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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: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi47 – 471Zinc 1
Metal bindingi62 – 621Zinc 1; via pros nitrogen
Metal bindingi321 – 3211Zinc 2
Metal bindingi325 – 3251Zinc 2; via tele nitrogen
Metal bindingi372 – 3721Zinc 1
Metal bindingi373 – 3731Zinc 1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1162-MONOMER.
BRENDAi3.2.1.4. 5244.

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 Componenti: Chromosome

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi74 ↔ 159Combined sources

Interactioni

Protein-protein interaction databases

STRINGi70601.PH1171.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO58925.

Family & Domainsi

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000225207.
KOiK01179.
OMAiWGCGDTA.

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

        10         20         30         40         50
MEGNTILKIV LICTILAGLF GQVVPVYAEN TTYQTPTGIY YEVRGDTIYM
60 70 80 90 100
INVTSGEETP IHLFGVNWFG FETPNHVVHG LWKRNWEDML LQIKSLGFNA
110 120 130 140 150
IRLPFCTESV KPGTQPIGID YSKNPDLRGL DSLQIMEKII KKAGDLGIFV
160 170 180 190 200
LLDYHRIGCT HIEPLWYTED FSEEDFINTW IEVAKRFGKY WNVIGADLKN
210 220 230 240 250
EPHSVTSPPA AYTDGTGATW GMGNPATDWN LAAERIGKAI LKVAPHWLIF
260 270 280 290 300
VEGTQFTNPK TDSSYKWGYN AWWGGNLMAV KDYPVNLPRN KLVYSPHVYG
310 320 330 340 350
PDVYNQPYFG PAKGFPDNLP DIWYHHFGYV KLELGYSVVI GEFGGKYGHG
360 370 380 390 400
GDPRDVIWQN KLVDWMIENK FCDFFYWSWN PDSGDTGGIL QDDWTTIWED
410 420 430 440 450
KYNNLKRLMD SCSKSSSSTQ SVIRSTTPTK SNTSKKICGP AILIILAVFS

LLLRRAPR
Length:458
Mass (Da):51,930
Last modified:August 1, 1998 - v1
Checksum:iCAE48AD43A8EE654
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30271.1.
PIRiE71059.
RefSeqiNP_143072.1. NC_000961.1.
WP_010885255.1. NC_000961.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1171.

Protein family/group databases

CAZyiGH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Phylogenomic databases

eggNOGiCOG2730.
HOGENOMiHOG000225207.
KOiK01179.
OMAiWGCGDTA.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1162-MONOMER.
BRENDAi3.2.1.4. 5244.

Miscellaneous databases

EvolutionaryTraceiO58925.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3Imported.
  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), DISULFIDE BONDS.
  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, DISULFIDE BONDS.
  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), DISULFIDE BONDS.
  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 (1.75 ANGSTROMS) OF 34-410, DISULFIDE BONDS.
  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, DISULFIDE BONDS.
  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, DISULFIDE BONDS.

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: July 22, 2015
This is version 103 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sources, Complete proteomeImported

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.