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}.
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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
//