LYSK_PYRAE
ID LYSK_PYRAE Reviewed; 341 AA.
AC Q8ZUG2;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Putative [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=PAE2798;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
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; AE009441; AAL64445.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8ZUG2; -.
DR SMR; Q8ZUG2; -.
DR STRING; 178306.PAE2798; -.
DR EnsemblBacteria; AAL64445; AAL64445; PAE2798.
DR KEGG; pai:PAE2798; -.
DR PATRIC; fig|178306.9.peg.2088; -.
DR eggNOG; arCOG01107; Archaea.
DR HOGENOM; CLU_021802_2_0_2; -.
DR InParanoid; Q8ZUG2; -.
DR OMA; HMDTVPG; -.
DR UniPathway; UPA00033; UER00039.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000002439; 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 HAMAP; MF_01120; LysK; 1.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR010175; LysK.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01902; dapE-lys-deAc; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cobalt; Cytoplasm;
KW Hydrolase; Lysine biosynthesis; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..341
FT /note="Putative [LysW]-lysine/[LysW]-ornithine hydrolase"
FT /id="PRO_0000185346"
FT ACT_SITE 64
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT ACT_SITE 115
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 309
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
SQ SEQUENCE 341 AA; 36759 MW; 1FA4F35EE6DEBE49 CRC64;
MDVGELLEDV LRIYSPSHGE ADLAKYLLEY LKRFVPDVWI DEAGNVIAVK GSGGPVVWLH
AHMDTVPGPL PVKREGGVVW GRGAVDDKGP LVAYLKAFLD SNPRGTLVLA LVTAEEDDSA
GTEALLRGGP PRPDYVFVGE PTNLHIAYAY RGGAKVYIEL ESRGGHASSP IYDNIVEELF
AVYQEVKRAL GHAERYDAFT VTPTIIQCGE APNKVPTKCV MVLDVRIPPG KSCRDLAQAL
PPKARAGPCT EPVEVSPTNP AARALTRALL KLGVEPKLSR KWGTADFNLL VSLTKNIAAF
GPGDPALAHS EDERIDIAQV ELAAKALKLA VEELGIIPRR L
