ID A0A1X2LXP2_9MYCO Unreviewed; 446 AA.
AC A0A1X2LXP2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=B8W66_08385 {ECO:0000313|EMBL:OSC41401.1};
OS Mycobacterium decipiens.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=1430326 {ECO:0000313|EMBL:OSC41401.1, ECO:0000313|Proteomes:UP000193247};
RN [1] {ECO:0000313|EMBL:OSC41401.1, ECO:0000313|Proteomes:UP000193247}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBL 1200985 {ECO:0000313|EMBL:OSC41401.1,
RC ECO:0000313|Proteomes:UP000193247};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a
CC peptide, amide or arylamide. Xaa is preferably Ala, but may be most
CC amino acids including Pro (slow action). When a terminal hydrophobic
CC residue is followed by a prolyl residue, the two may be released as
CC an intact Xaa-Pro dipeptide.; EC=3.4.11.2;
CC Evidence={ECO:0000256|ARBA:ARBA00000098};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M1 family.
CC {ECO:0000256|ARBA:ARBA00010136}.
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:OSC41401.1}.
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DR EMBL; NCXP01000007; OSC41401.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X2LXP2; -.
DR STRING; 1430326.B8W66_08385; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000193247; 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 CDD; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 2.60.40.1730; tricorn interacting facor f3 domain; 1.
DR InterPro; IPR045357; Aminopeptidase_N-like_N.
DR InterPro; IPR042097; Aminopeptidase_N-like_N_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF63737; Leukotriene A4 hydrolase N-terminal domain; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 36..207
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 296..439
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 446 AA; 49675 MW; 51253EC0C94CE59F CRC64;
MKASAKTAKK APRSVGPAVF DEYLPHNGNS GYRVSRYELD LQYKVAINRL SGSATITAIT
LTELQQFTLD LSDALAVSKV TVNGKRAAQF SCRAGKLRVR LAAKLATGAA MSIVVRYGGS
PRPLPTVWGD VGFEELTEGV LVAGQPNGAA SWFPCNDHPS AKAAYRIQIS TESPYRVVAN
GKLVSRRVRA AQTVWTYEQP EPTSSYLVTL QIGRYEMAEL AKAPVPMRAA LPQRLRREFD
HDFARQPEMM ELFIDLFGPY PLASGYTVVV TDDPLEIPLE AQGISIFGAN HCDGTRGSER
LIAHELAHQW FGNSVTARRW RDIWLHEGFA CYAEWLWSEH SGGLSADELA RYHHERLCEE
PQDLLLADPG PGEMFDDRVY KRGALTLHAL RARIGDERFF ALLKDWTTRY RHATVATDDF
TGLAAAYSDE SLRPLWDGWL YAAKVP
//
