ID D4J9N2_9FIRM Unreviewed; 387 AA.
AC D4J9N2;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=Acetylornithine deacetylase or succinyl-diaminopimelate desuccinylase {ECO:0000313|EMBL:CBK81053.1};
DE EC=3.5.1.16 {ECO:0000313|EMBL:CBK81053.1};
DE EC=3.5.1.18 {ECO:0000313|EMBL:CBK81053.1};
GN ORFNames=CC1_23920 {ECO:0000313|EMBL:CBK81053.1};
OS Coprococcus catus GD/7.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=717962 {ECO:0000313|EMBL:CBK81053.1, ECO:0000313|Proteomes:UP000008798};
RN [1] {ECO:0000313|EMBL:CBK81053.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81053.1,
RC ECO:0000313|Proteomes:UP000008798};
RG metaHIT consortium -- http://www.metahit.eu/;
RA Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT "The genome sequence of Coprococcus catus GD/7.";
RL Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:CBK81053.1, ECO:0000313|Proteomes:UP000008798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD/7 {ECO:0000313|EMBL:CBK81053.1,
RC ECO:0000313|Proteomes:UP000008798};
RA Pajon A.;
RL Submitted (MAR-2010) 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; FP929038; CBK81053.1; -; Genomic_DNA.
DR AlphaFoldDB; D4J9N2; -.
DR STRING; 717962.CC1_23920; -.
DR KEGG; cct:CC1_23920; -.
DR PATRIC; fig|717962.3.peg.2291; -.
DR HOGENOM; CLU_021802_2_0_9; -.
DR Proteomes; UP000008798; Chromosome.
DR GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR CDD; cd08659; M20_ArgE_DapE-like; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 2.
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 Hydrolase {ECO:0000313|EMBL:CBK81053.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 179..276
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 387 AA; 42425 MW; 0EB6231FA1BD411E CRC64;
MSLLTSAVSM TKAMVQIDST DPGTYEKAMA DWIEQQLSDL SNVLITRENV LPGRPNLMAE
IPGPKHLPAL VMICHMDTVV IGDGWTLPPF EAIEKDGKIY GRGACDMKSG LACCLSAFIM
AARTLHASGQ TPKRTLKLIC SMDEEDFMRG SEACIRSGWV TSKDWVIDAE PTNGQIQMAH
KGRTWYEIDV EGHTAHASTP WKGADAIAAM AEIISALRQD ILNAPSHPDM GISTVTFGQI
TGGYRPYVVP DHCKLWIDMR LVPPLNTAKT TEFVQNAIYL AEEKVPGVKA AYTITGDRPP
IEMDPDSPLL TELKKACHHV TGHQPEVSCF TGYTDTAVIA GQLDNQNCMS YGPGCLEAAH
QPDEWVVIDD IIRCEKVYHQ LISSNIL
//
