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Q9KF53 (PUR9_BACHD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 85. 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:BH0633
OrganismBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125) [Complete proteome] [HAMAP]
Taxonomic identifier272558 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length511 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 – 511511Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_0000192069

Sequences

Sequence LengthMass (Da)Tools
Q9KF53 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 13EF1768AA84B485

FASTA51155,578
        10         20         30         40         50         60 
MKRRALVSVS NKEGIVPFAK ALVEHEVEIV STGGTKRALQ EAGIPVTGIS DVTGFPEILD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLAMRER DEHLAQLNEH HIRPIDFVVV NLYPFQQTIA KPEATFADAI 

       130        140        150        160        170        180 
ENIDIGGPSM LRAAAKNHQH VTVVVDPVDY ETVLKELADQ GNVATETKRR LAAKVFRHTA 

       190        200        210        220        230        240 
AYDAMIAEYL TDAVGEESPE SLTVTFEKKQ DLRYGENPHQ KATFYQKPLG AKASIAHAKQ 

       250        260        270        280        290        300 
LHGKELSYNN INDADAALSI VKEFKEPAAV AVKHMNPCGV GTGETIKEAF DKAYEADPVS 

       310        320        330        340        350        360 
IFGGIIALNR EVDVETAKTL KEIFLEIIIA PSFSEEALDV LTSKKNLRLL TLPLNEENQA 

       370        380        390        400        410        420 
EKRITSIHGG ALVQEEDTYG FEEAEIKIPT KREPTEAEWE ALKLAWRVVK HVKSNAIVLA 

       430        440        450        460        470        480 
DGQMTVGVGA GQMNRVGAAK IAIEQAGEKA AGSVMGSDAF FPMGDTVELA AKAGITAIIQ 

       490        500        510 
PGGSIRDEES IENADKHGIA MVFTGVRHFK H 

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References

[1]"Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans and genomic sequence comparison with Bacillus subtilis."
Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F., Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.
Nucleic Acids Res. 28:4317-4331(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000004 Genomic DNA. Translation: BAB04352.1.
PIRA83729.
RefSeqNP_241499.1. NC_002570.2.

3D structure databases

ProteinModelPortalQ9KF53.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272558.BH0633.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB04352; BAB04352; BAB04352.
GeneID893121.
KEGGbha:BH0633.
PATRIC18938256. VBIBacHal18977_0666.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycBHAL272558:GJC5-691-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_BACHD
AccessionPrimary (citable) accession number: Q9KF53
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2002
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 85 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