Reviewed, UniProtKB/Swiss-Prot Q46480 (PUR9_CHRVI)

Names and origin

Protein names

Recommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC

Gene names

Name:

purH

Organism

Chromatium vinosum (Allochromatium vinosum)

Taxonomic identifier

1049 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Chromatiales › Chromatiaceae › Allochromatium

Protein attributes

Sequence length	78 AA.
Sequence status	Fragment.
Sequence processing	The displayed sequence is not processed.
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.
Sequence similarities	Belongs to the purH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
Technical term	Multifunctional enzyme
Gene Ontology (GO)
Biological process	IMP biosynthetic process Inferred from electronic annotation. Source: InterPro
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 – 78	›78	Bifunctional purine biosynthesis protein purH HAMAP MF_00139		PRO_0000192083
Experimental info
	Non-terminal residue	1	1

Sequences

	Sequence		Length	Mass (Da)
	Q46480-1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 62A1B9008138B610	FASTA	78	8,096
	10 20 30 40 50 60 NSARIAAIKA EHAGLTVAGS VMASDAFFPF RDGIDQAAAA GIKAVIQPGG SMRDAEVIAA 70 ANEHGMAMVF TGMRHFRH

References

[1]	Chen Y.L., Knaff D.B. Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: ATCC 17899 / DSM 180 / D.

Cross-references

Sequence databases
EMBLGenBankDDBJ	L76417 Genomic DNA. Translation: AAB02978.1.
3D structure databases
HSSP	HSSP built from PDB template 1G8M based on UniProtKB P31335.
ModBase	Search...
Enzyme and pathway databases
BRENDA	2.1.2.3. 2799. 3.5.4.10. 2799.
Family and domain databases
HAMAP	MF_00139. [Tree]
InterPro	IPR002695. AICARFT_IMPCHas. [Graphical view]
PANTHER	PTHR11692. AICARFT_IMPCHas. 1 hit.
ProtoNet	Search...

Entry information

Entry name

PUR9_CHRVI

Accession

Primary (citable) accession number: Q46480

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	November 1, 1996
Last modified:	January 20, 2009
This is version 43 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)