ID A0A0B2BXT5_9SPHN Unreviewed; 334 AA.
AC A0A0B2BXT5;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=GTP 3',8-cyclase {ECO:0000256|ARBA:ARBA00012167, ECO:0000256|HAMAP-Rule:MF_01225};
DE EC=4.1.99.22 {ECO:0000256|ARBA:ARBA00012167, ECO:0000256|HAMAP-Rule:MF_01225};
DE AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000256|HAMAP-Rule:MF_01225};
GN Name=moaA {ECO:0000256|HAMAP-Rule:MF_01225};
GN ORFNames=PK98_08275 {ECO:0000313|EMBL:KHL26423.1};
OS Croceibacterium mercuriale.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Croceibacterium.
OX NCBI_TaxID=1572751 {ECO:0000313|EMBL:KHL26423.1, ECO:0000313|Proteomes:UP000030988};
RN [1] {ECO:0000313|EMBL:KHL26423.1, ECO:0000313|Proteomes:UP000030988}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Coronado {ECO:0000313|EMBL:KHL26423.1,
RC ECO:0000313|Proteomes:UP000030988};
RA Coil D.A., Eisen J.A.;
RT "Draft genome sequence of Kirrobacter mercurialis.";
RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC dihydroguanosine 5'-triphosphate. {ECO:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000034, ECO:0000256|HAMAP-
CC Rule:MF_01225};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|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:0000256|HAMAP-Rule:MF_01225};
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC {ECO:0000256|HAMAP-Rule:MF_01225}.
CC -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_01225}.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC {ECO:0000256|HAMAP-Rule:MF_01225}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KHL26423.1}.
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DR EMBL; JTDN01000001; KHL26423.1; -; Genomic_DNA.
DR RefSeq; WP_039095688.1; NZ_JTDN01000001.1.
DR AlphaFoldDB; A0A0B2BXT5; -.
DR STRING; 1572751.PK98_08275; -.
DR OrthoDB; 9763993at2; -.
DR UniPathway; UPA00344; -.
DR Proteomes; UP000030988; Unassembled WGS sequence.
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 CDD; cd01335; Radical_SAM; 1.
DR CDD; cd21117; Twitch_MoaA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_01225_B; MoaA_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; IPR007197; rSAM.
DR NCBIfam; TIGR02666; moaA; 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; PF06463; Mob_synth_C; 1.
DR Pfam; PF04055; Radical_SAM; 1.
DR SFLD; SFLDG01383; cyclic_pyranopterin_phosphate; 1.
DR SFLD; SFLDG01067; SPASM/twitch_domain_containing; 1.
DR SMART; SM00729; Elp3; 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 4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01225};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_01225};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_01225};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_01225};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01225};
KW Molybdenum cofactor biosynthesis {ECO:0000256|ARBA:ARBA00023150,
KW ECO:0000256|HAMAP-Rule:MF_01225};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01225}; Reference proteome {ECO:0000313|Proteomes:UP000030988};
KW S-adenosyl-L-methionine {ECO:0000256|ARBA:ARBA00022691, ECO:0000256|HAMAP-
KW Rule:MF_01225}.
FT DOMAIN 11..236
FT /note="Radical SAM core"
FT /evidence="ECO:0000259|PROSITE:PS51918"
FT BINDING 20
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 27
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:0000256|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:0000256|HAMAP-Rule:MF_01225"
FT BINDING 33
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 34
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:0000256|HAMAP-Rule:MF_01225"
FT BINDING 69
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 73
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 102
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 126
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 162
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 196
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 259
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 262
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 264..266
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT BINDING 276
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_label="2"
FT /ligand_note="4Fe-4S-substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
SQ SEQUENCE 334 AA; 36647 MW; ACB35E85A9B04B3D CRC64;
MSCSSGPLVD AFDRRITYLR LSVTDRCDLR CTYCMPERMQ FLPRKEVLSL EEMHRLALAM
IDRGIRKIRL TGGEPLVRRD VIELVQALGR RLGDGLDELT LTTNGTQLAT HAEALFAAGI
RRVNVSLDTL DPGLFFALTR RDQLAEVLGG IRAAAAAGLQ VKLNIVALKG LNRHEIPDLV
AWAHGQGHEV TLIEVMPLGE VEGERVDHYL PLTAVRDDLE QRWTLVESTH RSGGPARYVD
VAETGGRLGF ITPLTNNFCA TCNRIRVTAT GQLFACLGGA EQVDLRAALR SDTPDVLLAQ
ALDTAMAIKP ERHHFSHIRG AAPAQPRHMS LTGG
//
