ID MOCOS_DROME Reviewed; 781 AA.
AC Q9VRA2; Q9U9P1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 142.
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, ECO:0000269|PubMed:6801056};
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=CG1692;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-758, AND FUNCTION.
RC STRAIN=Canton-S;
RX PubMed=11029694; DOI=10.1046/j.1365-2958.2000.02119.x;
RA Amrani L., Primus J., Glatigny A., Arcangeli L., Scazzocchio C.,
RA Finnerty V.;
RT "Comparison of the sequences of the Aspergillus nidulans hxB and Drosophila
RT melanogaster ma-l genes with nifS from Azotobacter vinelandii suggests a
RT mechanism for the insertion of the terminal sulphur atom in the
RT molybdopterin cofactor.";
RL Mol. Microbiol. 38:114-125(2000).
RN [5]
RP ENZYME ACTIVITY.
RX PubMed=6801056; DOI=10.1016/s0021-9258(18)34876-2;
RA Wahl R.C., Warner C.K., Finnerty V., Rajagopalan K.V.;
RT "Drosophila melanogaster ma-l mutants are defective in the sulfuration of
RT desulfo Mo hydroxylases.";
RL J. Biol. Chem. 257:3958-3962(1982).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-734, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
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 ECO:0000269|PubMed:11029694}.
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 ECO:0000269|PubMed:6801056};
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 -!- SEQUENCE CAUTION:
CC Sequence=AAD50777.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AE014298; AAF50901.1; -; Genomic_DNA.
DR EMBL; AY118319; AAM48348.1; -; mRNA.
DR EMBL; AF162681; AAD50777.1; ALT_FRAME; Genomic_DNA.
DR RefSeq; NP_001285493.1; NM_001298564.1.
DR RefSeq; NP_523423.1; NM_078699.3.
DR AlphaFoldDB; Q9VRA2; -.
DR SMR; Q9VRA2; -.
DR BioGRID; 59334; 1.
DR IntAct; Q9VRA2; 1.
DR STRING; 7227.FBpp0311241; -.
DR iPTMnet; Q9VRA2; -.
DR PaxDb; 7227-FBpp0076998; -.
DR DNASU; 33045; -.
DR EnsemblMetazoa; FBtr0077306; FBpp0076998; FBgn0002641.
DR EnsemblMetazoa; FBtr0344987; FBpp0311241; FBgn0002641.
DR GeneID; 33045; -.
DR KEGG; dme:Dmel_CG1692; -.
DR AGR; FB:FBgn0002641; -.
DR CTD; 4118; -.
DR FlyBase; FBgn0002641; mal.
DR VEuPathDB; VectorBase:FBgn0002641; -.
DR eggNOG; KOG2142; Eukaryota.
DR HOGENOM; CLU_010913_0_1_1; -.
DR InParanoid; Q9VRA2; -.
DR OMA; PCTRCQM; -.
DR OrthoDB; 448292at2759; -.
DR PhylomeDB; Q9VRA2; -.
DR Reactome; R-DME-947581; Molybdenum cofactor biosynthesis.
DR BioGRID-ORCS; 33045; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 33045; -.
DR PRO; PR:Q9VRA2; -.
DR Proteomes; UP000000803; Chromosome X.
DR Bgee; FBgn0002641; Expressed in spermathecum and 21 other cell types or tissues.
DR ExpressionAtlas; Q9VRA2; baseline and differential.
DR Genevisible; Q9VRA2; DM.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008265; F:Mo-molybdopterin cofactor sulfurase activity; IMP: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; IMP:FlyBase.
DR GO; GO:0043545; P:molybdopterin cofactor metabolic process; IMP:UniProtKB.
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 1: Evidence at protein level;
KW Molybdenum cofactor biosynthesis; Phosphoprotein; Pyridoxal phosphate;
KW Reference proteome; Transferase.
FT CHAIN 1..781
FT /note="Molybdenum cofactor sulfurase"
FT /id="PRO_0000249956"
FT DOMAIN 635..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:0000269|PubMed:18327897"
FT CONFLICT 133
FT /note="E -> A (in Ref. 4; AAD50777)"
FT /evidence="ECO:0000305"
FT CONFLICT 156
FT /note="H -> Y (in Ref. 4; AAD50777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 781 AA; 88104 MW; D2B2D5F52FDDF712 CRC64;
MTSYRPEFSA SEQSQIDAEF SRLASNKSVY LDHAGTTLYA ESQVTAAAEQ LQRNVICNPH
TCRLTGDFVD QVRFKILEFF NTTAEDYHVI FTANATAALS LVAENFDFGS SGEFHFCQEN
HTSVLGMRER VRENGIYMLR ENEISGGKHK ANGKVHEVSG KTGNSLLTFS AQCNFSGYKI
PLEVIEQIQI DGLAKPGKEL WSSLGEKKKN MHNDYYICLD AASFVATSPL DLQKYRPDYV
CLSFYKIFGY PTGVGALLVS RRGAEVFQKR RFFGGGTINY AYPHAMDYQL RETFHQRYED
GTLPFLSIVG LLEGFRTLER LVPRTDEFST MERISRHVFG LAKYLEDQLR QLHHPNGEPL
VKLYNKVGYQ DKSRQGGIVA FNVRTESGSF VGFGEIACVA ALHGILLRTG CFCNIGACQY
YLGLDEDALD AIYKRAGRIC GDYFDLIDGQ PTGAVRVSFG YMTTIQDVDK LLQMLRSSYL
ATKPLQRIQF IEEQAEQLPP LLKERVQLLR PKLLQMAIYP VKSCAAFKIE LPGSWPLTDQ
GLKYDREWMI VDMNGMALTQ KRCTELCLIR PVIKVDQLEL QFGENSTISV PLSLDDQAAD
TAKCVSKVCR QPVEGLDCGD RVAQWLSENL GMEGLRLLRQ SGQRNSSKDQ QKLSLVNQAQ
FLLLNKSSVR SLQFEEPLDE TVDRFRANII IDTGSAFEEL TYKALSIGGI QFQVEGPCQR
CDMICINQRT GERSPETLTT ISRLQKGRMR FGIYITRIPQ DTKELEPKEQ HMTCGDVVLV
E
//
