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B8JHC9 (PUR9_ANAD2) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 37. 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:A2cp1_1487
OrganismAnaeromyxobacter dehalogenans (strain 2CP-1 / ATCC BAA-258) [Complete proteome] [HAMAP]
Taxonomic identifier455488 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaMyxococcalesCystobacterineaeMyxococcaceaeAnaeromyxobacter

Protein attributes

Sequence length524 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 – 524524Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122942

Sequences

Sequence LengthMass (Da)Tools
B8JHC9 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: DF5AA7439C96ED59

FASTA52455,939
        10         20         30         40         50         60 
MTRRALVSVS DKTGLVPFAR RLAALGVELL STGGTQKALA EAGVPVVGVG DYTQAPEILG 

        70         80         90        100        110        120 
GRVKTLHPRV HGGILYRRGL ASDEADVKAR DIPPIDLVVV NLYPFREAVA AGKPFETCVE 

       130        140        150        160        170        180 
EIDIGGPTMV RSAAKNSAHV GVVVDPADYE KVAAELEATR TLSAATRFYL MKKAFAHTAA 

       190        200        210        220        230        240 
YDAAISEYLT AREAPEAAPA HFPATLAAVY TKAYDLRYGE NPHQAGAFYR AAREPEEPSV 

       250        260        270        280        290        300 
AFADVLQGKE LSYNNLLDLQ AALAGVMEFD ETACVIIKHN TPCGVSTGRT AGEAFARARE 

       310        320        330        340        350        360 
CDPVSAFGGI VALNRPVDEA TASELTSLFL ECVIAPGYDA AARAALAVKK NLRLLEAPRL 

       370        380        390        400        410        420 
GAARATWRRR PEEGRELRSI PGGLLVMDRD LGSVRRDDCK VMTKRAPTEQ EWKDLLFAWK 

       430        440        450        460        470        480 
VVKHVKSNAI VFAKDDRTVA IGGGQTSRVE SVKTAVMKAA LDVRGSSVGS DAFFPFADGV 

       490        500        510        520 
EEIIKAGATA IIQPGGSMRD AEVIAAADKA GIAMVATGMR HFRH 

« Hide

References

[1]"Complete sequence of Anaeromyxobacter dehalogenans 2CP-1."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Beliaev A.S., Richardson P.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 2CP-1 / ATCC BAA-258.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001359 Genomic DNA. Translation: ACL64831.1.
RefSeqYP_002491897.1. NC_011891.1.

3D structure databases

ProteinModelPortalB8JHC9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING455488.A2cp1_1487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACL64831; ACL64831; A2cp1_1487.
GeneID7296895.
KEGGacp:A2cp1_1487.
PATRIC20909838. VBIAnaDeh28364_1512.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMAYRRECED.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycADEH455488:GH35-1503-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_ANAD2
AccessionPrimary (citable) accession number: B8JHC9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: May 14, 2014
This is version 37 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