(data stored in ACNUC7421 zone)

SWISSPROT: MOAA_RHILO

ID   MOAA_RHILO              Reviewed;         331 AA.
AC   Q98MK6;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   11-DEC-2019, entry version 107.
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=mlr0541;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(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}.
DR   EMBL; BA000012; BAB48107.1; -; Genomic_DNA.
DR   RefSeq; WP_010909463.1; NC_002678.2.
DR   STRING; 266835.14021495; -.
DR   PRIDE; Q98MK6; -.
DR   EnsemblBacteria; BAB48107; BAB48107; BAB48107.
DR   KEGG; mlo:mlr0541; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228680; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   OrthoDB; 1199289at2; -.
DR   BioCyc; MLOT266835:G1G20-445-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000552; 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   SMART; SM00729; Elp3; 1.
DR   TIGRFAMs; TIGR02666; moaA; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q98MK6.
DR   SWISS-2DPAGE; Q98MK6.
KW   4Fe-4S; GTP-binding; Iron; Iron-sulfur; Lyase; Metal-binding;
KW   Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   S-adenosyl-L-methionine.
FT   CHAIN           1..331
FT                   /note="GTP 3',8-cyclase"
FT                   /id="PRO_0000152985"
FT   NP_BIND         260..262
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           22
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           26
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           29
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           255
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           258
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   METAL           272
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         15
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         28
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         64
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         68
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         98
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         122
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         158
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
FT   BINDING         192
FT                   /note="S-adenosyl-L-methionine; via amide nitrogen and
FT                   carbonyl oxygen"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01225"
SQ   SEQUENCE   331 AA;  36919 MW;  697033CBF2D5090A CRC64;
     MNMIDPFGRT ISYLRVSVTD RCDFRCTYCM AEDMAFLPKK DLLSLEELDR LCSVFIEKGV
     RRLRLTGGEP LVRKNIMHLV RQLSRHLDSG ALEELTLTTN GSQLSRFAAE LADCGVKRIN
     VSLDTLDADK FHQITRWGHL DKVMQGIDAA QAAGLKVKLN AVALKDFNDA ELPDMMRWAH
     GRGMDLTVIE TMPMGEIDAD RTDQYLPLSL LRASLERQFT LTDIPFKTGG PARYVHVAET
     GGKLGFITPM THNFCESCNR VRLTCTGTLY MCLGQEDAAD LRAPLRASEG NELVADAIDE
     AIGRKPKGHD FIIDRRTSRP SVSRHMSVTG G
//

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