ID A0A3E2XPY8_9FIRM Unreviewed; 498 AA.
AC A0A3E2XPY8;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 15.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=DW747_03475 {ECO:0000313|EMBL:RGC50445.1};
OS Coprococcus catus.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Coprococcus.
OX NCBI_TaxID=116085 {ECO:0000313|EMBL:RGC50445.1, ECO:0000313|Proteomes:UP000261231};
RN [1] {ECO:0000313|EMBL:RGC50445.1, ECO:0000313|Proteomes:UP000261231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AM28-39 {ECO:0000313|EMBL:RGC50445.1,
RC ECO:0000313|Proteomes:UP000261231};
RA Zou Y., Xue W., Luo G.;
RT "A genome reference for cultivated species of the human gut microbiota.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Broad specificity carboxypetidase that releases amino acids
CC sequentially from the C-terminus, including neutral, aromatic, polar
CC and basic residues. {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of a C-terminal amino acid with broad specificity,
CC except for -Pro.; EC=3.4.17.19;
CC Evidence={ECO:0000256|PIRNR:PIRNR006615};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR006615-1};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR006615-1};
CC -!- SIMILARITY: Belongs to the peptidase M32 family.
CC {ECO:0000256|PIRNR:PIRNR006615}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RGC50445.1}.
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DR EMBL; QVFD01000002; RGC50445.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3E2XPY8; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000261231; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004181; F:metallocarboxypeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR CDD; cd06460; M32_Taq; 1.
DR Gene3D; 1.10.1370.30; -; 1.
DR InterPro; IPR001333; Peptidase_M32_Taq.
DR PANTHER; PTHR34217:SF1; CARBOXYPEPTIDASE 1; 1.
DR PANTHER; PTHR34217; METAL-DEPENDENT CARBOXYPEPTIDASE; 1.
DR Pfam; PF02074; Peptidase_M32; 1.
DR PIRSF; PIRSF006615; Zn_crbxpep_Taq; 1.
DR PRINTS; PR00998; CRBOXYPTASET.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000313|EMBL:RGC50445.1}; Hydrolase {ECO:0000256|PIRNR:PIRNR006615};
KW Metal-binding {ECO:0000256|PIRNR:PIRNR006615,
KW ECO:0000256|PIRSR:PIRSR006615-1};
KW Metalloprotease {ECO:0000256|PIRNR:PIRNR006615};
KW Protease {ECO:0000256|PIRNR:PIRNR006615};
KW Reference proteome {ECO:0000313|Proteomes:UP000261231};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 265
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 264
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 268
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 294
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 498 AA; 57022 MW; 2A4C9EB36406BEA6 CRC64;
MELKSALEQL GLLQKKLYAY QTASSSLYLD SVTVAPKDTS EGRGVALGIL AGESQKLMTA
PETGELLAFL ADQKDNLSFV EQRQVEELKR SFDRLSRIPA DEYMDYAMLT NEASDVWHRA
KETSDFTLFA PILEKLVAYN RKFAGYYDSS KKPYDALLDE YERGADMAFL DTFFETVRER
LVPLIHAIGE KPQIDDSFLH LHYPVDIQRK FSDYLMEVME LDRGHCTIGE TEHPFTLEFN
NKDVRITTNY KEDNVVDSMY SVIHEGGHAK YELGIRDDLQ YTCLTGGVSM GVHESQSRFY
ENIIGRSLPF VKAIFPKMQE FFPEQLKHVT AEQMYCAVNK VQPSLIRTEA DELTYSLHVM
VRYEIEKQLI DGSLEVKDIP EVWNRLYKEY LGVDVPDDRR GCLQDSHWSG GSFGYFPSYA
LGSAYGAQML CNMEKDFPVW KEVRAGKLTG VSAWLKEKVH QYGSLLTPGE IVKNACGDFD
PTVYTDYLTE KYNKLYDL
//
