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:	BR1816

From

Brucella suis

[TaxID: 29461]

[HAMAP proteome]

Taxonomy

Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; Brucellaceae; Brucella.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=1330 / Biovar 1;
DOI=10.1073/pnas.192319099; PubMed=12271122 [NCBI, ExPASy, EBI, Israel, Japan]
Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F., Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J., Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E., Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L., Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
"The Brucella suis genome reveals fundamental similarities between animal and plant pathogens and symbionts.";
Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(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

AE014291; AAN30711.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_698796.1; -.

3D structure databases

HSSP

P31335; 1G8M. [HSSP ENTRY / PDB]

ModBase

P67540.

Enzyme and pathway databases

BioCyc

BSUI204722:BR_1816-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

P67540.

Genome annotation databases

1167509; -.

AE014291_GR; BR1816.

bms:BR1816; -.

BR1816; -.

Phylogenomic databases

HOGENOM

P67540; -.

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`	`1 538`	`538`		`Bifunctional purine biosynthesis protein purH.`	`PRO_0000192075`

Sequence information

Length: 538 AA [This is the length of the unprocessed precursor]

Molecular weight: 56481 Da [This is the MW of the unprocessed precursor]

CRC64: 099349D5160AC19F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MAVSSKHIPA PDLHRVRRAL LSVSDKTGLI DFAKALHANG VEILSTGGTA KSIAAAGIPV 

        70         80         90        100        110        120 
KDVSEITGFP EIMDGRVKTL HPAVHGGLLA VRNDPEHVAA MEEHGIGGID LAVINLYPFE 

       130        140        150        160        170        180 
EVRFKGGDYD TTVENIDIGG PAMIRASAKN HAYVATVVDP ADYADVVAEL EKHSGSLPLA 

       190        200        210        220        230        240 
FRKKLAAKAF SRTAAYDAAI SNWFAEAIDE ETPTYRAVAG KLHSVMRYGE NPHQTAGFYL 

       250        260        270        280        290        300 
TGEKRPGVAT ATQLQGKQLS YNNINDTDAA FELVAEFDPA RTAAVAIIKH ANPCGVAEAS 

       310        320        330        340        350        360 
TIKEAYLKAL ACDPVSAFGG IVALNRTLDE EAAEEIVKTF TEVIIAPDAT EGAQAIVAAK 

       370        380        390        400        410        420 
KNLRLLVTGG LPDPRAKGIA AKTVAGGLLV QSRDNGVVDD LDLKVVTKRA PTEAELNDLK 

       430        440        450        460        470        480 
FAFRVGKHVK SNAIVYVKDG ATVGIGAGQM SRVDSARIAA RKAEDAAEAA GLAAPLTKGC 

       490        500        510        520        530 
VVASDAFFPF ADGLLSAVEA GATAVIQPGG SMRDDEVIAA ADEHGIAMVM TGMRHFRH

P67540 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

	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