ID LYSK_SULIK Reviewed; 346 AA.
AC C4KJ24;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 75.
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}; OrderedLocusNames=M164_1984;
OS Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=426118;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M.16.4 / Kamchatka #3;
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;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01120};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000255|HAMAP-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}.
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DR EMBL; CP001402; ACR42588.1; -; Genomic_DNA.
DR RefSeq; WP_012736078.1; NC_012726.1.
DR AlphaFoldDB; C4KJ24; -.
DR SMR; C4KJ24; -.
DR MEROPS; M20.975; -.
DR GeneID; 84062289; -.
DR KEGG; sid:M164_1984; -.
DR HOGENOM; CLU_021802_2_0_2; -.
DR UniPathway; UPA00033; UER00039.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001479; 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_1000213614"
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; 38768 MW; 5DE6A11EEF0414FC CRC64;
MQQEKELVKQ KAKELLLDLL SIYTPSKNET NATKFFEKIS NEFNLKLEIL PDSNSFILGE
GEILLASHVD TVPGYIEPKI ENEVIYGRGA VDAKGPLISM IIAAWLLNEK GIKVMVSGLA
DEESTSIGAK ELTLKNFNFK HIIVGEPSNG TDIVVEYRGS IQLDIMCKST PEHSSSAKSN
LIVDISKKII EVYKQPENYD KPSIVPTIIR AGESYNVTPA KLYLHFDVRY AINNKRDDLI
NEIKDKFQEC GLKIVDETPP VKVSINNPVV KSLTRALLKQ NIKPRLVRKA GTSDMNILQK
ITTSIATYGP GNSMLEHTNQ EKITLDEIYI GVKTYMLAIE ELWQKS
//
