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
//