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P31335

- PUR9_CHICK

UniProt

P31335 - PUR9_CHICK

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Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Bifunctional enzyme that catalyzes 2 steps in purine biosynthesis.1 Publication

Catalytic activityi

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.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei138 – 1381Proton acceptorSequence Analysis
Sitei267 – 2671Transition state stabilizerSequence Analysis
Active sitei268 – 2681Proton acceptorCurated
Binding sitei317 – 3171AICAR; via carbonyl oxygen1 Publication
Binding sitei340 – 3401AICAR1 Publication
Binding sitei432 – 4321AICAR; shared with dimeric partnerBy similarity
Binding sitei452 – 4521AICAR; shared with dimeric partnerBy similarity
Binding sitei542 – 5421AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity
Binding sitei589 – 5891AICAR; shared with dimeric partner1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 153IMP
Nucleotide bindingi35 – 384IMP
Nucleotide bindingi65 – 684IMP
Nucleotide bindingi102 – 1054IMP
Nucleotide bindingi126 – 1283IMP

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: Reactome
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: Reactome
  3. protein homodimerization activity Source: UniProtKB

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: Reactome
  2. nucleobase-containing small molecule metabolic process Source: Reactome
  3. purine nucleobase metabolic process Source: Reactome
  4. small molecule metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

ReactomeiREACT_116007. De novo synthesis of IMP.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
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 namesi
Name:ATIC
Synonyms:PURH
OrganismiGallus gallus (Chicken)
Taxonomic identifieri9031 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
ProteomesiUP000000539: Unplaced

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 593593Bifunctional purine biosynthesis protein PURHPRO_0000192155Add
BLAST

Proteomic databases

PaxDbiP31335.
PRIDEiP31335.

Interactioni

Subunit structurei

Homodimer.2 Publications

Structurei

Secondary structure

1
593
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137
Helixi18 – 2710
Beta strandi31 – 344
Helixi36 – 449
Beta strandi49 – 513
Helixi52 – 565
Helixi62 – 643
Beta strandi66 – 683
Helixi71 – 788
Helixi83 – 919
Beta strandi97 – 1037
Helixi107 – 1115
Beta strandi113 – 1153
Helixi118 – 1225
Helixi128 – 13811
Turni139 – 1424
Beta strandi144 – 1463
Helixi149 – 1513
Helixi152 – 1609
Helixi169 – 19830
Turni201 – 2033
Beta strandi204 – 2085
Beta strandi210 – 2123
Beta strandi218 – 2214
Beta strandi223 – 2264
Beta strandi228 – 2347
Helixi238 – 25821
Beta strandi262 – 2676
Beta strandi270 – 2767
Helixi282 – 2876
Turni291 – 2933
Helixi294 – 2963
Helixi299 – 30911
Turni312 – 3176
Beta strandi318 – 3247
Helixi328 – 3358
Beta strandi339 – 3457
Helixi349 – 3579
Helixi358 – 3614
Beta strandi364 – 3685
Beta strandi376 – 3827
Beta strandi385 – 3906
Helixi398 – 4014
Beta strandi406 – 4083
Helixi413 – 42715
Beta strandi429 – 4324
Beta strandi434 – 4385
Beta strandi441 – 4466
Helixi452 – 46817
Helixi472 – 4754
Helixi485 – 49713
Helixi504 – 5107
Beta strandi513 – 5153
Helixi522 – 5298
Beta strandi535 – 5417
Helixi547 – 5537
Turni554 – 5563
Beta strandi557 – 5637
Helixi569 – 57911
Beta strandi582 – 5876

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliP31335.
SMRiP31335. Positions 4-593.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31335.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni208 – 2092AICAR binding

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiP31335.
KOiK00602.
PhylomeDBiP31335.

Family and domain databases

Gene3Di1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERiPTHR11692. PTHR11692. 1 hit.
PfamiPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFiPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTiSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMiSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR00355. purH. 1 hit.

Sequencei

Sequence statusi: Complete.

