MOCOS_DROER
ID MOCOS_DROER Reviewed; 781 AA.
AC B3NY19;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=GG19684;
OS Drosophila erecta (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7220;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14021-0224.01;
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH954180; EDV47540.1; -; Genomic_DNA.
DR RefSeq; XP_001978613.1; XM_001978577.2.
DR AlphaFoldDB; B3NY19; -.
DR SMR; B3NY19; -.
DR STRING; 7220.FBpp0138230; -.
DR EnsemblMetazoa; FBtr0139738; FBpp0138230; FBgn0111886.
DR GeneID; 6549751; -.
DR KEGG; der:6549751; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B3NY19; -.
DR Proteomes; UP000008711; 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 Transferase.
FT CHAIN 1..781
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369371"
FT DOMAIN 619..781
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 413
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 734
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 781 AA; 87930 MW; 6FC3D6E9CD252766 CRC64;
MTPYRPEFSA AEQSRIDAEF SRLARNKTVY LDHAGTTLYA ENQVTAAAEQ LQRNVICNPH
TCRLTGDFVD QVRFKILEFF NTTAEDYHVI FTANATAALS LVAENFDFGS SGDFHFCQEN
HTSVLGMRER VRANGIYMLR EKEISGGGAK ENGTVHQVSG KTGNSLVTFS AQCNFSGYKI
PLDSIEKIQN YGLSKPGKQL WSALGDKKEH THNDYYICLD AASFVATSPL DLRKYRPDYV
CLSFYKIFGY PTGVGALLVS RRGAEVFQKR RFFGGGTINY AFPHAMDYQL RETFHQRYED
GTLPFLSIVG LLEGFRTLER LVPKTDEFST MERISRHVFG LAKYVEDQLR QLQHPNGEPL
VELYNKVGYQ DKARQGGIVA FNVRTESGSF VGFGEIACVA ALHGILLRTG CFCNIGACQY
YLGLDEDALD SIYKRAGRIC GDYFDLVDGQ PTGAVRVSFG YMTTIQDVEQ LLQMLRSSYL
ATKPLQRIQF IEEQAEQLPP LLKERVQLLR PKLLQMAIYP VKSCAAFKIE SPGSWPLTDQ
GLKYDREWMI VDMNGMALTQ KRCTELCLIR PVIKVDQLEL QFGDNSHFSV PLSLEDQAAD
SAKCVSKVCR QPVEGLDCGD AVAQWLSENL GLEGLRLLRQ SGQRNSSKDQ QKLSLVNQAQ
FLLLNRSSVR SLQFEEPLDE TVDRFRANII IDTGSAFEEL TYKALSIGGI QFQVEGPCQR
CDMICINQRT GERSPETLTT ISRLQKGRMR FGIYITRIPP DTKDLEPKEQ HMTCGDVVIV
E
