ID G4Q459_ACIIR Unreviewed; 419 AA.
AC G4Q459;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=tripeptide aminopeptidase {ECO:0000256|ARBA:ARBA00012563};
DE EC=3.4.11.4 {ECO:0000256|ARBA:ARBA00012563};
GN OrderedLocusNames=Acin_0613 {ECO:0000313|EMBL:AEQ21853.1};
OS Acidaminococcus intestini (strain RyC-MR95).
OC Bacteria; Bacillota; Negativicutes; Acidaminococcales; Acidaminococcaceae;
OC Acidaminococcus.
OX NCBI_TaxID=568816 {ECO:0000313|EMBL:AEQ21853.1, ECO:0000313|Proteomes:UP000007093};
RN [1] {ECO:0000313|EMBL:AEQ21853.1, ECO:0000313|Proteomes:UP000007093}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RyC-MR95 {ECO:0000313|EMBL:AEQ21853.1,
RC ECO:0000313|Proteomes:UP000007093};
RX PubMed=22123762; DOI=10.1128/JB.06301-11;
RA D'Auria G., Galan J.C., Rodriguez-Alcayna M., Moya A., Baquero F.,
RA Latorre A.;
RT "Complete genome sequence of Acidaminococcus intestini RYC-MR95, a Gram-
RT negative bacterium from the phylum Firmicutes.";
RL J. Bacteriol. 193:7008-7009(2011).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4; Evidence={ECO:0000256|ARBA:ARBA00000870};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR037215-2};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000256|PIRSR:PIRSR037215-
CC 2};
CC -!- SIMILARITY: Belongs to the peptidase M20B family.
CC {ECO:0000256|ARBA:ARBA00009692}.
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DR EMBL; CP003058; AEQ21853.1; -; Genomic_DNA.
DR RefSeq; WP_009016223.1; NC_016077.1.
DR AlphaFoldDB; G4Q459; -.
DR STRING; 568816.Acin_0613; -.
DR GeneID; 72310598; -.
DR KEGG; ain:Acin_0613; -.
DR PATRIC; fig|568816.4.peg.595; -.
DR eggNOG; COG2195; Bacteria.
DR HOGENOM; CLU_053676_0_0_9; -.
DR InParanoid; G4Q459; -.
DR Proteomes; UP000007093; Chromosome.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006518; P:peptide metabolic process; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR010161; Peptidase_M20B.
DR NCBIfam; TIGR01882; peptidase-T; 1.
DR PANTHER; PTHR42994; PEPTIDASE T; 1.
DR PANTHER; PTHR42994:SF1; PEPTIDASE T; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR037215-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000007093};
KW Zinc {ECO:0000256|PIRSR:PIRSR037215-2}.
FT DOMAIN 216..312
FT /note="Peptidase M20 dimerisation"
FT /evidence="ECO:0000259|Pfam:PF07687"
FT ACT_SITE 88
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT ACT_SITE 183
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-1"
FT BINDING 86
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 149
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 207
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
FT BINDING 390
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR037215-2"
SQ SEQUENCE 419 AA; 46603 MW; 3B9824DA4F314823 CRC64;
MEIRETLVNR FYDYVAIPSQ SCANGGTKVP STEGQWDMAR AVQKDLERLG LEDIHLSEYG
VLTARLPAHL PAGFTKKVPA VGFCTHLDTV DVNLSPVVHP HMVKNYDGKD LVLNADQQIV
MTTKDHPELL RYQGDDLIVT DGTSVLGSDN KAAVTNVVTA LETLTSDPSL YHGDIYVAFV
PDEEVGLFGS KHIDFSRFPV DFAYTIDCCE LGEVVYETFN AGSGKVTIHG VSAHPMSAKG
VLVNPTLLAV DFINLFDRKE TPECTEGKEG YIWCQAVQSN QSTAVVTLNI RDHDKTRYEA
RKALIRENVE RLKKMEPRAR VELELVDIYG NIADAVTDEN HKAIDYIYDA MKELGITPKT
IAMRGGTDGS YISTQKIMTP NYFTGGMNFH SRFEFLPVSS FVKSYEMTMK LLELIVKNA
//
