Skip Header

Contribute Send feedback
Read comments (?) or add your own

P69848 (MOAA_STAA8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 51. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Molybdenum cofactor biosynthesis protein A
Gene names
Name:moaA
Ordered Locus Names:SAOUHSC_02536
OrganismStaphylococcus aureus (strain NCTC 8325)
Taxonomic identifier93061 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Staphylococcus

Protein attributes

Sequence length340 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Together with MoaC, is involved in the conversion of a guanosine derivative (5'-GTP) into molybdopterin precursor Z By similarity.

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 MF_01225_B

Subunit structure

Monomer and homodimer By similarity. HAMAP MF_01225_B

Sequence similarities

Belongs to the radical SAM superfamily. MoaA family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 340340Molybdenum cofactor biosynthesis protein A HAMAP MF_01225_B
PRO_0000152995

Regions

Region266 – 2683GTP binding By similarity

Sites

Metal binding241Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding281Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding311Iron-sulfur 1 (4Fe-4S-S-AdoMet) By similarity
Metal binding2611Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Metal binding2641Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Metal binding2781Iron-sulfur 2 (4Fe-4S-substrate) By similarity
Binding site171GTP By similarity
Binding site301S-adenosyl-L-methionine By similarity
Binding site711GTP By similarity
Binding site751S-adenosyl-L-methionine; via carbonyl oxygen By similarity
Binding site1021GTP By similarity
Binding site1261S-adenosyl-L-methionine By similarity
Binding site1631GTP By similarity
Binding site1971S-adenosyl-L-methionine; via amide nitrogen and carbonyl oxygen By similarity

Secondary structure

1 ............................................................ 340
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P69848 [UniParc].

Last modified May 24, 2005. Version 1.
Checksum: BDCDFE1014E98306

FASTA34039,078
        10         20         30         40         50         60 
MVEQIKDKLG RPIRDLRLSV TDRCNFRCDY CMPKEVFGDD FVFLPKNELL TFDEMARIAK 

        70         80         90        100        110        120 
VYAELGVKKI RITGGEPLMR RDLDVLIAKL NQIDGIEDIG LTTNGLLLKK HGQKLYDAGL 

       130        140        150        160        170        180 
RRINVSLDAI DDTLFQSINN RNIKATTILE QIDYATSIGL NVKVNVVIQK GINDDQIIPM 

       190        200        210        220        230        240 
LEYFKDKHIE IRFIEFMDVG NDNGWDFSKV VTKDEMLTMI EQHFEIDPVE PKYFGEVAKY 

       250        260        270        280        290        300 
YRHKDNGVQF GLITSVSQSF CSTCTRARLS SDGKFYGCLF ATVDGFNVKA FIRSGVTDEE 

       310        320        330        340 
LKEQFKALWQ IRDDRYSDER TAQTVANRQR KKINMNYIGG

« Hide

References

[1]"The Staphylococcus aureus NCTC8325 genome."
Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 8325.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000253 Genomic DNA. Translation: ABD31551.1.
RefSeqYP_501000.1. NC_007795.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2FB2X-ray2.25A/B1-340[»]
2FB3X-ray2.35A/B1-340[»]
ProteinModelPortalP69848.
SMRP69848. Positions 3-329.
ModBaseSearch...

Protein-protein interaction databases

STRINGP69848.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBSTAT00000029112; EBSTAP00000028063; EBSTAG00000029110.
GeneID3921126.
GenomeReviewsGene locus SAOUHSC_02536 in contig CP000253_GR.
KEGGsao:SAOUHSC_02536.
PATRIC19582362. VBIStaAur99865_2287.

Phylogenomic databases

eggNOGCOG2896.
GeneTreeEBGT00050000024402.
HOGENOMHBG529885.
OMATFRRMND.
ProtClustDBCLSK885853.

Enzyme and pathway databases

BioCycSAUR93061:SAOUHSC_02536-MONOMER.

Family and domain databases

HAMAPMF_01225_B. MoaA_B.
[Tree]
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]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK03639.
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_STAA8
AccessionPrimary (citable) accession number: P69848
Secondary accession number(s): Q2FVY5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 24, 2005
Last sequence update: May 24, 2005
Last modified: January 25, 2012
This is version 51 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents