ID A1B9Z8_PARDP Unreviewed; 546 AA.
AC A1B9Z8;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:ABL72342.1};
GN OrderedLocusNames=Pden_4278 {ECO:0000313|EMBL:ABL72342.1};
OS Paracoccus denitrificans (strain Pd 1222).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=318586 {ECO:0000313|EMBL:ABL72342.1, ECO:0000313|Proteomes:UP000000361};
RN [1] {ECO:0000313|Proteomes:UP000000361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pd 1222 {ECO:0000313|Proteomes:UP000000361};
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA Richardson P.;
RT "Complete sequence of chromosome 2 of Paracoccus denitrificans PD1222.";
RL Submitted (DEC-2006) 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}.
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DR EMBL; CP000490; ABL72342.1; -; Genomic_DNA.
DR RefSeq; WP_011750504.1; NC_008687.1.
DR AlphaFoldDB; A1B9Z8; -.
DR STRING; 318586.Pden_4278; -.
DR EnsemblBacteria; ABL72342; ABL72342; Pden_4278.
DR GeneID; 75503660; -.
DR KEGG; pde:Pden_4278; -.
DR eggNOG; COG2303; Bacteria.
DR HOGENOM; CLU_002865_7_1_5; -.
DR OrthoDB; 9785276at2; -.
DR Proteomes; UP000000361; Chromosome 2.
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};
KW Reference proteome {ECO:0000313|Proteomes:UP000000361}.
FT DOMAIN 85..108
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 258..272
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 222
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 546 AA; 59943 MW; 613A7F0BDBE8EC44 CRC64;
MSHEANVPDY IVVGAGSAGC VVANRLSADP AVRVTLLEAG NRDSSPWIHI PVGYFQTMHN
PRFDWCYETE PDPGLAGRSL HWPRGKVLGG SSSLNGLLYV RGQREDYDRW AQMGNDGWSW
REVGPLFEEL ETFQRGEGEG RGMHGALQVS DPRLRRRICE LWIEAAKANG IPYNPDYNGP
VQDGVGHFQL TVDKGRRCSA AVAFLRPIRH RQNLQVVTRS LVRRIVIEQG RATGVEIQRP
DGSREVIRAA REVILCAGAI GSPQILMLSG VGDADHLRDL GIAVQHHSPE VGRNLQDHLQ
ARLVFKCREA TLNDEVRSLV NKARIGLEYA LFRTGPMTMA ASLVFGFLRT RPGLATPDIQ
FHIQPWSADS PGEGVHPFSA FTQSVCQLRP ESRGTITLRS ADPSAVPVIA PNYLATQTDC
DTLVAGIEIA RKLARTEPLK SAISEEFRPT ADVQGHDEIL DWARMNSTTI YHPTGTCRMG
ADARAVVDPR LRVRGIRGLR VADCSIMPEI VSGNTNAPAM MIGAKLARLV LEDRRTEGGA
DTTKAA
//
