ID   Q1AX76_RUBXD            Unreviewed;       426 AA.
AC   Q1AX76;
DT   11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2006, sequence version 1.
DT   27-MAR-2024, entry version 91.
DE   SubName: Full=Acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:ABG04002.1};
GN   OrderedLocusNames=Rxyl_1036 {ECO:0000313|EMBL:ABG04002.1};
OS   Rubrobacter xylanophilus (strain DSM 9941 / NBRC 16129 / PRD-1).
OC   Bacteria; Actinomycetota; Rubrobacteria; Rubrobacterales; Rubrobacteraceae;
OC   Rubrobacter.
OX   NCBI_TaxID=266117 {ECO:0000313|EMBL:ABG04002.1, ECO:0000313|Proteomes:UP000006637};
RN   [1] {ECO:0000313|EMBL:ABG04002.1, ECO:0000313|Proteomes:UP000006637}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9941 / NBRC 16129 / PRD-1
RC   {ECO:0000313|Proteomes:UP000006637};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., da Costa M.S.,
RA   Rainey F.A., Empadinhas N., Jolivet E., Battista J.R., Richardson P.;
RT   "Complete sequence of Rubrobacter xylanophilus DSM 9941.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000386; ABG04002.1; -; Genomic_DNA.
DR   RefSeq; WP_011564020.1; NC_008148.1.
DR   AlphaFoldDB; Q1AX76; -.
DR   STRING; 266117.Rxyl_1036; -.
DR   KEGG; rxy:Rxyl_1036; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_0_0_11; -.
DR   OrthoDB; 7055905at2; -.
DR   PhylomeDB; Q1AX76; -.
DR   Proteomes; UP000006637; Chromosome.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
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; TIGR01910; DapE-ArgE; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF3; ACETYLORNITHINE DEACETYLASE-RELATED; 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   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006637}.
FT   DOMAIN          200..313
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   426 AA;  44796 MW;  8E4643B87925B834 CRC64;
     MNDGALLDAV AAEAGWMEEL LVSLVEAPTT LGNEEPGQRV MEEALADCGL KVRSVPLDAD
     ALRSAEGASP FSWDVSGKRN VVADWPAGGG GGRSLILNGH IDVVPPAAEE LWARPPFAAA
     REGDWLYGRG AGDMKAGLAA MAGAVRALSR AGYAPLAPVQ LQSVVEEECT GHGALQCLLD
     GARADACVIT EPHPDHLTTA QVGVLWFHVD IAGVPAHAAR ASRLGVGAVE AACAVLAALR
     RLERRLNEDP PPPFDALEHP INLNPGVISG GDWPSTVAAT CTLSCRIGLY PGQSPDEMRA
     LVEGAVAEAA SEDPRLAQRP PRVRYDGFAC EGAVVDGEEP VVRALAAAYE RVRGERPGLE
     ATTATTDARH FVRAGIPAVC FGPRAENIHG IDERVSLRSV VETAQVLGLF IRDWCGLVRG
     PGKEER
//