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Q2YNT7 (MOAA_BRUA2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 63. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:BAB1_0973
OrganismBrucella abortus (strain 2308) [Complete proteome] [HAMAP]
Taxonomic identifier359391 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length344 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 phosphate + 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.

Binds 1 S-adenosyl-L-methionine per subunit By similarity.

Pathway

Cofactor biosynthesis; molybdopterin biosynthesis. HAMAP-Rule MF_01225

Subunit structure

Monomer and homodimer By similarity. HAMAP-Rule MF_01225

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Cyclic pyranopterin monophosphate synthase HAMAP-Rule MF_01225
PRO_1000054175

Regions

Region273 – 2753GTP binding By similarity

Sites

Metal binding351Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding391Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding421Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding2681Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Metal binding2711Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Metal binding2851Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Binding site281GTP By similarity
Binding site411S-adenosyl-L-methionine By similarity
Binding site771GTP By similarity
Binding site811S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1111GTP By similarity
Binding site1351S-adenosyl-L-methionine By similarity
Binding site1711GTP By similarity
Binding site2051S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2YNT7 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 50B8258570E51148

FASTA34438,687
        10         20         30         40         50         60 
MRNVQDQPLV SPTEPMIDPF GRAVTYLRVS VTDRCDFRCT YCMAEHMTFL PKKDLLTLEE 

        70         80         90        100        110        120 
LDRLCSVFIE KGVRKLRLTG GEPLVRKNIM HLIGNLSRHL KSGALDELTL TTNGSQLARF 

       130        140        150        160        170        180 
AGELADCGVR RINVSLDTLN PEKFRTITRW GDLSRVLEGI DAAQKAAIHV KINAVALKDF 

       190        200        210        220        230        240 
NDAEIPELIR WAHGRGMDVT LIETMPMGEI EFDRTDQYLP LSQVRADLAS QFTLADIPYR 

       250        260        270        280        290        300 
TGGPARYVTI SETGGRLGFI TPMTYNFCES CNRVRLTCTG MLYMCLGQND DADLRKALRE 

       310        320        330        340 
SESDEHLSQA IDEAISRKPK GHDFIIDREH NRPSVARHMS LTGG 

« Hide

References

[1]"Whole-genome analyses of speciation events in pathogenic Brucellae."
Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A., Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.
Infect. Immun. 73:8353-8361(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2308.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM040264 Genomic DNA. Translation: CAJ10929.1.
RefSeqYP_414393.1. NC_007618.1.

3D structure databases

ProteinModelPortalQ2YNT7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING359391.BAB1_0973.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ10929; CAJ10929; BAB1_0973.
GeneID3787635.
KEGGbmf:BAB1_0973.
PATRIC17844877. VBIBruMel86222_1015.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2896.
HOGENOMHOG000228680.
KOK03639.
OMAMFHQITG.
OrthoDBEOG64XXNN.

Enzyme and pathway databases

BioCycBABO359391:GKDV-989-MONOMER.
BMEL359391:GJOQ-989-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_BRUA2
AccessionPrimary (citable) accession number: Q2YNT7
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 63 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella abortus strain 2308

Brucella abortus (strain 2308): entries and gene names