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P32173 (MOBA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 121. 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·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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 biosynthesis protein A
Molybdopterin-guanine dinucleotide synthase
Short name=MGD synthase
Protein FA
Gene names
Name:mobA
Synonyms:chlB, mob, narB
Ordered Locus Names:b3857, JW3829
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Is also involved in the biosynthesis of the bis-MGD form of the Moco cofactor (Mo-bisMGD) in which the metal is symmetrically ligated by the dithiolene groups of two MGD molecules. Is necessary and sufficient for the in vitro activation of the DMSOR molybdoenzyme that uses the Mo-bisMGD form of molybdenum cofactor, which implies formation and efficient insertion of the cofactor into the enzyme without the need of a chaperone. Is specific for GTP since other nucleotides such as ATP and GMP can not be utilized. Ref.5 Ref.6 Ref.7 Ref.9

Catalytic activity

GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor. Ref.7 Ref.9

Cofactor

Magnesium or manganese. Both divalent cations appear to be equally efficient in an vitro reconstitution assay. Ref.7 Ref.10

Subunit structure

Monomer. An equilibrium exists between a monomeric and oligomeric form of the enzyme, which could be an octamer; whether this oligomeric arrangement is of functional relevance is unclear. Interacts with MoeA and MobB in vivo. Ref.5 Ref.8 Ref.10

Subcellular location

Cytoplasm HAMAP-Rule MF_00316.

Induction

Is expressed at very low levels under both aerobic and anaerobic growth conditions. Ref.4

Domain

The N-terminal domain determines nucleotide recognition and specific binding, while the C-terminal domain determines the specific binding to the target protein. When the N-terminal domain of MobA is fused to the C-terminal domain of MocA, comparable kinetic constants as wild-type MobA are obtained with GTP, and the activity with CTP is completely lost. Consistent results are obtained when the N-terminal domain of MocA is fused to the C-terminal domain of MobA: the kinetic constants with CTP are comparable with the ones found for wild-type MocA, although no activity with GTP is detected. Ref.9

Disruption phenotype

Cells lacking this gene are chlorate-resistant, fail to synthesize MGD and accumulate elevated quantities of MPT. Ref.6

Sequence similarities

Belongs to the MobA family.

Biophysicochemical properties

Kinetic parameters:

KM=6.5 µM for GTP Ref.9

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

moeAP122813EBI-1133881,EBI-554393

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Molybdenum cofactor guanylyltransferase HAMAP-Rule MF_00316
PRO_0000134887

Regions

Nucleotide binding12 – 143GTP HAMAP-Rule MF_00316

Sites

Metal binding1011Magnesium
Binding site251GTP
Binding site531GTP
Binding site711GTP
Binding site1011GTP

Experimental info

Mutagenesis12 – 143LAG → TAA: 7.5-fold decrease in affinity for GTP and nearly no effect on catalytic activity. Displays a 3-fold decrease in activity with GTP and gains a low activity with CTP as substrate; when associated with 79-LLTS-82. Ref.9
Mutagenesis151G → L: Complete loss of catalytic activity. Still capable of binding MPT and MGD and interacting with both MoeA and MobB. Ref.12
Mutagenesis191R → A: Slight reduction in catalytic activity. Ref.12
Mutagenesis221G → L: Nearly no effect on catalytic activity. Ref.12
Mutagenesis251K → A: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. Ref.12
Mutagenesis781G → L: Nearly no effect on catalytic activity. Ref.12
Mutagenesis79 – 824PLAG → LLTS: 11-fold decrease in affinity for GTP and nearly no effect on catalytic activity. Displays a 3-fold decrease in activity with GTP and gains a low activity with CTP as substrate; when associated with 12-TAA-14. Ref.9 Ref.12
Mutagenesis821G → L: Slight reduction in catalytic activity. Ref.12
Mutagenesis1011D → A: Complete loss of catalytic activity. Ref.12
Mutagenesis1011D → N: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. Ref.12
Mutagenesis1561R → A: Nearly no effect on catalytic activity. Ref.12
Mutagenesis1801N → D: Nearly no effect on catalytic activity. Ref.12
Mutagenesis1821N → D: Nearly no effect on catalytic activity. Ref.12

Secondary structure

....................................... 194
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P32173 [UniParc].

Last modified October 1, 1993. Version 1.
Checksum: B79B32DD7348DD48

FASTA19421,643
        10         20         30         40         50         60 
MNLMTTITGV VLAGGKARRM GGVDKGLLEL NGKPLWQHVA DALMTQLSHV VVNANRHQEI 

        70         80         90        100        110        120 
YQASGLKVIE DSLADYPGPL AGMLSVMQQE AGEWFLFCPC DTPYIPPDLA ARLNHQRKDA 

       130        140        150        160        170        180 
PVVWVHDGER DHPTIALVNR AIEPLLLEYL QAGERRVMVF MRLAGGHAVD FSDHKDAFVN 

