MOCS1_DICDI
ID MOCS1_DICDI Reviewed; 630 AA.
AC Q54NM6;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
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; ORFNames=DDB_G0285137;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
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;
CC IsoId=Q54NM6-1; Sequence=Displayed;
CC Name=mocs1a;
CC IsoId=Q54NM6-2; Sequence=VSP_036828, VSP_036829;
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}.
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DR EMBL; AAFI02000074; EAL64881.1; -; Genomic_DNA.
DR RefSeq; XP_639890.1; XM_634798.1.
DR AlphaFoldDB; Q54NM6; -.
DR SMR; Q54NM6; -.
DR STRING; 44689.DDB0267168; -.
DR PaxDb; Q54NM6; -.
DR PRIDE; Q54NM6; -.
DR EnsemblProtists; EAL64881; EAL64881; DDB_G0285137.
DR GeneID; 8624961; -.
DR KEGG; ddi:DDB_G0285137; -.
DR dictyBase; DDB_G0285137; mocs1.
DR eggNOG; KOG2876; Eukaryota.
DR HOGENOM; CLU_009273_7_1_1; -.
DR InParanoid; Q54NM6; -.
DR OMA; IRDAKPF; -.
DR PhylomeDB; Q54NM6; -.
DR Reactome; R-DDI-947581; Molybdenum cofactor biosynthesis.
DR UniPathway; UPA00344; -.
DR PRO; PR:Q54NM6; -.
DR Proteomes; UP000002195; Chromosome 4.
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 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..630
FT /note="Molybdenum cofactor biosynthesis protein 1"
FT /id="PRO_0000331260"
FT DOMAIN 61..298
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 402..629
FT /note="Molybdenum cofactor biosynthesis protein C"
FT ACT_SITE 599
FT /note="For molybdenum cofactor biosynthesis protein C
FT activity"
FT /evidence="ECO:0000255"
FT BINDING 70
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 77
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 81
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 83
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
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 120
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 124
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 151
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000250"
FT BINDING 312
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 315
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 317..319
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 329
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 384..385
FT /note="GE -> GG (in isoform mocs1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_036828"
FT VAR_SEQ 386..630
FT /note="Missing (in isoform mocs1a)"
FT /evidence="ECO:0000305"
FT /id="VSP_036829"
SQ SEQUENCE 630 AA; 71582 MW; 4E7B95E81E71CF94 CRC64;
MTNIIKSFIT RNTYLNKLSP SPYQFNKYYS NSISTPPTHS YEKKQQPIQN VDDKKYILTD
RFNRHHTYLR ISLTERCNLR CKYCMPEEGV MLSQADKILT TDEIIRLSKL FVSAGVNKIR
FTGGEPLVRK DVEPLIEEVG KIKGLQKIGI TTNGILLSRK LDRLHKAGVN LLNISLDTLN
SDKFTLITRR LGWDRVFQSI DNALKLDNIK VKVNCVIMKG LNDMEICDFV EMTRDKSVEI
RFIEYMPFDG NLWSDKKFLS YTDMIKIIHE KYPTFKKYTI EEEEPNNTSK TYHVPGFKGK
VGFITSMSEH FCSSCNRLRI TADGNLKVCL FGNTEVNLRD RIRDGASDQQ LLEIINAAVL
KKKASHAGMY EIAQNKNRPM ILIGEKSKIQ INFKNKSIKQ KKEVKNYLLK LINSSFINSN
NNNNNNNNNN NNSKLQYIQQ RNYSTNKNNQ NLENNEFSHI TKDGKLPTMV DISDKIITKR
TAHAQSILEF PSNVLSQLLN LEKNNDIDND NNISKNKEIV SKKGPVFATS IVAGTMAVKN
TSNLIPFCHP IPIESCKIEI TIIDSTSVKV DCIVSMSGKT GVEMEALTGA TITSLTIYDM
CKALSKDIVI KETKLISKFG GKSSSPQITK
