIGDEEL
     LRKHGIDVVK HLPGVGENLQ DHLEVYIQYE TTKSTDSSQP YLEKWRWPFM GLQWLLTHRG
     PVATSHFEGG GFVRSNENEA YPNLMFHFLP MAVRYDGNKA DVKHGFQWHV GPMFSDTKGH
     VRIKSADIHD KPEILFNYLR TDQDRREWVE AIRVARSLLD TEAMEEVGAR EFSPGSDVQT
     DEEILEWVRN DGETALHPSC TTKMGTKDDP MAVVDPETMQ VWGIEGLYIA DAGVFPSVPN
     GNIYAPVMMV GEKAADLIAG KSPLEPEYTS WYKAGEDMPL YAEGETVRDH KHAIKGADY
//
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