MOCS1_CAEEL
ID MOCS1_CAEEL Reviewed; 600 AA.
AC Q20624; A0A2C9C399; A0A2C9C3F0; Q8T8M9; Q8T8N0;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 3.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Molybdenum cofactor biosynthesis protein moc-5 {ECO:0000305};
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=moc-5 {ECO:0000312|WormBase:F49E2.1b};
GN ORFNames=F49E2.1 {ECO:0000312|WormBase:F49E2.1b};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
CC -!- FUNCTION: [Isoform a]: Probably forms a complex with isoform b that
CC catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate
CC (cPMP) (By similarity). Catalyzes the cyclization of GTP to (8S)-3',8-
CC cyclo-7,8-dihydroguanosine 5'-triphosphate and mocs1b catalyzes the
CC subsequent conversion of (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-
CC triphosphate to cPMP (By similarity). {ECO:0000250|UniProtKB:Q9NZB8}.
CC -!- FUNCTION: [Isoform b]: Probably forms a complex with isoform a that
CC catalyzes the conversion of 5'-GTP to cyclic pyranopterin monophosphate
CC (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 a and isoform b probably form a heterooligomer.
CC {ECO:0000250|UniProtKB:Q9NZB8}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=b {ECO:0000312|WormBase:F49E2.1b};
CC IsoId=Q20624-1; Sequence=Displayed;
CC Name=a {ECO:0000312|WormBase:F49E2.1a};
CC IsoId=Q20624-2; Sequence=VSP_011903, VSP_011904;
CC Name=c {ECO:0000312|WormBase:F49E2.1c};
CC IsoId=Q20624-3; Sequence=VSP_060751, VSP_060752;
CC Name=d {ECO:0000312|WormBase:F49E2.1d};
CC IsoId=Q20624-4; Sequence=VSP_060750;
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}.
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DR EMBL; BX284606; CAC42301.1; -; Genomic_DNA.
DR EMBL; BX284606; CAC42302.1; -; Genomic_DNA.
DR EMBL; BX284606; SOF58879.1; -; Genomic_DNA.
DR EMBL; BX284606; SOF58880.1; -; Genomic_DNA.
DR PIR; T22460; T22460.
DR RefSeq; NP_509611.3; NM_077210.5. [Q20624-2]
DR RefSeq; NP_509612.2; NM_077211.4. [Q20624-1]
DR AlphaFoldDB; Q20624; -.
DR SMR; Q20624; -.
DR IntAct; Q20624; 1.
DR STRING; 6239.F49E2.1b; -.
DR EPD; Q20624; -.
DR PaxDb; Q20624; -.
DR PeptideAtlas; Q20624; -.
DR EnsemblMetazoa; F49E2.1a.1; F49E2.1a.1; WBGene00009885. [Q20624-2]
DR EnsemblMetazoa; F49E2.1a.2; F49E2.1a.2; WBGene00009885. [Q20624-2]
DR EnsemblMetazoa; F49E2.1a.3; F49E2.1a.3; WBGene00009885. [Q20624-2]
DR EnsemblMetazoa; F49E2.1b.1; F49E2.1b.1; WBGene00009885. [Q20624-1]
DR EnsemblMetazoa; F49E2.1c.1; F49E2.1c.1; WBGene00009885. [Q20624-3]
DR EnsemblMetazoa; F49E2.1d.1; F49E2.1d.1; WBGene00009885. [Q20624-4]
DR EnsemblMetazoa; F49E2.1d.2; F49E2.1d.2; WBGene00009885. [Q20624-4]
DR EnsemblMetazoa; F49E2.1d.3; F49E2.1d.3; WBGene00009885. [Q20624-4]
DR EnsemblMetazoa; F49E2.1d.4; F49E2.1d.4; WBGene00009885. [Q20624-4]
DR GeneID; 181176; -.
DR KEGG; cel:CELE_F49E2.1; -.
DR UCSC; F49E2.1b; c. elegans. [Q20624-1]
DR CTD; 181176; -.
