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:	Bcen2424_0691

From

Burkholderia cenocepacia (strain HI2424)

[TaxID: 331272]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., LiPuma J.J., Gonzalez C.F., Konstantinidis K., Tiedje J.M., Richardson P.;
"Complete sequence of chromosome 1 of Burkholderia cenocepacia HI2424.";
Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.

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

CP000458; ABK07444.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_834337.1; -.

3D structure databases

ModBase

A0K4L7.

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

4448040; -.

GenomeReviews

CP000458_GR; Bcen2424_0691.

KEGG

bch:Bcen2424_0691; -.

Phylogenomic databases

HOGENOM

A0K4L7; -.

Genome annotation databases

CMR

A0K4L7; Bcen2424_0691.

Other

ProtoNet

A0K4L7.

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`	`1 521`	`521`		`Bifunctional purine biosynthesis protein purH.`	`PRO_1000018852`

Sequence information

Length: 521 AA [This is the length of the unprocessed precursor]

Molecular weight: 55547 Da [This is the MW of the unprocessed precursor]

CRC64: FDEF1818ED045DEF [This is a checksum on the sequence]

        10         20         30         40         50         60 
MIKQALISVS DKTGIVDFAK SLSDLGVKLL STGGTAKLLA DAGLPVTEVA DYTGFPEMLD 

        70         80         90        100        110        120 
GRVKTLHPKV HGGILARRDL PEHMQALEQH GIPTIDLLVV NLYPFVATIA KDDCTLADAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRSAAKNHRD VTVVVDPADY AVVLDEMKAN GNTVGYPTNF RLATKVFAHT 

       190        200        210        220        230        240 
AQYDGAITNY LTSLTDELKH ASRSTYPATL NLAFDKVQDL RYGENPHQSA AFYRDLATPA 

       250        260        270        280        290        300 
GALANYRQLQ GKELSYNNIA DSDAAWECVK TFDAPACVII KHANPCGVAV GNDSADAYAK 

       310        320        330        340        350        360 
AFQTDPTSAF GGIIAFNREV DEAAAQAVAK QFVEVLIAPS FSDAAKQVFA AKQNVRLLEI 

       370        380        390        400        410        420 
ALGDGHNAFD LKRVGGGLLV QSLDSRNVQP SELRVVTKRQ PTAKEMDDLL FAWRVAKYVK 

       430        440        450        460        470        480 
SNAIVFCGNG MTLGVGAGQM SRVDSARIAS IKAQNAGLTL AGSAVASDAF FPFRDGLDVV 

       490        500        510        520 
VAAGATCVIQ PGGSMRDDEV IAAADEHGIA MVLTGVRHFR H

A0K4L7 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