ID MOCOS_DROGR Reviewed; 770 AA.
AC B4JXP7;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 77.
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=GH17731;
OS Drosophila grimshawi (Hawaiian fruit fly) (Idiomyia grimshawi).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Hawaiian Drosophila.
OX NCBI_TaxID=7222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15287-2541.00;
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; CH916376; EDV95146.1; -; Genomic_DNA.
DR RefSeq; XP_001995494.1; XM_001995458.1.
DR AlphaFoldDB; B4JXP7; -.
DR SMR; B4JXP7; -.
DR STRING; 7222.B4JXP7; -.
DR EnsemblMetazoa; FBtr0153145; FBpp0151637; FBgn0125201.
DR GeneID; 6569472; -.
DR KEGG; dgr:6569472; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; B4JXP7; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR PhylomeDB; B4JXP7; -.
DR Proteomes; UP000001070; 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:0043545; P:molybdopterin cofactor metabolic process; ISS:UniProtKB.
DR GO; GO:0006727; P:ommochrome biosynthetic process; IEA:EnsemblMetazoa.
DR Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 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; MOCOS_middle.
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 PANTHER; PTHR14237:SF19; MOLYBDENUM COFACTOR SULFURASE; 1.
DR PANTHER; PTHR14237; MOLYBDOPTERIN COFACTOR SULFURASE MOSC; 1.
DR Pfam; PF00266; Aminotran_5; 2.
DR Pfam; PF03473; MOSC; 1.
DR Pfam; PF03476; MOSC_N; 1.
DR SUPFAM; SSF141673; MOSC N-terminal domain-like; 1.
DR SUPFAM; SSF50800; PK beta-barrel domain-like; 1.
DR SUPFAM; SSF53383; PLP-dependent transferases; 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..770
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369372"
FT DOMAIN 611..769
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 405
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 243
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 726
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 770 AA; 86441 MW; 87CA02BD0809C1BC CRC64;
MGDYTAEFTP DEQALIDAEF ARLSDSTYLD HAGTTLYAHN QVSDAAQQLQ RDVICNPHTC
RVTGDYVDQV RYKILEFFNT NADEYHVVFT ANASAALRLV ADHFDFGTNG NFHYCQENHT
SVLGMRQLVS ANRIYMLTKD QILLNNGTPA GATAAAATAH SDNSLVVFSA QCNFSGYKMP
LTVIEKIQQD GLREPGKCID CKLQSDPGQS NYYVCLDAAS YAASSPLDLR RHRPDYVCLS
FYKIFGYPTG VGALLVSKRG AELLKKRFYG GGTVNFAYPH TMEHQLRSTF HERFEDGTLP
FLSIVELLQG FQTLQRLVPG RSMERISRHV HSLARYCEQQ LLQMQYPNGA PLVTLYNHAG
YEDRMQQGGI VAFNVRTAAG DYVGFGEIAS VAALHRILLR TGCFCNVGAC QHFMNLNGDA
MDAIYKLAGR ICGDYYDLLD GRPTGAVRVS FGYMTRLQDV DRLLQMLRDS YLSVKWHQRL
DFIEQRVQQL PKLLQQRAQQ LRPQLLQLAI YPVKSCAALK MPASALTDQG LQYDREWMIV
DLNGMALTQK RCTDLCLIQP RIVADQLQLH FNGDGSTTFV SVPLSLTDQA TNSARCQSKV
CRQSVEGYDC GDEVANWLCQ QLGLDGLRLL RQSAQRRAPG DRQQLSLVNQ AQFLLVNRAS
VRSLGFEEPL DETVDRFRSN IVIDTGVPFE ELEFGQLRIG EVLFQVEGPC QRCDMICINQ
RTGQRSPDTL TTIARIQSGK MRFGIYISRL PNENRMQPQL ACGDPITVLR
//
