ID B8NV99_ASPFN Unreviewed; 478 AA.
AC B8NV99;
DT 03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 82.
DE SubName: Full=Glutamate carboxypeptidase, putative {ECO:0000313|EMBL:EED46728.1};
GN ORFNames=AFLA_103940 {ECO:0000313|EMBL:EED46728.1};
OS Aspergillus flavus (strain ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357
OS / JCM 12722 / SRRC 167).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=332952 {ECO:0000313|EMBL:EED46728.1, ECO:0000313|Proteomes:UP000001875};
RN [1] {ECO:0000313|EMBL:EED46728.1, ECO:0000313|Proteomes:UP000001875}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 200026 / FGSC A1120 / IAM 13836 / NRRL 3357 / JCM 12722 /
RC SRRC 167 {ECO:0000313|Proteomes:UP000001875};
RX PubMed=25883274; DOI=10.1128/genomeA.00168-15;
RA Nierman W.C., Yu J., Fedorova-Abrams N.D., Losada L., Cleveland T.E.,
RA Bhatnagar D., Bennett J.W., Dean R., Payne G.A.;
RT "Genome sequence of Aspergillus flavus NRRL 3357, a strain that causes
RT aflatoxin contamination of food and feed.";
RL Genome Announc. 3:E0016815-E0016815(2015).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|PIRSR:PIRSR037242-3};
CC Note=Binds 2 manganese ions per subunit.
CC {ECO:0000256|PIRSR:PIRSR037242-3};
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; EQ963484; EED46728.1; -; Genomic_DNA.
DR RefSeq; XP_002384264.1; XM_002384223.1.
DR AlphaFoldDB; B8NV99; -.
DR STRING; 332952.B8NV99; -.
DR EnsemblFungi; EED46728; EED46728; AFLA_103940.
DR VEuPathDB; FungiDB:AFLA_010634; -.
DR eggNOG; KOG2276; Eukaryota.
DR HOGENOM; CLU_029469_3_0_1; -.
DR OMA; HITIPGF; -.
DR Proteomes; UP000001875; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:EnsemblFungi.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IEA:EnsemblFungi.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070573; F:metallodipeptidase activity; IEA:EnsemblFungi.
DR GO; GO:0008242; F:omega peptidase activity; IEA:EnsemblFungi.
DR GO; GO:0006751; P:glutathione catabolic process; IEA:EnsemblFungi.
DR CDD; cd05676; M20_dipept_like_CNDP; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR017153; CNDP/DUG1.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43270; BETA-ALA-HIS DIPEPTIDASE; 1.
DR PANTHER; PTHR43270:SF4; CARNOSINE DIPEPTIDASE 2, ISOFORM A; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037242; CNDP_dipeptidase; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000313|EMBL:EED46728.1};
KW Hydrolase {ECO:0000313|EMBL:EED46728.1};
KW Manganese {ECO:0000256|PIRSR:PIRSR037242-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR037242-3};
KW Protease {ECO:0000313|EMBL:EED46728.1};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 209..366
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 100
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT ACT_SITE 166
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-1"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 132
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 167
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 195
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 228
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 330
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 343
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 417
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT BINDING 445
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-3"
FT BINDING 445
FT /ligand="substrate"
FT /ligand_note="ligand shared between homodimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-2"
FT SITE 228
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000256|PIRSR:PIRSR037242-4"
SQ SEQUENCE 478 AA; 52912 MW; 8F415BB5DDC38ABB CRC64;
MAPQLEPFFK QVDGLAESFI ERLRKAVAIP SVSAQDENRK DVFRMAQFLA SELEALGAEV
HQRPLGKQPG KEHLDLPPVV IARYGNDKNK RTILVYGHYD VQPALKEDGW ATEPFQLTVD
NQGRMYGRGS TDDKGPVLGW LNVIEAHRKA GVELPVNLLC CFEGMEEYGS EGLEEFIQAE
SKGFFKDADA VCISDNYWLG TEKPCLTYGL RGCNYYSVGV TGPAQDLHSG VFGGSAHEPM
TDLVHVMSKL VDTHGNILIP GIMDLVEPLT EEEKALYPNI SYTMDDLHQS LGSKTSIHPT
KERTLMARWR YPSLSLHGIE GAYSAPGAKT VIPAKVIGKF SIRTVPNMES EDVNKLVFDY
IKAEFAKLNS KNTLDVWLQH DGKWWVASPK HWNFTAAGKA VKQVFGVEPD MTREGGSIPV
TLSFEQATGK NVLLLPMGSS TDAAHSINEK LDKRNYIEGV KLLGAYLHYV AEEPMVAA
//
