ID E1VQR2_9GAMM Unreviewed; 506 AA.
AC E1VQR2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Metal-dependent carboxypeptidase {ECO:0000256|PIRNR:PIRNR006615};
DE EC=3.4.17.19 {ECO:0000256|PIRNR:PIRNR006615};
GN ORFNames=HDN1F_35710 {ECO:0000313|EMBL:CBL47154.1};
OS gamma proteobacterium HdN1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=83406 {ECO:0000313|EMBL:CBL47154.1, ECO:0000313|Proteomes:UP000002677};
RN [1] {ECO:0000313|EMBL:CBL47154.1, ECO:0000313|Proteomes:UP000002677}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HdN1 {ECO:0000313|Proteomes:UP000002677};
RA Widdel F., Rabus R., Grundmann O., Werner I., Schreiber F., Ehrenreich P.,
RA Behrends A., Wilkes H., Kube M., Reinhardt R., Zedelius J.;
RT "Alkane degradation by a new type of denitrifying bacterium with possible
RT involvement of the electron acceptor in substrate activation.";
RL Environ. Microbiol. 0:0-0(2010).
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; FP929140; CBL47154.1; -; Genomic_DNA.
DR AlphaFoldDB; E1VQR2; -.
DR STRING; 83406.HDN1F_35710; -.
DR KEGG; gpb:HDN1F_35710; -.
DR eggNOG; COG2317; Bacteria.
DR HOGENOM; CLU_032916_1_0_6; -.
DR OrthoDB; 9772308at2; -.
DR Proteomes; UP000002677; Chromosome.
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:CBL47154.1}; 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:UP000002677};
KW Zinc {ECO:0000256|PIRSR:PIRSR006615-1}.
FT ACT_SITE 276
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-2"
FT BINDING 275
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 279
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
FT BINDING 305
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR006615-1"
SQ SEQUENCE 506 AA; 57455 MW; 45F3BA29BA7126D1 CRC64;
MLIEKRVPPM SYQRIEQHQR QLSRYHHLQA ICGWDQSAMM PTGGNEARAE ALASLDVLIH
NRLTEPSVAD WIATASDEPL TPEQRANLRE FRRQWQNASL IPPELVEAHS LANSHCEHAW
RSQRPANDWA GFAVNLSAVV ANTREIAKIR ADALGVSPYN ALLALYEPGA STTQLDTLFA
DLRQWLPSLI QRVAERQSVA EQQKGSAILI PQGPFPIEQQ KQLGLEVMQL LGFNFDRGRL
DVSAHPFCGG VPSDVRITTR YDEQDFTRSL MGVIHETGHA RYEQNLPYAW RDQAVFQGRS
MGIHESQSLF FEMQLARHPA FLALLTPLLN THFGAQPAFA AQNLQRLYTR VQPSLIRVDA
DEVTYPAHII LRYEIERALI EGDAEVEDIP ALWDQKMQEW LGLSTQGDYT NGCMQDIHWP
SGAFGYFPSY TLGAMYAAQF RFAIEAEYGD LGTLVERAQL PTVFSWLRKF IWQQGSLLET
DELVKNATGS TLNARWFRQH LEQRYG
//
