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B4S133 (PUR9_ALTMD) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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:MADE_1019740
OrganismAlteromonas macleodii (strain DSM 17117 / Deep ecotype) [Complete proteome] [HAMAP]
Taxonomic identifier314275 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesAlteromonadaceaeAlteromonas

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_1000096038

Sequences

Sequence LengthMass (Da)Tools
B4S133 [UniParc].

Last modified September 23, 2008. Version 1.
Checksum: CD824E4A13D207A5

FASTA53257,731
        10         20         30         40         50         60 
MQTPKPIKRA LLSVSDKTGI LDFATALHNA GVELLSTGGT AKLLAEAGLP VKEVSDHTGH 

        70         80         90        100        110        120 
PEIMAGRVKT LHPKIHGGIL ARRGVDEAVM EENNIAPIDL VVVNLYPFAA TVANEDCTLE 

       130        140        150        160        170        180 
DAIENIDIGG PTMVRAAAKN HKDVTIVVNA ADYSRVLAEM NDNNGSLTYS TRFDLAIKAF 

       190        200        210        220        230        240 
EHTAEYDGMI ANYFGARLDS TGCEADCDHQ HSEFPRTYNI QLTKKQDLRY GENSHQEAAF 

       250        260        270        280        290        300 
YVENNIQEAS VATATQLQGK ELSFNNIADT DAALECVKEF EEPACVIVKH ANPCGVAIGN 

       310        320        330        340        350        360 
DILTAYDRAF KTDPTSAFGG IIAFNRELDA KTAHAIVDRQ FVEVIIAPAV SDEAKEVVSA 

       370        380        390        400        410        420 
KKNVRLLACG DWAGQLTEGY DFKRVNGGLL VQERDFGMVE MEDLEVVTKR KPSEEELRDL 

       430        440        450        460        470        480 
MFCWKVAKYV KSNAIVYCKD GMTVGVGAGQ MSRVYSAKIA GIKAADENLE VAGSVMASDA 

       490        500        510        520        530 
FFPFRDGIDA AAHAGIKAVI QPGGSMRDQE VIDAADEHGI AMVFTGMRHF RH 

« Hide

References

[1]"Comparative genomics of two ecotypes of the marine planktonic copiotroph Alteromonas macleodii suggests alternative lifestyles associated with different kinds of particulate organic matter."
Ivars-Martinez E., Martin-Cuadrado A.-B., D'Auria G., Mira A., Ferriera S., Johnson J., Friedman R., Rodriguez-Valera F.
ISME J. 2:1194-1212(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 17117 / Deep ecotype.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001103 Genomic DNA. Translation: AEB00071.1.

3D structure databases

ProteinModelPortalB4S133.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING314275.MADE_03939.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAEB00071; AEB00071; MADE_1019740.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
OMADLLFAWK.
ProtClustDBCLSK2315354.

Enzyme and pathway databases

BioCycAMAC314275:GHA7-3978-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_ALTMD
AccessionPrimary (citable) accession number: B4S133
Secondary accession number(s): F2GBJ4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 23, 2008
Last modified: February 19, 2014
This is version 44 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