MOCS1_DROME
ID MOCS1_DROME Reviewed; 565 AA.
AC Q8IQF1; Q9NIG3; Q9NIG4; Q9VTE4;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Molybdenum cofactor biosynthesis protein 1;
DE Includes:
DE RecName: Full=GTP 3',8-cyclase;
DE EC=4.1.99.22 {ECO:0000250|UniProtKB:P69848};
DE AltName: Full=Molybdenum cofactor biosynthesis protein A;
DE Includes:
DE RecName: Full=Cyclic pyranopterin monophosphate synthase;
DE EC=4.6.1.17 {ECO:0000250|UniProtKB:Q9NZB8};
DE AltName: Full=Molybdenum cofactor biosynthesis protein C;
GN Name=Mocs1; Synonyms=lxd; ORFNames=CG33048;
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 [MRNA] (ISOFORM MOCS1A), AND ALTERNATIVE SPLICING.
RX PubMed=10917590; DOI=10.1017/s1355838200000182;
RA Gray T.A., Nicholls R.D.;
RT "Diverse splicing mechanisms fuse the evolutionarily conserved bicistronic
RT MOCS1A and MOCS1B open reading frames.";
RL RNA 6:928-936(2000).
RN [2]
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 [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MOCS1A).
RC STRAIN=Berkeley;
RA Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M.,
RA Park S., Wan K.H., Yu C., Celniker S.E.;
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Isoform Mocs1a and isoform Mocs1b probably form a complex
CC that catalyzes the conversion of 5'-GTP to cyclic pyranopterin
CC monophosphate (cPMP). Mocs1a catalyzes the cyclization of GTP to (8S)-
CC 3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate and Mocs1b catalyzes
CC the subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-
CC triphosphate to cPMP. {ECO:0000250|UniProtKB:Q9NZB8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A + H(+) + L-
CC methionine; Xref=Rhea:RHEA:49576, ChEBI:CHEBI:13193,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17319, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:37565, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789,
CC ChEBI:CHEBI:131766; EC=4.1.99.22;
CC Evidence={ECO:0000250|UniProtKB:P69848};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic
CC pyranopterin phosphate + diphosphate; Xref=Rhea:RHEA:49580,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:59648, ChEBI:CHEBI:131766;
CC EC=4.6.1.17; Evidence={ECO:0000250|UniProtKB:Q9NZB8};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000250|UniProtKB:Q9NZB8};
CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster coordinated
CC with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1
CC [4Fe-4S] cluster coordinated with 3 cysteines and the GTP-derived
CC substrate. {ECO:0000250|UniProtKB:Q9NZB8};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Isoform Mocs1a and isoform Mocs1b probably form a
CC heterooligomer. {ECO:0000250|UniProtKB:Q9NZB8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=Mocs1b; Synonyms=C;
CC IsoId=Q8IQF1-1; Sequence=Displayed;
CC Name=Mocs1a; Synonyms=A;
CC IsoId=Q8IQF1-2; Sequence=VSP_036853, VSP_036854;
CC -!- MISCELLANEOUS: Isoform Mocs1a seems to be translated from a bicistronic
CC transcript while isoform Mocs1b seems to be translated from a
CC monocistronic mRNA that is derived by alternative splicing.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoaC family.
CC {ECO:0000305}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. MoaA family. {ECO:0000305}.
CC -!- CAUTION: The C-terminus of Mocs1a was previously believed to be
CC thiocarboxylated, but it is now known not to be the case.
CC {ECO:0000250|UniProtKB:Q9NZB8}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF67856.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR EMBL; AF214021; AAF67855.1; -; mRNA.
DR EMBL; AF214021; AAF67856.1; ALT_SEQ; mRNA.
DR EMBL; AE014296; AAN11896.1; -; Genomic_DNA.
DR EMBL; AE014296; AAF50108.2; -; Genomic_DNA.
DR EMBL; BT024947; ABE01177.1; -; mRNA.
DR RefSeq; NP_788494.1; NM_176316.2. [Q8IQF1-1]
DR RefSeq; NP_788495.1; NM_176317.2. [Q8IQF1-2]
DR AlphaFoldDB; Q8IQF1; -.
DR SMR; Q8IQF1; -.
DR BioGRID; 64613; 3.
DR IntAct; Q8IQF1; 1.
DR STRING; 7227.FBpp0075935; -.
DR PaxDb; Q8IQF1; -.
DR PRIDE; Q8IQF1; -.
DR DNASU; 39238; -.
DR EnsemblMetazoa; FBtr0076204; FBpp0075934; FBgn0263241. [Q8IQF1-2]
DR EnsemblMetazoa; FBtr0076205; FBpp0075935; FBgn0263241. [Q8IQF1-1]
DR GeneID; 39238; -.
