Q0SV48 (PUR9_CLOPS) 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:	CPR_0675

Organism

Clostridium perfringens (strain SM101 / Type A) [Complete proteome] [HAMAP]

Taxonomic identifier

289380 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Clostridia › Clostridiales › Clostridiaceae › Clostridium

Protein attributes

Sequence length	501 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
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 – 501	501	Bifunctional purine biosynthesis protein PurH HAMAP MF_00139		PRO_1000018881

Sequences

	Sequence		Length	Mass (Da)
	Q0SV48 [UniParc]. Last modified September 5, 2006. Version 1. Checksum: BE889F267E4A911D	FASTA	501	56,108
	10 20 30 40 50 60 MKKRALISVF DKDGVLELAK FLRDRDVEII SSGGTYKYLK ENNIEVKEIS EITDFPEMLD 70 80 90 100 110 120 GRVKTLHPLV HAGILAIRDN KEHMKTLEKR EINTIDYVVV NLYPFFEKVR ENLSFEEKVE 130 140 150 160 170 180 FIDIGGPTML RAAAKNFKDV VVLSDKKDYE KVMNEIKENN CVSFKLRKTL AGKVFNLMSA 190 200 210 220 230 240 YDAAISNFLL EGEEEYPEYL SVSYKKIQDL RYGENPHQGA AYYSSTEFDG AMNSFEILNG 250 260 270 280 290 300 KALSYNNIKD LDIAWKVACE FEETACCALK HNTPCGVAVG ENSKEVYLKA YDADPVSIFG 310 320 330 340 350 360 GIVAINRKID KATAEEMVKI FLEVVAAPDF DEDALEVLRT KKNLRVIKCK NTPQAKNYMV 370 380 390 400 410 420 TVDGGILVQG EDNKLANEYK VVTKKEPTEM ELRDMIFGMK VVKYVKSNAI VVVKDGVATG 430 440 450 460 470 480 IGGGQVNRIW ATKEALERGK GGAVLASDAF FPFRDCVDEA AKNGIKAIIQ PGGSIRDEES 490 500 VEACNEHGIS MVFTGVRHFK H

References

[1]

"Skewed genomic variability in strains of the toxigenic bacterial pathogen, Clostridium perfringens." Myers G.S.A., Rasko D.A., Cheung J.K., Ravel J., Seshadri R., DeBoy R.T., Ren Q., Varga J., Awad M.M., Brinkac L.M., Daugherty S.C., Haft D.H., Dodson R.J., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Khouri H. , Dimitrov G.I., Watkins K.L., Mulligan S., Benton J., Radune D., Fisher D.J., Atkins H.S., Hiscox T., Jost B.H., Billington S.J., Songer J.G., McClane B.A., Titball R.W., Rood J.I., Melville S.B., Paulsen I.T. Genome Res. 16:1031-1040(2006) [PubMed: 16825665] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: SM101 / Type A.

Cross-references

Sequence databases
EMBL GenBank DDBJ	CP000312 Genomic DNA. Translation: ABG87320.1.
RefSeq	YP_698002.1. NC_008262.1.
3D structure databases
ProteinModelPortal	Q0SV48.
ModBase	Search...
Protein-protein interaction databases
STRING	Q0SV48.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
GeneID	4206513.
GenomeReviews	Gene locus CPR_0675 in contig CP000312_GR.
KEGG	cpr:CPR_0675.
PATRIC	19489641. VBICloPer122123_0652.
TIGR	CPR_0675.
Phylogenomic databases
eggNOG	COG0138.
HOGENOM	HBG498048.
OMA	FTGTRHF.
ProtClustDB	PRK00881.
Enzyme and pathway databases
BioCyc	CPER289380:CPR_0675-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_CLOPS

Accession

Primary (citable) accession number: Q0SV48

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 15, 2008
Last sequence update:	September 5, 2006
Last modified:	January 25, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program