ID A0A1N6UG93_9GAMM Unreviewed; 450 AA.
AC A0A1N6UG93;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-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=SAMN05421546_1649 {ECO:0000313|EMBL:SIQ64688.1};
OS Lysobacter tolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1604334 {ECO:0000313|EMBL:SIQ64688.1, ECO:0000313|Proteomes:UP000241788};
RN [1] {ECO:0000313|EMBL:SIQ64688.1, ECO:0000313|Proteomes:UP000241788}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UM1 {ECO:0000313|EMBL:SIQ64688.1,
RC ECO:0000313|Proteomes:UP000241788};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-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}.
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DR EMBL; FTLW01000003; SIQ64688.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6UG93; -.
DR STRING; 1604334.SAMN05421546_1649; -.
DR Proteomes; UP000241788; 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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..450
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012726638"
FT DOMAIN 43..204
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 298..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 450 AA; 50286 MW; FC054E2DFAEAF213 CRC64;
MRIRAMLMIL ACLGLMPIGV WATPAKEKSP QGDVAPLRSF DVQHYSVHLD PDVDAGTLRG
QVVIQLDLVA AGATRLDFDV GALTIDAVRA DGQSLPFEVA DRRLQVTLAR KHPRGKRLRI
EVDYHGAPKF GMEFHPQRGE IYTIFSTSQW MPCIDAPDER ASLDLRVLLP IDARMIGNGS
EISARKQRDG RRLHHWRLRE SVPSFTYGFA AGRYREVALH DGGLSLRYLS GALDERQLRR
VFAETPDMLR FFGEKTGIPY RGRYSQALVA KTIGQEMAGL AVLSEAYGQG VLDGSHDVGL
IAHEVAHQWW GVGVTCLDWG HFWLNEGLVT FMTAAYLQHR HGDAVYRERV AGWKQRVERL
RAEGKDRPLV YARWVAPTAD DRAVVYVKGA YAIAQLREEL GEEAFWGGIR AYTQANQGQS
VVTSDLRAAM ERSSGRDLSA FFARWAGSGE
//
