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Database: UniProt
Entry: P56414
LinkDB: P56414
Original site: P56414 
ID   MOAA_HELPY              Reviewed;         321 AA.
AC   P56414;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-JUL-1998, sequence version 1.
DT   30-NOV-2016, entry version 105.
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};
GN   OrderedLocusNames=HP_0768;
OS   Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter
OS   pylori).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=85962;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700392 / 26695;
RX   PubMed=9252185; DOI=10.1038/41483;
RA   Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA   Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R.,
RA   Dougherty B.A., Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F.,
RA   Peterson S.N., Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G.,
RA   Glodek A., McKenney K., FitzGerald L.M., Lee N., Adams M.D.,
RA   Hickey E.K., Berg D.E., Gocayne J.D., Utterback T.R., Peterson J.D.,
RA   Kelley J.M., Cotton M.D., Weidman J.F., Fujii C., Bowman C.,
RA   Watthey L., Wallin E., Hayes W.S., Borodovsky M., Karp P.D.,
RA   Smith H.O., Fraser C.M., Venter J.C.;
RT   "The complete genome sequence of the gastric pathogen Helicobacter
RT   pylori.";
RL   Nature 388:539-547(1997).
CC   -!- FUNCTION: Catalyzes the cyclization of GTP to (8S)-3',8-cyclo-7,8-
CC       dihydroguanosine 5'-triphosphate. {ECO:0000255|HAMAP-
CC       Rule:MF_01225}.
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:0000255|HAMAP-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
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: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; AE000511; AAD07817.1; -; Genomic_DNA.
DR   PIR; H64615; H64615.
DR   RefSeq; NP_207561.1; NC_000915.1.
DR   RefSeq; WP_001863441.1; NC_018939.1.
DR   ProteinModelPortal; P56414; -.
DR   STRING; 85962.HP0768; -.
DR   PaxDb; P56414; -.
DR   EnsemblBacteria; AAD07817; AAD07817; HP_0768.
DR   GeneID; 899338; -.
DR   KEGG; heo:C694_03945; -.
DR   KEGG; hpy:HP0768; -.
DR   PATRIC; 20592825; VBIHelPyl33062_0801.
DR   eggNOG; ENOG4105CM1; Bacteria.
DR   eggNOG; COG2896; LUCA.
DR   KO; K03639; -.
DR   OMA; TKLNCVV; -.
DR   BioCyc; HPY:HP0768-MONOMER; -.
DR   UniPathway; UPA00344; -.
DR   Proteomes; UP000000429; Chromosome.
DR   GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 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;
KW   4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur; Lyase;
KW   Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding;
KW   Reference proteome; S-adenosyl-L-methionine.
FT   CHAIN         1    321       GTP 3',8-cyclase.
FT                                /FTId=PRO_0000152967.
FT   NP_BIND     254    256       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL        21     21       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL        25     25       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL        28     28       Iron-sulfur 1 (4Fe-4S-S-AdoMet).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL       249    249       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL       252    252       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   METAL       266    266       Iron-sulfur 2 (4Fe-4S-substrate).
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      14     14       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      27     27       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      64     64       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING      68     68       S-adenosyl-L-methionine; via carbonyl
FT                                oxygen. {ECO:0000255|HAMAP-
FT                                Rule:MF_01225}.
FT   BINDING      95     95       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING     119    119       S-adenosyl-L-methionine.
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING     155    155       GTP. {ECO:0000255|HAMAP-Rule:MF_01225}.
FT   BINDING     189    189       S-adenosyl-L-methionine; via amide
FT                                nitrogen and carbonyl oxygen.
FT                                {ECO:0000255|HAMAP-Rule:MF_01225}.
SQ   SEQUENCE   321 AA;  36657 MW;  3308D812C8A6950C CRC64;
     MLVDSFNRVI DYIRVSVTKQ CNFRCQYCMP ATPLNFFDNE ELLPLDNVLE FLKIAIDEGV
     KKIRITGGEP LLRKGLDEFI AKLHAYNKEV ELVLSTNGFL LKKMAKDLKN AGLAQVNVSL
     DSLKSDRVLK ISQKDALKNT LEGIEESLKV GLKLKLNTVV IKSVNDDEIL ELLEYAKNRH
     IQIRYIEFME NTHAKSLVKG LKEREILDLI AQKYQIIEAE KPKQGSSKIY TLENGYQFGI
     IAPHSDDFCQ SCNRIRLASD GKICPCLYYQ DAIDAKEAII NKDTKNIKRL LKQSVINKPE
     KNMWNDKNSE TPTRAFYYTG G
//
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