MOAA_PYRAE
ID MOAA_PYRAE Reviewed; 310 AA.
AC Q8ZYE5;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Probable GTP 3',8-cyclase {ECO:0000255|HAMAP-Rule:MF_01225};
DE EC=4.1.99.22 {ECO:0000255|HAMAP-Rule:MF_01225};
DE AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01225};
GN Name=moaA {ECO:0000255|HAMAP-Rule:MF_01225}; OrderedLocusNames=PAE0814;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate. {ECO:0000255|HAMAP-Rule:MF_01225}.
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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01225};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01225};
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:0000255|HAMAP-Rule:MF_01225};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01225}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC {ECO:0000255|HAMAP-Rule:MF_01225}.
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DR EMBL; AE009441; AAL63048.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZYE5; -.
DR SMR; Q8ZYE5; -.
DR STRING; 178306.PAE0814; -.
DR EnsemblBacteria; AAL63048; AAL63048; PAE0814.
DR KEGG; pai:PAE0814; -.
DR PATRIC; fig|178306.9.peg.597; -.
DR eggNOG; arCOG00930; Archaea.
DR HOGENOM; CLU_009273_0_1_2; -.
DR InParanoid; Q8ZYE5; -.
DR OMA; IEFMPIG; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
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-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IBA:GO_Central.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01225_A; MoaA_A; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR013485; MoaA_arc.
DR InterPro; IPR010505; Mob_synth_C.
DR InterPro; IPR007197; rSAM.
DR Pfam; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SMART; SM00729; Elp3; 1.
DR TIGRFAMs; TIGR02668; moaA_archaeal; 1.
DR PROSITE; PS51918; RADICAL_SAM; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..310
FT /note="Probable GTP 3',8-cyclase"
FT /id="PRO_0000153023"
FT DOMAIN 5..218
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 14
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 21
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:0000255|HAMAP-Rule:MF_01225"
FT BINDING 25
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:0000255|HAMAP-Rule:MF_01225"
FT BINDING 28
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:0000255|HAMAP-Rule:MF_01225"
FT BINDING 62
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 66
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 91
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 115
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 153
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 251
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 254
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 268
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
SQ SEQUENCE 310 AA; 34472 MW; AAFE22A14F4D986A CRC64;
MLFDKYGRSL QKLRYVVNDE CNYNCVFCHF EGQSRRQGRY LTAEDYGFVT SVFKSLGVAD
FKITGGEPLL RGDIDLIVAN IAKTGAYVTL TTNGYLLRKW VRKLQAAGLK RANVSIHTTD
PEKYSKITGV PPSAFREVLR GLTEARDVGI SLKLNAVVLR GINTDRDSVK NLVKLAASLG
AALQFIELMP SGWGASVFNE LYEPIETLVN IIFELGGRPA GVRKELHNRP LYNIAGVTVE
LIKNFSNPTF CSGCTTMRLT SDGKLKTCIY ADSSVDLMPY IKSRDVEGLL YAVRTALARR
EPRFKLYSSS
