ID A0A3P5X2C5_9RHOB Unreviewed; 492 AA.
AC A0A3P5X2C5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-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=XINFAN_02065 {ECO:0000313|EMBL:VDC28289.1};
OS Pseudogemmobacter humi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudogemmobacter.
OX NCBI_TaxID=2483812 {ECO:0000313|EMBL:VDC28289.1, ECO:0000313|Proteomes:UP000277498};
RN [1] {ECO:0000313|EMBL:VDC28289.1, ECO:0000313|Proteomes:UP000277498}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACIP111625 {ECO:0000313|EMBL:VDC28289.1};
RA Criscuolo A.;
RL Submitted (NOV-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}.
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DR EMBL; UXAW01000067; VDC28289.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3P5X2C5; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000277498; 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:VDC28289.1};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006615, ECO:0000313|EMBL:VDC28289.1};
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:UP000277498};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 258
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 257
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 261
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 287
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 492 AA; 54080 MW; 5D4264C38A70AC9B CRC64;
MAKNAYESLL FHARETAALE QVAGRLGWDQ ETVMPRGSAA QRGEELAAME GVLHARRTEP
RIAEWLAGAE PADEVAAAQL AKIRRAHERA LKVPARLSQE IARVTSLAQG IWAGARARED
LAGFLPVLGD VVRLKREEGA ALAGGGDIYD AMIDDYEPGM TGAEIETMFA ALRPRLVALR
ERILGAAYHP PALDGSFGAD AQLRLSRDLA QVFGYDFSRG RIDMAVHPFC SGGGNDVRIT
TRVAEADPFN CLYSTIHETG HAAYEQNIDP DYLLTPIGGG VSMGVHESQS RICENQLGRS
RAFTGWLLEQ MRERFGEFGV TDPGVFYAMV NRVGPGFIRT EADEVHYNLH IMMRFDLERA
LMGGDLAVGD LEAAWNDRFL ADFGVAVDRP SHGMLQDVHW SVGLFGYFPT YTLGNLYAGC
LHKALRAALP DLDRDLAAGD LSRANDWLHE NLRRHGGLYQ PRELITRACG EAPSAGPLLD
YLEEKFAGLY RL
//
