ID A0A0M8T334_9ACTN Unreviewed; 874 AA.
AC A0A0M8T334;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=ADK56_13275 {ECO:0000313|EMBL:KOU50681.1};
OS Streptomyces sp. MMG1522.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1415545 {ECO:0000313|EMBL:KOU50681.1, ECO:0000313|Proteomes:UP000037713};
RN [1] {ECO:0000313|EMBL:KOU50681.1, ECO:0000313|Proteomes:UP000037713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MMG1522 {ECO:0000313|EMBL:KOU50681.1,
RC ECO:0000313|Proteomes:UP000037713};
RA Noorani M.;
RL Submitted (JUL-2015) 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:KOU50681.1}.
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DR EMBL; LGDF01000111; KOU50681.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8T334; -.
DR PATRIC; fig|1415545.3.peg.2852; -.
DR Proteomes; UP000037713; 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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 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 Aminopeptidase {ECO:0000313|EMBL:KOU50681.1};
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 113..204
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 246..461
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 551..860
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 874 AA; 95974 MW; CCF0ED00B3F0DFF4 CRC64;
MAGNAAYQVA HLGDDRVPGT NLTREEAQER ARLLTVDAYE IDLDLSGAQE GGTYRSVTTV
RFDSAESGAE SFIDLVAPTV HEVVLNGEAL DAAAVFSDSR IALPGLREGA NELKVVADCA
YTNTGEGLHR FVDPVDEQAY LYTQFEVPDA RRVFASFEQP DLKATFRFTV KAPAGWTVIS
NSPTPEPKDD VWSFEPTPRI STYITALIAG PYHAVHSTYE KDGQTVPLGI YCRPSLAEYL
DADEIFDVTR QGFAWFQEKF DYAYPFAKYD QLFVPEFNAG AMENAGAVTI RDQYVFRSKV
TDAAYEVRAE TILHELAHMW FGDLVTMEWW NDLWLNESFA TYTSIACQAD AAGSKWPHSW
TTFANSMKTW AYRQDQLPST HPIMADISDL DDVLVNFDGI TYAKGASVLK QLVAYVGKDA
FFQGVQAYFK AHAFGNTRLS DLLGALEETS GRDLKTWSKA WLETAGINIL RPEIETDENG
VVTSFTVLQE APALPAGAKG EPTLRPHRIA IGAYDLDADG RLVRGDRIEL DVDGERTEVP
ALVGKARPAV VLLNDDDLSY AKVRLDEESL RVVTQHLGDF AESLPRALSW ASAWDMTRDG
ELATRDYLAL VLAGIGKESD IGVVQSLHRQ VKMALDLYAA PETREGALNQ WTDATLAHLR
ASEPGSDHQL AWARAFAATA RNPQQLDLLQ SLLDGTESIE GLAVDTELRW AFVERLAAAG
LLDEEEIAAE YERDRTAAGE RHAASARAAQ PTEAAKAEAW ASVVESDKLP NSLQEAVIGG
FVQTDQRELL APYTEKFFAA VKDVWDSRSH EMAQQVAVGL YPALQVSQET LDATDAWLAS
AEPSAALRRL MSESRSGVER ALRAQAADAA AATA
//
