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Reviewed, UniProtKB/Swiss-Prot B4UJ61 (PUR9_ANASK)

Last modified February 9, 2010. Version 13. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional purine biosynthesis protein purH
Including the following 2 domains:
    1- Recommended name:
            Phosphoribosylaminoimidazolecarboxamide formyltransferase
              EC=2.1.2.3
        Alternative name(s):
            AICAR transformylase
    2- Recommended name:
            IMP cyclohydrolase
              EC=3.5.4.10
        Alternative name(s):
            Inosinicase
            IMP synthetase
            ATIC
Gene names
Name: purH
Ordered Locus Names: AnaeK_1391
OrganismAnaeromyxobacter sp. (strain K) [Complete proteome] [HAMAP]
Taxonomic identifier447217 [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 MF_00139

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

Sequence similarities

Belongs to the purH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 524524Bifunctional purine biosynthesis protein purH HAMAP MF_00139
PRO_1000096039

Sequences

Sequence LengthMass (Da)Tools
B4UJ61-1 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: 9E4BB6528D87F982

FASTA52455,969
        10         20         30         40         50         60 
MTRRALVSVS DKTGLVPFAR RLAALGVELL STGGTQKTLA 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 

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References

[1]"Complete sequence of Anaeromyxobacter sp. K."
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., Ovchinnikiva G., Beliaev A.
Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001131 Genomic DNA. Translation: ACG72622.1.
RefSeqYP_002133751.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID6785935.
GenomeReviewsGene locus AnaeK_1391 in contig CP001131_GR.
KEGGank:AnaeK_1391.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG498048.
OMAVVKHVKS.

Family and domain databases

HAMAPMF_00139. PurH.
[Tree]
InterProIPR002695. AICARFT_IMPCHas.
IPR013982. AICARFT_IMPCHase_bienz.
IPR011607. MGS.
[Graphical view]
PANTHERPTHR11692. AICARFT_IMPCHas. 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]
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_ANASK
AccessionPrimary (citable) accession number: B4UJ61
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 9, 2010
This is version 13 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents