(data stored in SCRATCH zone)

SWISSPROT: D1YWA3_METPS

ID   D1YWA3_METPS            Unreviewed;       312 AA.
AC   D1YWA3;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 63.
DE   RecName: Full=Probable GTP 3',8-cyclase {ECO:0000256|HAMAP-Rule:MF_01225};
DE            EC=4.1.99.22 {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   ECO:0000313|EMBL:BAI60725.1};
GN   OrderedLocusNames=MCP_0653 {ECO:0000313|EMBL:BAI60725.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60725.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
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; Evidence={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   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC       {ECO:0000256|HAMAP-Rule:MF_01225}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01225}.
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DR   EMBL; AP011532; BAI60725.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0653; -.
DR   EnsemblBacteria; BAI60725; BAI60725; MCP_0653.
DR   KEGG; mpd:MCP_0653; -.
DR   PATRIC; fig|304371.9.peg.674; -.
DR   eggNOG; arCOG00930; Archaea.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228680; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001882; 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_A; MoaA_A; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR006638; Elp3/MiaB/NifB.
DR   InterPro; IPR013485; MoaA_arc.
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; TIGR02668; moaA_archaeal; 1.
DR   PROSITE; PS01305; MOAA_NIFB_PQQE; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YWA3.
DR   SWISS-2DPAGE; D1YWA3.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   DOMAIN          14..211
FT                   /note="Elp3"
FT                   /evidence="ECO:0000259|SMART:SM00729"
FT   NP_BIND         249..251
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   METAL           24
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   METAL           28
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   METAL           31
FT                   /note="Iron-sulfur 1 (4Fe-4S-S-AdoMet)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   METAL           244
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   METAL           247
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   METAL           261
FT                   /note="Iron-sulfur 2 (4Fe-4S-substrate)"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         17
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         30
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         64
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         68
FT                   /note="S-adenosyl-L-methionine; via carbonyl oxygen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         92
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         116
FT                   /note="S-adenosyl-L-methionine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
FT   BINDING         154
FT                   /note="GTP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01225"
SQ   SEQUENCE   312 AA;  35219 MW;  673DF0F9F4B8DF15 CRC64;
     MQESLVDNYG RRVTSLRMSL TNRCNLQCIY CHNEGESGSG GEITVDEIAR LVRIATKYGV
     DRVKFSGGEP LLRTDLEDIL RALPPLKDIS LTTNGTLLAP RAKGLKEAGL DRVNISLDTM
     DSGRFDLITQ RKGQFSRVMD GINAAIDAGL TPVKLNMVYL KGINEDEIER MIEFIRGRPL
     VLQVIELMNF KGAFKYHADI SALEHSLKAR ADDYKCREMH RRTKYYLNGA EVEIVRPIDN
     SEFCMNCNRL RVTSDFKLKP CLLRNDNLVS LRGLDDEGLE KALRYTVGIR EPFFKAAPVA
     MPKKSEKVPS EN
//

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