ID A0A1Q5M6S9_9ACTN Unreviewed; 464 AA.
AC A0A1Q5M6S9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=AMK09_33690 {ECO:0000313|EMBL:OKK09918.1};
OS Streptomyces sp. CB02488.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703920 {ECO:0000313|EMBL:OKK09918.1, ECO:0000313|Proteomes:UP000186200};
RN [1] {ECO:0000313|EMBL:OKK09918.1, ECO:0000313|Proteomes:UP000186200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02488 {ECO:0000313|EMBL:OKK09918.1,
RC ECO:0000313|Proteomes:UP000186200};
RX PubMed=27999165; DOI=10.1128/mbio.02104-16;
RA Yan X., Ge H., Huang T., Hindra, Yang D., Teng Q., Crnovcic I., Li X.,
RA Rudolf J.D., Lohman J.R., Gansemans Y., Zhu X., Huang Y., Zhao L.X.,
RA Jiang Y., Van Nieuwerburgh F., Rader C., Duan Y., Shen B.;
RT "Strain Prioritization and Genome Mining for Enediyne Natural Products.";
RL MBio 7:e02104-e02116(2016).
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:OKK09918.1}.
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DR EMBL; LIVO01000019; OKK09918.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5M6S9; -.
DR STRING; 1703920.AMK09_33690; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000186200; 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 Reference proteome {ECO:0000313|Proteomes:UP000186200};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 41..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 303..443
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 464 AA; 50052 MW; A1BE0510666E5966 CRC64;
MGILAGSVLL TAVPSAATTG GGSGVGDPYF PDDGNPGYDV SHYDVRVAYD PARPGHLDGD
TTVTATATDR LDRFHLDLEG FQVGSVTVDG VPVRSVTRSG AHELVITPAG LIAKGAKFAV
RVRYSGKPVG ESWHRLTNGG VSVTGEPHSA TAWYPANDHP SDKATFRLTA TVPDTWTVIG
NGRPGPTTSP AKGRKTFRWY EDKPLATYLS TLAIDKFTVH TSKLADGTPV INAYSPGAVI
DPESEALLPE IIGFLASKFG PYPFSSAGGI VINGEADAGG NGPLALETQS RPTYSGMMFD
ASMVHEYAHQ WFGDSVSFSD WRDGCIAECV AQYANQLWEE KGGADLDTGF YAGMVKQSEQ
DPGFWNVKLY DPGQGKELDP ALYDKGSMMM HALRRTIGDA AFFGTLRQWQ KEHRYGNATW
PQFEALAKRI SGRPDLTGFF DAWAHGTTVP ERKYLYPGSL GRLR
//