P31335-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAARQQLALL SVSEKAGLVE FARSLNALGL GLIASGGTAT ALRDAGLPVR
60 70 80 90 100
DVSDLTGFPE MLGGRVKTLH PAVHAGILAR NIPEDNADMN KQDFSLVRVV
110 120 130 140 150
VCNLYPFVKT VSSPGVTVPE AVEKIDIGGV ALLRAAAKNH ARVTVVCDPA
160 170 180 190 200
DYSSVAKEMA ASKDKDTSVE TRRHLALKAF THTAQYDAAI SDYFRKEYSK
210 220 230 240 250
GVSQLPLRYG MNPHQSPAQL YTTRPKLPLT VVNGSPGFIN LCDALNAWQL
260 270 280 290 300
VKELKQALGI PAAASFKHVS PAGAAVGIPL SEEEAQVCMV HDLHKTLTPL
310 320 330 340 350
ASAYARSRGA DRMSSFGDFI ALSDICDVPT AKIISREVSD GVVAPGYEEE
360 370 380 390 400
ALKILSKKKN GGYCVLQMDP NYEPDDNEIR TLYGLQLMQK RNNAVIDRSL
410 420 430 440 450
FKNIVTKNKT LPESAVRDLI VASIAVKYTQ SNSVCYAKDG QVIGIGAGQQ
460 470 480 490 500
SRIHCTRLAG DKANSWWLRH HPRVLSMKFK AGVKRAEVSN AIDQYVTGTI
510 520 530 540 550
GEDEDLVKWQ AMFEEVPAQL TEAEKKQWIA KLTAVSLSSD AFFPFRDNVD
560 570 580 590
RAKRIGVQFI VAPSGSAADE VVIEACNELG ITLIHTNLRL FHH
Length:593
Mass (Da):64,415
Last modified:July 1, 1993 - v1
Checksum:iBD1A34F03D96A136
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S64492 mRNA. Translation: AAB20309.1.
PIRiJQ1281. DTCHPH.
RefSeqiNP_990509.1. NM_205178.1.
UniGeneiGga.4556.

Genome annotation databases

GeneIDi396091.
KEGGigga:396091.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
S64492 mRNA. Translation: AAB20309.1 .
PIRi JQ1281. DTCHPH.
RefSeqi NP_990509.1. NM_205178.1.
UniGenei Gga.4556.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1G8M X-ray 1.75 A/B 1-593 [» ]
1M9N X-ray 1.93 A/B 1-593 [» ]
1OZ0 X-ray 2.50 A/B 1-593 [» ]
1THZ X-ray 1.80 A/B 1-593 [» ]
2B1G X-ray 2.10 A/B/C/D 1-593 [» ]
2B1I X-ray 2.02 A/B 1-593 [» ]
2IU0 X-ray 2.53 A/B 1-593 [» ]
2IU3 X-ray 2.90 A/B 1-593 [» ]
ProteinModelPortali P31335.
SMRi P31335. Positions 4-593.
ModBasei Search...
MobiDBi Search...

Proteomic databases

PaxDbi P31335.
PRIDEi P31335.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 396091.
KEGGi gga:396091.

Organism-specific databases

CTDi 471.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230372.
HOVERGENi HBG006912.
InParanoidi P31335.
KOi K00602.
PhylomeDBi P31335.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
Reactomei REACT_116007. De novo synthesis of IMP.

Miscellaneous databases

EvolutionaryTracei P31335.
NextBioi 20816149.
PROi P31335.

Family and domain databases

Gene3Di 1.10.287.440. 1 hit.
3.40.140.20. 3 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_dom.
IPR024050. AICAR_Tfase_insert_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view ]
PANTHERi PTHR11692. PTHR11692. 1 hit.
Pfami PF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view ]
PIRSFi PIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTi SM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view ]
SUPFAMi SSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsi TIGR00355. purH. 1 hit.
ProtoNeti Search...

Publicationsi

  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.

Entry informationi

Entry nameiPUR9_CHICK
AccessioniPrimary (citable) accession number: P31335
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: October 1, 2014
This is version 97 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3