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Database: UniProt
Entry: Q7Q7G4_ANOGA
LinkDB: Q7Q7G4_ANOGA
Original site: Q7Q7G4_ANOGA 
ID   Q7Q7G4_ANOGA            Unreviewed;       334 AA.
AC   Q7Q7G4;
DT   15-DEC-2003, integrated into UniProtKB/TrEMBL.
DT   07-DEC-2004, sequence version 2.
DT   27-MAR-2024, entry version 134.
DE   SubName: Full=AGAP005323-PA {ECO:0000313|EMBL:EDO63640.1};
DE   SubName: Full=AGAP005323-PB {ECO:0000313|EMBL:EAA11815.2};
GN   Name=1276030 {ECO:0000313|EnsemblMetazoa:AGAP005323-PA};
GN   ORFNames=AgaP_AGAP005323 {ECO:0000313|EMBL:EAA11815.2};
OS   Anopheles gambiae (African malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=7165 {ECO:0000313|EMBL:EAA11815.2};
RN   [1] {ECO:0000313|EMBL:EAA11815.2, ECO:0000313|Proteomes:UP000007062}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA11815.2,
RC   ECO:0000313|Proteomes:UP000007062};
RX   PubMed=12364791; DOI=10.1126/science.1076181;
RA   Holt R.A., Subramanian G.M., Halpern A., Sutton G.G., Charlab R.,
RA   Nusskern D.R., Wincker P., Clark A.G., Ribeiro J.M.C., Wides R.,
RA   Salzberg S.L., Loftus B.J., Yandell M.D., Majoros W.H., Rusch D.B., Lai Z.,
RA   Kraft C.L., Abril J.F., Anthouard V., Arensburger P., Atkinson P.W.,
RA   Baden H., de Berardinis V., Baldwin D., Benes V., Biedler J., Blass C.,
RA   Bolanos R., Boscus D., Barnstead M., Cai S., Center A., Chaturverdi K.,
RA   Christophides G.K., Chrystal M.A.M., Clamp M., Cravchik A., Curwen V.,
RA   Dana A., Delcher A., Dew I., Evans C.A., Flanigan M.,
RA   Grundschober-Freimoser A., Friedli L., Gu Z., Guan P., Guigo R.,
RA   Hillenmeyer M.E., Hladun S.L., Hogan J.R., Hong Y.S., Hoover J.,
RA   Jaillon O., Ke Z., Kodira C.D., Kokoza E., Koutsos A., Letunic I.,
RA   Levitsky A.A., Liang Y., Lin J.-J., Lobo N.F., Lopez J.R., Malek J.A.,
RA   McIntosh T.C., Meister S., Miller J.R., Mobarry C., Mongin E., Murphy S.D.,
RA   O'Brochta D.A., Pfannkoch C., Qi R., Regier M.A., Remington K., Shao H.,
RA   Sharakhova M.V., Sitter C.D., Shetty J., Smith T.J., Strong R., Sun J.,
RA   Thomasova D., Ton L.Q., Topalis P., Tu Z.J., Unger M.F., Walenz B.,
RA   Wang A.H., Wang J., Wang M., Wang X., Woodford K.J., Wortman J.R., Wu M.,
RA   Yao A., Zdobnov E.M., Zhang H., Zhao Q., Zhao S., Zhu S.C., Zhimulev I.,
RA   Coluzzi M., della Torre A., Roth C.W., Louis C., Kalush F., Mural R.J.,
RA   Myers E.W., Adams M.D., Smith H.O., Broder S., Gardner M.J., Fraser C.M.,
RA   Birney E., Bork P., Brey P.T., Venter J.C., Weissenbach J., Kafatos F.C.,
RA   Collins F.H., Hoffman S.L.;
RT   "The genome sequence of the malaria mosquito Anopheles gambiae.";
RL   Science 298:129-149(2002).
RN   [2] {ECO:0000313|EMBL:EAA11815.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA11815.2};
RG   The Anopheles Genome Sequencing Consortium;
RL   Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:EAA11815.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA11815.2};
RX   PubMed=14747013; DOI=10.1016/j.pt.2003.11.003;
RA   Mongin E., Louis C., Holt R.A., Birney E., Collins F.H.;
RT   "The Anopheles gambiae genome: an update.";
RL   Trends Parasitol. 20:49-52(2004).
