ID A0A0Q6TXN8_9CAUL Unreviewed; 555 AA.
AC A0A0Q6TXN8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KQV58782.1};
GN ORFNames=ASC62_08420 {ECO:0000313|EMBL:KQV58782.1};
OS Caulobacter sp. Root342.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1736519 {ECO:0000313|EMBL:KQV58782.1, ECO:0000313|Proteomes:UP000051656};
RN [1] {ECO:0000313|EMBL:KQV58782.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV58782.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQV58782.1, ECO:0000313|Proteomes:UP000051656}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root342 {ECO:0000313|EMBL:KQV58782.1,
RC ECO:0000313|Proteomes:UP000051656};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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, 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:KQV58782.1}.
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DR EMBL; LMDD01000006; KQV58782.1; -; Genomic_DNA.
DR RefSeq; WP_056049162.1; NZ_LMDD01000006.1.
DR AlphaFoldDB; A0A0Q6TXN8; -.
DR STRING; 1736519.ASC62_08420; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000051656; 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; 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}.
FT DOMAIN 94..117
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 266..280
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 555 AA; 59180 MW; 5581BD5D3A1243CC CRC64;
MTGTLEADYV IVGAGSAGCV LAARLSEGGR LKVLLLEAGG DDRPTKNLGQ FASNLMIHIP
VGYSSTLKDP KVNWLYTTEP DPGTGGRTHV WPRGKVLGGS SSINGLLYIR GQHADYDGWR
QLGCEGWGWD DVASYFRRAE HQERGDCDWH ATGGPLNVSD VTTKHPVSDA VIEACEQAGI
PRNDDVNGSA QEGATYYQLT VKNGQRCSAA VAYLHPAMTR PNLRVETNAL AGKILFEGKR
AVGVAFTQNG VQRVAKARGE VILAGGAINS PQLLQLSGVG PAELLIRNGV PVVADLPGVG
ENLQDHYVMS VRYRLKPGVV SVNEQSKGGR LAGEALRYLF QRKGLLTLSA AHIAAFCKSR
PDLAGPDIQF HILPATMDLA KLNNEQKMVL EDAPGLTIAP CQLRPESRGH VRIKSADPST
YPTIFANYLA DPLDQEVAVA GLKWARRIGA APALSPYVES ELNPGGAFAT DEQLLAYARL
SGSTIYHPVG TCQMGQGPMA VVDAQLRVRG IEGLRVVDAS VMPRLVSGNT NAPTIMIAEK
ASDMIRAAAR EAVAA
//
