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Database: UniProt
Entry: A0A0G4MNX9_9PEZI
LinkDB: A0A0G4MNX9_9PEZI
Original site: A0A0G4MNX9_9PEZI 
ID   A0A0G4MNX9_9PEZI        Unreviewed;       743 AA.
AC   A0A0G4MNX9;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Succinyl-diaminopimelate desuccinylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BN1708_016483 {ECO:0000313|EMBL:CRK35862.1};
OS   Verticillium longisporum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX   NCBI_TaxID=100787 {ECO:0000313|EMBL:CRK35862.1, ECO:0000313|Proteomes:UP000044602};
RN   [1] {ECO:0000313|EMBL:CRK35862.1, ECO:0000313|Proteomes:UP000044602}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VL1 {ECO:0000313|EMBL:CRK35862.1};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
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; CVQH01023717; CRK35862.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G4MNX9; -.
DR   STRING; 100787.A0A0G4MNX9; -.
DR   OrthoDB; 5487978at2759; -.
DR   Proteomes; UP000044602; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016787; F:hydrolase activity; IEA:InterPro.
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; 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   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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000044602};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT   DOMAIN          34..345
FT                   /note="Tryptophan synthase beta chain-like PALP"
FT                   /evidence="ECO:0000259|Pfam:PF00291"
FT   DOMAIN          536..642
FT                   /note="Peptidase M20 dimerisation"
FT                   /evidence="ECO:0000259|Pfam:PF07687"
SQ   SEQUENCE   743 AA;  78402 MW;  FA83A8BD5E797DBB CRC64;
     MSSSKPLFFN NATGSVNIHD DVSLPRSLHC QMPGFAVTPL VSMESLAKKL GVKAVYVKDE
     SNRLGLPSFK ILGASWGTCR AIIDQFDLPL NSSFQDIARC AQQRSLILYT ASAGNHGRDL
     AATARLLGIQ SKVYVFKAVG PAAAEHIASE GAEVVVSQLD YDGAMREAHA ASQTDPSGLF
     IQDAAFDGYT DIPKWIVEGY ATLVAEVNAQ LASQGLKPDL VVTPCGVGSL AQAVVRHCKS
     GDRAYRVLAV EPDTAACLYE SLRQGKISSV ATSKTIMEGL NCGTVSLTAF DDLRAGVDAC
     PTRVLAEGGI NSGPCGGATL AGLQRLAASG QRPSWLKADS VVVVLNTESS RQHKEPLDVT
     VSDATGLTQI LTRIASANPD LSNDAGSDET AIAEYIFSWL RHRDLEAHWV ERTAGRPSIV
     GVLRGTGGGK SLMLNGHIDT VSLSSYGEGT DPLSGLLQDN RIYGRGSLDM KAGVASSMAV
     VAAFVKSGAE RLRGDIILAA ASDKENFSKG TEDVLAAAWK ADAALIPEPT SQAMVTAHRG
     FVWVEIDVLG KAAHGSEPHI GIDAILLAGS LQTALLEYGL TLPTHPLLGK AHLHGGKLVG
     GEEPSSYPAK CTLTIEFRTV PPQTPSSIMD DLSRLLKEVA AKTPGFQYAA PRMTFTRPGS
     ALEDDHSFVH TVRAVVGNVT GNVPEPDAAG FWCDAGLLNE AGIPSIVYGP KGEGLHAAVE
     WVDVDSLKEV TRVIENIART FCS
//
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