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Database: UniProt
Entry: A0A182YKY1_ANOST
LinkDB: A0A182YKY1_ANOST
Original site: A0A182YKY1_ANOST 
ID   A0A182YKY1_ANOST        Unreviewed;      2709 AA.
AC   A0A182YKY1;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Xanthine dehydrogenase {ECO:0008006|Google:ProtNLM};
OS   Anopheles stephensi (Indo-Pakistan malaria mosquito).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=30069 {ECO:0000313|EnsemblMetazoa:ASTEI09117-PA, ECO:0000313|Proteomes:UP000076408};
RN   [1] {ECO:0000313|Proteomes:UP000076408}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Indian {ECO:0000313|Proteomes:UP000076408};
RX   PubMed=25244985; DOI=10.1186/preaccept-1262842421127991;
RA   Jiang X., Peery A., Hall A.B., Sharma A., Chen X.G., Waterhouse R.M.,
RA   Komissarov A., Riehle M.M., Shouche Y., Sharakhova M.V., Lawson D.,
RA   Pakpour N., Arensburger P., Davidson V.L., Eiglmeier K., Emrich S.,
RA   George P., Kennedy R.C., Mane S.P., Maslen G., Oringanje C., Qi Y.,
RA   Settlage R., Tojo M., Tubio J.M., Unger M.F., Wang B., Vernick K.D.,
RA   Ribeiro J.M., James A.A., Michel K., Riehle M.A., Luckhart S.,
RA   Sharakhov I.V., Tu Z.;
RT   "Genome analysis of a major urban malaria vector mosquito, Anopheles
RT   stephensi.";
RL   Genome Biol. 15:459-459(2014).
RN   [2] {ECO:0000313|EnsemblMetazoa:ASTEI09117-PA}
RP   IDENTIFICATION.
RC   STRAIN=Indian {ECO:0000313|EnsemblMetazoa:ASTEI09117-PA};
RG   EnsemblMetazoa;
RL   Submitted (MAY-2020) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974};
CC   -!- COFACTOR:
CC       Name=Mo-molybdopterin; Xref=ChEBI:CHEBI:71302;
CC         Evidence={ECO:0000256|ARBA:ARBA00001924};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SUBCELLULAR LOCATION: Peroxisome {ECO:0000256|ARBA:ARBA00004275}.
CC   -!- SIMILARITY: Belongs to the xanthine dehydrogenase family.
CC       {ECO:0000256|ARBA:ARBA00006849}.
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DR   STRING; 30069.A0A182YKY1; -.
DR   EnsemblMetazoa; ASTEI09117-RA; ASTEI09117-PA; ASTEI09117.
DR   VEuPathDB; VectorBase:ASTE011456; -.
DR   VEuPathDB; VectorBase:ASTEI09117; -.
DR   VEuPathDB; VectorBase:ASTEI20_035495; -.
DR   VEuPathDB; VectorBase:ASTEI20_038906; -.
DR   VEuPathDB; VectorBase:ASTEI20_045971; -.
DR   OMA; LETNMEW; -.
DR   Proteomes; UP000076408; Unassembled WGS sequence.
DR   GO; GO:0005777; C:peroxisome; IEA:UniProtKB-SubCell.
DR   GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   CDD; cd00207; fer2; 2.
DR   Gene3D; 3.10.20.30; -; 3.
DR   Gene3D; 3.30.465.10; -; 2.
DR   Gene3D; 1.10.150.120; [2Fe-2S]-binding domain; 2.
DR   Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 2.
DR   Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 9.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 2.
DR   InterPro; IPR002888; 2Fe-2S-bd.
DR   InterPro; IPR036884; 2Fe-2S-bd_dom_sf.
DR   InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR   InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR   InterPro; IPR006058; 2Fe2S_fd_BS.
DR   InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR   InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR   InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR   InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR   InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR   InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR   InterPro; IPR012675; Beta-grasp_dom_sf.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR11908:SF132; ALDEHYDE OXIDASE 1-RELATED; 1.
DR   PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR   Pfam; PF01315; Ald_Xan_dh_C; 2.
