Phosphoribosylformylglycinamidine cyclo-ligase - Escherichia coli (strain K12)

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Reviewed, UniProtKB/Swiss-Prot P08178 (PUR5_ECOLI)

Last modified February 9, 2010. Version 98. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Phosphoribosylformylglycinamidine cyclo-ligase
    EC=6.3.3.1
Alternative name(s):
    AIRS
    Phosphoribosyl-aminoimidazole synthetase
    AIR synthase

Gene names

Name:	purM
Synonyms:	purG
Ordered Locus Names:	b2499, JW2484

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

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Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Catalytic activity	ATP + 2-(formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole. HAMAP MF_00741
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2. HAMAP MF_00741
Subunit structure	Homodimer. HAMAP MF_00741
Subcellular location	Cytoplasm HAMAP MF_00741.
Sequence similarities	Belongs to the AIR synthase family.

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Ontologies

Keywords
Biological process	Purine biosynthesis
Cellular component	Cytoplasm
Ligand	ATP-binding Nucleotide-binding
Molecular function	Ligase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW phosphoribosylformylglycinamidine cyclo-ligase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed Ref.6

Chain

2 – 345

344

Phosphoribosylformylglycinamidine cyclo-ligase HAMAP MF_00741

PRO_0000148211

Experimental info

Sequence conflict

A → D AA sequence Ref.5

Secondary structure

345

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P08178-1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 8DA61375E8180401
Show »

FASTA

345

36,854

        10         20         30         40         50         60 
MTDKTSLSYK DAGVDIDAGN ALVGRIKGVV KKTRRPEVMG GLGGFGALCA LPQKYREPVL 

        70         80         90        100        110        120 
VSGTDGVGTK LRLAMDLKRH DTIGIDLVAM CVNDLVVQGA EPLFFLDYYA TGKLDVDTAS 

       130        140        150        160        170        180 
AVISGIAEGC LQSGCSLVGG ETAEMPGMYH GEDYDVAGFC VGVVEKSEII DGSKVSDGDV 

       190        200        210        220        230        240 
LIALGSSGPH SNGYSLVRKI LEVSGCDPQT TELDGKPLAD HLLAPTRIYV KSVLELIEKV 

       250        260        270        280        290        300 
DVHAIAHLTG GGFWENIPRV LPDNTQAVID ESSWQWPEVF NWLQTAGNVE HHEMYRTFNC 

       310        320        330        340 
GVGMIIALPA PEVDKALALL NANGENAWKI GIIKASDSEQ RVVIE

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the purM gene encoding 5'-phosphoribosyl-5-aminoimidazole synthetase of Escherichia coli K12." Smith J.M., Daum H.A. III J. Biol. Chem. 261:10632-10636(1986) [PubMed: 3015935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[2]	"Construction of a contiguous 874-kb sequence of the Escherichia coli-K12 genome corresponding to 50.0-68.8 min on the linkage map and analysis of its sequence features." Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T. Horiuchi T. DNA Res. 4:91-113(1997) [PubMed: 9205837] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[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: 9278503] [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: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Purification and characterization of aminoimidazole ribonucleotide synthetase from Escherichia coli." Schrimsher J.L., Schendel F.J., Stubbe J., Smith J.M. Biochemistry 25:4366-4371(1986) [PubMed: 3530323] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, CHARACTERIZATION.
[6]	"Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Link A.J., Robison K., Church G.M. Electrophoresis 18:1259-1313(1997) [PubMed: 9298646] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE OF 2-12. Strain: K12 / EMG2.
[7]	"X-ray crystal structure of aminoimidazole ribonucleotide synthetase (PurM), from the Escherichia coli purine biosynthetic pathway at 2.5-A resolution." Li C., Kappock T.J., Stubbe J., Weaver T.M., Ealick S.E. Structure 7:1155-1166(1999) [PubMed: 10508786] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M13747 Genomic DNA. Translation: AAA83898.1.
U00096 Genomic DNA. Translation: AAC75552.1.
AP009048 Genomic DNA. Translation: BAA16387.1.

PIR

AJECPC. A25955.

RefSeq

AP_003085.1.
NP_416994.1.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CLI	X-ray	2.50	A/B/C/D	2-345	[»]

ModBase

Search...

Protein-protein interaction databases

STRING

P08178.

Genome annotation databases

GeneID

946975.

GenomeReviews

Gene locus JW2484 in contig AP009048_GR.
Gene locus b2499 in contig U00096_GR.

KEGG

ecj:JW2484.
eco:b2499.

Organism-specific databases

EchoBASE

EB0791.

EcoGene

EG10798. purM.

CMR

Search...

Phylogenomic databases

eggNOG

COG0150.

HOGENOM

HBG531222.

OMA

VHGLAHI.

Enzyme and pathway databases

BioCyc

EcoCyc:AIRS-MONOMER.
ECOL168927:B2499-MONOMER.
MetaCyc:AIRS-MONOMER.

Gene expression databases

Genevestigator

P08178.

Family and domain databases

HAMAP

MF_00741_B. AIRS_B.
[Tree]

InterPro

IPR000728. AIR_synth.
IPR010918. AIR_synth_C.
IPR004733. PurM_cligase.
IPR016188. PurM_N-like.
[Graphical view]

Pfam

PF00586. AIRS. 1 hit.
PF02769. AIRS_C. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00878. purM. 1 hit.

ProtoNet

Search...

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Entry information

Entry name

PUR5_ECOLI

Accession

Primary (citable) accession number: P08178

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 98 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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