ID A0A346PVI6_9EURY Unreviewed; 359 AA.
AC A0A346PVI6; A0A346PJU9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Putative [LysW]-lysine/[LysW]-ornithine hydrolase {ECO:0000256|HAMAP-Rule:MF_01120};
DE EC=3.5.1.130 {ECO:0000256|HAMAP-Rule:MF_01120};
DE EC=3.5.1.132 {ECO:0000256|HAMAP-Rule:MF_01120};
GN Name=lysK {ECO:0000256|HAMAP-Rule:MF_01120};
GN ORFNames=AArc1_3502 {ECO:0000313|EMBL:AXR79794.1}, AArcMg_3558
GN {ECO:0000313|EMBL:AXR83531.1};
OS Natrarchaeobaculum sulfurireducens.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Natrialbales;
OC Natrialbaceae; Natrarchaeobaculum.
OX NCBI_TaxID=2044521 {ECO:0000313|EMBL:AXR83531.1, ECO:0000313|Proteomes:UP000258613};
RN [1] {ECO:0000313|Proteomes:UP000258707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArc1 {ECO:0000313|Proteomes:UP000258707};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena Md.C., Ferrer M., Messina E.,
RA Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT reducing natronoarchaea from hypersaline soda lakes.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000258613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AArc-Mg {ECO:0000313|Proteomes:UP000258613};
RA Sorokin D.Y., Kublanov I.V., Roman P., Sinninghe Damste J.S.,
RA Golyshin P.N., Rojo D., Ciordia S., Mena M.D.C., Ferrer M., Messina E.,
RA Smedile F., La Spada G., La Cono V., Yakimov M.M.;
RT "Phenotypic and genomic properties of facultatively anaerobic sulfur-
RT reducing natronoarchaea from hypersaline soda lakes.";
RL Submitted (FEB-2018) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AXR83531.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=AArc-Mg {ECO:0000313|EMBL:AXR83531.1}, and AArc1
RC {ECO:0000313|EMBL:AXR79794.1};
RX PubMed=31166158;
RA Sorokin D.Y., Yakimov M., Messina E., Merkel A.Y., Bale N.J.,
RA Sinninghe Damste J.S.;
RT "Natronolimnobius sulfurireducens sp. nov. and Halalkaliarchaeum
RT desulfuricum gen. nov., sp. nov., the first sulfur-respiring alkaliphilic
RT haloarchaea from hypersaline alkaline lakes.";
RL Int. J. Syst. Evol. Microbiol. 69:2662-2673(2019).
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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01120};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01120};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_01120};
CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_01120};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis.
CC {ECO:0000256|HAMAP-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:0000256|HAMAP-Rule:MF_01120}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01120}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. LysK subfamily.
CC {ECO:0000256|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; CP024047; AXR79794.1; -; Genomic_DNA.
DR EMBL; CP027033; AXR83531.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A346PVI6; -.
DR KEGG; nag:AArcMg_3558; -.
DR KEGG; nan:AArc1_3502; -.
DR OrthoDB; 156068at2157; -.
DR UniPathway; UPA00033; UER00039.
DR UniPathway; UPA00068; -.
DR Proteomes; UP000258613; Chromosome.
DR Proteomes; UP000258707; 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 Gene3D; 3.40.630.10; Zn peptidases; 2.
DR HAMAP; MF_01120; LysK; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR010175; LysK.
DR InterPro; IPR002933; Peptidase_M20.
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; PF01546; Peptidase_M20; 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 {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW Rule:MF_01120}; Arginine biosynthesis {ECO:0000256|HAMAP-Rule:MF_01120};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285, ECO:0000256|HAMAP-Rule:MF_01120};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_01120};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_01120};
KW Lysine biosynthesis {ECO:0000256|ARBA:ARBA00023154, ECO:0000256|HAMAP-
KW Rule:MF_01120};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01120}; Reference proteome {ECO:0000313|Proteomes:UP000258613};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01120}.
FT ACT_SITE 74
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT ACT_SITE 125
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT BINDING 72
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT BINDING 100
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT BINDING 126
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT BINDING 150
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT BINDING 328
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
SQ SEQUENCE 359 AA; 38414 MW; CABC50AA5510DCA8 CRC64;
MSASMDDTTA VSLEDARTLL VDLVSIPSPS GEEREAAKRL VDFFEAHDRE VWIDAVGNVR
APADDSVLLT SHIDTVPGDI PVEVEATGDD EILWGRGSVD ATGPLAAMAA AAVRTGVSFV
GVVGEEVDSS GSRYLIDDRE TAPEAVVNGE PSGANGITLG YRGLLAGTYV ATSESGHTSR
PDPNAIQHAV SWWSAVEDRF EGGEYEPIFE QVTTKPVDIQ GGISEDGLSV EATMDVQLRV
PPALDVETVR EAAEAELEVG TVTWKDKVPP VMMSPRTEVA RAFRVAIRNE GEEPRLLRKT
GTSDMNVYAS AWDCPMATYG PGNSDLDHAP DERLSLAEFD RSVAILERVA TTLSEGDDE
//
