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Database: UniProt
Entry: A0A0V1N183_9BILA
LinkDB: A0A0V1N183_9BILA
Original site: A0A0V1N183_9BILA 
ID   A0A0V1N183_9BILA        Unreviewed;       602 AA.
AC   A0A0V1N183;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   SubName: Full=Glucose dehydrogenase [FAD, quinone] {ECO:0000313|EMBL:KRZ77600.1};
GN   Name=Gld {ECO:0000313|EMBL:KRZ77600.1};
GN   ORFNames=T10_3687 {ECO:0000313|EMBL:KRZ77600.1};
OS   Trichinella papuae.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=268474 {ECO:0000313|EMBL:KRZ77600.1, ECO:0000313|Proteomes:UP000054843};
RN   [1] {ECO:0000313|EMBL:KRZ77600.1, ECO:0000313|Proteomes:UP000054843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS1980 {ECO:0000313|EMBL:KRZ77600.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:KRZ77600.1}.
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DR   EMBL; JYDO01000018; KRZ77600.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V1N183; -.
DR   STRING; 268474.A0A0V1N183; -.
DR   Proteomes; UP000054843; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF188; NEITHER INACTIVATION NOR AFTERPOTENTIAL PROTEIN G; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000054843};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..602
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006883036"
FT   DOMAIN          44..340
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          450..590
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
SQ   SEQUENCE   602 AA;  66580 MW;  358070E239FC1696 CRC64;
     MLTTLLTLAS LYSTKLSQYP HEMFPDVTEN LHRRLDEIFA KPFDFVIVGS GYSGSLLARR
     LAAGGCERVL VIEAGGSPHF DSAVPFVNLG NKSNVEWNYL TTAQKKAAQE MINQKVHLHV
     AKALGGRSIL SSGAYVPANP DDFIRWAEST GFTDWSDIDR YMFKLSNIDE TDLAKSPITE
     KQLMNIIFKD SGMQVLDPLK LLWLHAGRAS NHTVAENENE LFEKGGFFIP RTLSFQGTKL
     NPAAVYLGRA KQNLVVVCHT EAIKLTQRTG QSFAISGIQV RDMLSGRLYN VRVRREIILA
     AGAIGTAKLL IQSGVGPMDH LKQLKIPAIK SLPVGVRLYD RVKVSLPVKI SNVAMKALIG
     QIDSKQTLKE YLTTGKGLLA NTSVIGMAFL DTDKSGSPDV MLELKPAALT GLKRMMEDEN
     FKSEVEKILD PSGELQNTVY LDMVITLLRP MSQGTMWLWR QSENNFVPRM NPSYLTDYRD
     VRKMIKAVKM VENMMQTPIM KQVGAVLLYP NIPKCSAATM PASEYYIECL LRHLATTGDH
     LTSTAALGEV VDDELRVKTI RGVRVVDESV FPSTVTGGIG ATLLALANRA ADMIKEQHDL
     KC
//
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