ID A0A1Q7T7L0_9CHLR Unreviewed; 499 AA.
AC A0A1Q7T7L0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Choline dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUG54_00650 {ECO:0000313|EMBL:OLD84517.1};
OS Ktedonobacter sp. 13_1_20CM_4_53_7.
OC Bacteria; Chloroflexota; Ktedonobacteria; Ktedonobacterales;
OC Ktedonobacteraceae; Ktedonobacter.
OX NCBI_TaxID=1805226 {ECO:0000313|EMBL:OLD84517.1, ECO:0000313|Proteomes:UP000186099};
RN [1] {ECO:0000313|EMBL:OLD84517.1, ECO:0000313|Proteomes:UP000186099}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27843720;
RA Butterfield C.N., Li Z., Andeer P.F., Spaulding S., Thomas B.C., Singh A.,
RA Hettich R.L., Suttle K.B., Probst A.J., Tringe S.G., Northen T., Pan C.,
RA Banfield J.F.;
RT "Proteogenomic analyses indicate bacterial methylotrophy and archaeal
RT heterotrophy are prevalent below the grass root zone.";
RL PeerJ 4:E2687-E2687(2016).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974,
CC ECO:0000256|PIRSR:PIRSR000137-2};
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:OLD84517.1}.
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DR EMBL; MNIQ01000043; OLD84517.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q7T7L0; -.
DR Proteomes; UP000186099; Unassembled WGS sequence.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR012132; GMC_OxRdtase.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
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; 2.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR000137-2};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630}.
FT DOMAIN 2..291
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 354..489
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
FT BINDING 80
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 215
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 499 AA; 54787 MW; 070DF915C25BC8BA CRC64;
MYDYIIVGAG SAGCVLANRL TENLETSVLL LEAGGNDDLP AIHDATAAPS LLQTAVDWAY
FTEEEPHLKH RKIYHPRGKV LGGSSSTNFM TYARGNQHDY DDWQELGNKG WSYADVLPYF
KKAENWESGT SDYRGVGGPI NVTDPSSINP LTEAFIEAGV ELGWPRNNDY NGASQGGFGF
HQSTVHHGKR SSTADGYLHP AENRPNLVVW MNTLVTRVLF EGTRAVGIAY LKDGKEQQER
VKKEVILSGG VFNSPQTLLL SGVGPADQLR ALDIRVVSHV PGVGHNLQDH PGFDMFFATK
PSFTQHGNEP GGIAFMKTQP DLPDADLQLL FCPFFLFPTV PGKGYTIVVL PTHPQSRGHL
TLRSTDPTQP PAIFANYLAH EADQQTLVKG MKLVRRLAQT TSFARYTERE TIPGSQVQSD
AQIVEFLREN VRTISHPVGT CKMGHDEMAV VDEQLRVRGV EGLRVVDASI MPIIPHGNTN
APTIMIAEKV ADMIAHNVQ
//
