Q81IP9 (PUR9_BACCR) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
   EC=2.1.2.3
   Alternative name(s):
   AICAR transformylase
2. IMP cyclohydrolase
   EC=3.5.4.10
   Alternative name(s):
   ATIC
   IMP synthase
   Inosinicase

Gene names

Name:	purH
Ordered Locus Names:	BC_0333

Organism

Bacillus cereus (strain ATCC 14579 / DSM 31)

Taxonomic identifier

226900 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length	511 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (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. HAMAP MF_00139 IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP MF_00139
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. HAMAP MF_00139 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. HAMAP MF_00139
Sequence similarities	Belongs to the PurH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
Technical term	Complete proteome Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological process	purine nucleotide biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: EC phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 511	511	Bifunctional purine biosynthesis protein PurH HAMAP MF_00139		PRO_1000018840

Sequences

	Sequence		Length	Mass (Da)
	Q81IP9 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 35601DD0B3417010	FASTA	511	55,574
	10 20 30 40 50 60 MKKRALVSVS DKTGVVEFVK GLLEQGIEVI STGGTKKLLE ENGLQVIGIS EVTGFPEIMD 70 80 90 100 110 120 GRVKTLHPNI HGGLLAVRDN ETHVTQMNEL GMEPIDFVVV NLYPFKETIA KPDVTFADAI 130 140 150 160 170 180 ENIDIGGPTM IRSAAKNHKF VSVIVDPVDY DIVLAELKEN GEVAEETKRK LAAKVFRHTA 190 200 210 220 230 240 AYDALISNYL TEQMGEESPE TLTVTFEKKQ DLRYGENPHQ KATFYKAPFA ATSSVAYAEQ 250 260 270 280 290 300 LHGKELSYNN INDADAALSI VKEFTEPAVV AVKHMNPCGV GVGTDIHEAY TRAYEADPVS 310 320 330 340 350 360 IFGGIIAANR EIDKATAEKL HEIFLEIVIA PSFSQEALEV LQSKKNLRLL TINIEKATSA 370 380 390 400 410 420 SKKLTSVQGG LLVQEEDTLS LDESTISIPT KREPSEQEWK DLKLAWKVVK HVKSNAIVLA 430 440 450 460 470 480 KDDMTIGVGA GQMNRVGSAK IAITQAGEKA QGSALASDAF FPMPDTLEEA AKAGITAIIQ 490 500 510 PGGSIRDEDS IKVADTYGIA MVFTGVRHFK H

References

[1]

"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis." Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C. Nature 423:87-91(2003) [PubMed: 12721630] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 14579 / DSM 31.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE016877 Genomic DNA. Translation: AAP07373.1.
RefSeq	NP_830172.1. NC_004722.1.
3D structure databases
HSSP	HSSP built from PDB template 1PKX based on UniProtKB P31939.
ProteinModelPortal	Q81IP9.
ModBase	Search...
Protein-protein interaction databases
STRING	Q81IP9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBBACT00000032644; EBBACP00000031850; EBBACG00000032635.
GeneID	1202686.
GenomeReviews	Gene locus BC_0333 in contig AE016877_GR.
KEGG	bce:BC0333.
PATRIC	32596296. VBIBacCer54481_0305.
Phylogenomic databases
eggNOG	COG0138.
GeneTree	EBGT00050000002320.
HOGENOM	HBG498048.
OMA	FTGTRHF.
PhylomeDB	Q81IP9.
ProtClustDB	PRK00881.
Enzyme and pathway databases
BioCyc	BCER226900:BC_0333-MONOMER.
Family and domain databases
HAMAP	MF_00139. PurH. [Tree]
InterPro	IPR024051. AICAR_Tfase_dom. IPR002695. AICARFT_IMPCHas. IPR016193. Cytidine_deaminase-like. IPR011607. MGS-like_dom. [Graphical view]
Gene3D	G3DSA:3.40.140.20. G3DSA:3.40.140.20. 2 hits. G3DSA:3.40.50.1380. MGS-like_dom. 1 hit.
KO	K00602.
PANTHER	PTHR11692. AICARFT_IMPCHas. 1 hit.
Pfam	PF01808. AICARFT_IMPCHas. 1 hit. PF02142. MGS. 1 hit. [Graphical view]
PIRSF	PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMART	SM00798. AICARFT_IMPCHas. 1 hit. SM00851. MGS. 1 hit. [Graphical view]
SUPFAM	SSF53927. Cytidine_deaminase-like. 1 hit. SSF52335. MGS-like_dom. 1 hit.
TIGRFAMs	TIGR00355. PurH. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_BACCR

Accession

Primary (citable) accession number: Q81IP9

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	June 1, 2003
Last modified:	January 25, 2012
This is version 55 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program