DR KEGG; dme:Dmel_CG33048; -.
DR UCSC; CG33048-RA; d. melanogaster.
DR UCSC; CG33048-RB; d. melanogaster.
DR UCSC; CG33048-RC; d. melanogaster. [Q8IQF1-1]
DR CTD; 4337; -.
DR FlyBase; FBgn0263241; Mocs1.
DR VEuPathDB; VectorBase:FBgn0263241; -.
DR eggNOG; KOG2876; Eukaryota.
DR GeneTree; ENSGT00390000016567; -.
DR HOGENOM; CLU_009273_7_2_1; -.
DR InParanoid; Q8IQF1; -.
DR OMA; IEFMPIG; -.
DR PhylomeDB; Q8IQF1; -.
DR Reactome; R-DME-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR BioGRID-ORCS; 39238; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 39238; -.
DR PRO; PR:Q8IQF1; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0263241; Expressed in antenna and 31 other tissues.
DR ExpressionAtlas; Q8IQF1; baseline and differential.
DR Genevisible; Q8IQF1; DM.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0061799; F:cyclic pyranopterin monophosphate synthase activity; ISS:FlyBase.
DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; ISS:FlyBase.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0002121; P:inter-male aggressive behavior; IMP:FlyBase.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; ISS:UniProtKB.
DR CDD; cd01420; MoaC_PE; 1.
DR Gene3D; 3.20.20.70; -; 1.
DR Gene3D; 3.30.70.640; -; 1.
DR HAMAP; MF_01225_B; MoaA_B; 1.
DR HAMAP; MF_01224_B; MoaC_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR023045; Mo_CF_biosynth-C.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR010505; Mob_synth_C.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55040; SSF55040; 1.
DR TIGRFAMs; TIGR02666; moaA; 1.
DR TIGRFAMs; TIGR00581; moaC; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 2: Evidence at transcript level;
KW 4Fe-4S; Alternative splicing; GTP-binding; Iron; Iron-sulfur; Lyase;
KW Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..565
FT /note="Molybdenum cofactor biosynthesis protein 1"
FT /id="PRO_0000369401"
FT DOMAIN 64..276
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 3..367
FT /note="Molybdenum cofactor biosynthesis protein A"
FT ACT_SITE 525
FT /note="For molybdenum cofactor biosynthesis protein C
FT activity"
FT /evidence="ECO:0000255"
FT BINDING 73
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 80
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 84
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 86
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 87
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="1"
FT /ligand_note="4Fe-4S-S-AdoMet"
FT /evidence="ECO:0000250"
FT BINDING 123
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 127
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 154
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 178
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 248
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 311
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000250"
FT BINDING 316..318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 328
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 368..385
FT /note="DAAPRLHHHLHPYSYHHA -> GMLNLSQMENRPMILIGG (in isoform
FT Mocs1a)"
FT /evidence="ECO:0000303|PubMed:10917590, ECO:0000303|Ref.4"
FT /id="VSP_036853"
FT VAR_SEQ 386..565
FT /note="Missing (in isoform Mocs1a)"
FT /evidence="ECO:0000303|PubMed:10917590, ECO:0000303|Ref.4"
FT /id="VSP_036854"
FT CONFLICT 116
FT /note="E -> D (in Ref. 1; AAF67855)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 565 AA; 63258 MW; 1E451AF7E57E3062 CRC64;
MRLLARHAIR LLGQENSAGE VASLSRGAIR LKATTGYLNL ATASVQPLEP EKQVLRKNSP
LTDSFGRHHT YLRISLTERC NLRCDYCMPA EGVPLQPKNK LLTTEEILRL ARIFVEQGVR
KIRLTGGEPT VRRDIVEIVA QMKALPELEQ IGITTNGLVL TRLLLPLQRA GLDNLNISLD
TLKRDRFEKI TRRKGWERVI AGIDLAVQLG YRPKVNCVLM RDFNEDEICD FVEFTRNRPV
DVRFIEYMPF SGNKWHTERL ISYKDTLQII RQRWPDFKAL PNGPNDTSKA YAVPGFKGQV
GFITSMTEHF CGTCNRLRLT ADGNIKVCLF GNKEFSLRDA MRDESVSEEQ LVDLIGAAVQ
RKKKQHADAA PRLHHHLHPY SYHHAYHTSR LQLQARNYSQ LTHVDGQGKA QMVDVGAKPS
TTRLARAEAT VQVGEKLTQL IADNQVAKGD VLTVAQIAGI MGAKRTAELI PLCHNISLSS
VKVQATLLKT EQSVRLEATV RCSGQTGVEM EALTAVSVAA LTVYDMCKAV SHDICITNVR
LLSKSGGKRD FQREEPQNGI VTEVE
