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P32173

- MOBA_ECOLI

UniProt

P32173 - MOBA_ECOLI

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Protein
Molybdenum cofactor guanylyltransferase
Gene
mobA, chlB, mob, narB, b3857, JW3829
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.4 Publications

Catalytic activityi

GTP + molybdenum cofactor = diphosphate + guanylyl molybdenum cofactor.2 Publications

Cofactori

Magnesium or manganese. Both divalent cations appear to be equally efficient in an vitro reconstitution assay.2 Publications

Kineticsi

  1. KM=6.5 µM for GTP1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei25 – 251GTP
Binding sitei53 – 531GTP
Binding sitei71 – 711GTP
Metal bindingi101 – 1011Magnesium
Binding sitei101 – 1011GTP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 143GTPUniRule annotation

GO - Molecular functioni

  1. GTP binding Source: UniProtKB-HAMAP
  2. guanylyltransferase activity Source: EcoCyc
  3. magnesium ion binding Source: EcoCyc
  4. molybdenum cofactor guanylyltransferase activity Source: UniProtKB-EC
  5. protein binding Source: IntAct

GO - Biological processi

  1. Mo-molybdopterin cofactor biosynthetic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

GTP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdenum cofactor guanylyltransferase (EC:2.7.7.77)
Short name:
MoCo guanylyltransferase
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 namesi
Name:mobA
Synonyms:chlB, mob, narB
Ordered Locus Names:b3857, JW3829
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG11829. mobA.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Disruption phenotypei

Cells lacking this gene are chlorate-resistant, fail to synthesize MGD and accumulate elevated quantities of MPT.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi12 – 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. 1 Publication
Mutagenesisi15 – 151G → L: Complete loss of catalytic activity. Still capable of binding MPT and MGD and interacting with both MoeA and MobB. 1 Publication
Mutagenesisi19 – 191R → A: Slight reduction in catalytic activity. 1 Publication
Mutagenesisi22 – 221G → L: Nearly no effect on catalytic activity. 1 Publication
Mutagenesisi25 – 251K → A: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. 1 Publication
Mutagenesisi78 – 781G → L: Nearly no effect on catalytic activity. 1 Publication
Mutagenesisi79 – 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. 2 Publications
Mutagenesisi82 – 821G → L: Slight reduction in catalytic activity. 1 Publication
Mutagenesisi101 – 1011D → A: Complete loss of catalytic activity. 1 Publication
Mutagenesisi101 – 1011D → N: Marked reduction in catalytic activity. Still capable of interacting with both MoeA and MobB. 1 Publication
Mutagenesisi156 – 1561R → A: Nearly no effect on catalytic activity. 1 Publication
Mutagenesisi180 – 1801N → D: Nearly no effect on catalytic activity. 1 Publication
Mutagenesisi182 – 1821N → D: Nearly no effect on catalytic activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Molybdenum cofactor guanylyltransferaseUniRule annotation
PRO_0000134887Add
BLAST

Proteomic databases

PaxDbiP32173.
PRIDEiP32173.

Expressioni

Inductioni

Is expressed at very low levels under both aerobic and anaerobic growth conditions.1 Publication

Gene expression databases

GenevestigatoriP32173.

Interactioni

Subunit structurei

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.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
moeAP122813EBI-1133881,EBI-554393

Protein-protein interaction databases

DIPiDIP-10233N.
IntActiP32173. 10 interactions.
MINTiMINT-1232345.
STRINGi511145.b3857.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 53
Beta strandi6 – 127
Beta strandi18 – 203
Helixi25 – 273
Beta strandi28 – 303
Helixi35 – 4612
Beta strandi50 – 534
Beta strandi55 – 573
Helixi58 – 625
Beta strandi67 – 693
Helixi79 – 8911
Beta strandi92 – 998
Helixi109 – 1157
Turni116 – 1194
Beta strandi121 – 1266
Beta strandi131 – 1399
Helixi142 – 15110
Helixi157 – 1637
Beta strandi167 – 1704
Turni175 – 1784
Helixi184 – 1885

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP32173.
SMRiP32173. Positions 4-191.

Miscellaneous databases

EvolutionaryTraceiP32173.

Family & Domainsi

Domaini

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.1 Publication

Sequence similaritiesi

Belongs to the MobA family.

Phylogenomic databases

eggNOGiCOG0746.
HOGENOMiHOG000280423.
KOiK03752.
OMAiAISANRH.
OrthoDBiEOG6PKFG0.
PhylomeDBiP32173.

