MOCO2_AEDAE
ID MOCO2_AEDAE Reviewed; 762 AA.
AC Q16P87;
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 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MCS 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MOS 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=MoCo sulfurase 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE EC=2.8.1.9 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Molybdenum cofactor sulfurtransferase 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE AltName: Full=Protein maroon-like 2 {ECO:0000255|HAMAP-Rule:MF_03050};
DE Short=Ma-l 2 {ECO:0000255|HAMAP-Rule:MF_03050};
GN Name=mal2 {ECO:0000255|HAMAP-Rule:MF_03050}; ORFNames=AAEL011727;
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; EAT36182.1; -; Genomic_DNA.
DR RefSeq; XP_001661863.1; XM_001661813.1.
DR AlphaFoldDB; Q16P87; -.
DR SMR; Q16P87; -.
DR STRING; 7159.AAEL011727-PA; -.
DR GeneID; 5575262; -.
DR KEGG; aag:5575262; -.
DR VEuPathDB; VectorBase:AAEL011727; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q16P87; -.
DR OMA; NNFNAAK; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; Q16P87; -.
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 Pfam; PF00266; Aminotran_5; 1.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 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..762
FT /note="Molybdenum cofactor sulfurase 2"
FT /id="PRO_0000369365"
FT DOMAIN 590..738
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 400
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 234
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
SQ SEQUENCE 762 AA; 85670 MW; CC35981C69E8D80D CRC64;
MEFEQEYTAE EALNIEKEFT RLKGKHYMDH AGTTLYAESQ IRAVHDMLAQ NLFCNPHSSP
LTGKLLQQVR HRLLRFFNTS PSDYSLVFTS GATASLKLVA ESFRFRPPDE PESSPDEGAF
VYLRDNHTSV LGMRSVVGTE RIDPLEPEEL LRHLKVSARC SGGTKPSLLV FPAQNNFNAA
KYPLDLVEEI QQNGLSGYDD ERFYVCLDAA SYVSTNFLDL GRYRPDFVCM SFYKIFGYPT
GLGALLIRNG SEDVLDKKYY GGGTIKIMLS GQNLHLKHDD LVTRFEDGTQ PFLSIISLLE
GMNTIQRLIP AANGYRPMER ISKHVFSLAK YCYRKLGTLQ HANGKKAILF YSDTRYETRD
RQGGIVTFNV LKDDGSHLGF SEFAKFAGQH QIYVRTGCFC NAGSCQKHLG LTDEDILMFY
EMGKVCGDDT DMIEGRPTGT VRVSFGYMNK KEDVNRLVDM INDCFVSKAV SNVAMVSPIR
NVIKNEGIAL KAIYLYPIRS CGGYRITAAW PLTERGLKYD REFTIVDSNG NPLMRNKHAE
MSTIHPKIDP SLNFLILTHP FMEDLILKIR KLPTEFNDGE SIDLGDAAAA WISKALRMPK
LRLLRTSATD RKPPHKLLMI NWDAMKTLSD DEGVESDATM SWLVDHFRGS LIVEGKAEED
LQGWKEVKIG KKRFKVQANC SRCPMIHVDQ SGEAIPADSL KAIANVFTKK IPLGVHLTAV
DEGFPEGVLE CGSILEPVRQ SDSPKAHIIK DSVSTRYNFL VK
