ID   B7IFI2_THEAB            Unreviewed;       403 AA.
AC   B7IFI2;
DT   10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT   10-FEB-2009, sequence version 1.
DT   04-NOV-2026, entry version 99.
DE   RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00022391};
DE            EC=3.5.1.18 {ECO:0000256|ARBA:ARBA00011921};
GN   OrderedLocusNames=THA_347 {ECO:0000313|EMBL:ACJ74846.1};
OS   Thermosipho africanus (strain TCF52B).
OC   Bacteria; Thermotogati; Thermotogota; Thermotogae; Thermotogales;
OC   Fervidobacteriaceae; Thermosipho.
OX   NCBI_TaxID=484019 {ECO:0000313|EMBL:ACJ74846.1, ECO:0000313|Proteomes:UP000002453};
RN   [1] {ECO:0000313|EMBL:ACJ74846.1, ECO:0000313|Proteomes:UP000002453}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCF52B {ECO:0000313|EMBL:ACJ74846.1,
RC   ECO:0000313|Proteomes:UP000002453};
RX   PubMed=19124572; DOI=10.1128/JB.01448-08;
RA   Nesboe C.L., Bapteste E., Curtis B., Dahle H., Lopez P., Macleod D.,
RA   Dlutek M., Bowman S., Zhaxybayeva O., Birkeland N.-K., Doolittle W.F.;
RT   "The genome of Thermosipho africanus TCF52B: lateral genetic connections to
RT   the Firmicutes and Archaea.";
RL   J. Bacteriol. 191:1974-1978(2009).
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. DapE subfamily.
CC       {ECO:0000256|ARBA:ARBA00006746}.
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DR   EMBL; CP001185; ACJ74846.1; -; Genomic_DNA.
DR   RefSeq; WP_012579514.1; NC_011653.1.
DR   AlphaFoldDB; B7IFI2; -.
DR   STRING; 484019.THA_347; -.
DR   KEGG; taf:THA_347; -.
DR   eggNOG; COG0624; Bacteria.
DR   HOGENOM; CLU_021802_2_1_0; -.
DR   OMA; AADCTIW; -.
DR   OrthoDB; 9792335at2; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000002453; Chromosome.
DR   GO; GO:0008777; F:acetylornithine deacetylase activity; IEA:TreeGrafter.
DR   GO; GO:0009014; F:succinyl-diaminopimelate desuccinylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006526; P:L-arginine biosynthetic process; IEA:TreeGrafter.
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   InterPro; IPR050072; Peptidase_M20A.
DR   InterPro; IPR017706; YgeY.
DR   NCBIfam; TIGR01910; DapE-ArgE; 1.
DR   NCBIfam; NF009555; PRK13004.1; 1.
DR   NCBIfam; TIGR03526; selenium_YgeY; 1.
DR   PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR   PANTHER; PTHR43808:SF31; N-ACETYL-L-CITRULLINE DEACETYLASE; 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.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002453};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          177..283
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   403 AA;  45732 MW;  68227AB06C2D6E17 CRC64;
     MNKALELAYK YKNEIVKFMS KLIKAKSYSG QEKEVVHVIK EEMEKVGFDE IKIDGLGNII
     GKIGNGKYKI AMDAHIDTVD VGNEKLWEKD PFSGDFDEKW VYGRGASDQK AGMCSMVYGA
     KILKELGLFD DFTLYITGTV MEEDCDGLCW RYIVEKEHLK PDFVVITEPT SLNIYRGHRG
     RIEFRIRTTG LSAHASAPER GVNAIYKMAK IINEIEKLND RLKSDSFLGK GTIVVSQIFF
     KSPSHNAVPD ECEIQIDRRI TEGETKETVF AEIKDVFKRA GIKDAEIIEL EYKKPSYTGE
     IFPTEKYFPV WTFPEDSFIV QAAKKNYIDV FGKEPFIDKW TFSTNGTVTA GVYEIPTVGF
     GPGEERFAHA PNEKVEIEHL VKAAAFYATF PKTIVELLKT RRG
//