Family and domain databases

Gene3Di3.90.550.10. 1 hit.
HAMAPiMF_00316. MobA.
InterProiIPR025877. MobA-like_NTP_Trfase_dom.
IPR013482. Molybde_CF_guanTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view]
PfamiPF12804. NTP_transf_3. 1 hit.
[Graphical view]
SUPFAMiSSF53448. SSF53448. 1 hit.
TIGRFAMsiTIGR02665. molyb_mobA. 1 hit.

Sequencei

Sequence statusi: Complete.

P32173-1 [UniParc]FASTAAdd to Basket

« Hide

MNLMTTITGV VLAGGKARRM GGVDKGLLEL NGKPLWQHVA DALMTQLSHV    50
VVNANRHQEI YQASGLKVIE DSLADYPGPL AGMLSVMQQE AGEWFLFCPC 100
DTPYIPPDLA ARLNHQRKDA PVVWVHDGER DHPTIALVNR AIEPLLLEYL 150
QAGERRVMVF MRLAGGHAVD FSDHKDAFVN VNTPEELARW QEKR 194
Length:194
Mass (Da):21,643
Last modified:October 1, 1993 - v1
Checksum:iB79B32DD7348DD48
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19201 Genomic DNA. Translation: AAB02992.1.
U00096 Genomic DNA. Translation: AAC76855.1.
AP009048 Genomic DNA. Translation: BAE77451.1.
PIRiS40803.
RefSeqiNP_418294.1. NC_000913.3.
YP_491592.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC76855; AAC76855; b3857.
BAE77451; BAE77451; BAE77451.
GeneIDi12931711.
948349.
KEGGiecj:Y75_p3328.
eco:b3857.
PATRICi32123211. VBIEscCol129921_3966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
L19201 Genomic DNA. Translation: AAB02992.1 .
U00096 Genomic DNA. Translation: AAC76855.1 .
AP009048 Genomic DNA. Translation: BAE77451.1 .
PIRi S40803.
RefSeqi NP_418294.1. NC_000913.3.
YP_491592.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E5K X-ray 1.35 A 1-194 [» ]
1FR9 X-ray 1.65 A 1-194 [» ]
1FRW X-ray 1.75 A 1-194 [» ]
1H4C X-ray 1.65 A 1-194 [» ]
1H4D X-ray 1.74 A 1-194 [» ]
1H4E X-ray 1.65 A 1-194 [» ]
1HJJ X-ray 1.65 A 1-194 [» ]
1HJL X-ray 2.00 A 1-194 [» ]
ProteinModelPortali P32173.
SMRi P32173. Positions 4-191.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-10233N.
IntActi P32173. 10 interactions.
MINTi MINT-1232345.
STRINGi 511145.b3857.

Proteomic databases

PaxDbi P32173.
PRIDEi P32173.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC76855 ; AAC76855 ; b3857 .
BAE77451 ; BAE77451 ; BAE77451 .
GeneIDi 12931711.
948349.
KEGGi ecj:Y75_p3328.
eco:b3857.
PATRICi 32123211. VBIEscCol129921_3966.

Organism-specific databases

EchoBASEi EB1776.
EcoGenei EG11829. mobA.

Phylogenomic databases

eggNOGi COG0746.
HOGENOMi HOG000280423.
KOi K03752.
OMAi AISANRH.
OrthoDBi EOG6PKFG0.
PhylomeDBi P32173.

Enzyme and pathway databases

BioCyci EcoCyc:EG11829-MONOMER.
ECOL316407:JW3829-MONOMER.
MetaCyc:EG11829-MONOMER.

Miscellaneous databases

EvolutionaryTracei P32173.
PROi P32173.

Gene expression databases

Genevestigatori P32173.

Family and domain databases

Gene3Di 3.90.550.10. 1 hit.
HAMAPi MF_00316. MobA.
InterProi IPR025877. MobA-like_NTP_Trfase_dom.
IPR013482. Molybde_CF_guanTrfase.
IPR029044. Nucleotide-diphossugar_trans.
[Graphical view ]
Pfami PF12804. NTP_transf_3. 1 hit.
[Graphical view ]
SUPFAMi SSF53448. SSF53448. 1 hit.
TIGRFAMsi TIGR02665. molyb_mobA. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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.

Entry informationi

Entry nameiMOBA_ECOLI
AccessioniPrimary (citable) accession number: P32173
Secondary accession number(s): Q2M8F5, Q9LBV0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1993
Last sequence update: October 1, 1993
Last modified: June 11, 2014
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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