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Database: UniProt
Entry: D4GYN7_HALVD
LinkDB: D4GYN7_HALVD
Original site: D4GYN7_HALVD 
ID   D4GYN7_HALVD            Unreviewed;       381 AA.
AC   D4GYN7; L9UH14;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 81.
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=argE {ECO:0000313|EMBL:ADE02924.1};
GN   Synonyms=lysK {ECO:0000256|HAMAP-Rule:MF_01120};
GN   OrderedLocusNames=HVO_0042 {ECO:0000313|EMBL:ADE02924.1};
OS   Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS   NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloferax.
OX   NCBI_TaxID=309800 {ECO:0000313|EMBL:ADE02924.1, ECO:0000313|Proteomes:UP000008243};
RN   [1] {ECO:0000313|EMBL:ADE02924.1, ECO:0000313|Proteomes:UP000008243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 /
RC   VKM B-1768 / DS2 {ECO:0000313|Proteomes:UP000008243};
RX   PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA   Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA   Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA   Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT   "The complete genome sequence of Haloferax volcanii DS2, a model
RT   archaeon.";
RL   PLoS ONE 5:E9605-E9605(2010).
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}.
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DR   EMBL; CP001956; ADE02924.1; -; Genomic_DNA.
DR   RefSeq; WP_004045045.1; NZ_AOHU01000105.1.
DR   AlphaFoldDB; D4GYN7; -.
DR   STRING; 309800.HVO_0042; -.
DR   PaxDb; 309800-C498_18443; -.
DR   EnsemblBacteria; ADE02924; ADE02924; HVO_0042.
DR   GeneID; 8925359; -.
DR   KEGG; hvo:HVO_0042; -.
DR   PATRIC; fig|309800.29.peg.3587; -.
DR   eggNOG; arCOG01107; Archaea.
DR   HOGENOM; CLU_021802_2_0_2; -.
DR   OMA; HMDTVPG; -.
DR   OrthoDB; 156068at2157; -.
DR   UniPathway; UPA00033; UER00039.
DR   UniPathway; UPA00068; -.
DR   Proteomes; UP000008243; 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-RELATED; 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:UP000008243};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01120}.
FT   REGION          1..32
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..17
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        18..32
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        104
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   ACT_SITE        151
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   BINDING         102
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         126
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   BINDING         152
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
FT   BINDING         353
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01120"
SQ   SEQUENCE   381 AA;  41031 MW;  FC112E7B2479578A CRC64;
     MNAEIDREGH DESETEAESA AETAADTEVD ADADTDALDE GEWVDARHLL YDMVSTPSVS
     GDEEAAAEVL KAFFEAHDRE VWIDEVGNVR APADDAVLLT SHVDTVPGDV PVKVEDGVLW
     GRGSVDATGP LCTMAAAAVE TGVSFVGVVG EETSSRGAWH LVEDREEPDA VVNGEPSGWD
     GVTLGYRGFL SGTYISTSEL GHSSRPEENA IQSAVAWWSR VADFFDEDRD GVFDTVTTKP
     VTFDGGPTED GLAVEATVDV QFRVPPRLSI DDVREVAESE LTRGGVHWNK PIPPVMMSPR
     TDVARAFRVA IRNVGGVKPR LLRKTGTSDM NIFAGTWDCP MATYGPGDSD LDHAPNEHLD
     LAEFDSAIDV LVDVCERLAD D
//
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