Bifunctional purine biosynthesis protein PURH

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O35567 (PUR9_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 86. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Bifunctional purine biosynthesis protein PURH

Including the following 2 domains:

Phosphoribosylaminoimidazolecarboxamide formyltransferase
EC=2.1.2.3
Alternative name(s):
5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
AICAR transformylase
IMP cyclohydrolase
EC=3.5.4.10
Alternative name(s):
ATIC
IMP synthase
Inosinicase

Gene names

Name:	Atic
Synonyms:	Purh

Organism

Rattus norvegicus (Rat) [Reference proteome]

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	592 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis By similarity.
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. IMP + H₂O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
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. Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.
Subunit structure	Homodimer By similarity.
Tissue specificity	Expressed in liver. Ref.1
Domain	The IMP cyclohydrolase activity resides in the N-terminal region.
Sequence similarities	Belongs to the PurH family.

Ontologies

Keywords
Biological process	Purine biosynthesis
Molecular function	Hydrolase Transferase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme Reference proteome
Gene Ontology (GO)
Biological_process	'de novo' IMP biosynthetic process Inferred from direct assay Ref.1. Source: RGD brainstem development Inferred from expression pattern PubMed 7057182. Source: RGD cerebellum development Inferred from expression pattern PubMed 7057182. Source: RGD cerebral cortex development Inferred from expression pattern PubMed 7057182. Source: RGD cobalamin metabolic process Traceable author statement PubMed 3994693. Source: RGD dihydrofolate metabolic process Inferred from direct assay PubMed 8948466. Source: RGD nucleoside metabolic process Inferred from direct assay PubMed 7370986. Source: RGD organ regeneration Inferred from expression pattern Ref.1. Source: RGD response to inorganic substance Inferred from expression pattern PubMed 4078017. Source: RGD tetrahydrofolate biosynthetic process Inferred from direct assay PubMed 7057182. Source: RGD
Cellular_component	mitochondrion Inferred from electronic annotation. Source: Compara
Molecular_function	IMP cyclohydrolase activity Inferred from direct assay Ref.1. Source: RGD phosphoribosylaminoimidazolecarboxamide formyltransferase activity Inferred from direct assay Ref.1. Source: RGD protein homodimerization activity Inferred from sequence or structural similarity. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 592

592

Bifunctional purine biosynthesis protein PURH

PRO_0000270214

Regions

Nucleotide binding

12 – 14

IMP By similarity

Nucleotide binding

34 – 37

IMP By similarity

Nucleotide binding

64 – 67

IMP By similarity

Nucleotide binding

101 – 104

IMP By similarity

Nucleotide binding

125 – 127

IMP By similarity

Region

207 – 208

AICAR binding By similarity

Sites

Active site

137

Proton acceptor Potential

Active site

267

Proton acceptor Probable

Binding site

316

AICAR; via carbonyl oxygen By similarity

Binding site

339

AICAR By similarity

Binding site

431

AICAR; shared with dimeric partner By similarity

Binding site

451

AICAR; shared with dimeric partner By similarity

Binding site

541

AICAR; via carbonyl oxygen; shared with dimeric partner By similarity

Binding site

588

AICAR; shared with dimeric partner By similarity

Site

266

Transition state stabilizer Potential

Amino acid modifications

Modified residue

199

N6-acetyllysine By similarity

Experimental info

Sequence conflict

L → H in BAA22837. Ref.1

Sequences

Sequence

Length

Mass (Da)

Tools

O35567 [UniParc].

