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Protein

Molybdopterin adenylyltransferase

Gene

mog

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor.1 Publication

Catalytic activityi

ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.

Pathwayi: molybdopterin biosynthesis

This protein is involved in the pathway molybdopterin biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway molybdopterin biosynthesis and in Cofactor biosynthesis.

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc
  • molybdopterin adenylyltransferase activity Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Molybdenum cofactor biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11511-MONOMER.
ECOL316407:JW0008-MONOMER.
MetaCyc:EG11511-MONOMER.
BRENDAi2.7.7.75. 2026.
UniPathwayiUPA00344.

Names & Taxonomyi

Protein namesi
Recommended name:
Molybdopterin adenylyltransferase (EC:2.7.7.75)
Short name:
MPT adenylyltransferase
Gene namesi
Name:mog
Synonyms:chlG, mogA, yaaG
Ordered Locus Names:b0009, JW0008
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11511. mog.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi49 – 491D → A: Loss of activity. 1 Publication
Mutagenesisi82 – 821D → A: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 195195Molybdopterin adenylyltransferasePRO_0000170982Add
BLAST

Proteomic databases

EPDiP0AF03.
PaxDbiP0AF03.
PRIDEiP0AF03.

2D gel databases

SWISS-2DPAGEP0AF03.

Interactioni

Subunit structurei

Homotrimer. Interacts with MoeA and MobB in vivo.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4261931. 11 interactions.
DIPiDIP-35784N.
IntActiP0AF03. 9 interactions.
MINTiMINT-1238245.
STRINGi511145.b0009.

Structurei

Secondary structure

1
195
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 129Combined sources
Helixi24 – 3512Combined sources
Beta strandi40 – 4910Combined sources
Helixi51 – 6313Combined sources
Beta strandi68 – 747Combined sources
Beta strandi77 – 793Combined sources
Helixi84 – 907Combined sources
Beta strandi93 – 953Combined sources
Helixi97 – 10812Combined sources
Helixi112 – 1165Combined sources
Beta strandi121 – 1244Combined sources
Beta strandi127 – 1326Combined sources
Helixi136 – 1449Combined sources
Beta strandi145 – 1473Combined sources
Beta strandi153 – 1564Combined sources
Helixi158 – 1614Combined sources
Helixi162 – 1687Combined sources
Turni178 – 1803Combined sources
Helixi187 – 1893Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DI6X-ray1.45A3-195[»]
1DI7X-ray1.60A3-195[»]
ProteinModelPortaliP0AF03.
SMRiP0AF03. Positions 3-191.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0AF03.

Family & Domainsi

Sequence similaritiesi

Belongs to the MoaB/Mog family.Curated

Phylogenomic databases

eggNOGiENOG4108RIR. Bacteria.
COG0521. LUCA.
HOGENOMiHOG000281103.
InParanoidiP0AF03.
KOiK03831.
OMAiAAVPYCL.
OrthoDBiEOG6SV58B.
PhylomeDBiP0AF03.

Family and domain databases

Gene3Di3.40.980.10. 1 hit.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 1 hit.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0AF03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNTLRIGLVS ISDRASSGVY QDKGIPALEE WLTSALTTPF ELETRLIPDE
60 70 80 90 100
QAIIEQTLCE LVDEMSCHLV LTTGGTGPAR RDVTPDATLA VADREMPGFG
110 120 130 140 150
EQMRQISLHF VPTAILSRQV GVIRKQALIL NLPGQPKSIK ETLEGVKDAE
160 170 180 190
GNVVVHGIFA SVPYCIQLLE GPYVETAPEV VAAFRPKSAR RDVSE
Length:195
Mass (Da):21,222
Last modified:December 20, 2005 - v1
Checksum:i3610EBDB4BE97872
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67700 Genomic DNA. Translation: CAA47930.1.
U00096 Genomic DNA. Translation: AAC73120.1.
AP009048 Genomic DNA. Translation: BAB96587.2.
PIRiB56688.
RefSeqiNP_414550.1. NC_000913.3.
WP_001295414.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73120; AAC73120; b0009.
BAB96587; BAB96587; BAB96587.
GeneIDi944760.
KEGGiecj:JW0008.
eco:b0009.
PATRICi32115113. VBIEscCol129921_0008.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X67700 Genomic DNA. Translation: CAA47930.1.
U00096 Genomic DNA. Translation: AAC73120.1.
AP009048 Genomic DNA. Translation: BAB96587.2.
PIRiB56688.
RefSeqiNP_414550.1. NC_000913.3.
WP_001295414.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DI6X-ray1.45A3-195[»]
1DI7X-ray1.60A3-195[»]
ProteinModelPortaliP0AF03.
SMRiP0AF03. Positions 3-191.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261931. 11 interactions.
DIPiDIP-35784N.
IntActiP0AF03. 9 interactions.
MINTiMINT-1238245.
STRINGi511145.b0009.

2D gel databases

SWISS-2DPAGEP0AF03.

Proteomic databases

EPDiP0AF03.
PaxDbiP0AF03.
PRIDEiP0AF03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73120; AAC73120; b0009.
BAB96587; BAB96587; BAB96587.
GeneIDi944760.
KEGGiecj:JW0008.
eco:b0009.
PATRICi32115113. VBIEscCol129921_0008.

Organism-specific databases

EchoBASEiEB1473.
EcoGeneiEG11511. mog.

Phylogenomic databases

eggNOGiENOG4108RIR. Bacteria.
COG0521. LUCA.
HOGENOMiHOG000281103.
InParanoidiP0AF03.
KOiK03831.
OMAiAAVPYCL.
OrthoDBiEOG6SV58B.
PhylomeDBiP0AF03.

Enzyme and pathway databases

UniPathwayiUPA00344.
BioCyciEcoCyc:EG11511-MONOMER.
ECOL316407:JW0008-MONOMER.
MetaCyc:EG11511-MONOMER.
BRENDAi2.7.7.75. 2026.

Miscellaneous databases

EvolutionaryTraceiP0AF03.
PROiP0AF03.

Family and domain databases

Gene3Di3.40.980.10. 1 hit.
InterProiIPR001453. MoaB/Mog_dom.
IPR008284. MoCF_biosynth_CS.
[Graphical view]
PfamiPF00994. MoCF_biosynth. 1 hit.
[Graphical view]
SMARTiSM00852. MoCF_biosynth. 1 hit.
[Graphical view]
SUPFAMiSSF53218. SSF53218. 1 hit.
TIGRFAMsiTIGR00177. molyb_syn. 1 hit.
PROSITEiPS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Five open reading frames upstream of the dnaK gene of E. coli."
    James R., Dean D.O., Debbage J.
    DNA Seq. 3:327-332(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
    Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
    Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  4. "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], SEQUENCE REVISION.
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  5. "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.
  6. "In vitro molybdenum ligation to molybdopterin using purified components."
    Nichols J.D., Rajagopalan K.V.
    J. Biol. Chem. 280:7817-7822(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS MPT ADENYLYL TRANSFERASE.
  7. "Crystal structure of the gephyrin-related molybdenum cofactor biosynthesis protein MogA from Escherichia coli."
    Liu M.T.W., Wuebbens M.M., Rajagopalan K.V., Schindelin H.
    J. Biol. Chem. 275:1814-1822(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS), SUBUNIT, MUTAGENESIS OF ASP-49 AND ASP-82.

Entry informationi

Entry nameiMOG_ECOLI
AccessioniPrimary (citable) accession number: P0AF03
Secondary accession number(s): P28694, Q8KMY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 16, 2016
This is version 93 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, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.