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O68799 (MOBA_PSEAE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 74. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Molybdenum cofactor guanylyltransferase

Short name=MoCo guanylyltransferase
EC=2.7.7.77
Alternative name(s):
GTP:molybdopterin guanylyltransferase
Mo-MPT guanylyltransferase
Molybdopterin guanylyltransferase
Molybdopterin-guanine dinucleotide synthase
Short name=MGD synthase
Gene names
Name:mobA
Ordered Locus Names:PA3030
OrganismPseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228) [Reference proteome] [HAMAP]
Taxonomic identifier208964 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length198 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo-MPT) cofactor (Moco or molybdenum cofactor) to form Mo-molybdopterin guanine dinucleotide (Mo-MGD) cofactor By similarity. HAMAP-Rule MF_00316

Catalytic activity

GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor. HAMAP-Rule MF_00316

Cofactor

Magnesium By similarity. HAMAP-Rule MF_00316

Subunit structure

Monomer By similarity. HAMAP-Rule MF_00316

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00316.

Domain

The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein By similarity. HAMAP-Rule MF_00316

Sequence similarities

Belongs to the MobA family.

Ontologies

Keywords
   Biological processMolybdenum cofactor biosynthesis
   Cellular componentCytoplasm
   LigandGTP-binding
Magnesium
Metal-binding
Nucleotide-binding
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processMo-molybdopterin cofactor biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionGTP binding

Inferred from electronic annotation. Source: HAMAP

guanylyltransferase activity

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 198198Molybdenum cofactor guanylyltransferase HAMAP-Rule MF_00316
PRO_0000134899

Regions

Nucleotide binding14 – 163GTP By similarity

Sites

Metal binding1031Magnesium By similarity
Binding site271GTP By similarity
Binding site731GTP By similarity
Binding site1031GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
O68799 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 6E2AE65FE3464BBA

FASTA19821,870
        10         20         30         40         50         60 
MPDSALPPCS ILLLAGGRGQ RMGGRDKGLI EWQGLPLIAH LHRLVRPLTD DLIVSCNRNQ 

        70         80         90        100        110        120 
ERYAAYADRV VSDDSRDFPG PLAGIRAGLA VARHPWLLVL PCDAPRIDRA LLETLLQAAG 

       130        140        150        160        170        180 
RTPARPWMLR CGGQWEPLFS LIPTHLAEEI EHAWRQGDRS PRHVLLPLGA EAIELAAGDP 

       190 
RLANLNTPEL LANHRELK 

« Hide

References

« Hide 'large scale' references
[1]"Identification of a cytochrome c precursor gene in Pseudomonas aeruginosa."
Kerschen J., Hassett D.J., Rowe J.J.
Submitted (MAR-1998) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.
[2]"Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic pathogen."
Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P., Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M., Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y., Brody L.L., Coulter S.N., Folger K.R. expand/collapse author list , Kas A., Larbig K., Lim R.M., Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.
Nature 406:959-964(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF053982 Genomic DNA. Translation: AAC15714.1.
AE004091 Genomic DNA. Translation: AAG06418.1.
PIRE83266.
RefSeqNP_251720.1. NC_002516.2.

3D structure databases

ProteinModelPortalO68799.
SMRO68799. Positions 12-192.
ModBaseSearch...

Protein-protein interaction databases

STRING208964.PA3030.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID882980.
KEGGpae:PA3030.
PATRIC19840619. VBIPseAer58763_3179.

Organism-specific databases

PseudoCAPPA3030.

Phylogenomic databases

eggNOGCOG0746.
HOGENOMHOG000280423.
KOK03752.
OMANTPELLS.
ProtClustDBPRK00317.

Family and domain databases

HAMAPMF_00316. MobA.
InterProIPR025877. MobA-like_NTP_Trfase_dom.
IPR013482. Molybde_CF_guanTrfase.
[Graphical view]
PfamPF12804. NTP_transf_3. 1 hit.
[Graphical view]
TIGRFAMsTIGR02665. molyb_mobA. 1 hit.
ProtoNetSearch...

Entry information

Entry nameMOBA_PSEAE
AccessionPrimary (citable) accession number: O68799
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: August 1, 1998
Last modified: May 1, 2013
This is version 74 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