MOCOS_DROPE
ID MOCOS_DROPE Reviewed; 796 AA.
AC B4H0S8;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=GL15793;
OS Drosophila persimilis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7234;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSH-3 / Tucson 14011-0111.49;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(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; CH479201; EDW29993.1; -; Genomic_DNA.
DR RefSeq; XP_002024552.1; XM_002024516.1.
DR AlphaFoldDB; B4H0S8; -.
DR SMR; B4H0S8; -.
DR STRING; 7234.FBpp0179900; -.
DR EnsemblMetazoa; FBtr0181408; FBpp0179900; FBgn0153397.
DR GeneID; 6599378; -.
DR KEGG; dpe:6599378; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR OMA; WCLVHQG; -.
DR PhylomeDB; B4H0S8; -.
DR Proteomes; UP000008744; 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:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:EnsemblMetazoa.
DR GO; GO:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IEA:EnsemblMetazoa.
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..796
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369374"
FT DOMAIN 650..796
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 418
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 752
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 796 AA; 88779 MW; 820E8344A29E994E CRC64;
MSSYQSEYNA DEQAAIDKEF TRLANNKSIY LDHAGTTLYA ESQVTAAAEQ LQRDVICNPH
TCRVTGDYVD QVRFKLLEFF NTKEDEYHVI FTANATAALS LVAENFDFGR QGNFHYCQEN
HTSVLGMRER VQARAMYMLK EEEITGMASV PSAANGVSGS SPGDNSLVTF SAQCNFSGYK
IPLAAIAGIQ KQGLPHGLGK KISGEAPQTT DNNNYYVCLD AASFVATNPL DLQRYRPDYV
CISFYKIFGY PTGVGALLVS RRGAEAFRKK RNFFGGGTIN YAYPHAMDHQ LREVFHQRYE
DGTLPFLSIV GLLEGFRTLE RLVPRRSVNG GDVATMERIS RHVHGLAQHL EKQLRQLKYP
NGQPLIELYN RVGYEERHRQ GGIVAFNVRT DAGPFVGFGE IACVAALQGI LLRTGCFCNI
GACQRYLGLD ETMMDAIYKR AGRICGDYYD LIDGQPTGAV RVSFGYMTRR QDVDELLKML
HLSYLATKPQ QRLQLIEEQA GELPKALKER AQRLRPQLLQ LAIYPVKSCA AFKIEEGGGS
GGGGSGGTWP LTAQGLQYDR EWMIVDMNGM AVTQKRCSEL CLIRPLIRDD QLVLHFGDSP
DGVSLPLSLA DQAENSSRCR SKVCRQPVEG LDCGDEVALW LSQHLGLEGL RLLRQSSQRS
TTNGVRQQQK LSLVNQAQFL LVNRSSVRSL QFEESLDETV DRFRANIIID TGSAFEELSY
KQLTIGQVQF QVEGPCQRCD MICINQRTGE RSPETLTTIS RLQSGKMRFG IYISRISTEN
NKESQHLTCG DVVVVT
