ID A0A1W2TM91_ROSNE Unreviewed; 749 AA.
AC A0A1W2TM91;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Probable succinyl-diaminopimelate desuccinylase {ECO:0000256|ARBA:ARBA00016853};
GN ORFNames=SAMD00023353_4000800 {ECO:0000313|EMBL:GAP89440.1};
OS Rosellinia necatrix (White root-rot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Xylariomycetidae; Xylariales; Xylariaceae; Rosellinia.
OX NCBI_TaxID=77044 {ECO:0000313|EMBL:GAP89440.1};
RN [1] {ECO:0000313|EMBL:GAP89440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=W97 {ECO:0000313|EMBL:GAP89440.1};
RA Kanematsu S.;
RT "Draft genome sequence of Rosellinia necatrix.";
RL Submitted (MAR-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; DF977485; GAP89440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W2TM91; -.
DR STRING; 77044.A0A1W2TM91; -.
DR OMA; SDYEAHQ; -.
DR OrthoDB; 5487978at2759; -.
DR UniPathway; UPA00034; UER00021.
DR Proteomes; UP000054516; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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 Reference proteome {ECO:0000313|Proteomes:UP000054516};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 37..349
FT /note="Tryptophan synthase beta chain-like PALP"
FT /evidence="ECO:0000259|Pfam:PF00291"
FT DOMAIN 541..644
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
SQ SEQUENCE 749 AA; 79294 MW; CE5FF668F6BD36D7 CRC64;
MNSKRRPVLF NPHAQPRVVK NDSSAETVAS FHRQLPDYGR TPLVSLDDVA KELGLGAVRL
KDESSRLGLP SFKILGASWG TFRAIIQTAG LPLSTSFDAV RQAVAGHRTS LHAATDGNHG
RAVARMGSIL SIPAEIWVPA GMHPSTIELI RSEGAEVVEA GGDYDHAILE AQKSAERSGG
ILIQDFAFGD YNEIPQWIVD GYATMMLEID EQMGGEPIDL VIAPVGVGSF AQAVVSHYKG
KESPTAVLTV EPDTAACFYK SLRKGEMTTE RTSSTVMAGL DCGNVSSIAW PILRHGVDAS
LSVSDYEAHE ASIYLKNYGI SSAPCGAATL AALRRLGESE RAALGLNSKS SVLLLSTEGA
REYVKPVDVG IDDAVALTQT LVQIDSVNST LVPGAGGETA IARYIKAWLE HRDIESHWIE
PVEGRPSVIG VVRGNGGGKS LMFNGHIDTV TLSGYDGDPL SGRIKDGKIY GRGAADMKGG
VAAAMVALAS VQGAGLSGDV MFAGVADEEA ESLGTENILQ AGWRADAAIV SEPTNVAIIH
AHKGFVWLEV DIFGLAAHGS RPDLGVDAIV KAGYFLVELD KYAARLKGRG SDSPVGAPSV
HASIIKGGEE LSSYPALCSV SIERRTIAGE TQETVEQEVR SILEGLKDTV ADFTFDVRTT
FSRPPFLIPT DHPFVLTTVD AVQQSLGEKP VLRGEAFWAD SALLSAEGIA TLIWGPSGEG
FHSKEEYVSS DSVRCVAAAL STIARVYCG
//