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O58925

- O58925_PYRHO

UniProt

O58925 - O58925_PYRHO

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Protein
Submitted name:

458aa long hypothetical endo-1,4-beta-glucanase

Gene
PH1171
Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Unreviewed - Annotation score: 2 out of 5 - Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Zinc 1Imported
Metal bindingi62 – 621Zinc 1; via pros nitrogenImported
Binding sitei190 – 1901Phosphate 3
Binding sitei191 – 1911Phosphate 2; via amide nitrogen
Binding sitei191 – 1911Phosphate 4Imported
Metal bindingi321 – 3211Zinc 2Imported
Metal bindingi325 – 3251Zinc 2; via tele nitrogenImported
Metal bindingi372 – 3721Zinc 1Imported
Metal bindingi373 – 3731Zinc 1Imported

GO - Molecular functioni

  1. hydrolase activity, hydrolyzing O-glycosyl compounds Source: InterPro
  2. metal ion binding Source: UniProtKB-KW

GO - Biological processi

  1. carbohydrate metabolic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

Metal-bindingImported, ZincImported

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1162-MONOMER.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Names & Taxonomyi

Protein namesi
Submitted name:
458aa long hypothetical endo-1,4-beta-glucanaseImported
Gene namesi
Ordered Locus Names:PH1171Imported
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)Imported
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000000752: Chromosome

Interactioni

Protein-protein interaction databases

STRINGi70601.PH1171.

Structurei

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
ProteinModelPortaliO58925.

Miscellaneous databases

EvolutionaryTraceiO58925.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni118 – 1192Phosphate 1 bindingImported

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000225207.
KOiK01179.
OMAiKYKNDDT.

Family and domain databases

Gene3Di3.20.20.80. 1 hit.
InterProiIPR027552. CGP_CTERM.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamiPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMiSSF51445. SSF51445. 1 hit.
TIGRFAMsiTIGR04288. CGP_CTERM. 1 hit.
PROSITEiPS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O58925-1 [UniParc]FASTAAdd to Basket

« Hide

MEGNTILKIV LICTILAGLF GQVVPVYAEN TTYQTPTGIY YEVRGDTIYM    50
INVTSGEETP IHLFGVNWFG FETPNHVVHG LWKRNWEDML LQIKSLGFNA 100
IRLPFCTESV KPGTQPIGID YSKNPDLRGL DSLQIMEKII KKAGDLGIFV 150
LLDYHRIGCT HIEPLWYTED FSEEDFINTW IEVAKRFGKY WNVIGADLKN 200
EPHSVTSPPA AYTDGTGATW GMGNPATDWN LAAERIGKAI LKVAPHWLIF 250
VEGTQFTNPK TDSSYKWGYN AWWGGNLMAV KDYPVNLPRN KLVYSPHVYG 300
PDVYNQPYFG PAKGFPDNLP DIWYHHFGYV KLELGYSVVI GEFGGKYGHG 350
GDPRDVIWQN KLVDWMIENK FCDFFYWSWN PDSGDTGGIL QDDWTTIWED 400
KYNNLKRLMD SCSKSSSSTQ SVIRSTTPTK SNTSKKICGP AILIILAVFS 450
LLLRRAPR 458
Length:458
Mass (Da):51,930
Last modified:August 1, 1998 - v1
Checksum:iCAE48AD43A8EE654
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA30271.1.
PIRiE71059.
RefSeqiNP_143072.1. NC_000961.1.
WP_010885255.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30271; BAA30271; BAA30271.
GeneIDi1443490.
KEGGipho:PH1171.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
BA000001 Genomic DNA. Translation: BAA30271.1 .
PIRi E71059.
RefSeqi NP_143072.1. NC_000961.1.
WP_010885255.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2ZUM X-ray 1.95 A 1-458 [» ]
2ZUN X-ray 2.00 A/B/C 1-458 [» ]
3AXX X-ray 1.90 A/B/C 1-458 [» ]
3QHM X-ray 2.01 A/B/C 1-458 [» ]
3QHN X-ray 1.99 A/B/C 1-458 [» ]
3QHO X-ray 1.65 A/B/C 1-458 [» ]
3VVG X-ray 1.90 A/B/C 34-410 [» ]
3W6L X-ray 1.75 A/B/C 34-410 [» ]
3W6M X-ray 1.95 A/B/C 34-410 [» ]
4DM1 X-ray 1.75 A/B/C 34-410 [» ]
4DM2 X-ray 1.95 A/B/C 34-410 [» ]
ProteinModelPortali O58925.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 70601.PH1171.

Protein family/group databases

CAZyi GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai BAA30271 ; BAA30271 ; BAA30271 .
GeneIDi 1443490.
KEGGi pho:PH1171.

Phylogenomic databases

eggNOGi COG2730.
HOGENOMi HOG000225207.
KOi K01179.
OMAi KYKNDDT.

Enzyme and pathway databases

BioCyci PHOR70601:GJWR-1162-MONOMER.

Miscellaneous databases

EvolutionaryTracei O58925.

Family and domain databases

Gene3Di 3.20.20.80. 1 hit.
InterProi IPR027552. CGP_CTERM.
IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view ]
Pfami PF00150. Cellulase. 1 hit.
[Graphical view ]
SUPFAMi SSF51445. SSF51445. 1 hit.
TIGRFAMsi TIGR04288. CGP_CTERM. 1 hit.
PROSITEi PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. 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 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.

Entry informationi

Entry nameiO58925_PYRHO
AccessioniPrimary (citable) accession number: O58925
Entry historyi
Integrated into UniProtKB/TrEMBL: August 1, 1998
Last sequence update: August 1, 1998
Last modified: September 3, 2014
This is version 93 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureImported, Complete proteome

External Data

Dasty 3

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