ID   G0GD73_SPITZ            Unreviewed;       422 AA.
AC   G0GD73;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:AEJ62148.1};
GN   OrderedLocusNames=Spith_1890 {ECO:0000313|EMBL:AEJ62148.1};
OS   Spirochaeta thermophila (strain ATCC 700085 / DSM 6578 / Z-1203).
OC   Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC   Spirochaeta.
OX   NCBI_TaxID=869211 {ECO:0000313|EMBL:AEJ62148.1, ECO:0000313|Proteomes:UP000007254};
RN   [1] {ECO:0000313|EMBL:AEJ62148.1, ECO:0000313|Proteomes:UP000007254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700085 / DSM 6578 / Z-1203
RC   {ECO:0000313|Proteomes:UP000007254};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Mikailova N., Pagani I.,
RA   Chertkov O., Detter J.C., Tapia R., Han C., Land M., Hauser L.,
RA   Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S.,
RA   Merkhoffer B., Schneider S., Klenk H.-P., Eisen J.A.;
RT   "The complete genome of Spirochaeta thermophila DSM 6578.";
RL   Submitted (JUN-2011) 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}.
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; CP002903; AEJ62148.1; -; Genomic_DNA.
DR   RefSeq; WP_014625473.1; NC_017583.1.
DR   AlphaFoldDB; G0GD73; -.
DR   STRING; 869211.Spith_1890; -.
DR   KEGG; stq:Spith_1890; -.
DR   HOGENOM; CLU_021802_2_2_12; -.
DR   OrthoDB; 9792335at2; -.
DR   Proteomes; UP000007254; 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:UP000007254}.
FT   DOMAIN          214..322
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   422 AA;  46701 MW;  381F4676E6935633 CRC64;
     MHEDTSKRML SYMEAHTEEM VELQRLLTSH PALSPEVGGR GEWEKAQALV EWLEAHLLRE
     AREKGVAASL SVVEVPDERA ERGSRPSILV ELWHDRNGPA FWIMTHLDVV PPGEVALWNG
     DPFTAVVKEG RIYGRGTEDN QQSMTSSIFA ARALVALGLA PERPLKLLFV ADEEFGNRYG
     IQALVTSHRS LFKEGDVFLV PDGGLPDGSM IEVAEKQLLW LKFTTRGRQC HASRPDLGKN
     AFVAASDLVV RLSRLDERFP RRNDLFVPPC STFVPSRKDP NVPNINTVPG EDVFYMDCRV
     LPEVDLAEVM GAVEALCREV EAAYGVEISV EVVQRIVSRP TPADAPLVDA LKAAVEEVYG
     VEARPMGIGG GTVAAPLRNE GFDCVVWSTV DETAHQPNEY CVIEHMVKDA GVMALLALRF
     RR
//