ID A0A1X7DRM8_9PROT Unreviewed; 383 AA.
AC A0A1X7DRM8;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Glutamate carboxypeptidase {ECO:0000313|EMBL:SMF20117.1};
GN ORFNames=SAMN02982917_0879 {ECO:0000313|EMBL:SMF20117.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF20117.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF20117.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF20117.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
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DR EMBL; FXAK01000001; SMF20117.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7DRM8; -.
DR STRING; 286727.SAMN02982917_0879; -.
DR OrthoDB; 9776600at2; -.
DR Proteomes; UP000192936; Unassembled WGS sequence.
DR GO; GO:0004180; F:carboxypeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd03885; M20_CPDG2; 1.
DR Gene3D; 3.30.70.360; -; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR017150; Pept_M20_glutamate_carboxypep.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR PANTHER; PTHR43808; ACETYLORNITHINE DEACETYLASE; 1.
DR PANTHER; PTHR43808:SF9; BLL0789 PROTEIN; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037238; Carboxypeptidase_G2; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
PE 4: Predicted;
KW Carboxypeptidase {ECO:0000313|EMBL:SMF20117.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protease {ECO:0000313|EMBL:SMF20117.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 184..285
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 89
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
FT ACT_SITE 149
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037238-1"
SQ SEQUENCE 383 AA; 39635 MW; 22C2DD584E6F1ABD CRC64;
MTPLAQRASD WLATRRAEME EMLQRIVDID SGSRDGAGID AVGDIMAAML EADGIAVTRF
PNETYGAVLK ADIPGNDGGA PVLVMGHRDT VYPKGTVAAR PFTRDGDTAR GPGVADMKGG
LVVDVFVLRA LKAAGGTGFP LIGLFTADEE IGSPSGRKII EEVARGARAA FNAEPGRVSG
NVVTARKGGL TLDITVTGRA AHSGVNHADG ASAIGALAAK ITALHALTDY DSGITTNVGV
IRGGRTHNTV ADHAEAALDI RFRSVEQLDG ILARVEAILA AEDVPGTSAT YQRGHLFMPL
EERHSADLFA RYKAAAAEVG FEVDGEFTGG CADSGFTGAL GVPSLCGLGP VGGAAHTERE
WCRLETLVPR AQALAVTIAG LEK
//