(data stored in SCRATCH zone)

SWISSPROT: Q144S8_PARXL

ID   Q144S8_PARXL            Unreviewed;       356 AA.
AC   Q144S8;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 101.
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   ORFNames=Bxe_A3837 {ECO:0000313|EMBL:ABE29161.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE29161.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE29161.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE29161.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE29161.1; -; Genomic_DNA.
DR   RefSeq; WP_011486971.1; NZ_CP008760.1.
DR   STRING; 266265.Bxe_A3837; -.
DR   EnsemblBacteria; ABE29161; ABE29161; Bxe_A3837.
DR   GeneID; 4002549; -.
DR   KEGG; bxe:Bxe_A3837; -.
DR   PATRIC; fig|266265.5.peg.649; -.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   HOGENOM; HOG000228681; -.
DR   KO; K03639; -.
DR   OMA; DYLRMSV; -.
DR   OrthoDB; 1199289at2; -.
DR   BioCyc; BXEN266265:BXE_RS03075-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000001817; Chromosome 1.
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:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
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; Q144S8.
DR   SWISS-2DPAGE; Q144S8.
KW   4Fe-4S {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138299};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   GTP-binding {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138126};
KW   Hydrolase {ECO:0000313|EMBL:ABE29161.1};
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:UP000001817};
KW   S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01225,
KW   ECO:0000256|SAAS:SAAS00138251}.
FT   DOMAIN       24    237       Elp3. {ECO:0000259|SMART:SM00729}.
FT   NP_BIND     281    283       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        34     34       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        38     38       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   METAL        41     41       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      27     27       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      40     40       S-adenosyl-L-methionine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      81     81       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING      85     85       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000256|HAMAP-Rule:
FT                                MF_01225}.
FT   BINDING     116    116       GTP. {ECO:0000256|HAMAP-Rule:MF_01225}.
FT   BINDING     140    140       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   356 AA;  38674 MW;  0FCFB2266C825A5A CRC64;
     MASRFGVTAG GVVSTFDKLG RPLRDLRLSV IDQCNFRCTY CMPRETFGAD YPFLASSERM
     SFEQILKLAK AFTLLGVEKI RITGGEPLLR RGLESLIEQL AKLTTASGKP VELALTTNGS
     LLAAKARSLR DAGLGRVTVS LDAVEDAVFR RMSDVDMSVA RILDGIEAAR AVGLEPIKVN
     SVIERGVNES QILPLVRQFR GTGVAVRFIE YMDVGGAGGW SNTKVMTARE IRGIVESEFP
     LVPVVVREQS GTAVNYLHAD GAGEVGFIAS VSQPFCGSCS RARVSADGQL YSCLFATHGT
     DLRPWLTDTA TAGQLAERVR SRWTQRDDRY SELRSTQRKP ASGKVYPTVR MSLVGG
//

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