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B9MS89 (PUR9_CALBD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 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:Athe_1445
OrganismCaldicellulosiruptor bescii (strain ATCC BAA-1888 / DSM 6725 / Z-1320) (Anaerocellum thermophilum) [Complete proteome] [HAMAP]
Taxonomic identifier521460 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacterales Family III. Incertae SedisCaldicellulosiruptor

Protein attributes

Sequence length513 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 – 513513Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000122943

Sequences

Sequence LengthMass (Da)Tools
B9MS89 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: DDB36EA33E928206

FASTA51358,040
        10         20         30         40         50         60 
MNKRAIISVY DKNGIVEFAK KLKEFGYDII STGGTMKYLT ENGIEVINIS DVTRFPEILD 

        70         80         90        100        110        120 
GRVKTLHPNI HAGILAMKDN REHLETLKAL DILPIDMVVV NLYPFKETIF KEDVTLDNVI 

       130        140        150        160        170        180 
ENIDIGGPTM IRAAAKNFKY TTVIVDPEDY DIVAMEIEKN GEVSYETRFY LATKVFEYTS 

       190        200        210        220        230        240 
YYDSMIFNYF KHVRKDQSFS KHFTVPLELL QYLRYGENPH QKACFYKISL PFIETSNIVN 

       250        260        270        280        290        300 
CTQLHGKELS YNNILDSDSA IELLKEFDEP TCVAIKHNNP CAVASAENIN EAYKKVYESD 

       310        320        330        340        350        360 
PISIFGGIVA FNRKVDKNVA EQLKKIFLEI VIAPEFDEDA LSILCSKKDL RVLKLASLEK 

       370        380        390        400        410        420 
TDTFYDIKSV NGGALVQEKD RMLLADQLQV VTERKPSEKE LEDLIFAWKV VKHVKSNAIV 

       430        440        450        460        470        480 
VAKDKMTLGI GTGQTNRIWA VEHAISRSRF DLKGAVLASD AFFPFSDSVE AAGKAGISAI 

       490        500        510 
IQPGGSIRDK DSIEMANRFN IAMVFTGMRH FRH 

« Hide

References

[1]"Complete sequence of chromosome of Anaerocellum thermophilum DSM 6725."
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Meincke L., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Kataeva I., Adams M.W.W.
Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-1888 / DSM 6725 / Z-1320.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001393 Genomic DNA. Translation: ACM60543.1.
RefSeqYP_002573316.1. NC_012034.1.

3D structure databases

ProteinModelPortalB9MS89.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING521460.Athe_1445.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM60543; ACM60543; Athe_1445.
GeneID7408103.
KEGGate:Athe_1445.
PATRIC20900000. VBIAnaThe135187_1513.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230373.
KOK00602.
OrthoDBEOG6QCDFF.
ProtClustDBCLSK2473383.

Enzyme and pathway databases

BioCycCBES521460:GH8H-1464-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_CALBD
AccessionPrimary (citable) accession number: B9MS89
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: February 19, 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