MOAA_STAS1
ID MOAA_STAS1 Reviewed; 340 AA.
AC Q49ZI6;
DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=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=SSP0645;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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 -!- SUBUNIT: Monomer and homodimer. {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; AP008934; BAE17790.1; -; Genomic_DNA.
DR RefSeq; WP_011302584.1; NZ_MTGA01000036.1.
DR AlphaFoldDB; Q49ZI6; -.
DR SMR; Q49ZI6; -.
DR STRING; 342451.SSP0645; -.
DR EnsemblBacteria; BAE17790; BAE17790; SSP0645.
DR GeneID; 66866793; -.
DR KEGG; ssp:SSP0645; -.
DR PATRIC; fig|342451.11.peg.648; -.
DR eggNOG; COG2896; Bacteria.
DR HOGENOM; CLU_009273_0_1_9; -.
DR OMA; IEFMPIG; -.
DR OrthoDB; 1199289at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000006371; 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:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR Gene3D; 3.20.20.70; -; 1.
DR HAMAP; MF_01225_B; MoaA_B; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR006638; Elp3/MiaB/NifB.
DR InterPro; IPR013483; MoaA.
DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS.
DR InterPro; IPR010505; Mob_synth_C.
DR InterPro; IPR007197; rSAM.
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 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; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Reference proteome;
KW S-adenosyl-L-methionine.
FT CHAIN 1..340
FT /note="GTP 3',8-cyclase"
FT /id="PRO_0000153000"
FT DOMAIN 8..227
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 24
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 30
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 31
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 71
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 75
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 163
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 197
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 261
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 264
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 266..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 278
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 340 AA; 39148 MW; 59D31D8F0CC140EE CRC64;
MVEQITDKLG RPIRDLRLSV TDRCNFRCDY CMPKEIFGDD FVFLPKDELL TFDEMVRIAQ
VYTQLGVKKI RITGGEPLLR RDLDKLIYQL NQLEGVEDIG LTTNGLLLKK HGQKLYDAGL
RRINVSLDAI DDAVFQAINN RNIKASTILQ QIDYAVAIGF QVKVNVVVQK GVNDDQIVPM
VQYFKDKDVQ IRFIEFMDVG NDNGWDFSKV VSKDEMLEMI EQNFDIEPVA PKYYGEVAKY
YQHKDNKAQF GLITSVSQSF CSTCTRARLS SDGKFYGCLF STVDGFNVKS FMRNGATDNE
LFEQFKALWN IRDDRYSDER TEQTVANRKR KKINMNYIGG
