LYSK_THET8
ID LYSK_THET8 Reviewed; 361 AA.
AC Q5SHH3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=[LysW]-lysine hydrolase {ECO:0000255|HAMAP-Rule:MF_01120};
DE EC=3.5.1.130 {ECO:0000255|HAMAP-Rule:MF_01120};
GN Name=lysK {ECO:0000255|HAMAP-Rule:MF_01120}; OrderedLocusNames=TTHA1757;
OS Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=300852;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27634 / DSM 579 / HB8;
RA Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT "Complete genome sequence of Thermus thermophilus HB8.";
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the release of L-lysine from [LysW]-gamma-L-lysine.
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 -!- 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 -!- 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; AP008226; BAD71580.1; -; Genomic_DNA.
DR RefSeq; WP_011228894.1; NC_006461.1.
DR RefSeq; YP_145023.1; NC_006461.1.
DR AlphaFoldDB; Q5SHH3; -.
DR SMR; Q5SHH3; -.
DR STRING; 300852.55773139; -.
DR MEROPS; M20.022; -.
DR PRIDE; Q5SHH3; -.
DR EnsemblBacteria; BAD71580; BAD71580; BAD71580.
DR GeneID; 3170012; -.
DR KEGG; ttj:TTHA1757; -.
DR PATRIC; fig|300852.9.peg.1728; -.
DR eggNOG; COG0624; Bacteria.
DR HOGENOM; CLU_021802_2_0_0; -.
DR OMA; HMDTVPG; -.
DR PhylomeDB; Q5SHH3; -.
DR UniPathway; UPA00033; UER00039.
DR Proteomes; UP000000532; 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:0019878; P:lysine biosynthetic process via aminoadipic acid; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01120; LysK; 1.
DR InterPro; IPR010175; LysK.
DR InterPro; IPR002933; Peptidase_M20.
DR Pfam; PF01546; Peptidase_M20; 1.
DR TIGRFAMs; TIGR01902; dapE-lys-deAc; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Cobalt; Cytoplasm; Hydrolase; Lysine biosynthesis;
KW Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..361
FT /note="[LysW]-lysine hydrolase"
FT /id="PRO_1000065261"
FT ACT_SITE 69
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT ACT_SITE 124
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 67
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 91
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 125
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 148
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 326
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
SQ SEQUENCE 361 AA; 39594 MW; 8D410C5DD6EC294E CRC64;
MSKSALDPVE FLKGALEIPS PSGKERAVAE YLAEGMQKLG LKGFVDEADN ARGQVGEGPV
QVVLLGHIDT VPGQIPVRLE GGRLFGRGAV DAKGPFVAMI FAAAGLSEEA RRRLTVHLVG
ATEEEAPSSK GARFVAPRLK PHYAVIGEPS GWEGITLGYK GRLLVKARRE KDHFHSAHHE
PNAAEELISY FVAIKAWAEA MNVGQRPFDQ VQYTLRDFRV HPAELRQVAE MFFDLRLPPR
LPPEEAIRHL TAYAPPTIEL EFFGREVPYQ GPKDTPLTRA FRQAIRKAGG RPVFKLKTGT
SDMNVLAPHW PVPMVAYGPG DSTLDHTPYE HVEVAEFLKG IEVLRGALEA LAQTHAGEKE
G
