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A6TLS7 (PUR9_ALKMQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 50. 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:Amet_0925
OrganismAlkaliphilus metalliredigens (strain QYMF) [Complete proteome] [HAMAP]
Taxonomic identifier293826 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length508 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 – 508508Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000203245

Sequences

Sequence LengthMass (Da)Tools
A6TLS7 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: 7E6190820F5D06B0

FASTA50855,879
        10         20         30         40         50         60 
MKRVLISVSN KEGIIPFARK LVHLGIEIIS TGGTATLLRE AEIDVMEVSE LTGFPECLEG 

        70         80         90        100        110        120 
RVKTLHPVVH GGILADRSKD SHMKTLEELK IKPIDLVVIN LYPFKETIQK KNVTLEEAIE 

       130        140        150        160        170        180 
NIDIGGPTML RAAAKNYRHV TVITNPEDYH AVLEEIEAKG NTEETTRYEL AKKVFQHTSQ 

       190        200        210        220        230        240 
YDTLIAGYLG KDELVFPEQL TVTYEKVQDL RYGENPHQKG AFYREIGCEE GTLASAKQLQ 

       250        260        270        280        290        300 
GKELSFNNIN DANGALALLK EFQEPTVVAV KHTNPCGVAS AKNIDEAWDK AYAADPTSVF 

       310        320        330        340        350        360 
GGIIAANQVI DAETATKLLE VFLEVVIAPG YTPEALVLFK QKKNLRVLEL SSILAEPKGQ 

       370        380        390        400        410        420 
MDMKKVLGGL LIQEYNTGLI GNLKTVTEKE PTTEEIEDLL FAYKVVKHTK SNGIVVVRNQ 

       430        440        450        460        470        480 
QTLAIGPGQT SRIWALENAI GNCIHPLEGS VLASDAFFPF KDCVEVGAKA GIKSIIQPGG 

       490        500 
SMRDQESIDA CNERGMAMVF AGVRHFKH 

« Hide

References

[1]"Complete sequence of Alkaliphilus metalliredigens QYMF."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Ye Q., Zhou J., Fields M., Richardson P.
Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QYMF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000724 Genomic DNA. Translation: ABR47145.1.
RefSeqYP_001318804.1. NC_009633.1.

3D structure databases

ProteinModelPortalA6TLS7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING293826.Amet_0925.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABR47145; ABR47145; Amet_0925.
GeneID5310968.
KEGGamt:Amet_0925.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMAGIGQADN.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycAMET293826:GI5P-942-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_ALKMQ
AccessionPrimary (citable) accession number: A6TLS7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: August 21, 2007
Last modified: May 14, 2014
This is version 50 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