ID O58925_PYRHO Unreviewed; 458 AA. AC O58925; DT 01-AUG-1998, integrated into UniProtKB/TrEMBL. DT 01-AUG-1998, sequence version 1. DT 27-MAR-2024, entry version 146. DE SubName: Full=458aa long hypothetical endo-1,4-beta-glucanase {ECO:0000313|EMBL:BAA30271.1}; GN OrderedLocusNames=PH1171 {ECO:0000313|EMBL:BAA30271.1}; OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC OS 100139 / OT-3). OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae; OC Pyrococcus. OX NCBI_TaxID=70601 {ECO:0000313|EMBL:BAA30271.1, ECO:0000313|Proteomes:UP000000752}; RN [1] {ECO:0000313|EMBL:BAA30271.1, ECO:0000313|Proteomes:UP000000752} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3 RC {ECO:0000313|Proteomes:UP000000752}; RX PubMed=9679194; DOI=10.1093/dnares/5.2.55; RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., RA Otuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T., RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Nakamura Y., RA Robb T.F., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.; RT "Complete sequence and gene organization of the genome of a hyper- RT thermophilic archaebacterium, Pyrococcus horikoshii OT3."; RL DNA Res. 5:55-76(1998). RN [2] {ECO:0007829|PDB:2ZUN} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS), AND DISULFIDE BONDS. RA Kim H.-W., Ishikawa K.; RT "Functional Analysis of Hyperthermophilic Endocellulase from the Archaeon RT Pyrococcus horikoshii."; RL Submitted (OCT-2008) to the PDB data bank. RN [3] {ECO:0007829|PDB:2ZUM} RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH ZINC, AND DISULFIDE RP BONDS. RX PubMed=19847920; DOI=10.1002/prot.22602; RA Kim H.W., Ishikawa K.; RT "Structure of hyperthermophilic endocellulase from Pyrococcus horikoshii."; RL Proteins 78:496-500(2010). RN [4] {ECO:0007829|PDB:3AXX, ECO:0007829|PDB:3QHM} RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS), AND DISULFIDE BONDS. RX PubMed=21557724; DOI=10.1042/BJ20110292; RA Kim H.W., Ishikawa K.; RT "Functional analysis of hyperthermophilic endocellulase from Pyrococcus RT horikoshii by crystallographic snapshots."; RL Biochem. J. 437:223-230(2011). RN [5] {ECO:0007829|PDB:4DM1, ECO:0007829|PDB:4DM2} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 34-410, X-RAY CRYSTALLOGRAPHY RP (1.95 ANGSTROMS) OF 34-410, AND DISULFIDE BONDS. RA Kim H.-W., Ishikawa K.; RT "Contribution of disulfide bond toward thermostability in hyperthermostable RT endocellulase."; RL Submitted (FEB-2012) to the PDB data bank. RN [6] {ECO:0007829|PDB:3VVG} RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 34-410, AND DISULFIDE BONDS. RA Ishikawa K., Maeno Y., Kataoka M.; RT "The Crystal Structure of Cellulase-Inhibitor Complex."; RL Submitted (JUL-2012) to the PDB data bank. RN [7] {ECO:0007829|PDB:3W6L, ECO:0007829|PDB:3W6M} RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 34-410, AND DISULFIDE BONDS. RX PubMed=23624891; DOI=10.1007/s00792-013-0542-8; RA Kim H.W., Ishikawa K.; RT "The role of disulfide bond in hyperthermophilic endocellulase."; RL Extremophiles 17:593-599(2013). CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BA000001; BAA30271.1; -; Genomic_DNA. DR PIR; E71059; E71059. DR RefSeq; WP_010885255.1; NC_000961.1. DR PDB; 2ZUM; X-ray; 1.95 A; A=1-458. DR PDB; 2ZUN; X-ray; 2.00 A; A/B/C=1-458. DR PDB; 3AXX; X-ray; 1.90 A; A/B/C=1-458. DR PDB; 3QHM; X-ray; 2.01 