GenomeNet

Database: UniProt
Entry: A0A0N1AHV7_9PROT
LinkDB: A0A0N1AHV7_9PROT
Original site: A0A0N1AHV7_9PROT 
ID   A0A0N1AHV7_9PROT        Unreviewed;       497 AA.
AC   A0A0N1AHV7;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 24.
DE   RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE            EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN   ORFNames=IP80_04480 {ECO:0000313|EMBL:KPF50233.1};
OS   beta proteobacterium AAP65.
OC   Bacteria; Pseudomonadota; Betaproteobacteria.
OX   NCBI_TaxID=1523424 {ECO:0000313|EMBL:KPF50233.1, ECO:0000313|Proteomes:UP000037849};
RN   [1] {ECO:0000313|EMBL:KPF50233.1, ECO:0000313|Proteomes:UP000037849}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAP65 {ECO:0000313|EMBL:KPF50233.1,
RC   ECO:0000313|Proteomes:UP000037849};
RA   Zeng Y., Feng F., Liu Y., Koblizek M.;
RT   "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT   Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL   Submitted (AUG-2015) 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:KPF50233.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LJHW01000004; KPF50233.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N1AHV7; -.
DR   STRING; 1523424.IP80_04480; -.
DR   PATRIC; fig|1523424.3.peg.2845; -.
DR   OrthoDB; 9772308at2; -.
DR   Proteomes; UP000037849; 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   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:UP000037849};
KW   Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT   ACT_SITE        266
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT   BINDING         265
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         269
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT   BINDING         295
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ   SEQUENCE   497 AA;  56020 MW;  E16CACD819E7E279 CRC64;
     MSTATPAYEQ LAATWTRLHH LEHLQAIAGW DHAANMPPKG NEARAAALAE MAALLHRMRT
     DAALGSGLQH AEQEPLSEEQ RANLREMQRQ WRAATALPES LVQRQQIVTS RCEHAWRQQR
     PANDWAGFAP QLKEVLALAR EEAALLADKS GLRAYDALMD RFEPGMRCTQ VDQVFGEVRR
     WLPGLIQQVI AKQAQEDVIQ PVGPFAQDKQ RALCEQVIRL LGFDFEAGRL DVSTHPFCGG
     VPEDVRLTTR FRDDEFITSL MGTIHETGHG RYEQNLPREW LGQPMAQARS MALHESQSLS
     FEMQLGSHPG FVARLAPMVT ATFGAQPAFT PQNLHRLITR VKPGYIRVDA DEVTYPAHVI
     LRYEIERALI EGEVEVDDIP ALWDAKMMEL LGVDTRGNFK DGPMQDVHWP SGLFGYFPCY
     SLGAMYAAQW FATMRRQMPD LDARIGAGDL APVFDWLRSN IWSQASRWTT DELARRASGE
     PLNAAHFKLH LEARYLG
//
DBGET integrated database retrieval system