NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/ng.2007.38; PubMed=18037886 [NCBI, ExPASy, EBI, Israel, Japan]
Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G., Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
"Genomic analysis of Bartonella identifies type IV secretion systems as host adaptability factors.";
Nat. Genet. 39:1469-1476(2007).

Comments

CATALYTIC ACTIVITY: ATP + 2-(formamido)-N¹-(5-phospho-D-ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D-ribosyl)imidazole.
PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/5 .
SUBCELLULAR LOCATION: Cytoplasm (By similarity).
SIMILARITY: Belongs to the AIR synthase 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

AM260525; CAK01703.1; -; Genomic_DNA.

[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

YP_001609698.1; -.

3D structure databases

ModBase

A9IVF6.

Ontologies

GO:0005737;	Cellular component: cytoplasm (inferred from electronic annotation from HAMAP).
GO:0004641;	Molecular function: phosphoribosylformylglycinamidine cyclo-ligase activity (inferred from electronic annotation from HAMAP).
GO:0006189;	Biological process: 'de novo' IMP biosynthetic process (inferred from electronic annotation from InterPro).
QuickGo view.

Family and domain databases

HAMAP

MF_00741; -; 1.
PBIL [Tree]

InterPro

IPR004733; PurM_cligase.
Graphical view of domain structure.

TIGRFAMs

TIGR00878; purM; 1.

Genome annotation databases

GeneID

5830178; -.

GenomeReviews

AM260525_GR; BT1341.

CMR

A9IVF6; BT1341.

Other

ProtoNet

A9IVF6.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Cytoplasm; Ligase; Purine biosynthesis.

Features

Feature table viewer

`Key`	`From To`	`Length`		`Description`	`FTId`
`CHAIN`	`1 363`	`363`		`Phosphoribosylformylglycinamidine cyclo-ligase.`	`PRO_1000083450`

Sequence information

Length: 363 AA [This is the length of the unprocessed precursor]

Molecular weight: 38539 Da [This is the MW of the unprocessed precursor]

CRC64: 215D535BE70E7D3A [This is a checksum on the sequence]

        10         20         30         40         50         60 
MSNQDLINNK SKAGLTYAKA GVNIDMGNAM VEKIKPFIRA TKRAGADAEI GGFGGLFDLK 

        70         80         90        100        110        120 
AAGFTDPILV AANDGVGTKL KIAIEVGHHN TVGIDLVAMC VNDLLVQGAE PLFFLDYFAT 

       130        140        150        160        170        180 
GKLDPEQGAA IVSGIAEGCK QSGAALIGGE TAEMPGMYAE GDYDLAGFAV GACERSMLLP 

       190        200        210        220        230        240 
SKNLTEGDII LGLSASGIHS NGFSLVRRII EQNDLKWNDP APFDPSNNLG VALLTPTRIY 

       250        260        270        280        290        300 
VKSLLPIMRK YEGVKALAHI TGGGFLENIP RVIPSSLCAE INLSTINVPS VFSWIAKQGK 

       310        320        330        340        350        360 
IEETEMLRTF NCGIGMIIIV GQHTAEAVTQ ALEKNGETVT PLGILTKRQD QNKGILYRGV 


LHL

A9IVF6 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