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:	blr0581

From

Bradyrhizobium japonicum

[TaxID: 375]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Bradyrhizobiaceae; Bradyrhizobium.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=USDA 110;
DOI=10.1093/dnares/9.6.189; PubMed=12597275 [NCBI, ExPASy, EBI, Israel, Japan]
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110.";
DNA Res. 9:189-197(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

BA000040; BAC45846.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_767221.1; -.

3D structure databases

HSSP

P31335; 1G8M. [HSSP ENTRY / PDB]

ModBase

Q89WU7.

Enzyme and pathway databases

BioCyc

BJAP224911:BLR0581-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.

TIGR00355; purH; 1.

Genome annotation databases

GeneID

1049554; -.

GenomeReviews

BA000040_GR; blr0581.

KEGG

bja:blr0581; -.

NMPDR

fig|224911.1.peg.581; -.

Phylogenomic databases

HOGENOM

Q89WU7; -.

Genome annotation databases

CMR

Q89WU7; blr0581.

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`	`1 530`	`530`		`Bifunctional purine biosynthesis protein purH.`	`PRO_0000192073`

Sequence information

Length: 530 AA [This is the length of the unprocessed precursor]

Molecular weight: 56465 Da [This is the MW of the unprocessed precursor]

CRC64: A7DD03550120605C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTDHPRRVTR ALLSVSDKTG LIEFAKALAA HDVELVSTGG TAKAIAAAGL KVKDVSELTG 

        70         80         90        100        110        120 
FPEMMDGRVK TLHPKVHGGL LAIRDNKDHA DAMKAHGIAP IDLLVVNLYP FEATVDKGAG 

       130        140        150        160        170        180 
FEDCIENIDI GGPAMIRAAA KNHDDVAVVV EAEDYKAVLD ELAANKGATT LKLRRRLAAK 

       190        200        210        220        230        240 
AYARTAAYDA AISNWFNRQL EIDAPDFRAF GGKLIQSLRY GENPHQTAAF YATPDKRPGV 

       250        260        270        280        290        300 
STARQLQGKE LSYNNINDTD AAYECIGEFD AKRTAACVIV KHANPCGVAE GSDLVSAYRK 

       310        320        330        340        350        360 
ALACDSTSAF GGIIAMNRAL DADTAREITK IFTEVIIAPD ASEEAIAIIG ARKNLRLLLA 

       370        380        390        400        410        420 
GSLPDPRAPG LTAKTVAGGL LVQSRDNAVV DDMTFKVVTK RAPTDAEMRD LKFAFRVAKH 

       430        440        450        460        470        480 
VKSNTIIYAK DLATVGIGAG QMSRVDSARI AARKAQDAAV ELKLAEPLTK GSVVASDAFF 

       490        500        510        520        530 
PFADGMLACI EAGATAVVQP GGSMRDDEVI KAADEHGIAM VFTGTRHFRH

Q89WU7 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