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:	BUsg_032

From

Buchnera aphidicola subsp. Schizaphis graminum

[TaxID: 98794]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Buchnera.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1126/science.1071278; PubMed=12089438 [NCBI, ExPASy, EBI, Israel, Japan]
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
"50 million years of genomic stasis in endosymbiotic bacteria.";
Science 296:2376-2379(2002).

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

AE013218; AAM67603.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_660392.1; -.

3D structure databases

HSSP

P31335; 1G8M. [HSSP ENTRY / PDB]

ModBase

Q8KA70.

Enzyme and pathway databases

BioCyc

BAPH198804:BUSG032-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.

Genome annotation databases

GeneID

1005848; -.

GenomeReviews

AE013218_GR; BUsg_032.

KEGG

bas:BUsg032; -.

Phylogenomic databases

HOGENOM

Q8KA70; -.

Genome annotation databases

CMR

Q8KA70; BUsg_032.

Other

ProtoNet

Q8KA70.

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`	`1 526`	`526`		`Bifunctional purine biosynthesis protein purH.`	`PRO_0000192077`

Sequence information

Length: 526 AA [This is the length of the unprocessed precursor]

Molecular weight: 59422 Da [This is the MW of the unprocessed precursor]

CRC64: 7F0F13954EF902A5 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSLNNIIKNA LVSLSDKTDL LKISKILAEK KINLFCTGGT ADVLKKNKIP VLEISDYTNF 

        70         80         90        100        110        120 
PEIMNGRLKT LHPKIIGGIL GRREKDQKIM KLHNLIPIDI VIVNFYPFEK IQNRKEFTIE 

       130        140        150        160        170        180 
EIIDNIDIGG PTLVRAAAKN YKDVIVIVDL SDFTSCIQLI NTNTVSLETR FDLATKAFKY 

       190        200        210        220        230        240 
TALYEEIISK YFLKKNPYRK KHQKNIFPNE FQLNFIKKQD LRYGENQHQK SSFYIEKEIL 

       250        260        270        280        290        300 
KSGTISSSNQ IQGKNLSYNN ICDADIALEC VKEFSKPTCV IVKHGNPCGV SESNSLIKAY 

       310        320        330        340        350        360 
FSAYNADPIS AFGGIIAFNC LLDLDTAQEI VKKQFVEVII APEIDEMAVK ILKRKKNIRL 

       370        380        390        400        410        420 
LICGKIEKNK KGLDFKRITN GLLIQEYDCD EINAKNFDFV TNRLPTEKEL EDAIFSWKVA 

       430        440        450        460        470        480 
KFVKSNAIVY SLNKTTIGIG AGQTSRIDAT KLANLKVKDR NHNNTTGATM ASDAFFPFRD 

       490        500        510        520 
GIDNAALIGI SCIIQPGGSI RDKEVIESAN EHNISMIFTK KRHFKH

Q8KA70 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