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Database: UniProt
Entry: Q03HV4_PEDPA
LinkDB: Q03HV4_PEDPA
Original site: Q03HV4_PEDPA 
ID   Q03HV4_PEDPA            Unreviewed;       383 AA.
AC   Q03HV4;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
DE            EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN   OrderedLocusNames=PEPE_0111 {ECO:0000313|EMBL:ABJ67218.1};
OS   Pediococcus pentosaceus (strain ATCC 25745 / CCUG 21536 / LMG 10740 /
OS   183-1w).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Pediococcus.
OX   NCBI_TaxID=278197 {ECO:0000313|EMBL:ABJ67218.1, ECO:0000313|Proteomes:UP000000773};
RN   [1] {ECO:0000313|EMBL:ABJ67218.1, ECO:0000313|Proteomes:UP000000773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25745 / CCUG 21536 / LMG 10740 / 183-1w
RC   {ECO:0000313|Proteomes:UP000000773};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-succinyl-(2S,6S)-2,6-diaminoheptanedioate =
CC         (2S,6S)-2,6-diaminoheptanedioate + succinate; Xref=Rhea:RHEA:22608,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:30031, ChEBI:CHEBI:57609,
CC         ChEBI:CHEBI:58087; EC=3.5.1.18;
CC         Evidence={ECO:0000256|ARBA:ARBA00001246};
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; L-lysine biosynthesis via DAP
CC       pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate
CC       (succinylase route): step 3/3. {ECO:0000256|ARBA:ARBA00005130}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; CP000422; ABJ67218.1; -; Genomic_DNA.
DR   RefSeq; WP_011672846.1; NC_008525.1.
DR   AlphaFoldDB; Q03HV4; -.
DR   STRING; 278197.PEPE_0111; -.
DR   DNASU; 4418745; -.
DR   GeneID; 33062754; -.
DR   KEGG; ppe:PEPE_0111; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_2_9; -.
DR   OrthoDB; 9792335at2; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000000773; 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; 1.
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: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.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABJ67218.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          177..281
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   383 AA;  41667 MW;  5EE9C9F9B801AACF CRC64;
     MDTMVSNSQT YLKILADLIK IKSVNDHELE VAEYLQDLFQ ENGIEAKILP LEGQRANLVA
     EIGEGAPVLA VSGHMDVVDP GNLAAWDNDP FTMTEKDGKL FGRGITDMKA GLAALVIAMI
     ELKKQGLPKK GTIRLLATAG EEVGEEGSAA FYRDHYMEDA AGLLIAEPST VYGTASEQKG
     SFDIKFTSKG TSVHSSTPEK GYNALVPLMQ LLNEANTYFE TIPAGEMGPV RFNIDVLNGG
     SQINSLPDLA TALVNVRTIP EYDNNQVAKQ IETFVKSYNA NGAQINTDLI MNEFPIATSP
     SNQLVKIIQS LGKEYAGRDI VVAASPGITD ASNLAKDKPH DFPFAVYGPG DGSQHQVNES
     LPKQMYLDFI EIYQKLFIEF LEK
//
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