GenomeNet

Database: UniProt
Entry: A0A0V8RX22_PYROC
LinkDB: A0A0V8RX22_PYROC
Original site: A0A0V8RX22_PYROC 
ID   A0A0V8RX22_PYROC        Unreviewed;       363 AA.
AC   A0A0V8RX22;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 28.
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=CF15_07700 {ECO:0000313|EMBL:KSW12589.1};
OS   Pyrodictium occultum.
OC   Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC   Pyrodictium.
OX   NCBI_TaxID=2309 {ECO:0000313|EMBL:KSW12589.1, ECO:0000313|Proteomes:UP000053352};
RN   [1] {ECO:0000313|EMBL:KSW12589.1, ECO:0000313|Proteomes:UP000053352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PL-19 {ECO:0000313|EMBL:KSW12589.1,
RC   ECO:0000313|Proteomes:UP000053352};
RA   Utturkar S., Huber H., Leptihn S., Brown S., Stetter K.O., Podar M.;
RT   "Genome sequence of Pyrodictium occultum PL-19, a marine hyperthermophilic
RT   archaeon isolated from Volcano, Italy.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KSW12589.1}.
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; LNTB01000001; KSW12589.1; -; Genomic_DNA.
DR   RefSeq; WP_058371271.1; NZ_LNTB01000001.1.
DR   AlphaFoldDB; A0A0V8RX22; -.
DR   STRING; 2309.CF15_07700; -.
DR   OMA; HMDTVPG; -.
DR   OrthoDB; 133929at2157; -.
DR   UniPathway; UPA00033; UER00039.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000053352; Unassembled WGS sequence.
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; 3.30.70.360; -; 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-RELATED; 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.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Amino-acid biosynthesis {ECO:0000256|ARBA:ARBA00022605, ECO:0000256|HAMAP-
KW   Rule:MF_01120};
KW   Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW   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:UP000053352};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01120}.
FT   DOMAIN          160..252
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   ACT_SITE        74
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   ACT_SITE        126
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         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   BINDING         96
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   BINDING         127
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         326
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
SQ   SEQUENCE   363 AA;  39037 MW;  2EA21150918411CD CRC64;
     MYYGSRAARL LQSLVEAYSP TFMERDAARL LVEEAWRLGY SQAYLDDAGN ARLLVEPMER
     VEEPPRIALV SHIDTVPGWV EPASPPCVVR GRGAVDAKAP LAAMVAAASL YRPRRAVVEV
     VAAVGEEGPS HGAWHLVKTG WRADAVIIGE PTNTTKVAIG YRGGARLRVH CLGEPGHASS
     SWLYRSACSL VVEAYQAVEE LSEATARGYT YTVTAMSCGS GGNVVADEAT LVVDLRIPPG
     GSLEEALEKL GRRLPEGCWA EKPGSWLPPV AVRPGSPAAR ALMRGLLAEG YRAQPVLKAG
     TSDMNILYRV AGSIAAYGPG RSELSHTRHE EVTLAELDLA VRVYINAIRW LEDTLAKTRR
     SAG
//
DBGET integrated database retrieval system