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O58925 (O58925_PYRHO) Unreviewed, UniProtKB/TrEMBL

Last modified December 11, 2013. Version 90. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein names
Gene names
Ordered Locus Names:PH1171 EMBL BAA30271.1
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP] EMBL BAA30271.1
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length458 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Region118 – 1192Phosphate 1 binding

Sites

Metal binding471Zinc 1 PDB 2ZUM
Metal binding621Zinc 1; via pros nitrogen PDB 2ZUM
Metal binding3211Zinc 2 PDB 2ZUM
Metal binding3251Zinc 2; via tele nitrogen PDB 2ZUM
Metal binding3721Zinc 1 PDB 2ZUM
Metal binding3731Zinc 1 PDB 2ZUM
Binding site721Acetate PDB 2ZUM
Binding site1561Acetate PDB 2ZUM
Binding site1901Phosphate 3 PDB 4DM1 PDB 3W6L
Binding site1911Phosphate 2; via amide nitrogen PDB 4DM1 PDB 3W6L
Binding site1911Phosphate 4 PDB 3VVG

Sequences

Sequence LengthMass (Da)Tools
O58925 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: CAE48AD43A8EE654

FASTA45851,930
        10         20         30         40         50         60 
MEGNTILKIV LICTILAGLF GQVVPVYAEN TTYQTPTGIY YEVRGDTIYM INVTSGEETP 

        70         80         90        100        110        120 
IHLFGVNWFG FETPNHVVHG LWKRNWEDML LQIKSLGFNA IRLPFCTESV KPGTQPIGID 

       130        140        150        160        170        180 
YSKNPDLRGL DSLQIMEKII KKAGDLGIFV LLDYHRIGCT HIEPLWYTED FSEEDFINTW 

       190        200        210        220        230        240 
IEVAKRFGKY WNVIGADLKN EPHSVTSPPA AYTDGTGATW GMGNPATDWN LAAERIGKAI 

       250        260        270        280        290        300 
LKVAPHWLIF VEGTQFTNPK TDSSYKWGYN AWWGGNLMAV KDYPVNLPRN KLVYSPHVYG 

       310        320        330        340        350        360 
PDVYNQPYFG PAKGFPDNLP DIWYHHFGYV KLELGYSVVI GEFGGKYGHG GDPRDVIWQN 

       370        380        390        400        410        420 
KLVDWMIENK FCDFFYWSWN PDSGDTGGIL QDDWTTIWED KYNNLKRLMD SCSKSSSSTQ 

       430        440        450 
SVIRSTTPTK SNTSKKICGP AILIILAVFS LLLRRAPR 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]"Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon Pyrococcus horikoshii."
Kim H.-W., Ishikawa K.
Submitted (OCT-2008) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
[3]"Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii."
Kim H.W., Ishikawa K.
Proteins 78:496-500(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ACETATE AND ZINC.
[4]"Functional analysis of hyperthermophilic endocellulase from Pyrococcus horikoshii by crystallographic snapshots."
Kim H.W., Ishikawa K.
Biochem. J. 437:223-230(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH PHOSPHATE.
[5]"Contribution of disulfide bond toward thermostability in hyperthermostable endocellulase."
Kim H.-W., Ishikawa K.
Submitted (FEB-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 34-410.
[6]"The Crystal Structure of Cellulase-Inhibitor Complex."
Ishikawa K., Maeno Y., Kataoka M.
Submitted (JUL-2012) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 34-410 IN COMPLEX WITH PHOSPHATE.
[7]"The role of disulfide bond in hyperthermophilic endocellulase."
Kim H.W., Ishikawa K.
Extremophiles 17:593-599(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 34-410 IN COMPLEX WITH PHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA30271.1.
PIRE71059.
RefSeqNP_143072.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2ZUMX-ray1.95A1-458[»]
2ZUNX-ray2.00A/B/C1-458[»]
3AXXX-ray1.90A/B/C1-458[»]
3QHMX-ray2.01A/B/C1-458[»]
3QHNX-ray1.99A/B/C1-458[»]
3QHOX-ray1.65A/B/C1-458[»]
3VVGX-ray1.90A/B/C34-410[»]
3W6LX-ray1.75A/B/C34-410[»]
3W6MX-ray1.95A/B/C34-410[»]
4DM1X-ray1.75A/B/C34-410[»]
4DM2X-ray1.95A/B/C34-410[»]
ProteinModelPortalO58925.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH1171.

Protein family/group databases

CAZyGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA30271; BAA30271; BAA30271.
GeneID1443490.
KEGGpho:PH1171.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000225207.
KOK01179.
OMAKYKNDDT.
ProtClustDBCLSK380027.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-1162-MONOMER.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR027552. CGP_CTERM.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
TIGRFAMsTIGR04288. CGP_CTERM. 1 hit.
PROSITEPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO58925.

Entry information

Entry nameO58925_PYRHO
AccessionPrimary (citable) accession number: O58925
Entry history
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: December 11, 2013
This is version 90 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)