P0AF03 (MOG_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Molybdopterin adenylyltransferase
Short name=MPT adenylyltransferase
EC=2.7.7.75

Gene names

Name:	mog
Synonyms:	chlG, mogA, yaaG
Ordered Locus Names:	b0009, JW0008

Organism

Escherichia coli (strain K12) [Reference proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia › Escherichia coli

Protein attributes

Sequence length	195 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Catalyzes the adenylation of molybdopterin as part of the biosynthesis of the molybdenum-cofactor. Ref.6
Catalytic activity	ATP + molybdopterin = diphosphate + adenylyl-molybdopterin.
Pathway	Cofactor biosynthesis; molybdopterin biosynthesis.
Subunit structure	Homotrimer. Interacts with MoeA and MobB in vivo. Ref.5 Ref.7
Sequence similarities	Belongs to the MoaB/Mog family.

Ontologies

Keywords
Biological process	Molybdenum cofactor biosynthesis
Ligand	ATP-binding Nucleotide-binding
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	Mo-molybdopterin cofactor biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW transferase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 195

195

Molybdopterin adenylyltransferase

PRO_0000170982

Experimental info

Mutagenesis

49

1

D → A: Loss of activity. Ref.7

Mutagenesis

82

1

D → A: Loss of activity. Ref.7

Secondary structure

1

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195

Helix Strand Turn

Details...

Beta strand

4 – 12

9

Helix

24 – 35

12

Beta strand

40 – 49

10

Helix

51 – 63

13

Beta strand

68 – 74

7

Beta strand

77 – 79

3

Helix

84 – 90

7

Beta strand

93 – 95

3

Helix

97 – 108

12

Helix

112 – 116

5

Beta strand

121 – 124

4

Beta strand

127 – 132

6

Helix

136 – 144

9

Beta strand

145 – 147

3

Beta strand

153 – 156

4

Helix

158 – 161

4

Helix

162 – 168

7

Turn

178 – 180

3

Helix

187 – 189

3

Sequences

	Sequence		Length	Mass (Da)
	P0AF03 [UniParc]. Last modified December 20, 2005. Version 1. Checksum: 3610EBDB4BE97872	FASTA	195	21,222
	10 20 30 40 50 60 MNTLRIGLVS ISDRASSGVY QDKGIPALEE WLTSALTTPF ELETRLIPDE QAIIEQTLCE 70 80 90 100 110 120 LVDEMSCHLV LTTGGTGPAR RDVTPDATLA VADREMPGFG EQMRQISLHF VPTAILSRQV 130 140 150 160 170 180 GVIRKQALIL NLPGQPKSIK ETLEGVKDAE GNVVVHGIFA SVPYCIQLLE GPYVETAPEV 190 VAAFRPKSAR RDVSE

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"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 277:1453-1474(1997) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X67700 Genomic DNA. Translation: CAA47930.1.
U00096 Genomic DNA. Translation: AAC73120.1.
AP009048 Genomic DNA. Translation: BAB96587.2.

PIR

B56688.

RefSeq

NP_414550.1. NC_000913.2.
YP_488315.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DI6	X-ray	1.45	A	3-195	[»]
1DI7	X-ray	1.60	A	3-195	[»]

ProteinModelPortal

P0AF03.

SMR

P0AF03. Positions 3-191.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35784N.

IntAct

P0AF03. 7 interactions.

MINT

MINT-1238245.

STRING

511145.b0009.

2D gel databases

SWISS-2DPAGE

P0AF03.

Proteomic databases

PaxDb

P0AF03.

PRIDE

P0AF03.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

AAC73120; AAC73120; b0009.
BAB96587; BAB96587; BAB96587.

GeneID

12932937.
944760.

KEGG

ecj:Y75_p0009.
eco:b0009.

PATRIC

32115113. VBIEscCol129921_0008.

Organism-specific databases

EchoBASE

EB1473.

EcoGene

EG11511. mog.

Phylogenomic databases

eggNOG

COG0521.

HOGENOM

HOG000281103.

KO

K03831.

OMA

VKAFRPK.

ProtClustDB

PRK09417.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11511-MONOMER.
ECOL316407:JW0008-MONOMER.
MetaCyc:EG11511-MONOMER.

UniPathway

UPA00344.

Gene expression databases

Genevestigator

P0AF03.

Family and domain databases

Gene3D

3.40.980.10. 1 hit.

InterPro

IPR020817. Mo_cofactor_synthesis.
IPR008284. MoCF_biosynth_CS.
IPR001453. Mopterin-bd_dom.
[Graphical view]

Pfam

PF00994. MoCF_biosynth. 1 hit.
[Graphical view]

SMART

SM00852. MoCF_biosynth. 1 hit.
[Graphical view]

SUPFAM

SSF53218. MoCF_biosynth. 1 hit.

TIGRFAMs

TIGR00177. molyb_syn. 1 hit.

PROSITE

PS01078. MOCF_BIOSYNTHESIS_1. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P0AF03.

Entry information

Entry name

MOG_ECOLI

Accession

Primary (citable) accession number: P0AF03
Secondary accession number(s): P28694, Q8KMY3

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 20, 2005
Last sequence update:	December 20, 2005
Last modified:	May 1, 2013
This is version 72 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program