ID I3LZG3_ICTTR Unreviewed; 633 AA.
AC I3LZG3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Molybdenum cofactor synthesis 1 {ECO:0000313|Ensembl:ENSSTOP00000001716.2};
GN Name=MOCS1 {ECO:0000313|Ensembl:ENSSTOP00000001716.2};
OS Ictidomys tridecemlineatus (Thirteen-lined ground squirrel) (Spermophilus
OS tridecemlineatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Sciuromorpha; Sciuridae;
OC Xerinae; Marmotini; Ictidomys.
OX NCBI_TaxID=43179 {ECO:0000313|Ensembl:ENSSTOP00000001716.2, ECO:0000313|Proteomes:UP000005215};
RN [1] {ECO:0000313|Proteomes:UP000005215}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RG The Broad Institute Genome Assembly & Analysis Group;
RG Computational R&D Group;
RG and Sequencing Platform;
RA Di Palma F., Alfoldi J., Johnson J., Berlin A., Gnerre S., Jaffe D.,
RA MacCallum I., Young S., Walker B.J., Lindblad-Toh K.;
RT "The Draft Genome of Spermophilus tridecemlineatus.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSSTOP00000001716.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00001637};
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:0000256|ARBA:ARBA00000034};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|ARBA:ARBA00005046}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the MoaC family.
CC {ECO:0000256|ARBA:ARBA00008484}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the radical SAM
CC superfamily. MoaA family. {ECO:0000256|ARBA:ARBA00009862}.
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DR EMBL; AGTP01010890; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AGTP01010891; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_005318782.1; XM_005318725.1.
DR AlphaFoldDB; I3LZG3; -.
DR STRING; 43179.ENSSTOP00000001716; -.
DR Ensembl; ENSSTOT00000001924.3; ENSSTOP00000001716.2; ENSSTOG00000001928.3.
DR GeneID; 101977695; -.
DR CTD; 4337; -.
DR eggNOG; KOG2876; Eukaryota.
DR GeneTree; ENSGT00390000016567; -.
DR HOGENOM; CLU_009273_7_3_1; -.
DR InParanoid; I3LZG3; -.
DR OMA; YDMCKYA; -.
DR OrthoDB; 9838at2759; -.
DR TreeFam; TF300424; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000005215; Unassembled WGS sequence.
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; IEA:UniProtKB-EC.
DR GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-EC.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:Ensembl.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd01420; MoaC_PE; 1.
DR CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21117; Twitch_MoaA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR Gene3D; 3.30.70.640; Molybdopterin cofactor biosynthesis C (MoaC) domain; 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/MiaA/NifB-like_rSAM.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR010505; MoaA_twitch.
DR InterPro; IPR023045; MoaC.
DR InterPro; IPR047594; MoaC_bact/euk.
DR InterPro; IPR036522; MoaC_sf.
DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom.
DR InterPro; IPR007197; rSAM.
DR NCBIfam; TIGR02666; moaA; 1.
DR NCBIfam; TIGR00581; moaC; 1.
DR PANTHER; PTHR22960:SF0; MOLYBDENUM COFACTOR BIOSYNTHESIS PROTEIN 1; 1.
DR PANTHER; PTHR22960; MOLYBDOPTERIN COFACTOR SYNTHESIS PROTEIN A; 1.
DR Pfam; PF13353; Fer4_12; 1.
DR Pfam; PF01967; MoaC; 1.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDS00029; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR SUPFAM; SSF55040; Molybdenum cofactor biosynthesis protein C, MoaC; 1.
DR SUPFAM; SSF102114; Radical SAM enzymes; 1.
DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000005215};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 64..277
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 19..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..477
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 437..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 633 AA; 69527 MW; A5A1A3189C20820A CRC64;
MAARPVSRML ERLVRSSVRG CSSGAPVTQP HPGEPSQPAT EDLSRKRPFL KEHVAPFSTF
LTDNFGRQHN YLRISLTEKC NLRCQYCMPE EGVPLTPKAD LLTTEEILTL ARLFVKEGVD
KIRLTGGEPL IRPDVVDIVA QLHRLEGLKT IGVTTNGINL ARLLPALQKA GLTAINISLD
TLVPAKFEFI VRRKGFHKVM EGIHKAIELG YSPVKVNCVV MRGLNEDELL DFVTLTKGLP
LDIRFIEYMP FDGNKWNFKK MVSYKEMLDT IRQQWPELEK LPEEECSTAK AFRIPGFLGQ
VSFITSMSEH FCGTCNRLRI TADGNLKVCL FGNSEVSLRD HLRAGASEEE LLKIIGAAVG
RKKPRHAGMF SISQMKNRPM ILIELFLLLQ DSSPPASLSI FSRDPLHVQG LRPTVSFSSQ
MATFWKGRGI PQTPSWMGSG CPQRHYSSHA DSDTNSKCLS PGSRVPAAHS GPWSTSDQLT
HVDSEGQAAM VDVGGKPDTE RVAVASAVVL LGPVAFKLVQ QNQLKKGDAL VVAQLAGIQA
AKITSQLIPL CHHVALNHVQ VQLELDSSRH AAVIQATCRA RGPTGVEMEA LTSAAVAALT
LYDMCKAVSR DIVVEEVKLI SKTGGQRGDF HRA
//
