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Protein

Molybdopterin adenylyltransferase

Gene

mog

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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

Keywordsi

Molecular functionTransferase
Biological processMolybdenum cofactor biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:EG11511-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

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-2DPAGEiP0AF03

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, 17 interactors
DIPiDIP-35784N
IntActiP0AF03, 9 interactors
STRINGi316385.ECDH10B_0009

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
OMAiEYLTSEW
PhylomeDBiP0AF03

Family and domain databases

CDDicd00886 MogA_MoaB, 1 hit
Gene3Di3.40.980.10, 1 hit
InterProiView protein in InterPro
IPR036425 MoaB/Mog-like_dom_sf
IPR001453 MoaB/Mog_dom
IPR008284 MoCF_biosynth_CS
PfamiView protein in Pfam
PF00994 MoCF_biosynth, 1 hit
SMARTiView protein in SMART
SM00852 MoCF_biosynth, 1 hit
SUPFAMiSSF53218 SSF53218, 1 hit
TIGRFAMsiTIGR00177 molyb_syn, 1 hit
PROSITEiView protein in PROSITE
PS01078 MOCF_BIOSYNTHESIS_1, 1 hit

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
PATRICifig|1411691.4.peg.2274

Similar proteinsi

Entry informationi

Entry nameiMOG_ECOLI
AccessioniPrimary (citable) accession number: P0AF03
Secondary accession number(s): P28694, Q8KMY3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 20, 2005
Last sequence update: December 20, 2005
Last modified: March 28, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

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