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Database: UniProt
Entry: G2J5A8_PSEUL
LinkDB: G2J5A8_PSEUL
Original site: G2J5A8_PSEUL 
ID   G2J5A8_PSEUL            Unreviewed;       394 AA.
AC   G2J5A8;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   SubName: Full=Acetylornithine deacetylase ArgE {ECO:0000313|EMBL:BAK77253.1};
GN   Name=argE {ECO:0000313|EMBL:BAK77253.1};
GN   OrderedLocusNames=NH8B_2439 {ECO:0000313|EMBL:BAK77253.1};
OS   Pseudogulbenkiania sp. (strain NH8B).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Chromobacteriaceae; Pseudogulbenkiania.
OX   NCBI_TaxID=748280 {ECO:0000313|EMBL:BAK77253.1, ECO:0000313|Proteomes:UP000001274};
RN   [1] {ECO:0000313|Proteomes:UP000001274}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NH8B {ECO:0000313|Proteomes:UP000001274};
RX   PubMed=22038961; DOI=10.1128/JB.06127-11;
RA   Ishii S., Tago T., Nishizawa T., Oshima K., Hattori M., Senoo K.;
RT   "Complete genome sequence of the denitrifying and N(2)O-reducing bacterium
RT   Pseudogulbenkiania sp. strain NH8B.";
RL   J. Bacteriol. 193:6395-6396(2011).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947};
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; AP012224; BAK77253.1; -; Genomic_DNA.
DR   RefSeq; WP_014087503.1; NC_016002.1.
DR   AlphaFoldDB; G2J5A8; -.
DR   STRING; 748280.NH8B_2439; -.
DR   KEGG; pse:NH8B_2439; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_4_4; -.
DR   OrthoDB; 9809784at2; -.
DR   Proteomes; UP000001274; Chromosome.
DR   GO; GO:0019213; F:deacetylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006526; P:arginine biosynthetic process; IEA:InterPro.
DR   CDD; cd03894; M20_ArgE; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR010169; AcOrn-deacetyl.
DR   InterPro; IPR010182; ArgE/DapE.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01892; AcOrn-deacetyl; 1.
DR   NCBIfam; TIGR01910; DapE-ArgE; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF8; M20_DIMER DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001274}.
FT   DOMAIN          175..287
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   394 AA;  42666 MW;  912984863E78D84C CRC64;
     MTASVHDLLA TLVAFDTTSR HSNLELIRWV QRYLDSFGVA SRLTFNADGS KANLFAQIGN
     PALPAVVLSG HTDVVPVDGQ AWQTPPFELV EREGKLYGRG SADMKGFIAC VLAKVPFFLE
     LADSGRLTQS VGIALSYDEE VGCLGVRGLI DDLQQSGIKV AGCIIGEPTD MKPVVAHKGI
     AHYRCHVSGR AAHSSLTPYG VNAIEYAARL ITHIRKLADT EASFGHRHTL YDVPFTTLQT
     GTIQGGTAPN IVPKDCEFVF ECRWLPGDQP ERYVDSVRDY ASNLLEEMRA VAEESDITIE
     PTVYCPAFEA VPESAVMQYV ETLTGCCQGE GVAYATEAGL FHQAGMPSVV CGPGSIQQAH
     RPDEYVEVEQ LYACSEWLAR LGELLCTPAA GRPA
//
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