DR   Pfam; PF03450; CO_deh_flav_C; 2.
DR   Pfam; PF00941; FAD_binding_5; 2.
DR   Pfam; PF00111; Fer2; 2.
DR   Pfam; PF01799; Fer2_2; 2.
DR   Pfam; PF02738; MoCoBD_1; 2.
DR   Pfam; PF20256; MoCoBD_2; 2.
DR   SMART; SM01008; Ald_Xan_dh_C; 2.
DR   SMART; SM01092; CO_deh_flav_C; 2.
DR   SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 3.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 2.
DR   SUPFAM; SSF47741; CO dehydrogenase ISP C-domain like; 2.
DR   SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 2.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 2.
DR   SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 2.
DR   PROSITE; PS00197; 2FE2S_FER_1; 3.
DR   PROSITE; PS51085; 2FE2S_FER_2; 3.
DR   PROSITE; PS51387; FAD_PCMH; 2.
PE   3: Inferred from homology;
KW   2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Iron {ECO:0000256|ARBA:ARBA00022714};
KW   Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022714};
KW   Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxisome {ECO:0000256|ARBA:ARBA00023140};
KW   Reference proteome {ECO:0000313|Proteomes:UP000076408}.
SQ   SEQUENCE   2709 AA;  297377 MW;  BB7EFFF419E46004 CRC64;
     MLSTLGSYIW GSTEADSPLA EVTFTINGKP YTVDPRTIPV DTSLNTFIRN HAHLTGTKFM
     CLEGGCGACI VNVSGVHPVT KEKKSWAVNS CLYPIYACHG LDVKTVEGIG NRKDGYHPIQ
     QRLAHLNGTQ CGYCSPGMVM NMYSLMEANR GAISMEDVEN AFGGNICRCT GYRPILDAFK
     SLTVDADEKL LDACQDIEDL TKRTCPKTGS PCAGKCVSAK DRIDPKRPVR MVFEDAREWH
     RVTQMSDIFA IFEQIGNKPY MLVAGNTAHG VYRRSPSLQV FIDINAVEEL HTHSSDANEL
     VVGANVSLTE FMHILDETAN KSPNFSHFKH LEKHIDLIAN VPVRSAGTIA GNLNIKNQHH
     EFPSDMYLIL ETAGAKLTVV ETGGKTSVIT PADFVRLDMQ KKVLKSITLP ALDISRYQFR
     SFKVMPRSQN AHAYVNGAFL VKFAEGGVTV ESAKICFGGI NPDFTHATAT EAFLVGKNMF
     DAETIQATMN QLSNEIRPDW VLPDASGEYR KNLAMALYYK YLLNVAPEGT VLVKPSFRSG
     GTVLERPLSS GQQTFDTYER NWPLTKNIPK IEALAQTSGE AKFTNDLPPQ PGELYAAFVI
     ATKPHTRIGT IDATDALKYP GVVAFYAAKD IPGTNNFMPP SLGNQEPEEV FCSGEVLYHG
     QPVGVILAET LNQANHAAGL VNILYERVSQ QQPVYPTLKS LVDNQAKARI FDEPSTTTRR
     GSNYRVKVSA ARKVTGRFEM AGQYHYTMET QSCVCVPIED GMDVHCSTQW VDLCQVAIAS
     MLKVPENSLN FSVRRLGGGY GSKISRAAQV ACACALAAHL QNRPVRFVLT IESNMSSIGK
     RYGCISDYEV DVETSGRIVK LTNNYMQDYG ASLNESVGEA TTEFFNNCYD TKTWKVVGKA
