ID LYSK_SULIY Reviewed; 346 AA. AC C3N866; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 16-JUN-2009, sequence version 1. DT 27-MAR-2024, entry version 76. DE RecName: Full=[LysW]-lysine/[LysW]-ornithine hydrolase {ECO:0000255|HAMAP-Rule:MF_01120}; DE EC=3.5.1.130 {ECO:0000255|HAMAP-Rule:MF_01120}; DE EC=3.5.1.132 {ECO:0000255|HAMAP-Rule:MF_01120}; GN Name=lysK {ECO:0000255|HAMAP-Rule:MF_01120}; GN OrderedLocusNames=YG5714_2101; OS Sulfolobus islandicus (strain Y.G.57.14 / Yellowstone #1). OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae; OC Sulfolobus. OX NCBI_TaxID=439386; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Y.G.57.14 / Yellowstone #1; RX PubMed=19435847; DOI=10.1073/pnas.0808945106; RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.; RT "Biogeography of the Sulfolobus islandicus pan-genome."; RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009). CC -!- FUNCTION: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine CC and the release of L-ornithine from [LysW]-L-ornithine. CC {ECO:0000255|HAMAP-Rule:MF_01120}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-lysyl)-L- CC glutamate + H2O = [amino-group carrier protein]-C-terminal-L- CC glutamate + L-lysine; Xref=Rhea:RHEA:48684, Rhea:RHEA-COMP:9693, CC Rhea:RHEA-COMP:9715, ChEBI:CHEBI:15377, ChEBI:CHEBI:32551, CC ChEBI:CHEBI:78525, ChEBI:CHEBI:78526; EC=3.5.1.130; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01120}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[amino-group carrier protein]-C-terminal-gamma-(L-ornithyl)-L- CC glutamate + H2O = [amino-group carrier protein]-C-terminal-L- CC glutamate + L-ornithine; Xref=Rhea:RHEA:52676, Rhea:RHEA-COMP:9693, CC Rhea:RHEA-COMP:13328, ChEBI:CHEBI:15377, ChEBI:CHEBI:46911, CC ChEBI:CHEBI:78525, ChEBI:CHEBI:136763; EC=3.5.1.132; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01120}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01120}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000255|HAMAP- CC Rule:MF_01120}; CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01120}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via AAA CC pathway; L-lysine from L-alpha-aminoadipate (Thermus route): step 5/5. CC {ECO:0000255|HAMAP-Rule:MF_01120}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01120}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01120}. CC -!- SIMILARITY: Belongs to the peptidase M20A family. LysK subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01120}. 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; CP001403; ACP46353.1; -; Genomic_DNA. DR RefSeq; WP_012711946.1; NC_012622.1. DR AlphaFoldDB; C3N866; -. DR SMR; C3N866; -. DR GeneID; 7807920; -. DR KEGG; siy:YG5714_2101; -. DR HOGENOM; CLU_021802_2_0_2; -. DR UniPathway; UPA00033; UER00039. DR UniPathway; UPA00068; -. DR Proteomes; UP000002308; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:UniProtKB-UniRule. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:UniProtKB-UniRule. DR GO; GO:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule. DR CDD; cd05653; M20_ArgE_LysK; 1. DR Gene3D; 3.30.70.360; -; 1. DR Gene3D; 3.40.630.10; Zn peptidases; 1. DR HAMAP; MF_01120; LysK; 1. DR InterPro; IPR001261; ArgE/DapE_CS. DR InterPro; IPR036264; Bact_exopeptidase_dim_dom. DR InterPro; IPR010175; LysK. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR NCBIfam; TIGR01902; dapE-lys-deAc; 1. DR PANTHER; PTHR43808:SF28; [LYSW]-LYSINE_[LYSW]-ORNITHINE HYDROLASE; 1. DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1. DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1. DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Cobalt; Cytoplasm; KW Hydrolase; Lysine biosynthesis; Metal-binding; Zinc. FT CHAIN 1..346 FT /note="[LysW]-lysine/[LysW]-ornithine hydrolase" FT /id="PRO_1000213618" FT ACT_SITE 70 FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT ACT_SITE 122 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT BINDING 68 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT BINDING 92 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT BINDING 123 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT BINDING 146 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="1" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" FT BINDING 317 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_label="2" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120" SQ SEQUENCE 346 AA; 38769 MW; BDE8A5BEEBA0BAF6 CRC64; MQQEKELVKQ KAKELLLDLL SIYTPSKNET NATKFFEKIS NEFNLKLEIL PDSNSFILGE GEILLASHVD TVPGYIEPKI ENEVIYGRGA VDAKGPLISM IIAAWLLNEK GIKVMVSGLA DEESTSIGAK ELTLKNFNFK HIIVGEPSNG TDIVVEYRGS IQLDIMCEST PEHSSSAKSN LIVDISKKII EVYKQPENYD KPSIVPTIIR AGESYNVTPA KLYLHFDVRY AINNKRDDLI NEIKDKFQEC GLKIVDETPP VKVSINNPVV KSLTRALLKQ NIKPRLVRKA GTSDMNILQK ITTSIATYGP GNSMLEHTNQ EKITLDEIYI GVKTYMLAIE ELWQKS //