Q6A6Y8 (PUR9_PROAC) 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:	PPA1747

Organism

Propionibacterium acnes (strain KPA171202 / DSM 16379) [Complete proteome] [HAMAP]

Taxonomic identifier

267747 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Propionibacterineae › Propionibacteriaceae › Propionibacterium › Propionibacterium acnes

Protein attributes

Sequence length	516 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-Rule MF_00139 IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule 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-Rule 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-Rule 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	'de novo' IMP biosynthetic process Inferred from electronic annotation. Source: UniProtKB-UniPathway
Molecular_function	IMP cyclohydrolase activity Inferred from electronic annotation. Source: HAMAP phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 516	516	Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139		PRO_1000057904

Sequences

	Sequence		Length	Mass (Da)
	Q6A6Y8 [UniParc]. Last modified September 13, 2004. Version 1. Checksum: 0A766E14EAF82C21	FASTA	516	54,992
	10 20 30 40 50 60 MSERQPIRRA LVSVYDKSGL DQLAKALIDA QVEVVSTGST AKELASHGVT VTEVSEITGF 70 80 90 100 110 120 PECLDGRVKT LHPKVHAGIL ADRRLTSHRE QLTALEVKPF DLVVCNLYPF AETVAQGGDF 130 140 150 160 170 180 DECIEKIDIG GPSMVRAAAK NHANVAVLTN PDQYEDLARA LSEGGYTMEE RRVLAARAFA 190 200 210 220 230 240 HTAAYDVAVA TWFGSRDGVA VDGVPTFVGT TGELSHPLRY GENSHQAAAV YRSSGEPGLA 250 260 270 280 290 300 GARQLHGKAM SYNNYVDTNS ARRAAFDFEA PCVAVIKHSN PCGIATGSDI AEAHRKAHAC 310 320 330 340 350 360 DSLSAFGGVI ATNRPVSVEM AEQVAEIFTE VVVAPGYEDG AVEILSRKKN IRLLECPAPH 370 380 390 400 410 420 LAGWELRQID GGLLAMETDL FQADGDDPAN WTLAAGDPVD DVTLADLSFA WRACRSVRSN 430 440 450 460 470 480 AILLAHDGAS VGVGMGQVNR VDSCRLAVER AGDRAAGSVA ASDAFFPFAD GPQVLIDAHI 490 500 510 AAIVEPGGSI RDDQTIEVCR TAGVPLYFTG TRHFFH

References

[1]

"The complete genome sequence of Propionibacterium acnes, a commensal of human skin." Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A., Strittmatter A., Hujer S., Duerre P., Gottschalk G. Science 305:671-673(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: KPA171202 / DSM 16379.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE017283 Genomic DNA. Translation: AAT83476.1.
RefSeq	YP_056434.1. NC_006085.1.
3D structure databases
HSSP	HSSP built from PDB template 1G8M based on UniProtKB P31335.
ProteinModelPortal	Q6A6Y8.
ModBase	Search...
Protein-protein interaction databases
STRING	267747.PPA1747.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAT83476; AAT83476; PPA1747.
GeneID	2932978.
KEGG	pac:PPA1747.
PATRIC	23038307. VBIProAcn64440_1803.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG0138.
HOGENOM	HOG000230373.
KO	K00602.
OMA	DLLFAWK.
ProtClustDB	PRK00881.
Enzyme and pathway databases
BioCyc	PACN267747:GHO9-1780-MONOMER.
UniPathway	UPA00074; UER00133. UPA00074; UER00135.
Family and domain databases
Gene3D	3.40.140.20. 2 hits. 3.40.50.1380. 1 hit.
HAMAP	MF_00139. PurH.
InterPro	IPR024051. AICAR_Tfase_dom. IPR002695. AICARFT_IMPCHas. IPR016193. Cytidine_deaminase-like. IPR011607. MGS-like_dom. [Graphical view]
PANTHER	PTHR11692. PTHR11692. 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_PROAC

Accession

Primary (citable) accession number: Q6A6Y8

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 5, 2008
Last sequence update:	September 13, 2004
Last modified:	May 1, 2013
This is version 59 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program