ID S4R6Q9_PETMA Unreviewed; 592 AA.
AC S4R6Q9;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE SubName: Full=Molybdenum cofactor synthesis 1 {ECO:0000313|Ensembl:ENSPMAP00000000889.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000000889.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000000889.1}
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 AlphaFoldDB; S4R6Q9; -.
DR STRING; 7757.ENSPMAP00000000889; -.
DR Ensembl; ENSPMAT00000000893.1; ENSPMAP00000000889.1; ENSPMAG00000000810.1.
DR GeneTree; ENSGT00390000016567; -.
DR HOGENOM; CLU_009273_7_3_1; -.
DR OMA; YDMCKYA; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000245300; Unplaced.
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: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; SFLDG01216; thioether_bond_formation_requi; 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:UP000245300};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691}.
FT DOMAIN 13..229
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT REGION 409..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 414..437
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 592 AA; 65651 MW; 63AAC12842BA12B1 CRC64;
EKLLPASDVL TDGFGRHHTY LRISITEKCN LRCQYCMPGE GVRLTSRPQL LTSEEIISLA
RLFVDAGVNK IRLTGGEPLI RPDAVPLVGE LSKLKGLDTL ALTTNGVNLP RLLPFLKLTR
LNLLNVSLDT LVPAKFEFIA RRKGNHWWNK VMEGIHKAID LGYSPVKVNC VVMRGLNEDE
LVDFVALTEK MPLDVRFIEY MPFDGNKWNF QKMVSYQEML DTIKQTYPTL AKLSNQPNDT
SKAYKVPGYQ GQLGFITSMS EHFCGSCNRL RITADGNLKV CLFGNAEVSL RDALRSGASE
EEMKSLVALA VGRKKKQHAG MFSIAQMKNR PMILIGINYN YVYNCDPTKM FTNKCNAITM
NRHGLNQQPQ TSDFFSKSTF STKLLSVSHD TNKRTTKFGL NEAHFKPGLW PHGTLQKQSA
TDTPQEAPRS ADNARPQLTH TDAAGRAKMV DVTHKPESHR TAIARARVTL GDVAFELVRQ
NRLKKGDALT VAQLAGIMAA KRTDELIPLC HVLPLSSVDV RLELDAESHA VIVTAQCRTV
GQTGVEMEAL VAVSVAALTV YDMCKAVTHD IVIGEIKLLS KTGGQRGDFN RA
//
