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A8MLI9 (PUR9_ALKOO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 43. 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:Clos_0541
OrganismAlkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain OhILAs)) [Complete proteome] [HAMAP]
Taxonomic identifier350688 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaClostridialesClostridiaceaeAlkaliphilus

Protein attributes

Sequence length512 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 – 512512Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057893

Sequences

Sequence LengthMass (Da)Tools
A8MLI9 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 6287884482E96EBF

FASTA51256,446
        10         20         30         40         50         60 
MVKRALLSVS DKEGIVQLAQ NLSSFNIEIL STGGTAKLLR ESGIDVRDVS EVTGFPECLD 

        70         80         90        100        110        120 
GRVKTLHPAV HGGILAIRDN ANHMDTLKEL EITPIDLVVI NLYPFKETIL KSDVTLAEAI 

       130        140        150        160        170        180 
ENIDIGGPTM LRAAAKNHRD VTVIIDPKDY HRVLEEIKEN GDTKLDTRYQ LALKVFQHTA 

       190        200        210        220        230        240 
QYDALIADYL GKQISEEKIG ANTITLTYEK VQDLRYGENP HQKAGFYKEI GANKGTLVDG 

       250        260        270        280        290        300 
VQLHGKELSF NNINDANGAL ELLKEFQEPT VVAVKHTNPC GVASGTNIEE AWHKAYESDP 

       310        320        330        340        350        360 
LSIFGGIVAA NRAVTKTMAA AMKEIFLEVI IAPNFTEEAL EVFKEKKNLR LIKIEDICNG 

       370        380        390        400        410        420 
NHHSYQIKKV QGGILLQEDD HILFEQLDVV TEKEPTEEEK EDLAFAFKIV KHVKSNGIVF 

       430        440        450        460        470        480 
VKNKQTLAIG PGQTSRIWAL ENAVKNTTHS LKGSVLASDA FFPFRDCVDT AFGAGVKAII 

       490        500        510 
QPGGSINDGV SIKACNEHGI SMVFTGFRHF KH 

« Hide

References

[1]"Complete genome of Alkaliphilus oremlandii OhILAs."
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E., Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.
Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OhILAs.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000853 Genomic DNA. Translation: ABW18103.1.
RefSeqYP_001512099.1. NC_009922.1.

3D structure databases

ProteinModelPortalA8MLI9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING350688.Clos_0541.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABW18103; ABW18103; Clos_0541.
GeneID5678038.
KEGGaoe:Clos_0541.
PATRIC20866183. VBIAlkOre124042_0560.

Organism-specific databases

CMRSearch...

Phylogenomic databases

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

Enzyme and pathway databases

BioCycAORE350688:GHBG-559-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_ALKOO
AccessionPrimary (citable) accession number: A8MLI9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: December 4, 2007
Last modified: February 19, 2014
This is version 43 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