ID A0A2G5UZF8_9PELO Unreviewed; 616 AA.
AC A0A2G5UZF8;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN Name=Cni-C34C6.4 {ECO:0000313|EMBL:PIC44656.1};
GN Synonyms=Cnig_chr_II.g4952 {ECO:0000313|EMBL:PIC44656.1};
GN ORFNames=B9Z55_004952 {ECO:0000313|EMBL:PIC44656.1};
OS Caenorhabditis nigoni.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=1611254 {ECO:0000313|EMBL:PIC44656.1, ECO:0000313|Proteomes:UP000230233};
RN [1] {ECO:0000313|Proteomes:UP000230233}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JU1422 {ECO:0000313|Proteomes:UP000230233};
RA Yin D., Schwarz E.M., Thomas C.G., Felde R.L., Korf I.F., Cutter A.D.,
RA Schartner C.M., Ralston E.J., Meyer B.J., Haag E.S.;
RT "Rapid genome shrinkage in a self-fertile nematode reveals novel sperm
RT competition proteins.";
RL Submitted (OCT-2017) 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:PIC44656.1}.
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DR EMBL; PDUG01000002; PIC44656.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5UZF8; -.
DR STRING; 1611254.A0A2G5UZF8; -.
DR Proteomes; UP000230233; Chromosome ii.
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.
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:UP000230233}.
FT DOMAIN 320..334
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 135
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 616 AA; 69791 MW; 540F4A87E29F1F08 CRC64;
MHHLAKIRPK LGYLHQKRCF NWRDSMREGT FSADVQENKP THIIVGAGSA GCVLANRLTE
DPSNRVLLIE AGPIDHKWDW RIHMPAALMY NLCSETYNWH YHTTAQKNLG NRTFYWPRGR
IRIFEFLNFR IPSRVWGGSS TLNAMCYVRG HAYDYDRWER EEGAEGWNYS NCLPYFKKAE
TYSHASGPDD PYRGSSGPLF VKKGDAENPL HKAWLKTGKE HPLGFTDDMN GERQEGISTM
DMTIHNGERW SASKAYVHPI RNRPNLITSS GITCTRVLFD KTKAIGIEFI RKLNFVGTDS
IDSYSREKIY CQGDVILAGG AINTPQILML SGVGPAEHLR SHEIPLVVDL PGVGQNLQDH
LEIYVQQESL KPVTLYNKSS WRFPHNMIKI GVEWFTNRTG LGASSHLETG GFARSDETVS
HPDIQFHFLP STVHDDGRTN GKCHGYQVHV GPMRSKSKGY IMLQAKDPRR APIINPNYMD
EDADWREFRK CIRLSRELFA SPAFDEFRGR ELAPGDDCQS DADIDKFVKE KAASAYHPSC
TCKMGNENDR MAVVDPKTMG VHGTENLKIV DASVMPSIVS GNLNAPVIMM AERAADLIKH
KKQMLPKSDV KVWTHK
//