DR WormBase; F49E2.1a; CE27759; WBGene00009885; moc-5. [Q20624-2]
DR WormBase; F49E2.1b; CE27760; WBGene00009885; moc-5. [Q20624-1]
DR WormBase; F49E2.1c; CE52186; WBGene00009885; moc-5. [Q20624-3]
DR WormBase; F49E2.1d; CE52073; WBGene00009885; moc-5. [Q20624-4]
DR eggNOG; KOG2876; Eukaryota.
DR GeneTree; ENSGT00390000016567; -.
DR HOGENOM; CLU_009273_7_2_1; -.
DR InParanoid; Q20624; -.
DR OMA; IRDAKPF; -.
DR OrthoDB; 721528at2759; -.
DR PhylomeDB; Q20624; -.
DR Reactome; R-CEL-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q20624; -.
DR Proteomes; UP000001940; Chromosome X.
DR Bgee; WBGene00009885; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q20624; baseline and differential.
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; IBA:GO_Central.
DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; IBA:GO_Central.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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 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 3: Inferred from homology;
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..600
FT /note="Molybdenum cofactor biosynthesis protein moc-5"
FT /id="PRO_0000153033"
FT DOMAIN 68..284
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 4..371
FT /note="Molybdenum cofactor biosynthesis protein A"
FT REGION 369..390
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..595
FT /note="Molybdenum cofactor biosynthesis protein C"
FT ACT_SITE 566
FT /note="For molybdenum cofactor biosynthesis protein C
FT activity"
FT /evidence="ECO:0000255"
FT BINDING 77
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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 88
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 90
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 91
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 127
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 158
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 218
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 252
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 316
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 319
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 321..323
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 333
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 1..550
FT /note="Missing (in isoform d)"
FT /evidence="ECO:0000305"
FT /id="VSP_060750"
FT VAR_SEQ 372..389
FT /note="VFRNGRSEEPAKSSNDSY -> GMDALKNLPNRPMILIGG (in isoform
FT a)"
FT /evidence="ECO:0000305"
FT /id="VSP_011903"
FT VAR_SEQ 390..600
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_011904"
FT VAR_SEQ 474..492
FT /note="LTAEISRQISENTIKKGDV -> VSFSTNYEIMLIWNKFFYF (in
FT isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060751"
FT VAR_SEQ 493..600
FT /note="Missing (in isoform c)"
FT /evidence="ECO:0000305"
FT /id="VSP_060752"
SQ SEQUENCE 600 AA; 67456 MW; 5F3789BA50C303AA CRC64;
MSCRAGKKLF QWSRVKSSTE EIVKQLTVPL REHAEPILTL TPEQKREAVR LKIQEIEHTK
GQPPFFDMFM REHTYLRISL TEKCNFRCLY CMPAEGVPLK PKDKMLSNSE VLRLVKLFAA
HGVDKVRLTG GEPTIRKDIV HIVEGISSTP GIKEVGITTN GLVLQRFLPQ LRDAGLTKIN
ISIDSLDREK FAKMTRRDGF DKVWKAIELA RGYYPKVKLN VVVLKHQNEN EVVDFVNLTK
DRNLDVRFIE FMPFGGNEFK NDNFIGYREM LNLIVDKYGD GVIRLSDSPN DTTKAYKIDG
FQGQFGFITS MSDHFCNTCN RLRITADGNL KVCLHGNSEV SLRDRIRCGD SDEQLSEVIQ
KAVNNKKARH AVFRNGRSEE PAKSSNDSYR GLTPVTSASS ILVHLPSSSL YHSHLHSSRH
FFISQIRCFS TTYSVSSITH LLTHVDNNGN AKQVDVSQKD TSTRTAVARG TIILTAEISR
QISENTIKKG DVLTVAKIAS ILGAKQVANL IPLCHPIRLD FVDTVFNHDI ENSKLHCIST
ARCSGNTGVE MEALTACTIA LLTVYDMCKA ISQKMMLTNI YLVHKSGGKT TYTIDNENQI