RN   [4] {ECO:0000313|EMBL:EAA11815.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA11815.2};
RX   PubMed=17210077; DOI=10.1186/gb-2007-8-1-r5;
RA   Sharakhova M.V., Hammond M.P., Lobo N.F., Krzywinski J., Unger M.F.,
RA   Hillenmeyer M.E., Bruggner R.V., Birney E., Collins F.H.;
RT   "Update of the Anopheles gambiae PEST genome assembly.";
RL   Genome Biol. 8:R5.1-R5.13(2007).
RN   [5] {ECO:0000313|EMBL:EAA11815.2}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PEST {ECO:0000313|EMBL:EAA11815.2};
RG   VectorBase;
RL   Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000313|EnsemblMetazoa:AGAP005323-PA}
RP   IDENTIFICATION.
RC   STRAIN=PEST {ECO:0000313|EnsemblMetazoa:AGAP005323-PA};
RG   EnsemblMetazoa;
RL   Submitted (JAN-2021) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000189-1};
CC   -!- SIMILARITY: Belongs to the DAMOX/DASOX family.
CC       {ECO:0000256|ARBA:ARBA00006730}.
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DR   EMBL; AAAB01008960; EAA11815.2; -; Genomic_DNA.
DR   EMBL; AAAB01008960; EDO63640.1; -; Genomic_DNA.
DR   RefSeq; XP_001688634.1; XM_001688582.1.
DR   RefSeq; XP_315337.2; XM_315337.4.
DR   AlphaFoldDB; Q7Q7G4; -.
DR   STRING; 7165.Q7Q7G4; -.
DR   PaxDb; 7165-AGAP005323-PA; -.
DR   EnsemblMetazoa; AGAP005323-RA; AGAP005323-PA; AGAP005323.
DR   EnsemblMetazoa; AGAP005323-RB; AGAP005323-PB; AGAP005323.
DR   GeneID; 1276030; -.
DR   KEGG; aga:AgaP_AGAP005323; -.
DR   VEuPathDB; VectorBase:AGAP005323; -.
DR   eggNOG; KOG3923; Eukaryota.
DR   HOGENOM; CLU_034311_0_2_1; -.
DR   InParanoid; Q7Q7G4; -.
DR   OMA; CHGGWKY; -.
DR   OrthoDB; 5359at2759; -.
DR   Proteomes; UP000007062; Chromosome 2L.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0003884; F:D-amino-acid oxidase activity; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IBA:GO_Central.
DR   Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR006181; D-amino_acid_oxidase_CS.
DR   InterPro; IPR023209; DAO.
DR   InterPro; IPR006076; FAD-dep_OxRdtase.
DR   PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR   PANTHER; PTHR11530:SF17; RE49860P; 1.
DR   Pfam; PF01266; DAO; 1.
DR   PIRSF; PIRSF000189; D-aa_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51971; Nucleotide-binding domain; 1.
DR   PROSITE; PS00677; DAO; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000189-1};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000189-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007062}.
FT   DOMAIN          3..322
FT                   /note="FAD dependent oxidoreductase"
FT                   /evidence="ECO:0000259|Pfam:PF01266"
FT   BINDING         33..34
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         45..47
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         183
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         222
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         306..311
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
FT   BINDING         307
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000189-1"
SQ   SEQUENCE   334 AA;  37021 MW;  929733DFFDEEAF91 CRC64;
     MNICVVGAGV VGLTTALELQ REMRNANVTI LSDRFEQDTC SDVAAGLFRP GTSFSGPTEE
     ITRKWISDAY SHWDELRRTE HSARAGVCQM SGYIFSSRDP AIVRNHYIEK VLPVYRAATE
     QELTICPGEW KYGSFFTTIL AECRLFQPWA TERFLDNGGR IVTVALNNLQ ELRGKYDVVV
     NCTGLGAKRL CNDHKLVPIR GQVIKVRASW VKTAFYADFD TYVIPGFEGV TLGGCRNFDS
     YNTDVSRHDS AAIRERCESL LPSLKGAPVL RESVGLRPHR DPVRVELELL PTANGSVRVV
     HNYGHGGYGV TTAPGTAKHA VKLVKEALQT NSKL
//
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