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A0LDB0 (PUR9_MAGSM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. 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:Mmc1_3468
OrganismMagnetococcus sp. (strain MC-1) [Complete proteome] [HAMAP]
Taxonomic identifier156889 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaMagnetococcalesMagnetococcaceaeMagnetococcus

Protein attributes

Sequence length532 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 – 532532Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000192978

Sequences

Sequence LengthMass (Da)Tools
A0LDB0 [UniParc].

Last modified December 12, 2006. Version 1.
Checksum: 9B4C77A1369F150C

FASTA53257,270
        10         20         30         40         50         60 
MAKIKRALIS VSDKTGLVPF CQGLAEHGVS FLSTGGTARL LRESGLDVMD VSEFTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGLLGLR DNASHQQQMG EHGIEPIDMV VVNLYPFEAT VAKEGCTLEE 

       130        140        150        160        170        180 
AIENIDIGGP SMLRSAAKNY RSVTVVTDPA DYARVLESLR AHDGQCDAGL NAQLARKVYA 

       190        200        210        220        230        240 
RTAAYDAAIS NWLSALDNEG RPGAFPETYT VQFKKVQGMR YGENPHQSAA FYAESPPSEE 

       250        260        270        280        290        300 
ASLATATQLQ GKELSFNNIH DANGALELVK EFSKPAAVVV KHANPCGVAV HDGDLLAAYR 

       310        320        330        340        350        360 
MARDTDPVSA FGGIIALNRC VDVAVAKEIA QLFVEVIIAP EYDEQALELF ATKKNLRLLR 

       370        380        390        400        410        420 
VPNIGVATAV STMDLKRVTG GLLLQDRDLK QLPEGSLKVV TERAPSEAEM RDLLFAWKVV 

       430        440        450        460        470        480 
KHVKSNAIVY AKEQRTLGVG AGQMSRVDAS RIAVWKAQDT AHTAGLRENP LLGAAMASDA 

       490        500        510        520        530 
FFPFRDGVDA AAKAGAKAVI QPGGSVRDEE VIAAANEHGM AMVFTGMRHF KH 

« Hide

References

[1]"Complete sequence of Magnetococcus sp. MC-1."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Kiss H., Goodwin L.A., Brettin T., Bruce D., Han C., Tapia R., Gilna P. expand/collapse author list , Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: MC-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000471 Genomic DNA. Translation: ABK45953.1.
RefSeqYP_867359.1. NC_008576.1.

3D structure databases

ProteinModelPortalA0LDB0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING156889.Mmc1_3468.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABK45953; ABK45953; Mmc1_3468.
GeneID4482824.
KEGGmgm:Mmc1_3468.
PATRIC22433603. VBIMagSp23654_3527.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycMSP156889:GH36-3515-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_MAGSM
AccessionPrimary (citable) accession number: A0LDB0
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: December 12, 2006
Last modified: May 14, 2014
This is version 57 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