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B2A5W1 (PUR9_NATTJ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 45. 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:Nther_0458
OrganismNatranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF) [Complete proteome] [HAMAP]
Taxonomic identifier457570 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaNatranaerobialesNatranaerobiaceaeNatranaerobius

Protein attributes

Sequence length509 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 – 509509Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000096075

Sequences

Sequence LengthMass (Da)Tools
B2A5W1 [UniParc].

Last modified May 20, 2008. Version 1.
Checksum: EA28F43364512FA1

FASTA50956,802
        10         20         30         40         50         60 
MTIQKINRVL LSVYDKTGLI TLAQELKDMG VELVSTGGTL RHLQTHGIPV YSVEEVTGFP 

        70         80         90        100        110        120 
EILSGRVKTL HPKIHGGILA KNRENEELSS LDIKTFDLVI VNLYPFEQVM QKAEATEEEV 

       130        140        150        160        170        180 
MENIDIGGPT MIRAAAKNWY RVGVCVDPTD YEVLTQQLKQ YHGLTDEFRK TLARKAFKHT 

       190        200        210        220        230        240 
AQYDKAIFNY FESVDTNKDD ETELKFPEFN LLESRELPYG ENPHQKASLL MESQKFIQHQ 

       250        260        270        280        290        300 
GKGLSYNNFQ DIDAAIKLVH EFQKPAVVAV KHTNPCGVGV SNTIEEAYDK AYQGDPVSIF 

       310        320        330        340        350        360 
GGIVACNRPV TEELASKLTE IFLDVIIAPE FEPRALEKLK SKSGTKVVEM DLEKMVGNKV 

       370        380        390        400        410        420 
EIKSTTFGYL CQEADYHHPH PQNWDRVAGE QAKPEEIDDL IIAEKIVKHV KSNAIVVVKE 

       430        440        450        460        470        480 
GQSLGIGAGQ MNRVGASRIA LENAGKESQN SVLASDAFFP FNDVVKLCSQ YGVSAIVQPG 

       490        500 
GSKRDQDSID LAQETGITMY FTGIRHFKH 

« Hide

References

[1]"Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-LF."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L. expand/collapse author list , Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.
Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001034 Genomic DNA. Translation: ACB84054.1.
RefSeqYP_001916642.1. NC_010718.1.

3D structure databases

ProteinModelPortalB2A5W1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING457570.Nther_0458.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACB84054; ACB84054; Nther_0458.
GeneID6315336.
KEGGnth:Nther_0458.
PATRIC22669538. VBINatThe92436_0479.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycNTHE457570:GHRL-484-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_NATTJ
AccessionPrimary (citable) accession number: B2A5W1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: May 20, 2008
Last modified: May 14, 2014
This is version 45 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