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:	AM1_5779

From

Acaryochloris marina (strain MBIC 11017)

[TaxID: 329726]

[HAMAP proteome]

Taxonomy

Bacteria; Cyanobacteria; Acaryochloris.

Protein existence

3: Inferred from homology;

References

[1]

NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1073/pnas.0709772105; PubMed=18252824 [NCBI, ExPASy, EBI, Israel, Japan]
Swingley W.D., Chen M., Cheung P.C., Conrad A.L., Dejesa L.C., Hao J., Honchak B.M., Karbach L.E., Kurdoglu A., Lahiri S., Mastrian S.D., Miyashita H., Page L., Ramakrishna P., Satoh S., Sattley W.M., Shimada Y., Taylor H.L., Tomo T., Tsuchiya T., Wang Z.T., Raymond J., Mimuro M., Blankenship R.E., Touchman J.W.;
"Niche adaptation and genome expansion in the chlorophyll d-producing cyanobacterium Acaryochloris marina.";
Proc. Natl. Acad. Sci. U.S.A. 105:2005-2010(2008).

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

CP000828; ABW30724.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001520043.1; -.

3D structure databases

ModBase

B0BZH9.

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).
QuickGo view.

Family and domain databases

HAMAP

MF_00139; -; 1.
PBIL [Tree]

InterPro

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

PANTHER

PTHR11692; AICARFT_IMPCHas; 1.

PIRSF

PIRSF000414; AICARFT_IMPCHas; 1.

SMART

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

TIGR00355; purH; 1.

Genome annotation databases

GeneID

5684566; -.

GenomeReviews

CP000828_GR; AM1_5779.

KEGG

amr:AM1_5779; -.

CMR

B0BZH9; AM1_5779.

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`	`1 524`	`524`		`Bifunctional purine biosynthesis protein purH.`	`PRO_1000076472`

Sequence information

Length: 524 AA [This is the length of the unprocessed precursor]

Molecular weight: 55848 Da [This is the MW of the unprocessed precursor]

CRC64: E979D0DFD30BA415 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MTRLALLSTS DKTGLVELAQ QLVNEYGFTL VSSGGTAVTI EKAGLPVTKV SDYTGSPEIL 

        70         80         90        100        110        120 
GGRVKTLHPR IHGGILARRS LESDVQDLTE NNIQGIDLVV VNLYPFEETI AKQKAQGITD 

       130        140        150        160        170        180 
PDQALADAVE QIDIGGPTMI RAAAKNHAHV TVLCDPQQYA SYLQELKHGE GETSLPFRQA 

       190        200        210        220        230        240 
CALKVFERMA SYDRAIATHL RQSLATTDSQ TQLSILGTAK QTLRYGENPH QNAVWYQESD 

       250        260        270        280        290        300 
TASGWAAAQQ LQGKELSYNN LVDLEAARRV IAEFAQAETQ PTVAILKHNN PCGVAQGETL 

       310        320        330        340        350        360 
LQAYEKALAA DSVSAFGGIV AMNRAIDTDT AQVLTKTFLE CIVAPECQPE AAAVLQAKSN 

       370        380        390        400        410        420 
LRVLVLPDLV SGPAVTVKAI AGGWLAQAAD ETLTPPADWQ IVTQAKPTEA QLAELLFAWK 

       430        440        450        460        470        480 
VVKHVKSNAI VVTKDHTTLG VGAGQMNRVG SVNIALQQAG EKAQGGTLAS DGFFPFDDSV 

       490        500        510        520 
RTAAAAGITA IIQPGGSIRD KDSIQAADEL GIVMAFTGTR HFLH

B0BZH9 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