ID   MOCOS_ANOGA             Reviewed;         770 AA.
AC   Q7QFL7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-APR-2009, sequence version 5.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=Molybdenum cofactor sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MCS {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MOS {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MoCo sulfurase {ECO:0000255|HAMAP-Rule:MF_03050};
DE            EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE   AltName: Full=Molybdenum cofactor sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_03050};
DE   AltName: Full=Protein maroon-like {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=Ma-l {ECO:0000255|HAMAP-Rule:MF_03050};
GN   Name=mal {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=AGAP000555;
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;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PEST;
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).
CC   -!- FUNCTION: Sulfurates the molybdenum cofactor. Sulfation of molybdenum
CC       is essential for xanthine dehydrogenase (XDH) and aldehyde oxidase
CC       (ADO) enzymes in which molybdenum cofactor is liganded by 1 oxygen and
CC       1 sulfur atom in active form. {ECO:0000255|HAMAP-Rule:MF_03050}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + L-cysteine + Mo-molybdopterin = A + H2O + L-alanine +
CC         thio-Mo-molybdopterin; Xref=Rhea:RHEA:42636, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:57972, ChEBI:CHEBI:71302, ChEBI:CHEBI:82685; EC=2.8.1.9;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03050};
CC   -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent
CC       aminotransferase family. MOCOS subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_03050}.
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DR   EMBL; AAAB01008846; EAA06295.5; -; Genomic_DNA.
DR   RefSeq; XP_310528.5; XM_310528.5.
DR   AlphaFoldDB; Q7QFL7; -.
DR   SMR; Q7QFL7; -.
DR   STRING; 7165.AGAP000555-PA; -.
DR   PaxDb; Q7QFL7; -.
DR   GeneID; 1271669; -.
DR   KEGG; aga:AgaP_AGAP000555; -.
DR   CTD; 1271669; -.
DR   VEuPathDB; VectorBase:AGAP000555; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   HOGENOM; CLU_010913_0_1_1; -.
DR   InParanoid; Q7QFL7; -.
DR   OMA; WCLVHQG; -.
DR   OrthoDB; 394559at2759; -.
DR   PhylomeDB; Q7QFL7; -.
DR   Proteomes; UP000007062; Chromosome X.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; ISS:UniProtKB.
DR   GO; GO:0102867; F:molybdenum cofactor sulfurtransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030151; F:molybdenum ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0044248; P:cellular catabolic process; IEA:UniProt.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
DR   GO; GO:1901575; P:organic substance catabolic process; IEA:UniProt.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_03050; MOCOS; 1.
DR   InterPro; IPR000192; Aminotrans_V_dom.
DR   InterPro; IPR005302; MoCF_Sase_C.
DR   InterPro; IPR028886; MoCo_sulfurase.
DR   InterPro; IPR005303; MOSC_N.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR011037; Pyrv_Knase-like_insert_dom_sf.
DR   Pfam; PF00266; Aminotran_5; 1.
DR   Pfam; PF03473; MOSC; 1.
DR   Pfam; PF03476; MOSC_N; 1.
DR   SUPFAM; SSF50800; SSF50800; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   PROSITE; PS51340; MOSC; 1.
PE   3: Inferred from homology;
KW   Molybdenum cofactor biosynthesis; Pyridoxal phosphate; Reference proteome;
KW   Transferase.
FT   CHAIN           1..770
FT                   /note="Molybdenum cofactor sulfurase"
FT                   /id="PRO_0000369367"
FT   DOMAIN          601..770
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         231
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   770 AA;  85736 MW;  D05535FC32B58A06 CRC64;
     MDFVEEFTDE ERLKIEQDFS RLADKCYLDH AGTALYGESQ LRAVQELLAG GLYCNPHTSR
     TMEDLIDLVR YRVLRWFQTR PADYSLVFTS GTTASLKLVA ESFEFGPGDA EPGSFVYLRD
     SHTSVLGMRE LVRTGRVQPI ERAELLQALN EPEDPRRQHP HRPSLLVFPA QCNFNGAKYP
     LELCELIERN GLRGYGGDAF HVCLDAASHV STSPLDLSRY RPSFVCLSFY KIFGYPTGLG
     ALLVRRDAEP LLRGKRYYGG GTVKIALSGP DRFHERRDAL PDRLEDGTIN FLSIAALLPC
     LETLTRLIPG PTMDRIQRHT FQLARHCYRE LQALQHANGG RVVDLYHDTA FGDARTQGAI
     VNFNVLNDDG GHVGFAEVAC MAANHGIYLR TGCFCNPGAC QRHLRLADDD LLRHYRAGHV
     CGDANDLIDG QPTGSVRVSF GYCTRRSDVD RLVAMVRRCY VRRSLTGPLS RADVLAQYKS
     YDRPRLVQLC LYPVKSCGPL RVTTGGWPLA PTGLLYDRAF LIVDEHGAAM TQKKLPTMCR
     IRPDIADGRL VLRHADLEDE PLTIGLEGGG EAGEPAAAHL CQTKVCRDSV QGVDCGERAA
     DWVSRALGVS GLRLLRQSGQ EPRRQRQTDR ALSLNNQAQL LLINRTSVRW LRDKVGDGDW
     DGADAPSLDA LVDRFRGNLI VETVRPLEES DWRQVLIGPS QFTVDGPCTR CQMICIDQAT
     GERTAEPLRT ISREFGGRMR FGVYLSLAGD WADRELPLGA TVSGVIEESE