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B7GFU2 (PUR9_ANOFW) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. 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:Aflv_0238
OrganismAnoxybacillus flavithermus (strain DSM 21510 / WK1) [Complete proteome] [HAMAP]
Taxonomic identifier491915 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeAnoxybacillus

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_1000117863

Sequences

Sequence LengthMass (Da)Tools
B7GFU2 [UniParc].

Last modified February 10, 2009. Version 1.
Checksum: 8142E20B885C4433

FASTA51155,923
        10         20         30         40         50         60 
MKRRAIISVS NKKGIVTFAK QLAELGVEII STGGTKRVLA EHGVPVISIS DVTNFPEILD 

        70         80         90        100        110        120 
GRVKTLHPNI HGGLLAVRDD ETHQQQLQAH NITPIDFVVV NLYPFQETIA KPNVTLMEAI 

       130        140        150        160        170        180 
EQIDIGGPTM LRAAAKNHAY VTAVVDPADY HLVIEQLKQY GEVLLETRRA LAAKVFRHTA 

       190        200        210        220        230        240 
AYDAMIAQYL TNIVGETYPE TMTMTFVKKQ SLRYGENPHQ TAAFYEKPLS SPFSIAAAKQ 

       250        260        270        280        290        300 
LHGKELSYNN INDANAALQI VAEFVEPAAV AVKHMNPCGV GVGETIAEAF QKAYEADPTS 

       310        320        330        340        350        360 
IFGGIVALNR EVDEQMAAKL HDIFLEIVIA PSFTEQALEI LTRKKNIRLL TVDFEVERKK 

       370        380        390        400        410        420 
EPFVVSVRGG LLVQDEDTYT IDDATLRVVT ERKPTEEEWS NLTFAWRVVK HVKSNAIVLA 

       430        440        450        460        470        480 
KNGMTIGVGA GQMNRVGAAK IAIEQAGDRA KGAVLASDAF FPMSDTVEAA AQAGVTAIIQ 

       490        500        510 
PGGSIRDEDS IQKANEYGIA MVFTGVRHFK H 

« Hide

References

[1]"Encapsulated in silica: genome, proteome and physiology of the thermophilic bacterium Anoxybacillus flavithermus WK1."
Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A., Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V., Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.
Genome Biol. 9:R161.1-R161.16(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 21510 / WK1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000922 Genomic DNA. Translation: ACJ32622.1.
RefSeqYP_002314607.1. NC_011567.1.

3D structure databases

ProteinModelPortalB7GFU2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING491915.Aflv_0238.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACJ32622; ACJ32622; Aflv_0238.
GeneID7036470.
KEGGafl:Aflv_0238.
PATRIC20952215. VBIAnoFla45531_0244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycAFLA491915:GHEO-288-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_ANOFW
AccessionPrimary (citable) accession number: B7GFU2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: February 10, 2009
Last modified: May 14, 2014
This is version 40 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