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Database: UniProt
Entry: A0A0C1R8L1_9ACTN
LinkDB: A0A0C1R8L1_9ACTN
Original site: A0A0C1R8L1_9ACTN 
ID   A0A0C1R8L1_9ACTN        Unreviewed;       553 AA.
AC   A0A0C1R8L1;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   13-SEP-2023, entry version 37.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=MB54_03070 {ECO:0000313|EMBL:KIE49922.1};
OS   marine actinobacterium MedAcidi-G2B.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1550401 {ECO:0000313|EMBL:KIE49922.1, ECO:0000313|Proteomes:UP000031352};
RN   [1] {ECO:0000313|EMBL:KIE49922.1, ECO:0000313|Proteomes:UP000031352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mizuno C.M., Rodriguez-Valera F., Ghai R.;
RT   "Novel reconstructed genomes of marine planktonic Acidimicrobiales.";
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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         ECO:0000256|PIRSR:PIRSR000137-2};
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KIE49922.1}.
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DR   EMBL; JUEO01000003; KIE49922.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C1R8L1; -.
DR   STRING; 1550401.MB54_03070; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000031352; Unassembled WGS sequence.
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|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW   ECO:0000313|EMBL:KIE49922.1}.
FT   DOMAIN          85..108
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          258..272
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         87
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         224
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   553 AA;  61644 MW;  324D4897A1077DC5 CRC64;
     MLTKTYDYVV IGGGSAGSAL ANRLSADPKN KVLLIEAGRS DWKIDPIIHM PAALSMGIGN
     RLYDWKYESE PEPQMNGRRV YHARGKVLGG SSSINGMIFQ RGNPMDFDRW AAIEGCEDWD
     WSHCLPYFKR METCLAGPDE WRGGEGPLKL ERGPATSPLF QAFFTAVQEA GHPLTTDVNG
     YRQEGFNAFD RNIYRGRRHS AARAYLHPVL RDRKNLHLIT RAHVTQLIMK KNRVTGVEYH
     KNKRRHRVEA TEVISCGGAF NSPQLLQLSG IGPSSVLSQA GISPVVDLPG VGENLQDHLE
     VYVQYACKEP VSMAPYLKNW RKPGVGLKWL FRKGPGATNH FEAGGFLRSN DGVLWPNLMF
     HFLPVAVRYD GTTITQGHGY QFHIGPMFSN STGWVRIQSN DPFAKPKIQF NYLSTPEDRK
     EWVEAIATAR NIMKQPAFEQ FNGGEISPGP EISEEKDVLD WVRRDSETAL HPCGTARMGE
     DAMGVVSPKT MRVHGVEGLR VVDASVMPTL TNGNIYAPVM MLAEKAADLI LGNTPLEPSR
     AGQYRHGVSE KDW
//
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