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Q9PNY2

- PUR9_CAMJE

UniProt

Q9PNY2 - PUR9_CAMJE

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Protein

Bifunctional purine biosynthesis protein PurH

Gene

purH

Organism
Campylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Status
Reviewed - Annotation score: 2 out of 5- Experimental evidence at protein leveli

Functioni

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.UniRule annotation
IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide.UniRule annotation

Pathwayi

GO - Molecular functioni

  1. IMP cyclohydrolase activity Source: UniProtKB-HAMAP
  2. phosphoribosylaminoimidazolecarboxamide formyltransferase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. 'de novo' IMP biosynthetic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Transferase

Keywords - Biological processi

Purine biosynthesis

Enzyme and pathway databases

BioCyciCJEJ192222:GJTS-928-MONOMER.
UniPathwayiUPA00074; UER00133.
UPA00074; UER00135.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional purine biosynthesis protein PurHUniRule annotation
Including the following 2 domains:
Phosphoribosylaminoimidazolecarboxamide formyltransferaseUniRule annotation (EC:2.1.2.3UniRule annotation)
Alternative name(s):
AICAR transformylaseUniRule annotation
IMP cyclohydrolaseUniRule annotation (EC:3.5.4.10UniRule annotation)
Alternative name(s):
ATICUniRule annotation
IMP synthaseUniRule annotation
InosinicaseUniRule annotation
Gene namesi
Name:purHUniRule annotation
Ordered Locus Names:Cj0953c
OrganismiCampylobacter jejuni subsp. jejuni serotype O:2 (strain NCTC 11168)
Taxonomic identifieri192222 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000000799: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 510510Bifunctional purine biosynthesis protein PurHPRO_0000192079Add
BLAST

Interactioni

Protein-protein interaction databases

IntActiQ9PNY2. 1 interaction.
STRINGi192222.Cj0953c.

Structurei

Secondary structure

1
510
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi2 – 98Combined sources
Helixi13 – 2210Combined sources
Beta strandi26 – 294Combined sources
Helixi31 – 399Combined sources
Beta strandi91 – 999Combined sources
Helixi103 – 1097Combined sources
Helixi113 – 1186Combined sources
Helixi124 – 13310Combined sources
Turni134 – 1374Combined sources
Beta strandi139 – 1413Combined sources
Helixi144 – 1463Combined sources
Helixi147 – 1559Combined sources
Helixi161 – 19030Combined sources
Beta strandi196 – 20914Combined sources
Beta strandi211 – 2133Combined sources
Beta strandi218 – 2258Combined sources
Helixi226 – 2305Combined sources
Beta strandi232 – 2365Combined sources
Helixi240 – 25314Combined sources
Beta strandi261 – 2666Combined sources
Beta strandi269 – 2757Combined sources
Helixi279 – 2879Combined sources
Helixi291 – 2944Combined sources
Beta strandi298 – 3058Combined sources
Helixi307 – 3137Combined sources
Beta strandi319 – 3268Combined sources
Helixi328 – 3325Combined sources
Beta strandi341 – 3444Combined sources
Beta strandi346 – 3494Combined sources
Beta strandi356 – 3627Combined sources
Beta strandi365 – 3706Combined sources
Turni376 – 3816Combined sources
Beta strandi382 – 3843Combined sources
Beta strandi386 – 3883Combined sources
Helixi392 – 40716Combined sources
Beta strandi413 – 4175Combined sources
Beta strandi420 – 4256Combined sources
Beta strandi427 – 4293Combined sources
Helixi431 – 44414Combined sources
Beta strandi453 – 4553Combined sources
Helixi464 – 4718Combined sources
Beta strandi476 – 4794Combined sources
Helixi486 – 49611Combined sources
Beta strandi499 – 5024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4EHIX-ray2.28A/B1-510[»]
ProteinModelPortaliQ9PNY2.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The IMP cyclohydrolase activity resides in the N-terminal region.UniRule annotation

Sequence similaritiesi

Belongs to the PurH family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0138.
HOGENOMiHOG000230373.
KOiK00602.
OMAiRAFKTDP.
OrthoDBiEOG6QCDFF.

Family and domain databases

Gene3Di3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPiMF_00139. PurH.
InterProiIPR024051. AICAR_Tfase_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.

Q9PNY2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MRALLSVSDK EGIVEFGKEL ENLGFEILST GGTFKLLKEN GIKVIEVSDF
60 70 80 90 100
TKSPELFEGR VKTLHPKIHG GILHKRSDEN HIKQAKENEI LGIDLVCVNL
110 120 130 140 150
YPFKKTTIMS DDFDEIIENI DIGGPAMIRS AAKNYKDVMV LCDPLDYEKV
160 170 180 190 200
IETLKKGQND ENFRLNLMIK AYEHTANYDA YIANYMNERF NGGFGASKFI
210 220 230 240 250
VGQKVFDTKY GENPHQKGAL YEFDAFFSAN FKALKGEASF NNLTDINAAL
260 270 280 290 300
NLASSFDKAP AIAIVKHGNP CGFAIKENLV QSYIHALKCD SVSAYGGVVA
310 320 330 340 350
INGTLDEALA NKINEIYVEV IIAANVDEKA LAVFEGKKRI KIFTQESPFL
360 370 380 390 400
IRSFDKYDFK HIDGGFVYQN SDEVGEDELK NAKLMSQREA SKEELKDLEI
410 420 430 440 450
AMKIAAFTKS NNVVYVKNGA MVAIGMGMTS RIDAAKAAIA KAKEMGLDLQ
460 470 480 490 500
GCVLASEAFF PFRDSIDEAS KVGVKAIVEP GGSIRDDEVV KAADEYGMAL
510
YFTGVRHFLH
Length:510
Mass (Da):56,402
Last modified:October 1, 2000 - v1
Checksum:i56F356F04B3A2092
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35073.1.
PIRiH81369.
RefSeqiYP_002344351.1. NC_002163.1.

Genome annotation databases

EnsemblBacteriaiCAL35073; CAL35073; Cj0953c.
GeneIDi905247.
KEGGicje:Cj0953c.
PATRICi20058866. VBICamJej33762_0937.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL111168 Genomic DNA. Translation: CAL35073.1 .
PIRi H81369.
RefSeqi YP_002344351.1. NC_002163.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
4EHI X-ray 2.28 A/B 1-510 [» ]
ProteinModelPortali Q9PNY2.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi Q9PNY2. 1 interaction.
STRINGi 192222.Cj0953c.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai CAL35073 ; CAL35073 ; Cj0953c .
GeneIDi 905247.
KEGGi cje:Cj0953c.
PATRICi 20058866. VBICamJej33762_0937.

Phylogenomic databases

eggNOGi COG0138.
HOGENOMi HOG000230373.
KOi K00602.
OMAi RAFKTDP.
OrthoDBi EOG6QCDFF.

Enzyme and pathway databases

UniPathwayi UPA00074 ; UER00133 .
UPA00074 ; UER00135 .
BioCyci CJEJ192222:GJTS-928-MONOMER.

Family and domain databases

Gene3Di 3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPi MF_00139. PurH.
InterProi IPR024051. AICAR_Tfase_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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: NCTC 11168.

Entry informationi

Entry nameiPUR9_CAMJE
AccessioniPrimary (citable) accession number: Q9PNY2
Secondary accession number(s): Q0P9U6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 20, 2003
Last sequence update: October 1, 2000
Last modified: October 29, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic 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