MOCS1_BOVIN
ID MOCS1_BOVIN Reviewed; 633 AA.
AC Q1JQD7; A8SMN8; Q58DL6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-APR-2009, sequence version 2.
DT 03-AUG-2022, entry version 108.
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;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MOCS1A).
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM MOCS1A), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 323-633 (ISOFORM MOCS1B).
RC STRAIN=Hereford; TISSUE=Ascending colon, and Uterus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (OCT-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;
CC IsoId=Q1JQD7-1; Sequence=Displayed;
CC Name=MOCS1A;
CC IsoId=Q1JQD7-2; Sequence=VSP_036847, VSP_036848;
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; BT021581; AAX46428.1; -; mRNA.
DR EMBL; BC116030; AAI16031.1; -; mRNA.
DR EMBL; BC126847; AAI26848.1; -; mRNA.
DR RefSeq; NP_001013615.1; NM_001013597.1.
DR RefSeq; NP_001159769.1; NM_001166297.1. [Q1JQD7-1]
DR AlphaFoldDB; Q1JQD7; -.
DR SMR; Q1JQD7; -.
DR STRING; 9913.ENSBTAP00000013792; -.
DR PaxDb; Q1JQD7; -.
DR PRIDE; Q1JQD7; -.
DR Ensembl; ENSBTAT00000013792; ENSBTAP00000013792; ENSBTAG00000010449. [Q1JQD7-1]
DR GeneID; 281917; -.
DR KEGG; bta:281917; -.
DR CTD; 4337; -.
DR VEuPathDB; HostDB:ENSBTAG00000010449; -.
DR eggNOG; KOG2876; Eukaryota.
DR GeneTree; ENSGT00390000016567; -.
DR HOGENOM; CLU_009273_7_3_1; -.
DR InParanoid; Q1JQD7; -.
DR OMA; IRDAKPF; -.
DR OrthoDB; 721528at2759; -.
DR TreeFam; TF300424; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000009136; Chromosome 23.
DR Bgee; ENSBTAG00000010449; Expressed in monocyte and 103 other tissues.
DR ExpressionAtlas; Q1JQD7; baseline and differential.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
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 GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IEA:Ensembl.
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 SFLD; SFLDS00029; 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; Acetylation; Alternative splicing; GTP-binding; Iron; Iron-sulfur;
KW Lyase; Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; S-adenosyl-L-methionine.
FT CHAIN 1..633
FT /note="Molybdenum cofactor biosynthesis protein 1"
FT /id="PRO_0000369399"
FT DOMAIN 61..295
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT REGION 1..380
FT /note="Molybdenum cofactor biosynthesis protein A"
FT REGION 410..633
FT /note="Molybdenum cofactor biosynthesis protein C"
FT REGION 446..480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..477
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 603
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 309
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 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 314..316
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 326
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 MOD_RES 61
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB8"
FT MOD_RES 195
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9NZB8"
FT MOD_RES 525
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKZ7"
FT VAR_SEQ 381..382
FT /note="EL -> GG (in isoform MOCS1A)"
FT /evidence="ECO:0000303|PubMed:16305752, ECO:0000303|Ref.2"
FT /id="VSP_036847"
FT VAR_SEQ 383..633
FT /note="Missing (in isoform MOCS1A)"
FT /evidence="ECO:0000303|PubMed:16305752, ECO:0000303|Ref.2"
FT /id="VSP_036848"
FT CONFLICT 65
FT /note="H -> R (in Ref. 1; AAX46428)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 633 AA; 69659 MW; CCB856C3CAC327BB CRC64;
MAAQPVSRVV RRVLRAGVRS CSSGAPVTQP CPGEPVVEVL SRPRPFLGEH AAPFSAFLTD
SFGRHHSYLR ISLTERCNLR CQYCMPEEGV PLTPKADLLT TEEILTLARL FVKEGVDKIR
LTGGEPLIRP DVVDIVAQLR QLEGLRTIGI TTNGINLARL LPQLQKAGLS AINISLDTLV
PAKFEFIVRR KGFHKVMEGI HKAIELGYSP VKVNCVVMRG LNEDELLDFV ALTEGLPLDV
RFIEYMPFDG NKWNFKKMVS YKEMLDTLRQ QWPELEKLPE EESSTAKAFK IPGFRGQVSF
ITSMSEHFCG TCNRLRITAD GNLKVCLFGN SEVSLRDHLR AGASEEELLR VIGAAVGRKK
RQHAGMFNIS QMKNRPMILI ELFLMRQDSP PALPSTFRNS LRVQVLRHRV SFSSQMVTLW
KGGGVPQAPL VAQRWLGSSL PQRHFSSHLD SDANPKCLSP TEPQAPAASS GPLPDSDQLT
HVDTEGRMAM VDVGRKPDTE RVAVASAVVL LGPVAFKLIQ ENQLKKGDAL AVAQLAGIQA
AKLTSQLIPL CHHVALSHVQ VQLELDRTRH AAVIQASCRA RGPTGVEMEA LTSAAVAALA
LYDMCKAVSR DIVLAEIKLV SKTGGQRGDF HRT
