ID A0A1A1YUC0_9MYCO Unreviewed; 567 AA.
AC A0A1A1YUC0;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Choline dehydrogenase {ECO:0000256|RuleBase:RU003969};
DE EC=1.1.99.1 {ECO:0000256|RuleBase:RU003969};
GN ORFNames=A5724_16235 {ECO:0000313|EMBL:OBF34917.1};
OS Mycobacterium sp. ACS1612.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1834117 {ECO:0000313|EMBL:OBF34917.1, ECO:0000313|Proteomes:UP000092025};
RN [1] {ECO:0000313|Proteomes:UP000092025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS1612 {ECO:0000313|Proteomes:UP000092025};
RA Sutton G., Brinkac L., Sanka R., Adams M., Lau E., Kiyimba A., Mayanja H.,
RA Musoke P., Ssengooba W., Joloba M.;
RL Submitted (JUN-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}.
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:OBF34917.1}.
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DR EMBL; LZHZ01000031; OBF34917.1; -; Genomic_DNA.
DR RefSeq; WP_067801767.1; NZ_LZHZ01000031.1.
DR AlphaFoldDB; A0A1A1YUC0; -.
DR STRING; 1834117.A5724_16235; -.
DR OrthoDB; 9785276at2; -.
DR UniPathway; UPA00529; UER00385.
DR Proteomes; UP000092025; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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 Reference proteome {ECO:0000313|Proteomes:UP000092025}.
FT DOMAIN 88..111
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 263..277
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 90
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 228
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 567 AA; 62574 MW; 5EB170E25F301FA8 CRC64;
MAGKVSTRYD FVIVGGGSAG CALANRLSAD PANKVLVLEA GRNDSLWDVF VHMPAALPFP
IGSRFYDWKY ESEPEPHMHG RRIYHARGKV LGGSSSINGM IFQRGNPMDY ERWGADPGMG
DWDFAHCLPY FNRMENCLAA TPDDPYRGHD GPLALERGPA TNPLFEAFFT AGEQAGYPRT
DDVNGYRQEG FAKFDRNIRN GRRLSAARAY LHPVMNRPNL DVLTRAFVER VVFDGKRAVG
VEYRRGRGEA QRVNAGQVVL CGGAINSPQL LQLSGIGNAA ELEALGVDVV HDLPGVGENL
QDHLEVYIQY ACKQPVTMQK YLKWRYRPWI GANWLFLHRG PGATNHFEGG GFVRSNNEVA
YPNLMFHFLP IAVRYDGSQP EGGEGYQVHV GPMYSDARGS LKIVSRDPKV HPALRFNYLS
TEQDRREWVE AVRVARNILN QPAMAPFNGG ETSPGPSVET DEEILDWVAR DAETALHPSC
TAKMGTDAMS VTDPQTMGVH GIEGLKVVDA SVLPYVTNGN IYAPVMMVAE KAADLILGNT
PLAPATVPFY RHQPKQQPSD SETVSRS
//
