Phosphoribosylaminoimidazolecarboxamide formyltransferase
     (EC 2.1.2.3)
     (AICAR transformylase)
IMP cyclohydrolase
     (EC 3.5.4.10)
     (Inosinicase)
     (IMP synthetase)
     (ATIC)

Gene name

	Name:	purH
	OrderedLocusNames:	Cj0953c

From

Campylobacter jejuni

[TaxID: 197]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales; Campylobacteraceae; Campylobacter.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=NCTC 11168 / Serotype O:2;
DOI=10.1038/35001088; PubMed=10688204 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences.";
Nature 403:665-668(2000).

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.
CATALYTIC ACTIVITY: IMP + H₂O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
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 .
PATHWAY: 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).
SIMILARITY: Belongs to the purH family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AL111168; CAL35073.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

PIR

H81369; H81369.

3D structure databases

HSSP

P31335; 1G8M. [HSSP ENTRY / PDB]

ModBase

Q9PNY2.

Protein-protein interaction databases

IntAct

Q9PNY2; -.

Enzyme and pathway databases

BioCyc

CJEJ192222:CJ0953C-MON; -.

Ontologies

GO:0003937;	Molecular function: IMP cyclohydrolase activity (inferred from electronic annotation from HAMAP).
GO:0004643;	Molecular function: phosphoribosylaminoimidazolecarboxamide formyltransferase activity (inferred from electronic annotation from HAMAP).
GO:0006188;	Biological process: IMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00139; -; 1.
PBIL [Tree]

InterPro

IPR002695; AICARFT_IMPCHas.
IPR013982; AICARFT_IMPCHas_formly.
IPR011607; MGS.
Graphical view of domain structure.

PANTHER

PTHR11692; AICARFT_IMPCHas; 1.

Pfam

PF01808; AICARFT_IMPCHas; 1.
PF02142; MGS; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000414; AICARFT_IMPCHas; 1.

SMART

SM00798; AICARFT_IMPCHas; 1.
SMART graphical view of domain structure.

TIGRFAMs

TIGR00355; purH; 1.

ProtoNet

Q9PNY2.

Genome annotation databases

GenomeReviews

AL111168_GR; Cj0953c.

KEGG

cje:Cj0953c; -.

CMR

Q9PNY2; Cj0953c.

Other

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Hydrolase; Multifunctional enzyme; Purine biosynthesis; Transferase.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 510`	`510`		`Bifunctional purine biosynthesis protein purH.`	`PRO_0000192079`

Sequence information

Length: 510 AA [This is the length of the unprocessed precursor]

Molecular weight: 56402 Da [This is the MW of the unprocessed precursor]

CRC64: 56F356F04B3A2092 [This is a checksum on the sequence]

        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

Q9PNY2 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools