MOCOS_DROMO
ID MOCOS_DROMO Reviewed; 779 AA.
AC B4L340;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 72.
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=GI15478;
OS Drosophila mojavensis (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila.
OX NCBI_TaxID=7230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 15081-1352.22;
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; CH933810; EDW06968.1; -; Genomic_DNA.
DR RefSeq; XP_002009651.1; XM_002009615.2.
DR AlphaFoldDB; B4L340; -.
DR SMR; B4L340; -.
DR STRING; 7230.FBpp0164695; -.
DR EnsemblMetazoa; FBtr0166203; FBpp0164695; FBgn0138227.
DR GeneID; 6583991; -.
DR KEGG; dmo:Dmoj_GI15478; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; B4L340; -.
DR OMA; WCLVHQG; -.
DR OrthoDB; 394559at2759; -.
DR PhylomeDB; B4L340; -.
DR Proteomes; UP000009192; 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; 1.
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..779
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000369373"
FT DOMAIN 624..779
FT /note="MOSC"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT ACT_SITE 409
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 247
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03050"
FT MOD_RES 732
FT /note="Phosphoserine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 779 AA; 87551 MW; 047B27B1AA2FB33A CRC64;
MVEYTAEFTA EEQALIDKEF ARLGESTYLD HAGTTLYAES QVLSAAQQLQ RDVICNPHTC
RATGDYVDQV RYRILEFFNT NADDYHVVFT ANATAALRLV ADHFDFAGDG NFHYCQENHT
SVLGMRQLVK AKGIYMLTKD DIELNVLDQP STPAPAAAAT AQANSLVTFS AQCNFSGYKM
PLTVIEQIQK RGLQQLGKCI WSAESQPAAK NVDSNYYVCL DAAAFAASSP LDLQRFRPDF
VCVSFYKIFG YPTGVGGLLV SRRGAEVLRK RFYGGGTINY AYPHTMEHQL RNVFHERFED
GTLPFLSIVE LLQGFRTLER LVPGRSIERI SRHVHGLARY CEHQLKQLKH PNGAPLITLY
NHAGYEDRAK QGGTVAFNVR TNTGDYVGFG EVACMAALHR ILLRTGCFCN VGACQHFLQL
NDETMDAIYK RAGRICGDYF DLLDGQPTGA VRVSFGYMTR IQDVDRFLQM LRNSYLVIAK
PQQRFSFIEQ QAELLPKALQ QRAQRLRPRL LQLAIYPVKS CAAFKIDSST GSWPLTKQGL
QYDREWMIVD MNGMALTQKR CTDLCLIQPR IVGDQLELHY AETSCSMPLS LSVQAANSAR
CHSKVCRQAI EGYDCGDEVA TWLSQSLGLE GVRLLRQSAQ RSAPGTQQQQ LSLVNQAQFL
LVNRASVRSL QFEESLDETV DRFRANIIID TGTPFEELTY TQLRIGDILF QVDGPCQRCD
MICINQRTGE RSPETLTTIA RMQSGKMRFG IYISRLPSET DDRLEQQQQL TCGDVIVVS
