Reviewed, UniProtKB/Swiss-Prot Q9PNY2 (PUR9_CAMJE)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC

Gene names

Name:	purH
Ordered Locus Names:	Cj0953c

Organism

Campylobacter jejuni [Complete proteome] [HAMAP]

Taxonomic identifier

197 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Epsilonproteobacteria › Campylobacterales › Campylobacteraceae › Campylobacter

Protein attributes

Sequence length	510 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

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
Technical term	Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
Molecular function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 510	510	Bifunctional purine biosynthesis protein purH HAMAP MF_00139		PRO_0000192079

Sequences

	Sequence		Length	Mass (Da)
	Q9PNY2-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: 56F356F04B3A2092	FASTA	510	56,402
	10 20 30 40 50 60 MRALLSVSDK EGIVEFGKEL ENLGFEILST GGTFKLLKEN GIKVIEVSDF TKSPELFEGR 70 80 90 100 110 120 VKTLHPKIHG GILHKRSDEN HIKQAKENEI LGIDLVCVNL YPFKKTTIMS DDFDEIIENI 130 140 150 160 170 180 DIGGPAMIRS AAKNYKDVMV LCDPLDYEKV IETLKKGQND ENFRLNLMIK AYEHTANYDA 190 200 210 220 230 240 YIANYMNERF NGGFGASKFI VGQKVFDTKY GENPHQKGAL YEFDAFFSAN FKALKGEASF 250 260 270 280 290 300 NNLTDINAAL NLASSFDKAP AIAIVKHGNP CGFAIKENLV QSYIHALKCD SVSAYGGVVA 310 320 330 340 350 360 INGTLDEALA NKINEIYVEV IIAANVDEKA LAVFEGKKRI KIFTQESPFL IRSFDKYDFK 370 380 390 400 410 420 HIDGGFVYQN SDEVGEDELK NAKLMSQREA SKEELKDLEI AMKIAAFTKS NNVVYVKNGA 430 440 450 460 470 480 MVAIGMGMTS RIDAAKAAIA KAKEMGLDLQ GCVLASEAFF PFRDSIDEAS KVGVKAIVEP 490 500 510 GGSIRDDEVV KAADEYGMAL YFTGVRHFLH

References

[1]

"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences." Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. , van Vliet A.H.M., Whitehead S., Barrell B.G. Nature 403:665-668(2000) [PubMed: 10688204] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AL111168 Genomic DNA. Translation: CAL35073.1.
PIR	H81369.
RefSeq	YP_002344351.1.
3D structure databases
SMR	Q9PNY2. Positions 2-510.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9PNY2. 1 interaction.
Genome annotation databases
GeneID	905247.
GenomeReviews	Gene locus Cj0953c in contig AL111168_GR.
KEGG	cje:Cj0953c.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG498048.
OMA	VVKHVKS.
Enzyme and pathway databases
BioCyc	CJEJ192222:CJ0953C-MONOMER.
BRENDA	2.1.2.3. 255835. 3.5.4.10. 255835.
Family and domain databases
HAMAP	MF_00139. PurH. [Tree]
InterPro	IPR002695. AICARFT_IMPCHas. IPR013982. AICARFT_IMPCHase_bienz. IPR011607. MGS. [Graphical view]
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]
TIGRFAMs	TIGR00355. purH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_CAMJE

Accession

Primary (citable) accession number: Q9PNY2
Secondary accession number(s): Q0P9U6

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2003
Last sequence update:	October 1, 2000
Last modified:	February 9, 2010
This is version 51 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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