       190 
VNTPEELARW QEKR 

« Hide

References

« Hide 'large scale' references
[1]"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes."
Plunkett G. III, Burland V., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 21:3391-3398(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[2]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]"The mob locus of Escherichia coli K12 required for molybdenum cofactor biosynthesis is expressed at very low levels."
Iobbi-Nivol C., Palmer T., Whitty P.W., McNairn E., Boxer D.H.
Microbiology 141:1663-1671(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], INDUCTION.
Strain: K12.
[5]"Isolation of protein FA, a product of the mob locus required for molybdenum cofactor biosynthesis in Escherichia coli."
Palmer T., Vasishta A., Whitty P.W., Boxer D.H.
Eur. J. Biochem. 222:687-692(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-5, FUNCTION IN MGD BIOSYNTHESIS, SUBUNIT.
[6]"Molybdenum cofactor biosynthesis in Escherichia coli. Requirement of the chlB gene product for the formation of molybdopterin guanine dinucleotide."
Johnson J.L., Indermaur L.W., Rajagopalan K.V.
J. Biol. Chem. 266:12140-12145(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN MGD BIOSYNTHESIS, DISRUPTION PHENOTYPE.
Strain: RK4353.
[7]"Mechanism of assembly of the bis(molybdopterin guanine dinucleotide)molybdenum cofactor in Rhodobacter sphaeroides dimethyl sulfoxide reductase."
Temple C.A., Rajagopalan K.V.
J. Biol. Chem. 275:40202-40210(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN BIS(MGD) AND MGD BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[8]"In vivo interactions between gene products involved in the final stages of molybdenum cofactor biosynthesis in Escherichia coli."
Magalon A., Frixon C., Pommier J., Giordano G., Blasco F.
J. Biol. Chem. 277:48199-48204(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MOEA AND MOBB.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]"Molybdopterin dinucleotide biosynthesis in Escherichia coli: identification of amino acid residues of molybdopterin dinucleotide transferases that determine specificity for binding of guanine or cytosine nucleotides."
Neumann M., Seduk F., Iobbi-Nivol C., Leimkuhler S.
J. Biol. Chem. 286:1400-1408(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, DOMAIN, MUTAGENESIS OF 12-LEU--GLY-14 AND 79-PRO--GLY-82.
[10]"The crystal structure of the Escherichia coli MobA protein provides insight into molybdopterin guanine dinucleotide biosynthesis."
Lake M.W., Temple C.A., Rajagopalan K.V., Schindelin H.
J. Biol. Chem. 275:40211-40217(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH MN-GTP, COFACTOR, SUBUNIT.
Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[11]"Crystal structure of the molybdenum cofactor biosynthesis protein MobA from Escherichia coli at near-atomic resolution."
Stevenson C.E., Sargent F., Buchanan G., Palmer T., Lawson D.M.
Structure 8:1115-1125(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
Strain: K12.
[12]"Biochemical and structural analysis of the molybdenum cofactor biosynthesis protein MobA."
Guse A., Stevenson C.E., Kuper J., Buchanan G., Schwarz G., Giordano G., Magalon A., Mendel R.R., Lawson D.M., Palmer T.
J. Biol. Chem. 278:25302-25307(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF MUTANTS ALA-19; LEU-22; ASN-101; ASP-180 AND ASP-182, MUTAGENESIS OF GLY-15; ARG-19; GLY-22; LYS-25; GLY-78; GLY-82; ASP-101; ARG-156; ASN-180 AND ASN-182.
Strain: K12.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L19201 Genomic DNA. Translation: AAB02992.1.
U00096 Genomic DNA. Translation: AAC76855.1.
AP009048 Genomic DNA. Translation: BAE77451.1.
PIRS40803.
RefSeqNP_418294.1. NC_000913.3.
YP_491592.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E5KX-ray1.35A1-194[»]
1FR9X-ray1.65A1-194[»]
1FRWX-ray1.75A1-194[»]
1H4CX-ray1.65A1-194[»]
1H4DX-ray1.74A1-194[»]
1H4EX-ray1.65A1-194[»]
1HJJX-ray1.65A1-194[»]
1HJLX-ray2.00A1-194[»]
ProteinModelPortalP32173.
SMRP32173. Positions 4-191.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-10233N.
IntActP32173. 10 interactions.
MINTMINT-1232345.
STRING511145.b3857.

Proteomic databases

PaxDbP32173.
PRIDEP32173.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC76855; AAC76855; b3857.
BAE77451; BAE77451; BAE77451.
GeneID12931711.
948349.
KEGGecj:Y75_p3328.
eco:b3857.
PATRIC32123211. VBIEscCol129921_3966.

Organism-specific databases

EchoBASEEB1776.
EcoGeneEG11829. mobA.

Phylogenomic databases

eggNOGCOG0746.
HOGENOMHOG000280423.
KOK03752.
OMAACDEERE.
OrthoDBEOG6PKFG0.
ProtClustDBPRK00317.

Enzyme and pathway databases

BioCycEcoCyc:EG11829-MONOMER.
ECOL316407:JW3829-MONOMER.
MetaCyc:EG11829-MONOMER.

Gene expression databases

GenevestigatorP32173.

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...

Other

EvolutionaryTraceP32173.
PROP32173.

Entry information

Entry nameMOBA_ECOLI
AccessionPrimary (citable) accession number: P32173
Secondary accession number(s): Q2M8F5, Q9LBV0
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: March 19, 2014
This is version 121 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene