MOAA_PAENI
ID MOAA_PAENI Reviewed; 355 AA.
AC Q44118;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 2.
DT 03-AUG-2022, entry version 106.
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};
OS Paenarthrobacter nicotinovorans (Arthrobacter nicotinovorans).
OG Plasmid pAO1.
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Paenarthrobacter.
OX NCBI_TaxID=29320;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTAGENESIS OF CYS-32; CYS-36;
RP TYR-38 AND CYS-39.
RX PubMed=8588735; DOI=10.1007/bf02525320;
RA Menendez C., Igloi G., Henninger H., Brandsch R.;
RT "A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter
RT nicotinovorans: characterization and site-directed mutagenesis of the
RT encoded protein.";
RL Arch. Microbiol. 164:142-151(1995).
RN [2]
RP CHARACTERIZATION, SUBUNIT, AND MUTAGENESIS OF CYS-277; CYS-280 AND CYS-294.
RX PubMed=8706892; DOI=10.1016/0014-5793(96)00712-0;
RA Menendez C., Siebert D., Brandsch R.;
RT "MoaA of Arthrobacter nicotinovorans pAO1 involved in Mo-pterin cofactor
RT synthesis is an Fe-S protein.";
RL FEBS Lett. 391:101-103(1996).
CC -!- FUNCTION: Catalyzes, together with MoaC, the conversion of 5'-GTP to
CC cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z).
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. {ECO:0000269|PubMed:8706892}.
CC -!- MISCELLANEOUS: PubMed:8706892 shows that MoaA seems to contain a 3Fe-4S
CC cluster, but it may actually be two 4Fe-4S clusters as was shown in the
CC crystallographic study of the protein homolog from Staphylococcus
CC aureus.
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC {ECO:0000255|HAMAP-Rule:MF_01225}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA55583.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; X78980; CAA55583.1; ALT_INIT; Genomic_DNA.
DR EMBL; Y10817; CAA71779.1; -; Genomic_DNA.
DR PIR; I39637; I39637.
DR PIR; T44850; T44850.
DR AlphaFoldDB; Q44118; -.
DR SMR; Q44118; -.
DR BRENDA; 4.1.99.22; 449.
DR UniPathway; UPA00344; -.
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 1: Evidence at protein level;
KW 4Fe-4S; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding;
KW Molybdenum cofactor biosynthesis; Nucleotide-binding; Plasmid;
KW S-adenosyl-L-methionine.
FT CHAIN 1..355
FT /note="GTP 3',8-cyclase"
FT /id="PRO_0000152947"
FT DOMAIN 16..242
FT /note="Radical SAM core"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01266"
FT BINDING 25
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
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 36
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 38
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 39
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 76
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 80
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 107
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 131
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 168
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 202
FT /ligand="S-adenosyl-L-methionine"
FT /ligand_id="ChEBI:CHEBI:59789"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 277
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 280
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 282..284
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT BINDING 294
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 MUTAGEN 32
FT /note="C->S: Loss of activity and loss of ability to
FT assemble an Fe-S cluster."
FT /evidence="ECO:0000269|PubMed:8588735"
FT MUTAGEN 36
FT /note="C->S: Loss of activity. Still able to assemble an
FT Fe-S cluster; when associated with S-280."
FT /evidence="ECO:0000269|PubMed:8588735"
FT MUTAGEN 38
FT /note="Y->A,P,S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8588735"
FT MUTAGEN 39
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8588735"
FT MUTAGEN 277
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8706892"
FT MUTAGEN 280
FT /note="C->S: Loss of activity. Still able to assemble an
FT Fe-S cluster; when associated with S-36."
FT /evidence="ECO:0000269|PubMed:8706892"
FT MUTAGEN 294
FT /note="C->S: Loss of activity."
FT /evidence="ECO:0000269|PubMed:8706892"
SQ SEQUENCE 355 AA; 38712 MW; 967C2F357F424C90 CRC64;
MPAARPAGAG VGLVDRYGRR ATDMRLSLTD KCNLRCTYCM PAEGLEWLSK QAVMSASEIV
RIVGIGVGRL GVRELRLTGG EPLVRHDLVD IIAELRRNHP ELPISMTTNG VGLAKKVAPL
KAAGLTRINV SLDSLHEETF TKLTRRPFLD QVLAGVDAAW AAGLGPVKLN AVLMRGINDA
EAPSLLAWAV ERGYELRFIE QMPLDADHGW TRRNMITAAE IRDLLSTDFV LTPDPRARDG
APAERFEVRR RVAGSGAGLG PVLGTVGIIA SVTEPFCSDC RRTRITAEGR IMSCLFSREE
FDLLVLLRSG ASDDDLARRW QDAMWLKPKA HGMDHVGLDA PDFVQPDRSM SAIGG
