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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   26-NOV-2014, entry version 97.
DE   RecName: Full=Cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01225};
DE            EC=4.1.99.18 {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, together with MoaC, the conversion of 5'-GTP
CC       to cyclic pyranopterin monophosphate (cPMP or molybdopterin
CC       precursor Z). {ECO:0000255|HAMAP-Rule:MF_01225}.
CC   -!- CATALYTIC ACTIVITY: GTP = cyclic pyranopterin phosphate +
CC       diphosphate. {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   -!- COFACTOR:
CC       Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01225};
CC       Note=Binds 1 S-adenosyl-L-methionine per subunit.
CC       {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}.
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DR   EMBL; AE000511; AAD07817.1; -; Genomic_DNA.
DR   PIR; H64615; H64615.
DR   RefSeq; NP_207561.1; NC_000915.1.
DR   RefSeq; YP_006934683.1; NC_018939.1.
DR   ProteinModelPortal; P56414; -.
DR   STRING; 85962.HP0768; -.
DR   PRIDE; P56414; -.
DR   EnsemblBacteria; AAD07817; AAD07817; HP_0768.
DR   GeneID; 13869952; -.
DR   GeneID; 899338; -.
DR   KEGG; heo:C694_03945; -.
DR   KEGG; hpy:HP0768; -.
DR   PATRIC; 20592825; VBIHelPyl33062_0801.
DR   eggNOG; COG2896; -.
DR   KO; K03639; -.
DR   OMA; REYPGDI; -.
DR   OrthoDB; EOG64XXNN; -.
DR   BioCyc; HPY:HP0768-MONOMER; -.
DR   UniPathway; UPA00344; -.
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:0061597; F:cyclic pyranopterin monophosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005525; F:GTP binding; 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       Cyclic pyranopterin monophosphate
FT                                synthase.
FT                                /FTId=PRO_0000152967.
FT   REGION      254    256       GTP binding. {ECO:0000255|HAMAP-
FT                                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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