ID A0A0J7XMU3_9SPHN Unreviewed; 539 AA.
AC A0A0J7XMU3;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:KMS52987.1};
GN ORFNames=V473_18495 {ECO:0000313|EMBL:KMS52987.1};
OS Sphingobium cupriresistens LL01.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1420583 {ECO:0000313|EMBL:KMS52987.1, ECO:0000313|Proteomes:UP000052232};
RN [1] {ECO:0000313|EMBL:KMS52987.1, ECO:0000313|Proteomes:UP000052232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LL01 {ECO:0000313|EMBL:KMS52987.1,
RC ECO:0000313|Proteomes:UP000052232};
RX PubMed=25850427; DOI=10.1534/g3.114.015933;
RA Pearce S.L., Oakeshott J.G., Pandey G.;
RT "Insights into Ongoing Evolution of the Hexachlorocyclohexane Catabolic
RT Pathway from Comparative Genomics of Ten Sphingomonadaceae Strains.";
RL G3 (Bethesda) 5:1081-1094(2015).
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:KMS52987.1}.
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DR EMBL; JACT01000005; KMS52987.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0J7XMU3; -.
DR STRING; 1420583.V473_18495; -.
DR PATRIC; fig|1420583.3.peg.3495; -.
DR Proteomes; UP000052232; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000052232}.
FT DOMAIN 82..105
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 255..269
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 220
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 539 AA; 57742 MW; F93641AE0616DAE8 CRC64;
MAMNPDYIVI GAGSAGSVLA NRLSGPGGGT VLLLEAGGAT RSLLYRMPLA ATKLWFNPKT
SWGLWSEPEP GLGGRKIPVP RGKGLGGSSA INGTIYNRGS PHDYDQWRDL GLNDWDYASL
LPYFRRIENH WRGKDAVHGA DGEVRISPVG SRSPFMPAFL ETARQMGWPV TDDFLCNDGE
GVGLSDLNVD ARGRRVSAAD AFLRPIASRA TLTVATHAQV RRIIIEDGRA IGVEYDHHGR
RKIVHAAREI ILAAGAIASP QILLLSGIGP ADELGAVGIK PVHDLPGVGR NFNDQPGGSF
EFTVKQPLSF TRSLRADRFV LSLAQWALGL GGVAAGPPIV SMGTIRTNSL DRSPDLRLNL
AAGTMLSKVW YPGITKAGPH KLMMSFGLAH PESRGSITLT SADPSMAPRI CFNLLMAKGD
MDRMRSYYRL LSGMIRQPAF ADIAGEITRP EANPVDDDAL DAYLRSVAGT TSHPMGSCKM
GLDDAAVVDA RCCVRGIKNL RVVDASIFPT QIAGNPHSAI MAVGDKVSDV ILNRPAMRD
//