Last modified January 9, 2007. Version 2.
Checksum: D9D710794BB12B95
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FASTA

592

64,208

        10         20         30         40         50         60 
MASSQLALFS VSDKTGLVEF ARNLASLGLS LVASGGTAKA IRDAGLAVRD VSELTGFPEM 

        70         80         90        100        110        120 
LGGRVKTLHP AVHAGILARN IPEDAADMAR LDFNLIRVVV CNLYPFVKTV ASPDVTVEAA 

       130        140        150        160        170        180 
VEQIDIGGVT LLRAAAKNHA RVTVVCEPED YGAVAAEMQG SGNKDTSLET RRHLALKAFT 

       190        200        210        220        230        240 
HTAQYDEAIS DYFRRQYSKG ISQMPLRYGM NPHQTPAQLY TLKPKLPITV LNGAPGFINL 

       250        260        270        280        290        300 
CDALNAWQLV TELRGAVDIP AAASFKHVSP AGAAVGVPLS EDEARVCMVY DLYPTLTPLA 

       310        320        330        340        350        360 
IAYARARGAD RMSSFGDFVA LSDVCDVPTA KIISREVSDG IVAPGYEEEA LKILSKKKNG 

       370        380        390        400        410        420 
SYCVLQMDQS YKPDENEVRT LFGLRLSQKR NNGVVDKSLF SNIVTKNKDL PESALRDLIV 

       430        440        450        460        470        480 
ATIAVKYTQS NSVCYAKDGQ VIGIGAGQQS RIHCTRLAGD KANSWWLRHH PRVLSMKFKA 

       490        500        510        520        530        540 
GVKRAEVSNA IDQYVTGTIG EGEDLVKWKA LFEEVPELLT EAEKKEWVDK LSGVSVSSDA 

       550        560        570        580        590 
FFPFRDNVDR AKRSGVAYIV APSGSTADKV VIEACDELGI VLAHTDLRLF HH

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Molecular cloning and expression of a rat cDNA encoding 5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase/IMP cyclohydrolase." Akira T., Komatsu M., Nango R., Tomooka A., Konaka K., Yamauchi M., Kitamura Y., Nomura S., Tsukamoto I. Gene 197:289-293(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Strain: Donryu. Tissue: Liver.
[2]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung.
[3]	Lubec G., Afjehi-Sadat L. Submitted (NOV-2006) to UniProtKB Cited for: PROTEIN SEQUENCE OF 178-194; 531-545 AND 570-588, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Spinal cord.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D89514 mRNA. Translation: BAA22837.1. BC072496 mRNA. Translation: AAH72496.1.
IPI	IPI00393333.
RefSeq	NP_112276.2. NM_031014.2.
UniGene	Rn.15114.
3D structure databases
HSSP	HSSP built from PDB template 1PKX based on UniProtKB P31939.
ProteinModelPortal	O35567.
SMR	O35567. Positions 5-592.
ModBase	Search...
Protein-protein interaction databases
STRING	10116.ENSRNOP00000021105.
Proteomic databases
PaxDb	O35567.
PRIDE	O35567.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSRNOT00000021105; ENSRNOP00000021105; ENSRNOG00000015511.
GeneID	81643.
KEGG	rno:81643.
UCSC	RGD:70879. rat.
Organism-specific databases
CTD	471.
RGD	70879. Atic.
Phylogenomic databases
eggNOG	COG0138.
GeneTree	ENSGT00390000004553.
HOGENOM	HOG000230372.
HOVERGEN	HBG006912.
InParanoid	O35567.
KO	K00602.
OMA	DLLFAWK.
OrthoDB	EOG43BMNG.
Enzyme and pathway databases
UniPathway	UPA00074; UER00133. UPA00074; UER00135.
Gene expression databases
Genevestigator	O35567.
Family and domain databases
Gene3D	1.10.287.440. 1 hit. 3.40.140.20. 3 hits. 3.40.50.1380. 1 hit.
InterPro	IPR024051. AICAR_Tfase_dom. IPR024050. AICAR_Tfase_insert_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...
Other
NextBio	615152.

Entry information

Entry name

PUR9_RAT

Accession

Primary (citable) accession number: O35567
Secondary accession number(s): Q6IN16

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 9, 2007
Last sequence update:	January 9, 2007
Last modified:	April 3, 2013
This is version 86 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 2 domains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents