ID   MOCO3_AEDAE             Reviewed;         764 AA.
AC   Q16P90;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Molybdenum cofactor sulfurase 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MCS 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MOS 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=MoCo sulfurase 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE            EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE   AltName: Full=Molybdenum cofactor sulfurtransferase 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE   AltName: Full=Protein maroon-like 3 {ECO:0000255|HAMAP-Rule:MF_03050};
DE            Short=Ma-l 3 {ECO:0000255|HAMAP-Rule:MF_03050};
GN   Name=mal3 {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=AAEL011729;
OS   Aedes aegypti (Yellowfever mosquito) (Culex aegypti).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Culicinae; Aedini; Aedes; Stegomyia.
OX   NCBI_TaxID=7159;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LVPib12;
RX   PubMed=17510324; DOI=10.1126/science.1138878;
RA   Nene V., Wortman J.R., Lawson D., Haas B.J., Kodira C.D., Tu Z.J.,
RA   Loftus B.J., Xi Z., Megy K., Grabherr M., Ren Q., Zdobnov E.M., Lobo N.F.,
RA   Campbell K.S., Brown S.E., Bonaldo M.F., Zhu J., Sinkins S.P.,
RA   Hogenkamp D.G., Amedeo P., Arensburger P., Atkinson P.W., Bidwell S.L.,
RA   Biedler J., Birney E., Bruggner R.V., Costas J., Coy M.R., Crabtree J.,
RA   Crawford M., DeBruyn B., DeCaprio D., Eiglmeier K., Eisenstadt E.,
RA   El-Dorry H., Gelbart W.M., Gomes S.L., Hammond M., Hannick L.I.,
RA   Hogan J.R., Holmes M.H., Jaffe D., Johnston S.J., Kennedy R.C., Koo H.,
RA   Kravitz S., Kriventseva E.V., Kulp D., Labutti K., Lee E., Li S.,
RA   Lovin D.D., Mao C., Mauceli E., Menck C.F., Miller J.R., Montgomery P.,
RA   Mori A., Nascimento A.L., Naveira H.F., Nusbaum C., O'Leary S.B., Orvis J.,
RA   Pertea M., Quesneville H., Reidenbach K.R., Rogers Y.-H.C., Roth C.W.,
RA   Schneider J.R., Schatz M., Shumway M., Stanke M., Stinson E.O.,
RA   Tubio J.M.C., Vanzee J.P., Verjovski-Almeida S., Werner D., White O.R.,
RA   Wyder S., Zeng Q., Zhao Q., Zhao Y., Hill C.A., Raikhel A.S., Soares M.B.,
RA   Knudson D.L., Lee N.H., Galagan J., Salzberg S.L., Paulsen I.T.,
RA   Dimopoulos G., Collins F.H., Bruce B., Fraser-Liggett C.M., Severson D.W.;
RT   "Genome sequence of Aedes aegypti, a major arbovirus vector.";
RL   Science 316:1718-1723(2007).
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; CH477791; EAT36178.1; -; Genomic_DNA.
DR   RefSeq; XP_001661859.1; XM_001661809.1.
DR   AlphaFoldDB; Q16P90; -.
DR   SMR; Q16P90; -.
DR   STRING; 7159.AAEL011729-PA; -.
DR   PRIDE; Q16P90; -.
DR   VEuPathDB; VectorBase:AAEL022615; -.
DR   eggNOG; KOG2142; Eukaryota.
DR   HOGENOM; CLU_010913_0_1_1; -.
DR   InParanoid; Q16P90; -.
DR   OMA; WCLVHQG; -.
DR   PhylomeDB; Q16P90; -.
DR   Proteomes; UP000008820; Unassembled WGS sequence.
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..764
FT                   /note="Molybdenum cofactor sulfurase 3"
FT                   /id="PRO_0000369366"
FT   DOMAIN          607..762
FT                   /note="MOSC"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   ACT_SITE        394
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT   MOD_RES         228
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ   SEQUENCE   764 AA;  86653 MW;  D84B2E8B93E152E9 CRC64;
     MEAMMNFTSQ YTVEEALAIE KEFSRLKEKC YLDHAGTTLY ADSQIRSVCE GLAQNLYCNP
     HTSRTTEDLL DQVRYRVLRH FNTRSSEYSL IFTSGTTASL KLLAESYEFA PEGAFVYLKD
     SHTSVLGMRE IVGTERIYPV EREQLLKELD SSERSDSEHS SLIVFPAQCN FNGVKYPLEL
     VRKIQRNGIS GYGKERFRVC LDAASFVSTS FLDLSKYQPD FVCLSFYKIF GYPTGLGALL
     VHHTAADQLR KKYYGGGTVK IAMAGRNFHV KRDPLVERFE DGTLAFTSII ALLQGFETLE
     RLVPSTAGLR TIERISQQTF HLGRYCYNRL KALRHSNGNA VVKLYHDTGF EDQGLQGGIV
     NFNILHEDGT YVGFAEVSYM ASLHNILLRT GCFCNPGACQ RHLQLSDEDV LKQFDAGHVC
     GDANDLIDGQ PTGSVRVSFG YMTRKEDIDC LLEMVEKCYI RKTIANGFTR TQIVSKYKSY
     DQPRLKMICL FPIKSCGAFK VTTRWPLSRR GLKHDREFVI VDENGVALTQ KKLTEMCLIR
     PQINLKTNEM TLSHPSMDDF VLDLDLLGES QRIKLCQTKV CQDNVQAIDC GDQVAEWISV
     ALQTSGLRLL KQSDEEVRTF QQSKQEIALA NQAQFLLINQ ASVRWLADKV PDWDELHEEP
     TLESLVDRFR GNLIVETPTS MEECDWKRVT IGYLEFAVDG PCSRCQMICI DQGTGVKTTE
     PLRTIGREFK GKMRFGIYLS HVNPLRDGSE QWLYCNSVVE GLSE