     AKTDAPSNTW CRAPGTTEGI AMIENIMEHV AWELGLDPLE LRLMNMPEGS KMRELLPQFR
     KDVEYNQRKA DIDTFNVNNR WRKRGIAVSL MRYPLGYFGA LHALVAIHAG DGTVSVTHGG
     IEMGQGMNTK AAQVAAYVLG LPLEKISIKP MTSLTSPNAI VTGGSMTSEA VCYAVKKACE
     ILLERIKPVR DAHKDAPWET ITQLCYAGSV DLCATYQYRA SELKPYIIWG LSCAEVEVDV
     LTGNVQLRRV DILEDTGESL SPGIDVGQIE GAFVMGVGYW LTEALVYAAE DGALLTNRTW
     TYKPPGAKDI PVDFRVRFLQ KSSNPAGVLR SKATGEPALN MSIVVLFALR NALRSARKDA
     GLADDWIPMG TASTPDQVHL LAGNSIEHPL SEVTFTINGK TYTASAESVP VDTSLNAFIR
     NHAHLTGTKF MCLEGGCGTC VVNASGLHPV TKENKTWSVN SCLFPVFACH GLDIKTVEAL
     GNRTDGYHPI QERLAHMNGS QCGYCSPGMV MTMYSLMESK QGSVTMEEVE NELGGNICRC
     TGYRPILDAF KSLASVTDKE LPDIEELQIC PKTNTACSAK CPQAANLIVP GCPVQVVASD
     DKEWHKVYTL AEIFAIFGKI DKRPYMLVGG NTAHGVYRRS ESLQVFIDIN SVEELRNYFL
     RTGELVVGAN VTITEFIEIL TKTANNRPNF SYCREIARHL GRIANPAVRN AGTVAGNLSI
     KNKYPQFPSD IYILLEAVGA KVIIADSLTK VLEKSAQDYA QTDMTKRLIK FISLPLINTF
     TTTFKSYRVA PRAQNAHAYV NAAFLVQFAK DKSTIKLATL CFGGINPKFT HASRTEKLLI
     GKKLFDAATI QQAIGSLASE IQPDWVLPDA SVEYRKNLAI ALFYKFLLSV ATDNNVPLNP
     RFKSGSTMLE RPLSSGQQNY DTNKKNWPVT KYVPKLEGLR QASGEAKYAN DFPPFPGELY
     AAFVVATQPN ATIGKIDPTD ALKLPGVAAF FSAKDIPGTN NFMSSAMNFY FPDVEEIFCS
     GRVLFHGQPV GVIVADRFDQ AIRAAKQVKI IYERVSDEPV CPTLKAVLMN QAKERIVDRP
     ASSREGPQID LAVSKQIVGT LELAGQYHFT MEPQTCVCVP IEDGMDIYAA TQWIDLSHVA
     VAAALKVPQN SLNFTVRRVG GGFGCKLTRV SQIVCACALA AHLTKRPVRF IMNIEANMGS
     IGKRYGCVSN YQVDVDAKGK ILKLTNNFMQ DYGSNLNENV IDDAKVVFGL SYNSSAWKVE
     GKAVLTDAPS STWMRAPGTT EAIAMIETIM EHIAWVTGVD PMQVRLSNMP AESKLQKLMP
     QFRQDVEFDK RKKLIDDFNA KNRWRKRGIA MIPMQYPLVH VGALHAQVSI HANDGTVSIS
     HGGIEVGQGI NTKAAQVAAF TLGIPLETIS IKPSNSMTSP NAVMTGASMT SEVVCLAIKR
     ACEILNTRLQ PVRSELKNAS WEKITQTCYI RDIDLSVLYQ YKKSDLKPYS IWGLSCAEME
     VDILTGNVQL TRVDILEDTG ESISPGIDVG QIEGAFITGL GYWLTESLVF DMTNGALLTN
     RTWNYKPPGA KDIPVDFRIR LIQTGDNQGG VLRSKATGEP AMTMTVVLLF ALRYALRSAQ
     KDAGRPDDWI PLGSASTPEQ IFLKASNNFE QFKLHVPVNT SLNAFIRNHT HLSGTKFMCL
     EGGCGACAVN VSGLHPVTKE NKTWSVYSCL FPVFACHGLD IKTVEALGNR TDDIPVDFRI
     RLVQTGENQV GSKATGEPAM SMAVVVVFAL RYAVRSAQKD AERPDDWISL GSAMTPEHIF
     LSAKYFTLF
//
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