P15639 (PUR9_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
   EC=2.1.2.3
   Alternative name(s):
   AICAR transformylase
2. IMP cyclohydrolase
   EC=3.5.4.10
   Alternative name(s):
   ATIC
   IMP synthase
   Inosinicase

Gene names

Name:	purH
Ordered Locus Names:	b4006, JW3970

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	529 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Catalytic activity	10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP MF_00139 IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP MF_00139
Pathway	Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP MF_00139 Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
Domain	The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP MF_00139
Sequence similarities	Belongs to the PurH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 529	529	Bifunctional purine biosynthesis protein PurH HAMAP MF_00139		PRO_0000192091
Amino acid modifications
	Modified residue	287	1	N6-acetyllysine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	P15639 [UniParc]. Last modified April 1, 1990. Version 1. Checksum: DC034ED01915DA68	FASTA	529	57,329
	10 20 30 40 50 60 MQQRRPVRRA LLSVSDKAGI VEFAQALSAR GVELLSTGGT ARLLAEKGLP VTEVSDYTGF 70 80 90 100 110 120 PEMMDGRVKT LHPKVHGGIL GRRGQDDAIM EEHQIQPIDM VVVNLYPFAQ TVAREGCSLE 130 140 150 160 170 180 DAVENIDIGG PTMVRSAAKN HKDVAIVVKS SDYDAIIKEM DDNEGSLTLA TRFDLAIKAF 190 200 210 220 230 240 EHTAAYDSMI ANYFGSMVPA YHGESKEAAG RFPRTLNLNF IKKLDMRYGE NSHQQAAFYI 250 260 270 280 290 300 EENVKEASVA TATQVQGKAL SYNNIADTDA ALECVKEFAE PACVIVKHAN PCGVAIGNSI 310 320 330 340 350 360 LDAYDRAYKT DPTSAFGGII AFNRELDAET AQAIISRQFV EVIIAPSASE EALKITAAKQ 370 380 390 400 410 420 NVRVLTCGQW GERVPGLDFK RVNGGLLVQD RDLGMVGAEE LRVVTKRQPS EQELRDALFC 430 440 450 460 470 480 WKVAKFVKSN AIVYAKNNMT IGIGAGQMSR VYSAKIAGIK AADEGLEVKG SSMASDAFFP 490 500 510 520 FRDGIDAAAA AGVTCVIQPG GSIRDDEVIA AADEHGIAML FTDMRHFRH

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence analysis of genes purH and purD involved in the de novo purine nucleotide biosynthesis of Escherichia coli." Aiba A., Mizobuchi K. J. Biol. Chem. 264:21239-21246(1989) [PubMed: 2687276] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Purine biosynthesis in Escherichia coli K12: structure and DNA sequence studies of the purHD locus." Flannigan K.A., Hennigan S.H., Vogelbacker H.H., Gots J.S., Smith J.M. Mol. Microbiol. 4:381-392(1990) [PubMed: 2192230] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12.
[3]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"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.
[5]	"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.
[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: PROTEIN SEQUENCE OF 1-12. Strain: K12 / EMG2.
[7]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-287, MASS SPECTROMETRY. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	J05126 Genomic DNA. Translation: AAA24454.1. X51950 Genomic DNA. Translation: CAA36212.1. U00006 Genomic DNA. Translation: AAC43104.1. U00096 Genomic DNA. Translation: AAC76980.1. AP009048 Genomic DNA. Translation: BAE77313.1.
PIR	DTECPH. B34193.
RefSeq	NP_418434.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P15639.
SMR	P15639. Positions 3-529.
ModBase	Search...
Protein-protein interaction databases
IntAct	P15639. 7 interactions.
2D gel databases
SWISS-2DPAGE	P15639.
Proteomic databases
PRIDE	P15639.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000001658; EBESCP00000001658; EBESCG00000001369. EBESCT00000016179; EBESCP00000015470; EBESCG00000015239.
GeneID	948503.
GenomeReviews	Gene locus JW3970 in contig AP009048_GR. Gene locus b4006 in contig U00096_GR.
KEGG	ecj:JW3970. eco:b4006.
PATRIC	32123537. VBIEscCol129921_4121.
Organism-specific databases
EchoBASE	EB0788.
EcoGene	EG10795. purH.
Phylogenomic databases
eggNOG	COG0138.
GeneTree	EBGT00050000010057.
HOGENOM	HBG498048.
OMA	FTGTRHF.
PhylomeDB	P15639.
ProtClustDB	PRK00881.
Enzyme and pathway databases
BioCyc	EcoCyc:AICARTRANSIMPCYCLO-CPLX. MetaCyc:AICARTRANSIMPCYCLO-CPLX.
Gene expression databases
Genevestigator	P15639.
Family and domain databases
HAMAP	MF_00139. PurH. [Tree]
InterPro	IPR024051. AICAR_Tfase_dom. IPR002695. AICARFT_IMPCHas. IPR016193. Cytidine_deaminase-like. IPR011607. MGS-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits. G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
KO	K00602.
PANTHER	PTHR11692. AICARFT_IMPCHas. 1 hit.
Pfam	PF01808. AICARFT_IMPCHas. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PIRSF	PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMART	SM00798. AICARFT_IMPCHas. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit. SSF52335. MGS-like_dom. 1 hit.
TIGRFAMs	TIGR00355. PurH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_ECOLI

Accession

Primary (citable) accession number: P15639
Secondary accession number(s): Q2M8U3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1990
Last sequence update:	April 1, 1990
Last modified:	January 25, 2012
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program