ID A0A101SVY4_9ACTN Unreviewed; 556 AA.
AC A0A101SVY4;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN ORFNames=AQJ64_24065 {ECO:0000313|EMBL:KUN81066.1};
OS Streptomyces griseoruber.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1943 {ECO:0000313|EMBL:KUN81066.1, ECO:0000313|Proteomes:UP000052982};
RN [1] {ECO:0000313|EMBL:KUN81066.1, ECO:0000313|Proteomes:UP000052982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 40281 {ECO:0000313|EMBL:KUN81066.1,
RC ECO:0000313|Proteomes:UP000052982};
RA Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT "Draft genome sequence of Streptomyces griseoruber DSM 40281, type strain
RT for the species Streptomyces griseoruber.";
RL Submitted (OCT-2015) 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:KUN81066.1}.
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DR EMBL; LMWW01000038; KUN81066.1; -; Genomic_DNA.
DR RefSeq; WP_055634573.1; NZ_LIQS01000208.1.
DR AlphaFoldDB; A0A101SVY4; -.
DR STRING; 1943.AQJ64_24065; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000052982; 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:KUN81066.1}.
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; 61437 MW; F6912A249BB3F2CA CRC64;
MASLQYDFVI VGGGSAGSAL ANRLSADPAN RVLVLEAGRS DYPWDVFIHM PAALTYPIGS
RFYDWKYESE PEPHMGGRRV YHARGKVLGG SSSINGMIFQ RGNPMDYERW AADPGMESWD
YAHCLPYFRR MENCLAADPD DEFRGHDGPL VLERGPASNP LFGAFLKATE EAGYPPTEDV
NGYRQEGFAK FDRNVSRGRR LSASKAYLKP ARKRPNLTVT TRALVTRVLF EGKKAVGVEY
RKGRGAPKQV RAKEVILCGG AINSPQLLQL SGVGNAEELR ALGIDVVHDL PGVGENMQDH
LEVYIQYGCK QPVSMQPYLA KWRAPFIGLQ WLFRKGPAAT NHFEAGGFAR SNEDVDYPNL
MFHFLPIAVR YDGSVPAGGH GYQVHVGPMY SDAIGSVKIK SKDPREHPAL RFNYLSTEQD
RREWVEAIRV ARKLLNQPAL APYNDGEISP GPSVESDEEI LEWVAKDGET ALHPSCTCKM
GTDEMSVVDP TSMRVHGVEG LRVVDASVMP YVTNGNIYAP VMMIAEKAAD LILGKEPLAP
SKAAYYRHRD AETQAG
//
