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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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
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)DescriptionActionsGraphical viewLength
Mutagenesisi49D → A: Loss of activity. 1 Publication1
Mutagenesisi82D → A: Loss of activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001709821 – 195Molybdopterin adenylyltransferaseAdd BLAST195

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 interactors.
DIPiDIP-35784N.
IntActiP0AF03. 9 interactors.
MINTiMINT-1238245.
STRINGi511145.b0009.

Structurei

Secondary structure

1195
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 12Combined sources9
Helixi24 – 35Combined sources12
Beta strandi40 – 49Combined sources10
Helixi51 – 63Combined sources13
Beta strandi68 – 74Combined sources7
Beta strandi77 – 79Combined sources3
Helixi84 – 90Combined sources7
Beta strandi93 – 95Combined sources3
Helixi97 – 108Combined sources12
Helixi112 – 116Combined sources5
Beta strandi121 – 124Combined sources4
Beta strandi127 – 132Combined sources6
Helixi136 – 144Combined sources9
Beta strandi145 – 147Combined sources3
Beta strandi153 – 156Combined sources4
Helixi158 – 161Combined sources4
Helixi162 – 168Combined sources7
Turni178 – 180Combined sources3
Helixi187 – 189Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DI6X-ray1.45A3-195[»]
1DI7X-ray1.60A3-195[»]
ProteinModelPortaliP0AF03.
SMRiP0AF03.
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.
OMAiYQDEGIP.
PhylomeDBiP0AF03.

Family and domain databases

CDDicd00886. MogA_MoaB. 1 hit.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DI6X-ray1.45A3-195[»]
1DI7X-ray1.60A3-195[»]
ProteinModelPortaliP0AF03.
SMRiP0AF03.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4261931. 11 interactors.
DIPiDIP-35784N.
IntActiP0AF03. 9 interactors.
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.
OMAiYQDEGIP.
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

CDDicd00886. MogA_MoaB. 1 hit.
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...

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: November 30, 2016
This is version 97 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.