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Q9JUQ8 (PUR9_NEIMA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:NMA1182
OrganismNeisseria meningitidis serogroup A / serotype 4A (strain Z2491) [Complete proteome] [HAMAP]
Taxonomic identifier122587 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length530 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

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. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

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. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 530530Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192108

Sequences

Sequence LengthMass (Da)Tools
Q9JUQ8 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 43704317F7B7610B

FASTA53057,435
        10         20         30         40         50         60 
MPSIKRALIS LSDKTGAVEF AQTLHKLGVE ILSTGGTAKL LADAGVPVIE VADYTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KIHGGILGRR DLPEHVAKME EHGIGNIDLV CVNLYPFAAT IAKPNCTLED 

       130        140        150        160        170        180 
AIENIDIGGP TMVRSAAKNW KHVAIVTDPA DFPAIAAEME ANNGALSDKT RFNLSRKAFS 

       190        200        210        220        230        240 
HTAQYDGMIS NYLTSLSDDV LSGTPEIGEF PSQFNQSWIK VQDMRYGENP HQRAAFYRDV 

       250        260        270        280        290        300 
YPAAGSLSAY KQLQGKELSY NNIADADAAW EAVKSFDAPA CVIVKHANPC GVAVAADTLT 

       310        320        330        340        350        360 
AYKLAYATDT TSAFGGIIAF NREVDGETVK QITDNQFMEV LMAPKFTAEA LEIAAAKKNV 

       370        380        390        400        410        420 
RVLQISLTTP LEAGANRFEL KRVGGGLLVQ TPDIYRLNRA DLKVVSKRQL TEQEWNDLMF 

       430        440        450        460        470        480 
VWNVAKYVKS NAIVFGKGGQ TYGIGAGQMS RVDSTRIAAR KAQDANLDLN GACAASDAFF 

       490        500        510        520        530 
PFRDGVDVIA EQGIKAIIHP AGSMRDQEVF DAADEHGIAM VVTGVRHFRH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL157959 Genomic DNA. Translation: CAM08384.1.
PIRH81885.
RefSeqYP_002342577.1. NC_003116.1.

3D structure databases

ProteinModelPortalQ9JUQ8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING122587.NMA1182.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAM08384; CAM08384; NMA1182.
GeneID907151.
KEGGnma:NMA1182.
PATRIC20363355. VBINeiMen132687_1385.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMADLLFAWK.
OrthoDBEOG6QCDFF.
ProtClustDBPRK00881.

Enzyme and pathway databases

BioCycNMEN122587:GI3Q-1093-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_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]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_NEIMA
AccessionPrimary (citable) accession number: Q9JUQ8
Secondary accession number(s): A1IRJ6
Entry history
Integrated into UniProtKB/Swiss-Prot: June 16, 2003
Last sequence update: October 1, 2000
Last modified: February 19, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways