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B2A242 (MOBA_NATTJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 30. 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:
Probable 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:Nther_1264
OrganismNatranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF) [Complete proteome] [HAMAP]
Taxonomic identifier457570 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Clostridia › Natranaerobiales › Natranaerobiaceae › Natranaerobius ›

Protein attributes

Sequence length205 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.

Subcellular location

Cytoplasm By similarity.

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
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 – 205205Probable molybdenum cofactor guanylyltransferase HAMAP-Rule MF_00316
PRO_1000115804

Regions

Nucleotide binding10 – 123GTP By similarity

Sites

Metal binding1001Magnesium By similarity
Binding site221GTP By similarity
Binding site691GTP By similarity
Binding site1001GTP By similarity

Sequences

Sequence LengthMass (Da)Tools
B2A242 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: 5E11D2ABE7325122

FASTA20523,631
        10         20         30         40         50         60 
MTDNVSAVIL AGGASRRMGT DKSMLKLKGK KMIEIVIESI SDIFDELVIV SNSPEKFDYK 

        70         80         90        100        110        120 
NNDFKVVSDK LTHLKRSSLR GIYTGLTEIS NEYGFIFAGD MPFISPELIK AMISEMRKDK 

       130        140        150        160        170        180 
WDIIIPVISG HYEPLFAVYH KNCHYTMKQQ LLHENFKITD SLKEFKVLEL TDNYCVQYDE 

       190        200 
YLASFFNINT PEDLEQARKY LGKTE

« Hide

References

[1]"Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-LF."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP001034 Genomic DNA. Translation: ACB84847.1.
RefSeqYP_001917435.1. NC_010718.1.

3D structure databases

ProteinModelPortalB2A242.
ModBaseSearch...

Protein-protein interaction databases

STRING457570.Nther_1264.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB84847; ACB84847; Nther_1264.
GeneID6314237.
KEGGnth:Nther_1264.
PATRIC22671194. VBINatThe92436_1299.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0746.
HOGENOMHOG000280425.
KOK03752.
OMAFVQVPVI.

Enzyme and pathway databases

BioCycNTHE457570:GHRL-1309-MONOMER.

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]
ProtoNetSearch...

Entry information

Entry nameMOBA_NATTJ
AccessionPrimary (citable) accession number: B2A242
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 1, 2013
This is version 30 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

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