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 29-MAY-2013, entry version 87.
DE RecName: Full=Cyclic pyranopterin monophosphate synthase;
DE EC=4.1.99.18;
DE AltName: Full=Molybdenum cofactor biosynthesis protein A;
GN Name=moaA; 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) (By similarity).
CC -!- CATALYTIC ACTIVITY: GTP = cyclic pyranopterin phosphate +
CC diphosphate.
CC -!- COFACTOR: 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 (By similarity).
CC -!- COFACTOR: Binds 1 S-adenosyl-L-methionine per subunit (By
CC similarity).
CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis.
CC -!- SUBUNIT: Monomer and homodimer (By similarity).
CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family.
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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 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; AQKYKIM; -.
DR ProtClustDB; PRK00164; -.
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: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: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 (By similarity).
FT METAL 21 21 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 25 25 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 28 28 Iron-sulfur 1 (4Fe-4S-S-AdoMet) (By
FT similarity).
FT METAL 249 249 Iron-sulfur 2 (4Fe-4S-substrate) (By
FT similarity).
FT METAL 252 252 Iron-sulfur 2 (4Fe-4S-substrate) (By
FT similarity).
FT METAL 266 266 Iron-sulfur 2 (4Fe-4S-substrate) (By
FT similarity).
FT BINDING 14 14 GTP (By similarity).
FT BINDING 27 27 S-adenosyl-L-methionine (By similarity).
FT BINDING 64 64 GTP (By similarity).
FT BINDING 68 68 S-adenosyl-L-methionine; via carbonyl
FT oxygen (By similarity).
FT BINDING 95 95 GTP (By similarity).
FT BINDING 119 119 S-adenosyl-L-methionine (By similarity).
FT BINDING 155 155 GTP (By similarity).
FT BINDING 189 189 S-adenosyl-L-methionine; via amide
FT nitrogen and carbonyl oxygen (By
FT similarity).
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
//
