(data stored in ACNUC7421 zone)

SWISSPROT: A8FPF9_SHESH

ID   A8FPF9_SHESH            Unreviewed;       328 AA.
AC   A8FPF9;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   07-JUN-2017, entry version 83.
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   OrderedLocusNames=Ssed_0119 {ECO:0000313|EMBL:ABV34732.1};
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104 {ECO:0000313|EMBL:ABV34732.1, ECO:0000313|Proteomes:UP000002015};
RN   [1] {ECO:0000313|EMBL:ABV34732.1, ECO:0000313|Proteomes:UP000002015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3 {ECO:0000313|EMBL:ABV34732.1,
RC   ECO:0000313|Proteomes:UP000002015};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) 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-
CC       Rule:MF_01225, ECO:0000256|SAAS:SAAS00808862}.
CC   -!- CATALYTIC ACTIVITY: GTP + S-adenosyl-L-methionine + reduced
CC       electron acceptor = (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-
CC       triphosphate + 5'-deoxyadenosine + L-methionine + oxidized
CC       electron acceptor. {ECO:0000256|HAMAP-Rule:MF_01225,
CC       ECO:0000256|SAAS:SAAS00817830}.
CC   -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00817832}.
CC   -!- SUBUNIT: Monomer and homodimer. {ECO:0000256|SAAS:SAAS00234447}.
CC   -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
CC       {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00808869}.
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DR   EMBL; CP000821; ABV34732.1; -; Genomic_DNA.
DR   RefSeq; WP_012004258.1; NC_009831.1.
DR   ProteinModelPortal; A8FPF9; -.
DR   STRING; 425104.Ssed_0119; -.
DR   EnsemblBacteria; ABV34732; ABV34732; Ssed_0119.
DR   KEGG; sse:Ssed_0119; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228680; -.
DR   KO; K03639; -.
DR   OMA; DYLRMSV; -.
DR   OrthoDB; POG091H01YJ; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0061798; F:GTP 3',8'-cyclase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP.
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; IPR034481; Main_SPASM_domain-containing.
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; SFLDG01383; cyclic_pyranopterin_phosphate_; 1.
DR   SFLD; SFLDG01386; main_SPASM_domain-containing; 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; A8FPF9.
DR   SWISS-2DPAGE; A8FPF9.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803661};
KW   Complete proteome {ECO:0000313|Proteomes:UP000002015};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817847};
KW   Iron {ECO:0000256|HAMAP-Rule:MF_01225, ECO:0000256|SAAS:SAAS00803669};
KW   Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803637};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817846};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803678};
KW   Molybdenum cofactor biosynthesis {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817827};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00817849};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00803656}.
FT   DOMAIN       13    216       Elp3. {ECO:0000259|SMART:SM00729}.
FT   NP_BIND     259    261       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        23     23       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        27     27       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        30     30       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       254    254       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       257    257       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL       271    271       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      16     16       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      29     29       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      65     65       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      69     69       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01225}.
FT   BINDING      96     96       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     120    120       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     157    157       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     191    191       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
SQ   SEQUENCE   328 AA;  36765 MW;  6FC2565E875353AB CRC64;
     MSLIVDTFGR KVEYLRLSVT DRCDFRCVYC MSEDPCFLNR EQVLSLEELA WVGQAFTELG
     VRKIRLTGGE PLVRTDCDQL VKLLGDLPGL SELSMTTNGS RLTKFAEKMR GSGLGRLNIS
     LDTLKPELFT ELTRNGKLER VIEGIDAAKA AGFTRIKINA VILRGQNDDE VLDLIEFCRG
     RELDIAFIEE MPLGIIDERK KSRHCSSEEV KSIISKRYEL SVSNKRTGGP ARYYTMPGSS
     IHVGFISPHS NNFCHECNRV RVTVEGRLLL CLGNEHSVDL KAILREFPGD IEKLKTAILD
     AIKLKPKEHV FGPEGDVQIL RFMNATGG
//

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