ID   A0A1G5UW47_9FIRM        Unreviewed;       457 AA.
AC   A0A1G5UW47;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=M18 family aminopeptidase {ECO:0000256|RuleBase:RU004387};
DE            EC=3.4.11.- {ECO:0000256|RuleBase:RU004387};
GN   ORFNames=SAMN02910343_00177 {ECO:0000313|EMBL:SDA37853.1};
OS   Allisonella histaminiformans.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Allisonella.
OX   NCBI_TaxID=209880 {ECO:0000313|EMBL:SDA37853.1, ECO:0000313|Proteomes:UP000199689};
RN   [1] {ECO:0000313|EMBL:SDA37853.1, ECO:0000313|Proteomes:UP000199689}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15230 {ECO:0000313|EMBL:SDA37853.1,
RC   ECO:0000313|Proteomes:UP000199689};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|ARBA:ARBA00001947,
CC         ECO:0000256|RuleBase:RU004387};
CC   -!- SIMILARITY: Belongs to the peptidase M18 family.
CC       {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR   EMBL; FMXA01000003; SDA37853.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5UW47; -.
DR   STRING; 209880.SAMN02910343_00177; -.
DR   OrthoDB; 89722at2; -.
DR   Proteomes; UP000199689; Unassembled WGS sequence.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001948; Peptidase_M18.
DR   InterPro; IPR023358; Peptidase_M18_dom2.
DR   PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR28570:SF2; M18 FAMILY AMINOPEPTIDASE 1-RELATED; 1.
DR   Pfam; PF02127; Peptidase_M18; 1.
DR   PRINTS; PR00932; AMINO1PTASE.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000256|RuleBase:RU004386};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU004386};
KW   Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW   ECO:0000256|RuleBase:RU004386};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199689};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ   SEQUENCE   457 AA;  51011 MW;  A393EBFEE2E62466 CRC64;
     MKETYSRTKP VWARMNEEER KATMEYGERY KKFLDTARTE RLAVTEILRQ AEEAGFKPLY
     DMKELKPGDK VFWNQKGKSV VLAVIGKKPV HDGLKIVGSH LDTPRLDLKG NPVHESDGVV
     YFRTHYYGGI KKYQWTCIPM ALIGVVYTRS GKKVEINVGM KDDDPVFYIS DLLIHMAQDQ
     MKKTLAQGIT GEQLQAICAT HSEENLAAKD ALMKFFKDTY GIEEEDFATA ELELVPATKS
     RDVGFDRSLI ASYGQDDRVC SYANLEAILH AEPGEYTQAA LLTDKEEIGS YGNTGMESSY
     FVKVVMKMLA LQGNGSLLEF YETMENSEML SADVNSCMDP MFPEVTEKDN SSLLGYGIAL
     TKYTGARGKA GSNDANAEFM HKVRTIFNEA GVAWQIGELG KVDQGGGGTI AFMMADWGCE
     VVDCGTAMLS MHSPYDLLSK ADAYETYLAY KAFFESR
//