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Q9ZL75 (MOAA_HELPJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Cyclic pyranopterin monophosphate synthase
EC=4.1.99.18
Alternative name(s):
Molybdenum cofactor biosynthesis protein A
Gene names
Name:moaA
Ordered Locus Names:jhp_0705
OrganismHelicobacter pylori (strain J99) (Campylobacter pylori J99) [Complete proteome] [HAMAP]
Taxonomic identifier85963 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Helicobacteraceae › Helicobacter ›

Protein attributes

Sequence length321 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes, together with MoaC, the conversion of 5'-GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin precursor Z) By similarity. HAMAP-Rule MF_01225

Catalytic activity

GTP = cyclic pyranopterin monophosphate + diphosphate. HAMAP-Rule MF_01225

Cofactor

Binds 2 4Fe-4S clusters. Binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate By similarity.

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis. HAMAP-Rule MF_01225

Subunit structure

Monomer and homodimer By similarity.

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 321321Cyclic pyranopterin monophosphate synthase HAMAP-Rule MF_01225
PRO_0000152968

Regions

Region254 – 2563GTP binding By similarity

Sites

Metal binding211Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding251Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding281Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding2491Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Metal binding2521Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Metal binding2661Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Binding site141GTP By similarity
Binding site271S-adenosyl-L-methionine By similarity
Binding site641GTP By similarity
Binding site681S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site951GTP By similarity
Binding site1191S-adenosyl-L-methionine By similarity
Binding site1551GTP By similarity
Binding site1891S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9ZL75 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: B7802F6FCC6D2197

FASTA32136,455
        10         20         30         40         50         60 
MLVDSFNRVI DYIRVSVTKQ CNFRCQYCMP TTPLDFFDDE ELLPLDNVLE FLKIAIDEGV 

        70         80         90        100        110        120 
KKIRITGGEP LLRKGLDEFI AKLHAYNKEV ALVLSTNGFS LKKMAKGLKD AGLSRVNVSL 

       130        140        150        160        170        180 
DSLKSDRVLK ISQKDALKNT LEGIEESLKV GLKLKLNTVV MKGVNDDEIL ELLEYAKNRS 

       190        200        210        220        230        240 
IQIRYIEFME NTHAKSLVKG LKEKEILDLI AQKYKIMGME KPKQGSSKIY TLENGYQFGI 

       250        260        270        280        290        300 
IAPHSDDFCQ SCNRIRLASD GKICPCLYYQ DAIDAKEAII NKDTKMMKRL LKQSIINKPE 

       310        320 
KNMWNDKNGG TPTRAFYYTG G

« Hide

References

[1]"Genomic sequence comparison of two unrelated isolates of the human gastric pathogen Helicobacter pylori."
Alm R.A., Ling L.-S.L., Moir D.T., King B.L., Brown E.D., Doig P.C., Smith D.R., Noonan B., Guild B.C., deJonge B.L., Carmel G., Tummino P.J., Caruso A., Uria-Nickelsen M., Mills D.M., Ives C., Gibson R., Merberg D. expand/collapse author list , Mills S.D., Jiang Q., Taylor D.E., Vovis G.F., Trust T.J.
Nature 397:176-180(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: J99.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE001439 Genomic DNA. Translation: AAD06280.1.
PIRA71900.
RefSeqNP_223423.1. NC_000921.1.

3D structure databases

ProteinModelPortalQ9ZL75.
ModBaseSearch...

Protein-protein interaction databases

STRING85963.jhp0705.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAD06280; AAD06280; jhp_0705.
GeneID890191.
KEGGhpj:jhp0705.
PATRIC20606133. VBIHelPyl98156_0772.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2896.
KOK03639.
OMAAQKYKIM.
ProtClustDBPRK00164.

Enzyme and pathway databases

BioCycHPYL85963:GJB9-717-MONOMER.
UniPathwayUPA00344.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_01225_B. MoaA_B.
InterProIPR013785. Aldolase_TIM.
IPR006638. Elp3/MiaB/NifB.
IPR013483. MoaA.
IPR000385. MoaA_NifB_PqqE_Fe-S-bd_CS.
IPR010505. Mob_synth_C.
IPR007197. rSAM.
[Graphical view]
PfamPF06463. Mob_synth_C. 1 hit.
PF04055. Radical_SAM. 1 hit.
[Graphical view]
SMARTSM00729. Elp3. 1 hit.
[Graphical view]
TIGRFAMsTIGR02666. moaA. 1 hit.
PROSITEPS01305. MOAA_NIFB_PQQE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameMOAA_HELPJ
AccessionPrimary (citable) accession number: Q9ZL75
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: May 1, 1999
Last modified: May 1, 2013
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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