MOCOS_DROWI
ID MOCOS_DROWI Reviewed; 789 AA.
AC B4N1V2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 70.
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=GK16373;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
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; CH963925; EDW78341.1; -; Genomic_DNA.
DR RefSeq; XP_002067355.1; XM_002067319.2.
DR AlphaFoldDB; B4N1V2; -.
DR SMR; B4N1V2; -.
DR STRING; 7260.FBpp0245516; -.
DR PRIDE; B4N1V2; -.
DR EnsemblMetazoa; FBtr0247024; FBpp0245516; FBgn0218375.
DR GeneID; 6644650; -.
DR KEGG; dwi:6644650; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; B4N1V2; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B4N1V2; -.
DR Proteomes; UP000007798; 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 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..789
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369376"
FT DOMAIN 628..789
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 422
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 251
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 741
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 789 AA; 89446 MW; 27A20E860C03E5A8 CRC64;
MSKLDMDTPE FSANEQELID KEFTRLERNQ STYLDHAGTT LYAESQVAHA AVQLHHDVIS
NPHTSRSTGD YVDQVRFKIL EFFHTQAEDY QVIFTANASA ALRLVAEHFD FGDKGNFHYC
QENHTSVLGM RQMIQANGTY MLRREELSEL REGHRVRRVM ANGSSSTGNS LVVFSAQCNF
SGYKMPLETI QLIQDDGLPH FGKLIAGQED KETNGTAYNY YVCLDAASYA ATNPLDLQKY
KPDFVCLSFY KIFGYPTGVG ALLVSRRGAE LLSRPRQFYG GGTINYAYAH AMDYKLRNTS
LHERFEDGTL PFLSIVELLE GFRSLERLIP TNSNTGISTM DRVSRHVFTL ARYLENQLKQ
LKYANGQPLI QFYNHQGYEQ RSRQGGIVAF NVRTESGGYV GFAEIACVAS LHGILLRTGC
FCNVGACQRY LQLDDQMMDV IYKRSGRICG DYNDLIDGQP TGAVRVSFGY MTRTSDVRKL
VEMLEKSYLS SRSPERWRFI EKQASQLPKA LQQRAQSLRP RLLELAIFPV KSCAALKAKK
WPLTAQGLKY DREWMIVDRN GLALTQKRCT DLCLIQPSID KDNLILMFNG DTNSSISLPL
FLSDDDLQAA ARCRSKICRQ PIEGSDCGDQ VAQWLDQNLG LDGLRLLRQS TQRSSSSHQL
SLVNQAQFLL VNRSSVRSLQ FEEPLDETVD RFRANLIIDT GAPFDELDYT SLSIGRIHFK
VEGPCQRCDM ICINQRTGER SPETLTTISR LQKGKMRFGI YITRLTDKED NAELNEEYHL
ICGETLEVD
