ID   A0A2H3TIX9_FUSOX        Unreviewed;       746 AA.
AC   A0A2H3TIX9;
DT   31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT   31-JAN-2018, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN   ORFNames=FRV6_05926 {ECO:0000313|EMBL:SCO81713.1};
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507 {ECO:0000313|EMBL:SCO81713.1, ECO:0000313|Proteomes:UP000219369};
RN   [1] {ECO:0000313|Proteomes:UP000219369}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=V64-1 {ECO:0000313|Proteomes:UP000219369};
RA   Guldener U.;
RL   Submitted (SEP-2016) 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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family.
CC       {ECO:0000256|ARBA:ARBA00006247}.
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DR   EMBL; FMJY01000003; SCO81713.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H3TIX9; -.
DR   VEuPathDB; FungiDB:FOC1_g10005961; -.
DR   VEuPathDB; FungiDB:FOC4_g10003469; -.
DR   VEuPathDB; FungiDB:FOIG_14477; -.
DR   VEuPathDB; FungiDB:FOMG_03500; -.
DR   VEuPathDB; FungiDB:FOXG_03758; -.
DR   VEuPathDB; FungiDB:FOZG_03422; -.
DR   VEuPathDB; FungiDB:HZS61_013941; -.
DR   OrthoDB; 5487978at2759; -.
DR   UniPathway; UPA00034; UER00021.
DR   Proteomes; UP000219369; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016829; F:lyase activity; 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   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.50.1100; -; 2.
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   InterPro; IPR001926; TrpB-like_PALP.
DR   InterPro; IPR036052; TrpB-like_PALP_sf.
DR   NCBIfam; TIGR01910; DapE-ArgE; 1.
DR   PANTHER; PTHR42937; -; 1.
DR   PANTHER; PTHR42937:SF1; DIAMINOPROPIONATE AMMONIA-LYASE; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF00291; PALP; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53686; Tryptophan synthase beta subunit-like PLP-dependent enzymes; 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   Lyase {ECO:0000313|EMBL:SCO81713.1};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          36..352
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   DOMAIN          538..646
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
FT   REGION          1..21
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   746 AA;  79718 MW;  D7F575E6D15990F1 CRC64;
     MTTRRHVHFN SKAKSWTSPE PASAEAIDRF HQSLPNYEPT PLVSLDSLAK EIGIGAVHVK
     DETNRFGLPA FKILGASWGA FRSITEKFGL PLDSDIDTVR EAAKSHQLTL YAATEGNHGR
     AVARMGAIFD ISAEIHVPAS MHPSTVKLIE SEGAKVVISK GRYEDAMLEA ESASKHEKGI
     MVQDHAFGDY QTWIVDGYGT MMREIDKQLG STKADLVIAP VGVGSFAQAV VSHFKRQGTS
     TSTLTVEPDT AACLWKSLEK GEFTEIPTTG TIMAGLNCGA PSTIAWDLLK NGVDASLTVS
     DYEAHQSVLY LQSQGINAGP CGASTLAALR RLTPDEKKAL GLNEKSTVVI FCTERNRDYD
     VPHGVSGTDP VALTQTLVQI NSASPDLGSV PGPGETTIAR YVAAWLEHRD LETHWVEYTK
     GRPSVVGVVR GSGGGKSVMF NGHLDTVTIM GYDDDPLSGK IVDGRLYGRG SADMKGGVAA
     GMIALANTKK LGLRGDVIFT GVADEESLSK GTEDILRAGW RADAAVVSES TNLEINHAHK
     GYCHVEIKVY GLAAHGSRAD LGIDAIVNAG HFLVEFGKYV QKLQEGPGDE TLGTGTAHAS
     VISGGEEASS YPAQCTIIAE RRTIPGETNE VVQKEFDDMI ASVAKEVTDF KAEAKIFFSR
     PPQFTAEDHP FTKLVSGVVG TVTGKDAVIA GAPFWTDCAL LAEKGIVPLL WGPKGEGFHG
     KEEFVHIKSI EQVAEGLANI AAEFCK
//