458aa long hypothetical endo-1,4-beta-glucanase - Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)

Preferred order of sections

Names and origin

Protein names

Submitted name:
458aa long hypothetical endo-1,4-beta-glucanase EMBL BAA30271.1

Gene names

Ordered Locus Names:

PH1171

Organism

Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]

Taxonomic identifier

70601 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	458 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

Ontologies

Keywords
Ligand	Metal-binding PDB 2ZUM Zinc PDB 2ZUM
Technical term	3D-structure PDB 2ZUM PDB 2ZUN Complete proteome
Gene Ontology (GO)
Biological process	carbohydrate metabolic process Inferred from electronic annotation. Source: InterPro
Molecular function	hydrolase activity, hydrolyzing O-glycosyl compounds Inferred from electronic annotation. Source: InterPro metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Sites

Metal binding

47

1

Zinc 1 PDB 2ZUM

Metal binding

62

1

Zinc 1; via pros nitrogen PDB 2ZUM

Metal binding

161

1

Zinc 2; via tele nitrogen PDB 2ZUM

Metal binding

372

1

Zinc 1 PDB 2ZUM

Metal binding

373

1

Zinc 1 PDB 2ZUM

Sequences

Sequence

Length

Mass (Da)

Tools

O58925 [UniParc].

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

FASTA

458

51,930

        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' referencesShow '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. Kikuchi H. DNA Res. 5:55-76(1998) [PubMed: 9679194] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 and OT3.
[2]	"Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii." Kim H.W., Ishikawa K. Proteins 78:496-500(2010) [PubMed: 19847920] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC.
[3]	"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).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

BA000001 Genomic DNA. Translation: BAA30271.1.

PIR

E71059.

RefSeq

NP_143072.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

O58925.

ModBase

Search...

Protein family/group databases

CAZy

GH5. Glycoside Hydrolase Family 5.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBPYRT00000000979; EBPYRP00000000979; EBPYRG00000000979.

GeneID

1443490.

GenomeReviews

Gene locus PH1171 in contig BA000001_GR.

KEGG

pho:PH1171.

NMPDR

fig|70601.1.peg.1143.

Organism-specific databases

CMR

Search...

Phylogenomic databases

GeneTree

EBGT00050000022752.

OMA

PDANNSG.

ProtClustDB

CLSK380027.

Enzyme and pathway databases

BioCyc

PHOR70601:PH1171-MONOMER.

Family and domain databases

InterPro

IPR001547. Glyco_hydro_5.
IPR018087. Glyco_hydro_5_CS.
IPR013781. Glyco_hydro_subgr_catalytic.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]

Gene3D

G3DSA:3.20.20.80. Glyco_hydro_cat. 1 hit.

KO

K01179.

Pfam

PF00150. Cellulase. 1 hit.
[Graphical view]

SUPFAM

SSF51445. Glyco_hydro_cat. 1 hit.

PROSITE

PS00659. GLYCOSYL_HYDROL_F5. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

O58925_PYRHO

Accession

Primary (citable) accession number: O58925

Entry history

Integrated into UniProtKB/TrEMBL:	August 1, 1998
Last sequence update:	August 1, 1998
Last modified:	November 16, 2011
This is version 73 of the entry and version 1 of the sequence. [Complete history]

Entry status

Unreviewed (UniProtKB/TrEMBL)