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Database: UniProt
Entry: I0I108_CALAS
LinkDB: I0I108_CALAS
Original site: I0I108_CALAS 
ID   I0I108_CALAS            Unreviewed;       408 AA.
AC   I0I108;
DT   13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT   13-JUN-2012, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN   OrderedLocusNames=CLDAP_09060 {ECO:0000313|EMBL:BAL98945.1};
OS   Caldilinea aerophila (strain DSM 14535 / JCM 11387 / NBRC 104270 /
OS   STL-6-O1).
OC   Bacteria; Chloroflexota; Caldilineae; Caldilineales; Caldilineaceae;
OC   Caldilinea.
OX   NCBI_TaxID=926550 {ECO:0000313|EMBL:BAL98945.1, ECO:0000313|Proteomes:UP000007880};
RN   [1] {ECO:0000313|EMBL:BAL98945.1, ECO:0000313|Proteomes:UP000007880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14535 / JCM 11387 / NBRC 104270 / STL-6-O1
RC   {ECO:0000313|Proteomes:UP000007880};
RA   Oguchi A., Hosoyama A., Sekine M., Fukai R., Kato Y., Nakamura S.,
RA   Hanada S., Yamazaki S., Fujita N.;
RT   "Complete genome sequence of Caldilinea aerophila DSM 14535 (= NBRC
RT   102666).";
RL   Submitted (FEB-2012) 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   -!- PATHWAY: Amino-acid biosynthesis. {ECO:0000256|ARBA:ARBA00029440}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; AP012337; BAL98945.1; -; Genomic_DNA.
DR   RefSeq; WP_014432186.1; NC_017079.1.
DR   AlphaFoldDB; I0I108; -.
DR   STRING; 926550.CLDAP_09060; -.
DR   KEGG; cap:CLDAP_09060; -.
DR   PATRIC; fig|926550.5.peg.955; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_2_0; -.
DR   OrthoDB; 9792335at2; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000007880; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway.
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; IPR001261; ArgE/DapE_CS.
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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007880};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          189..301
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   408 AA;  44440 MW;  9CFF0E913B042BB8 CRC64;
     MLSEVEQQVL ACIDDEELIR WVQELTRIPS VWKPESGEGE EAAARWVEAR CREIGLETHF
     EFVQPGRPNV IALHRMTDGP TLMFEGHTDV VTEGDPAAWR DPPFSAVIRD GRIYGRGAND
     MKAGLVAALT AIKAIVQSGV RLKGTLLLGA LCDEEGDMIG VKHFVERGWA DRVSAAIICE
     PEENHLCVTQ KGVMWIHVIL QGIMAHGAMP LTGVNSAYPM AKFLSLLRSL ELRVIAERGV
     DPFLGQPSIT PTIVMSPARG HGEAQKNVMP GVSEAVLDIR LIPGQEPEAL AHEIETLLQS
     VVASEAGLRY EFRVLEVRHP TFTDPDHPVV AALASAYTDL TGQPPVYGGV PGSTDGTILH
     ARRGIPIVTC GPGDIHIPHH IDEWVSIDEI KTAARMYVLA AIRYLGLA
//
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