MOCOS_DROPS
ID MOCOS_DROPS Reviewed; 792 AA.
AC Q29GM0;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 2.
DT 03-AUG-2022, entry version 88.
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=GA14218;
OS Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=46245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MV2-25 / Tucson 14011-0121.94;
RX PubMed=15632085; DOI=10.1101/gr.3059305;
RA Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA Weinstock G.M., Gibbs R.A.;
RT "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT gene, and cis-element evolution.";
RL Genome Res. 15:1-18(2005).
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; CH379064; EAL32089.2; -; Genomic_DNA.
DR AlphaFoldDB; Q29GM0; -.
DR SMR; Q29GM0; -.
DR STRING; 7237.FBpp0273842; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q29GM0; -.
DR OMA; WCLVHQG; -.
DR Proteomes; UP000001819; Genome assembly.
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:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
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; 2.
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; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..792
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249957"
FT DOMAIN 646..792
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 414
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 246
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 748
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 792 AA; 88401 MW; 22FCEBEB5A356E99 CRC64;
MSSYQSEFNA DEQAAIDKEF TRLANNKSIY LDHAGTTLYA ESQVTAAAEQ LQRDVICNPH
TCRVTGDYVD QVRFKVLEFF NTKEDDYHVI FTANATAALS LVAENFDFGR QGNFHYCQEN
HTSVLGMRER VQARAMYMLK EEEITGMASL PSAANGVDGS SPGDNSLVTF SAQCNFSGYK
IPLAAIAGIQ KQGLAHGLGK RVSGEAPQTT DNNNYYVCLD AASFVATNPL DLQRYRPDYV
CISFYKIFGY PTGVGALLVS RRGAEAFRKK RNFFGGGTIN YAYPHAMDHQ LREVFHQRYE
DGTLPFLSIV GLLEGFRTLG RLVPRRSDVA TMERISRHVH GLAQYLEKQL RQLKYPNGQP
LIELYNRVGY EERHRQGGIV AFNVRTDAGP FVGFGEIACV AALQGILLRT GCFCNIGACQ
RYLGLDETMM DAIYKRAGRI CGDYYDLIDG QPTGAVRVSF GYMTRRQDVD ELLKMLQLSY
LATKPQQRLQ LIEEQAGELP KALKERAQRL RPQLLQLAIY PVKSCAAFKI KEGGGGGGAG
AGRTWPLTAQ GLQYDREWMI VDMNGMAVTQ KRCSELCLIR PLIRDDQLVL HFGDSPAGVS
LPLSLADQAE NSSRCRSKVC RQPVEGLDCG DEVALWLSQH LGLEGLRLLR QSSQRSASNG
VRQQQKLSLV NQAQFLLVNR SSVRSLQFEE SLDETVDRFR ANIIIDTGSA FEELSYKQLT
IGQVQFQVEG PCQRCDMICI NQRTGERSPE TLTTISRLQS GKMRFGIYIS RISTENNKEQ
QHLTCGDVVV VT
