ID A0A0Q8QQ73_9SPHN Unreviewed; 536 AA.
AC A0A0Q8QQ73;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:KRB87746.1};
GN ORFNames=ASE22_23890 {ECO:0000313|EMBL:KRB87746.1};
OS Sphingomonas sp. Root720.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1736595 {ECO:0000313|EMBL:KRB87746.1, ECO:0000313|Proteomes:UP000051570};
RN [1] {ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|Proteomes:UP000051570};
RA Garrido-Oter R., Bai Y.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRB87746.1, ECO:0000313|Proteomes:UP000051570}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root720 {ECO:0000313|EMBL:KRB87746.1,
RC ECO:0000313|Proteomes:UP000051570};
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}.
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:KRB87746.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LMID01000016; KRB87746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q8QQ73; -.
DR STRING; 1736595.ASE22_23890; -.
DR Proteomes; UP000051570; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000051570}.
FT DOMAIN 256..270
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 86
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 536 AA; 58006 MW; 6450161E0CD81FE4 CRC64;
MKDLGSFDYV IAGAGTAGCL LANRLSADPT KRVLVLEAGG TDSWIWFHIP VGYLFAIGNP
RADWMFETAE EPGLGGRRLA YPRGKVIGGC SAINAMIYMR GQAADYDGWR ELGLAGWGWD
DVLPHFLRHE DHASASGSHH RRGGEWRVER PRLRWEVLDA VREAGAALGI APVDDFNGGD
NAGCGYFHVN QRGGRRVSAA GAFLKPALGR PNLRLETGVE IDRILFDDRR AAGLVFRRGN
EQWTARADGE VILATGAVGT PKLLQLSGVG EAARLKRLGI EPVHDLPGVG ANLQDHLQIR
PIFKVRGVRT LNTDYANLLR RAAMGLEYAL FRTGPLTMAP SQLGMFARSS DAHARPNLQF
HFQPLSLDAW GTGLHRFGAF TASVCNLRPT SRGRIDLAGA DPSAPPRIAP GYLSTEEDRR
TAVDSLRLAR KIAAQAPLAR YRPEEFRPGA ELDSDEQLLA AAAELGTTIF HPVGTAAMGG
DDDPGAVLDE RLRVRGLDGL RVVDASAMPR IPSGNTSSPT LMIAEKGAAM IIEDRR
//
