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P31335 (PUR9_CHICK) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PURH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    5-aminoimidazole-4-carboxamide ribonucleotide formyltransferase
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:ATIC
Synonyms:PURH
OrganismGallus gallus (Chicken) [Reference proteome]
Taxonomic identifier9031 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Neognathae › Galliformes › Phasianidae › Phasianinae › Gallus

Protein attributes

Sequence length593 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis. Ref.3

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. Ref.2 Ref.3

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity.

Sequence similarities

Belongs to the PurH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 593593Bifunctional purine biosynthesis protein PURH
PRO_0000192155

Regions

Nucleotide binding13 – 153IMP
Nucleotide binding35 – 384IMP
Nucleotide binding65 – 684IMP
Nucleotide binding102 – 1054IMP
Nucleotide binding126 – 1283IMP
Region208 – 2092AICAR binding

Sites

Active site1381Proton acceptor Potential
Active site2681Proton acceptor Probable
Binding site3171AICAR; via carbonyl oxygen
Binding site3401AICAR
Binding site4321AICAR; shared with dimeric partner By similarity
Binding site4521AICAR; shared with dimeric partner By similarity
Binding site5421AICAR; via carbonyl oxygen; shared with dimeric partner By similarity
Binding site5891AICAR; shared with dimeric partner
Site2671Transition state stabilizer Potential

Secondary structure

1 ................................................................................................................ 593
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P31335 [UniParc].

Last modified July 1, 1993. Version 1.
Checksum: BD1A34F03D96A136

FASTA59364,415
        10         20         30         40         50         60 
MAARQQLALL SVSEKAGLVE FARSLNALGL GLIASGGTAT ALRDAGLPVR DVSDLTGFPE 

        70         80         90        100        110        120 
MLGGRVKTLH PAVHAGILAR NIPEDNADMN KQDFSLVRVV VCNLYPFVKT VSSPGVTVPE 

       130        140        150        160        170        180 
AVEKIDIGGV ALLRAAAKNH ARVTVVCDPA DYSSVAKEMA ASKDKDTSVE TRRHLALKAF 

       190        200        210        220        230        240 
THTAQYDAAI SDYFRKEYSK GVSQLPLRYG MNPHQSPAQL YTTRPKLPLT VVNGSPGFIN 

       250        260        270        280        290        300 
LCDALNAWQL VKELKQALGI PAAASFKHVS PAGAAVGIPL SEEEAQVCMV HDLHKTLTPL 

       310        320        330        340        350        360 
ASAYARSRGA DRMSSFGDFI ALSDICDVPT AKIISREVSD GVVAPGYEEE ALKILSKKKN 

       370        380        390        400        410        420 
GGYCVLQMDP NYEPDDNEIR TLYGLQLMQK RNNAVIDRSL FKNIVTKNKT LPESAVRDLI 

       430        440        450        460        470        480 
VASIAVKYTQ SNSVCYAKDG QVIGIGAGQQ SRIHCTRLAG DKANSWWLRH HPRVLSMKFK 

       490        500        510        520        530        540 
AGVKRAEVSN AIDQYVTGTI GEDEDLVKWQ AMFEEVPAQL TEAEKKQWIA KLTAVSLSSD 

       550        560        570        580        590 
AFFPFRDNVD RAKRIGVQFI VAPSGSAADE VVIEACNELG ITLIHTNLRL FHH

« Hide

References

[1]"De novo purine nucleotide biosynthesis: cloning, sequencing and expression of a chicken PurH cDNA encoding 5-aminoimidazole-4-carboxamide-ribonucleotide transformylase-IMP cyclohydrolase."
Ni L., Guan K., Zalkin H., Dixon J.E.
Gene 106:197-205(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"Crystal structure of a bifunctional transformylase and cyclohydrolase enzyme in purine biosynthesis."
Greasley S.E., Horton P., Ramcharan J., Beardsley G.P., Benkovic S.J., Wilson I.A.
Nat. Struct. Biol. 8:402-406(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) IN COMPLEX WITH GMP, SUBUNIT.
[3]"Structural insights into the avian AICAR transformylase mechanism."
Wolan D.W., Greasley S.E., Beardsley G.P., Wilson I.A.
Biochemistry 41:15505-15513(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS) IN COMPLEX WITH AICAR AND XMP, FUNCTION, SUBUNIT.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		S64492 mRNA. Translation: AAB20309.1.
IPIIPI00600106.
PIRDTCHPH. JQ1281.
RefSeqNP_990509.1. NM_205178.1.
UniGeneGga.4556.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1G8MX-ray1.75A/B1-593[»]
1M9NX-ray1.93A/B1-593[»]
1OZ0X-ray2.50A/B1-593[»]
1THZX-ray1.80A/B1-593[»]
2B1GX-ray2.10A/B/C/D1-593[»]
2B1IX-ray2.02A/B1-593[»]
2IU0X-ray2.53A/B1-593[»]
2IU3X-ray2.90A/B1-593[»]
ProteinModelPortalP31335.
SMRP31335. Positions 4-593.
ModBaseSearch...

Proteomic databases

PaxDbP31335.
PRIDEP31335.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID396091.
KEGGgga:396091.

Organism-specific databases

CTD471.

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
HOVERGENHBG006912.
InParanoidP31335.
KOK00602.
OrthoDBEOG43BMNG.

Enzyme and pathway databases

ReactomeREACT_115655. Metabolism.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
InterProIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF53927. Cytidine_deaminase-like. 1 hit.
SSF52335. MGS-like_dom. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP31335.
NextBio20816149.

Entry information

Entry namePUR9_CHICK
AccessionPrimary (citable) accession number: P31335
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: April 3, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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