A; A/B/C=1-458. DR PDB; 3QHN; X-ray; 1.99 A; A/B/C=1-458. DR PDB; 3QHO; X-ray; 1.65 A; A/B/C=1-458. DR PDB; 3VVG; X-ray; 1.90 A; A/B/C=34-410. DR PDB; 3W6L; X-ray; 1.75 A; A/B/C=34-410. DR PDB; 3W6M; X-ray; 1.95 A; A/B/C=34-410. DR PDB; 4DM1; X-ray; 1.75 A; A/B/C=34-410. DR PDB; 4DM2; X-ray; 1.95 A; A/B/C=34-410. DR PDBsum; 2ZUM; -. DR PDBsum; 2ZUN; -. DR PDBsum; 3AXX; -. DR PDBsum; 3QHM; -. DR PDBsum; 3QHN; -. DR PDBsum; 3QHO; -. DR PDBsum; 3VVG; -. DR PDBsum; 3W6L; -. DR PDBsum; 3W6M; -. DR PDBsum; 4DM1; -. DR PDBsum; 4DM2; -. DR AlphaFoldDB; O58925; -. DR SMR; O58925; -. DR STRING; 70601.gene:9378132; -. DR CAZy; GH5; Glycoside Hydrolase Family 5. DR EnsemblBacteria; BAA30271; BAA30271; BAA30271. DR GeneID; 1443490; -. DR KEGG; pho:PH1171; -. DR eggNOG; arCOG07700; Archaea. DR OrthoDB; 103509at2157; -. DR BRENDA; 3.2.1.4; 5244. DR EvolutionaryTrace; O58925; -. DR Proteomes; UP000000752; Chromosome. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; Glycosidases; 1. DR InterPro; IPR027552; CGP_CTERM. DR InterPro; IPR001547; Glyco_hydro_5. DR InterPro; IPR018087; Glyco_hydro_5_CS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR NCBIfam; TIGR04288; CGP_CTERM; 1. DR PANTHER; PTHR35923:SF2; CELLULASE DOMAIN-CONTAINING PROTEIN; 1. DR PANTHER; PTHR35923; MAJOR EXTRACELLULAR ENDOGLUCANASE; 1. DR Pfam; PF00150; Cellulase; 1. DR SUPFAM; SSF51445; (Trans)glycosidases; 1. DR PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:2ZUM, ECO:0007829|PDB:2ZUN}; KW Glycosidase {ECO:0000256|ARBA:ARBA00023295}; KW Hydrolase {ECO:0000256|ARBA:ARBA00022801}; KW Metal-binding {ECO:0007829|PDB:2ZUM}; Zinc {ECO:0007829|PDB:2ZUM}. FT DOMAIN 65..382 FT /note="Glycoside hydrolase family 5" FT /evidence="ECO:0000259|Pfam:PF00150" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 62 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 76 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 108 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="3" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 201 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 321 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 325 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="5" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 342 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="4" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 349 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 372 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 373 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 400 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="6" FT /evidence="ECO:0007829|PDB:2ZUM" FT BINDING 410 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0007829|PDB:2ZUM" FT DISULFID 106..159 FT /evidence="ECO:0007829|PDB:2ZUM, ECO:0007829|PDB:2ZUN" SQ SEQUENCE 458 AA; 51930 MW; CAE48AD43A8EE654 CRC64; MEGNTILKIV LICTILAGLF GQVVPVYAEN TTYQTPTGIY YEVRGDTIYM INVTSGEETP IHLFGVNWFG FETPNHVVHG LWKRNWEDML LQIKSLGFNA IRLPFCTESV KPGTQPIGID YSKNPDLRGL DSLQIMEKII KKAGDLGIFV LLDYHRIGCT HIEPLWYTED FSEEDFINTW IEVAKRFGKY WNVIGADLKN EPHSVTSPPA AYTDGTGATW GMGNPATDWN LAAERIGKAI LKVAPHWLIF VEGTQFTNPK TDSSYKWGYN AWWGGNLMAV KDYPVNLPRN KLVYSPHVYG PDVYNQPYFG PAKGFPDNLP DIWYHHFGYV KLELGYSVVI GEFGGKYGHG GDPRDVIWQN KLVDWMIENK FCDFFYWSWN PDSGDTGGIL QDDWTTIWED KYNNLKRLMD SCSKSSSSTQ SVIRSTTPTK SNTSKKICGP AILIILAVFS LLLRRAPR //