(data stored in SCRATCH zone)

SWISSPROT: A4F790_SACEN

ID   A4F790_SACEN            Unreviewed;       349 AA.
AC   A4F790;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   08-MAY-2019, entry version 98.
DE   RecName: Full=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:CAL99914.1};
GN   OrderedLocusNames=SACE_0569 {ECO:0000313|EMBL:CAL99914.1};
OS   Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748
OS   / NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC   Bacteria; Actinobacteria; Pseudonocardiales; Pseudonocardiaceae;
OC   Saccharopolyspora.
OX   NCBI_TaxID=405948 {ECO:0000313|EMBL:CAL99914.1, ECO:0000313|Proteomes:UP000006728};
RN   [1] {ECO:0000313|EMBL:CAL99914.1, ECO:0000313|Proteomes:UP000006728}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 /
RC   NRRL 2338 {ECO:0000313|Proteomes:UP000006728};
RX   PubMed=17369815; DOI=10.1038/nbt1297;
RA   Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N.,
RA   Dickens S., Haydock S.F., Leadlay P.F.;
RT   "Complete genome sequence of the erythromycin-producing bacterium
RT   Saccharopolyspora erythraea NRRL23338.";
RL   Nat. Biotechnol. 25:447-453(2007).
CC   -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_01225, ECO:0000256|SAAS:SAAS01106981}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + GTP + S-adenosyl-L-methionine = (8S)-3',8-cyclo-
CC         7,8-dihydroguanosine 5'-triphosphate + 5'-deoxyadenosine + A +
CC         H(+) + L-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, ECO:0000256|SAAS:SAAS01128401};
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
CC       coordinated with 3 cysteines and an exchangeable S-adenosyl-L-
CC       methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and
CC       the GTP-derived substrate. {ECO:0000256|HAMAP-Rule:MF_01225};
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00138294}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|HAMAP-Rule:MF_01225,
CC       ECO:0000256|SAAS:SAAS00911699}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS01106980}.
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DR   EMBL; AM420293; CAL99914.1; -; Genomic_DNA.
DR   RefSeq; WP_009945202.1; NZ_PDBV01000001.1.
DR   STRING; 405948.SACE_0569; -.
DR   EnsemblBacteria; CAL99914; CAL99914; SACE_0569.
DR   KEGG; sen:SACE_0569; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228681; -.
DR   KO; K03639; -.
DR   OMA; IEFMPIG; -.
DR   BioCyc; SERY405948:SACE_RS02795-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000006728; 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; A4F790.
DR   SWISS-2DPAGE; A4F790.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138299};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006728};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138126};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00138256};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138121};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138219};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138296};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138110};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138119};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006728};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138251}.
FT   DOMAIN       32    237       Elp3. {ECO:0000259|SMART:SM00729}.
FT   NP_BIND     281    283       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        42     42       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        46     46       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        49     49       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       276    276       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       279    279       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       293    293       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      35     35       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      48     48       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      86     86       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      90     90       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01225}.
FT   BINDING     117    117       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     141    141       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     178    178       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     212    212       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
SQ   SEQUENCE   349 AA;  38695 MW;  9C506CEEFC4EA186 CRC64;
     MDLGIPVVRP TTDMSTRPDT PHLVDRFGRI ARDLRVSLID KCNLRCTYCM PAEGLPWLKR
     SELLDTGEMI RLIRIAVEEL GVTNVRFTGG EPLLRQDLVD IISATSELPS KPKTSLTTNG
     INLGRYADAL KRGGLNRVNV SLDTLDRDTF RELTRRDRFS DVLEGLEAAK AAGLEPVKVN
     TVLMRGLNGH EACDLLRYCV EHDYQLRFIE QMPLDPQHGW DRGQMITAEE ILEMLGAEFD
     LTPHTAERGS APAERWLVDG GPATVGVIGS VTRPFCATCD RTRLTADGQL RSCLFSTTET
     DLRGPMRAGA GDEEIMRLWQ ETMWAKKAGH GMDTEGFAQP SRPMSAIGG
//

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