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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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:
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 .
PIRi JQ1281. DTCHPH.
RefSeqi NP_990509.1. NM_205178.1.
UniGenei Gga.4556.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 98 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