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Protein

Bifunctional purine biosynthesis protein PURH

Gene

ATIC

Organism
Gallus gallus (Chicken)
Status
Reviewed-Annotation score: 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: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes 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).
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PURH (ATIC)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes 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), the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Pathwayi: IMP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.
Proteins known to be involved in this subpathway in this organism are:
  1. Bifunctional purine biosynthesis protein PURH (ATIC)
This subpathway is part of the pathway IMP biosynthesis via de novo pathway, which is itself part of Purine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide, the pathway IMP biosynthesis via de novo pathway and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei138Proton acceptorSequence analysis1
Sitei267Transition state stabilizerSequence analysis1
Active sitei268Proton acceptorCurated1
Binding sitei317AICAR; via carbonyl oxygen1 Publication1
Binding sitei340AICAR1 Publication1
Binding sitei432AICAR; shared with dimeric partnerBy similarity1
Binding sitei452AICAR; shared with dimeric partnerBy similarity1
Binding sitei542AICAR; via carbonyl oxygen; shared with dimeric partnerBy similarity1
Binding sitei589AICAR; shared with dimeric partner1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi13 – 15IMP3
Nucleotide bindingi35 – 38IMP4
Nucleotide bindingi65 – 68IMP4
Nucleotide bindingi102 – 105IMP4
Nucleotide bindingi126 – 128IMP3

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BRENDAi2.1.2.3. 1306.
3.5.4.10. 1306.
ReactomeiR-GGA-419140. De novo synthesis of IMP.
SABIO-RKP31335.
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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalloanseraeGalliformesPhasianidaePhasianinaeGallus
Proteomesi
  • UP000000539 Componenti: Unplaced

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001921551 – 593Bifunctional purine biosynthesis protein PURHAdd BLAST593

Proteomic databases

PaxDbiP31335.
PRIDEiP31335.

Interactioni

Subunit structurei

Homodimer.2 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005643.

Structurei

Secondary structure

1593
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi7 – 13Combined sources7
Helixi18 – 27Combined sources10
Beta strandi31 – 34Combined sources4
Helixi36 – 44Combined sources9
Beta strandi49 – 51Combined sources3
Helixi52 – 56Combined sources5
Helixi62 – 64Combined sources3
Beta strandi66 – 68Combined sources3
Helixi71 – 78Combined sources8
Helixi83 – 91Combined sources9
Beta strandi97 – 103Combined sources7
Helixi107 – 111Combined sources5
Beta strandi113 – 115Combined sources3
Helixi118 – 122Combined sources5
Helixi128 – 138Combined sources11
Turni139 – 142Combined sources4
Beta strandi144 – 146Combined sources3
Helixi149 – 151Combined sources3
Helixi152 – 160Combined sources9
Helixi169 – 198Combined sources30
Turni201 – 203Combined sources3
Beta strandi204 – 208Combined sources5
Beta strandi210 – 212Combined sources3
Beta strandi218 – 221Combined sources4
Beta strandi223 – 226Combined sources4
Beta strandi228 – 234Combined sources7
Helixi238 – 258Combined sources21
Beta strandi262 – 267Combined sources6
Beta strandi270 – 276Combined sources7
Helixi282 – 287Combined sources6
Turni291 – 293Combined sources3
Helixi294 – 296Combined sources3
Helixi299 – 309Combined sources11
Turni312 – 317Combined sources6
Beta strandi318 – 324Combined sources7
Helixi328 – 335Combined sources8
Beta strandi339 – 345Combined sources7
Helixi349 – 357Combined sources9
Helixi358 – 361Combined sources4
Beta strandi364 – 368Combined sources5
Beta strandi376 – 382Combined sources7
Beta strandi385 – 390Combined sources6
Helixi398 – 401Combined sources4
Beta strandi406 – 408Combined sources3
Helixi413 – 427Combined sources15
Beta strandi429 – 432Combined sources4
Beta strandi434 – 438Combined sources5
Beta strandi441 – 446Combined sources6
Helixi452 – 468Combined sources17
Helixi472 – 475Combined sources4
Helixi485 – 497Combined sources13
Helixi504 – 510Combined sources7
Beta strandi513 – 515Combined sources3
Helixi522 – 529Combined sources8
Beta strandi535 – 541Combined sources7
Helixi547 – 553Combined sources7
Turni554 – 556Combined sources3
Beta strandi557 – 563Combined sources7
Helixi569 – 579Combined sources11
Beta strandi582 – 587Combined sources6

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP31335.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni208 – 209AICAR binding2

Domaini

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

Sequence similaritiesi

Belongs to the PurH family.Curated

Phylogenomic databases

eggNOGiKOG2555. Eukaryota.
COG0138. LUCA.
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. 1 hit.
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
S64492 mRNA. Translation: AAB20309.1.
PIRiJQ1281. DTCHPH.
RefSeqiNP_990509.1. NM_205178.1.
UniGeneiGga.4556.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9031.ENSGALP00000005643.

Proteomic databases

PaxDbiP31335.
PRIDEiP31335.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi396091.
KEGGigga:396091.

Organism-specific databases

CTDi471.

Phylogenomic databases

eggNOGiKOG2555. Eukaryota.
COG0138. LUCA.
HOGENOMiHOG000230372.
HOVERGENiHBG006912.
InParanoidiP31335.
KOiK00602.
PhylomeDBiP31335.

Enzyme and pathway databases

UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.
BRENDAi2.1.2.3. 1306.
3.5.4.10. 1306.
ReactomeiR-GGA-419140. De novo synthesis of IMP.
SABIO-RKP31335.

Miscellaneous databases

EvolutionaryTraceiP31335.
PROiP31335.

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. 1 hit.
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.
ProtoNetiSearch...

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: November 2, 2016
This is version 109 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.