ID   A0A1K1RCL2_9PSEU        Unreviewed;       556 AA.
AC   A0A1K1RCL2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE            EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN   ORFNames=SAMN04489730_2999 {ECO:0000313|EMBL:SFW69555.1};
OS   Amycolatopsis australiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Amycolatopsis.
OX   NCBI_TaxID=546364 {ECO:0000313|EMBL:SFW69555.1, ECO:0000313|Proteomes:UP000182740};
RN   [1] {ECO:0000313|EMBL:SFW69555.1, ECO:0000313|Proteomes:UP000182740}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44671 {ECO:0000313|EMBL:SFW69555.1,
RC   ECO:0000313|Proteomes:UP000182740};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FPJG01000006; SFW69555.1; -; Genomic_DNA.
DR   RefSeq; WP_072476865.1; NZ_FPJG01000006.1.
DR   AlphaFoldDB; A0A1K1RCL2; -.
DR   STRING; 546364.SAMN04489730_2999; -.
DR   OrthoDB; 9785276at2; -.
DR   UniPathway; UPA00529; UER00385.
DR   Proteomes; UP000182740; 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}.
FT   DOMAIN          85..108
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          260..274
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         225
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   556 AA;  61659 MW;  4AB818930C52E81B CRC64;
     MSSETYDFVI VGGGSAGCAL ANRLSADPAN KVLVLEAGRS DYKWDVFIHM PAALTFPIGS
     KFYDWGYRSE PEPFMNRRRV YHARGKVLGG SSSINGMIFQ RGNPMDYERW GADPGMSTWD
     YAHCLPYFQR MENCLADPPD GKWRGHDGPL ELERGPASNP LFQAFFDAAE QAGYPRTDDV
     NGYRQEGFAP FDRNVRNGRR LSAARAYLHP VLHRPNLTVK THAFVSQILF DGTRAVGVEY
     AQGRKVPEEV YGKEIILCGG AINTPQLLQL SGVGNAAELE KLGIDVVKDL PGVGENLQDH
     LEVYIQYACQ QPVSMQPSLA KWKRPWIGAQ WLFLRSGPAA TNHFEGGGFV RSNDEVKYPN
     LMFHFLPVAI RYDGSAPTEG HGYQVHVGPM YADTRGSVKI TSTDPRQHPA IKFNYLSTEN
     DRREWVEAVR VARKILNQSA LDPYNGGEIS PGPRVETDEE ILDWVAKDAE TALHPSCTAR
     MGVDEKSVVD PQTMRVHGTE GLRVVDASVM PYITNGNIYA PVMMTAEKAA DLILGNTPLA
     PIKLPFYRHG DPTAAK
//