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Database: UniProt
Entry: B0XIJ4_CULQU
LinkDB: B0XIJ4_CULQU
Original site: B0XIJ4_CULQU 
ID   B0XIJ4_CULQU            Unreviewed;       578 AA.
AC   B0XIJ4;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=Alcohol dehydrogenase {ECO:0000313|EMBL:EDS29393.1, ECO:0000313|EnsemblMetazoa:CPIJ019194-PA};
GN   Name=6053363 {ECO:0000313|EnsemblMetazoa:CPIJ019194-PA};
GN   ORFNames=CpipJ_CPIJ019194 {ECO:0000313|EMBL:EDS29393.1};
OS   Culex quinquefasciatus (Southern house mosquito) (Culex pungens).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Culicini; Culex; Culex.
OX   NCBI_TaxID=7176;
RN   [1] {ECO:0000313|EMBL:EDS29393.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JHB {ECO:0000313|EMBL:EDS29393.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Atkinson P.W., Hemingway J., Christensen B.M., Higgs S., Kodira C.,
RA   Hannick L., Megy K., O'Leary S., Pearson M., Haas B.J., Mauceli E.,
RA   Wortman J.R., Lee N.H., Guigo R., Stanke M., Alvarado L., Amedeo P.,
RA   Antoine C.H., Arensburger P., Bidwell S.L., Crawford M., Camaro F.,
RA   Devon K., Engels R., Hammond M., Howarth C., Koehrsen M., Lawson D.,
RA   Montgomery P., Nene V., Nusbaum C., Puiu D., Romero-Severson J.,
RA   Severson D.W., Shumway M., Sisk P., Stolte C., Zeng Q., Eisenstadt E.,
RA   Fraser-Liggett C., Strausberg R., Galagan J., Birren B., Collins F.H.;
RT   "Annotation of Culex pipiens quinquefasciatus.";
RL   Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:CPIJ019194-PA}
RP   IDENTIFICATION.
RC   STRAIN=JHB {ECO:0000313|EnsemblMetazoa:CPIJ019194-PA};
RG   EnsemblMetazoa;
RL   Submitted (FEB-2021) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; DS233313; EDS29393.1; -; Genomic_DNA.
DR   RefSeq; XP_001869466.1; XM_001869431.1.
DR   AlphaFoldDB; B0XIJ4; -.
DR   STRING; 7176.B0XIJ4; -.
DR   EnsemblMetazoa; CPIJ019194-RA; CPIJ019194-PA; CPIJ019194.
DR   KEGG; cqu:CpipJ_CPIJ019194; -.
DR   VEuPathDB; VectorBase:CPIJ019194; -.
DR   VEuPathDB; VectorBase:CQUJHB006408; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_7_0_1; -.
DR   InParanoid; B0XIJ4; -.
DR   OMA; EEVWNSY; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000002320; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 2.
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:SF227; GLUCOSE DEHYDROGENASE [FAD, QUINONE]-LIKE PROTEIN; 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; 2.
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|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002320};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        13..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        46..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          270..284
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         125
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         129
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         544
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   578 AA;  65095 MW;  2F23F3401359D934 CRC64;
     MSLLGLISAK FTFIFYLIGT TLLCAFLNGS YRFYEYYYDN PPVKTSYEYI IVGTGTAGSI
     IAAGIPSRDV LVVEAGSMRT SLMDVPLFQP LLQGTQYDWQ YQTEPQRNAC RALEGQRSNW
     PMGKVFGGTH MLNNMIHFDM MGNTDFSGWF ETPELTRKFL DYFHRWGRDP TIPVERLQYG
     TEFGEDFFCE KMEELYSRLF AKPNVTARNG MRRTASHYYW EQRRPGHELL LNAHVLKINV
     ENGKAIGLVL EKSNRTYEIR ASKGIILSAG TVGSPKILLH SGIGPQKHLK AVRIPLVQNL
     PVGENLQDHI TTGMDLLLWP EKLPLRPLDL ISPLNLWNFF NGKNSSLLLP GCEGLGGMLL
     PDLPRGLILG LGFMVMPAGI ASDGGAHLHK LINLREKVYT QYFQRILEQN LQSVSILPVL
     LQPKSRGHIR LRDANPHSPP LIDPNYLQHP EDLDNLVLGI NIVKEYLEEM NSKKAELNPL
     PFPGCRKFTF DTKPYWECYV QSLTLTMYHP VGTCRMGPKR SKKAVVSNRD LAVHGVSGLY
     VVDGSAIPKL PTGNPNSAIA ALAHYFLKVK FNVDLLGR
//
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