LYSK_SULAC
ID LYSK_SULAC Reviewed; 346 AA.
AC Q4JAP7;
DT 15-FEB-2017, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=[LysW]-lysine/[LysW]-ornithine hydrolase {ECO:0000255|HAMAP-Rule:MF_01120, ECO:0000305};
DE EC=3.5.1.130 {ECO:0000255|HAMAP-Rule:MF_01120, ECO:0000305|PubMed:23434852};
DE EC=3.5.1.132 {ECO:0000255|HAMAP-Rule:MF_01120, ECO:0000305|PubMed:23434852};
GN Name=lysK {ECO:0000255|HAMAP-Rule:MF_01120, ECO:0000303|PubMed:23434852};
GN OrderedLocusNames=Saci_0756 {ECO:0000312|EMBL:AAY80132.1};
OS Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS 15157 / NCIMB 11770).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=330779;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT "The genome of Sulfolobus acidocaldarius, a model organism of the
RT Crenarchaeota.";
RL J. Bacteriol. 187:4992-4999(2005).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=23434852; DOI=10.1038/nchembio.1200;
RA Ouchi T., Tomita T., Horie A., Yoshida A., Takahashi K., Nishida H.,
RA Lassak K., Taka H., Mineki R., Fujimura T., Kosono S., Nishiyama C.,
RA Masui R., Kuramitsu S., Albers S.V., Kuzuyama T., Nishiyama M.;
RT "Lysine and arginine biosyntheses mediated by a common carrier protein in
RT Sulfolobus.";
RL Nat. Chem. Biol. 9:277-283(2013).
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, ECO:0000305|PubMed:23434852}.
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 ECO:0000305|PubMed:23434852};
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 ECO:0000305|PubMed:23434852};
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, ECO:0000305|PubMed:23434852}.
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_01120, ECO:0000305|PubMed:23434852}.
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; CP000077; AAY80132.1; -; Genomic_DNA.
DR RefSeq; WP_011277634.1; NC_007181.1.
DR AlphaFoldDB; Q4JAP7; -.
DR SMR; Q4JAP7; -.
DR STRING; 330779.Saci_0756; -.
DR EnsemblBacteria; AAY80132; AAY80132; Saci_0756.
DR GeneID; 3473287; -.
DR KEGG; sai:Saci_0756; -.
DR PATRIC; fig|330779.12.peg.725; -.
DR eggNOG; arCOG01107; Archaea.
DR HOGENOM; CLU_021802_2_0_2; -.
DR OMA; HMDTVPG; -.
DR BioCyc; MetaCyc:MON-18315; -.
DR UniPathway; UPA00033; UER00039.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000001018; 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; 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 Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01902; dapE-lys-deAc; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; Arginine biosynthesis; Cobalt; Cytoplasm;
KW Hydrolase; Lysine biosynthesis; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..346
FT /note="[LysW]-lysine/[LysW]-ornithine hydrolase"
FT /id="PRO_0000438982"
FT ACT_SITE 69
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT ACT_SITE 121
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 122
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01120"
FT BINDING 145
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; 38778 MW; 480233A17734558F CRC64;
MFLEKDYLKL KIKQFLPEFL SIYTPSGEEY KAKDFFEKIA SELDLSLQVT STNSYLLGDG
DILLVGHVDT VPGFINPKEE GEIIYGRGAV DDKGPLISMI IAASILNKNG YSVTVGALSD
EENKSKGARE ILRIGKKYDY IIVGEPTNTF GVVVEYRGVI HLDILCRARS EHSSSATSNL
IFEIAKKIIN TTRINTGYDD VSIVPTIFKS GEYLNVTPSN AVVHFDIRYS VRNSKDQIMS
EIHREFEGCE IHEVEDISPV KVDVNSDIVK VFMRSIIKEN YKPTILRKRG TSDMNILKDL
ALKGILAYGP GNSSLEHTDH EKISLDEIFI ATKVYINAIE ALWPKM
