MOAA2_PSEAE
ID MOAA2_PSEAE Reviewed; 331 AA.
AC Q9I3K7;
DT 19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=GTP 3',8-cyclase 2 {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 2 {ECO:0000255|HAMAP-Rule:MF_01225};
GN Name=moaA2; OrderedLocusNames=PA1505;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
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; AE004091; AAG04894.1; -; Genomic_DNA.
DR PIR; E83457; E83457.
DR RefSeq; NP_250196.1; NC_002516.2.
DR RefSeq; WP_003083204.1; NZ_QZGE01000005.1.
DR AlphaFoldDB; Q9I3K7; -.
DR SMR; Q9I3K7; -.
DR STRING; 287.DR97_517; -.
DR PaxDb; Q9I3K7; -.
DR PRIDE; Q9I3K7; -.
DR DNASU; 883031; -.
DR EnsemblBacteria; AAG04894; AAG04894; PA1505.
DR GeneID; 883031; -.
DR KEGG; pae:PA1505; -.
DR PATRIC; fig|208964.12.peg.1557; -.
DR PseudoCAP; PA1505; -.
DR HOGENOM; CLU_009273_0_1_6; -.
DR InParanoid; Q9I3K7; -.
DR OMA; FRHMSVT; -.
DR PhylomeDB; Q9I3K7; -.
DR BioCyc; PAER208964:G1FZ6-1532-MON; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000002438; 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_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 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..331
FT /note="GTP 3',8-cyclase 2"
FT /id="PRO_0000152981"
FT DOMAIN 9..234
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 18
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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 29
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 31
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 32
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 67
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 71
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 98
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 122
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 159
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 193
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 257
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 260
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 262..264
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 274
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 331 AA; 37214 MW; D77A1567C6D9C673 CRC64;
MSDSRLVDPF GRRITYLRLS VTDRCDFRCT YCMSEDMQFL PRDQVLSLEE LYAVADAFIG
LGVRRIRITG GEPLVRKGIT GLLARLGQRA ELEDLAITTN GSQLRERAAE LKAAGVRRLN
VSLDSLQRER FAAFTRSDRL EQVLDGIQAA REAGFERIKL NCVVQKGRND DEILDLVEYA
LANQLDISFI EEMPLGSITS HRRELTLCTS DEVRAIIERR WPLTPSLARS GGPSRYYQIG
DEPSRIGFIS PHSNNFCGDC NRVRVTAEGK LVLCLGHEGA LDLRELLRSH PGDRERLSAA
LVAALNLKPE RHHFDAQEQV QVLRFMSMTG G
