ID A0A1Q5N9A1_9ACTN Unreviewed; 511 AA.
AC A0A1Q5N9A1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=AMK16_04730 {ECO:0000313|EMBL:OKK23014.1};
OS Streptomyces sp. CB00455.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703927 {ECO:0000313|EMBL:OKK23014.1, ECO:0000313|Proteomes:UP000185643};
RN [1] {ECO:0000313|EMBL:OKK23014.1, ECO:0000313|Proteomes:UP000185643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB00455 {ECO:0000313|EMBL:OKK23014.1,
RC ECO:0000313|Proteomes:UP000185643};
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:OKK23014.1}.
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DR EMBL; LIVQ01000001; OKK23014.1; -; Genomic_DNA.
DR RefSeq; WP_073910487.1; NZ_LIVQ01000001.1.
DR AlphaFoldDB; A0A1Q5N9A1; -.
DR STRING; 1703927.AMK16_04730; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000185643; Unassembled WGS sequence.
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:SF174; ALANINE/ARGININE AMINOPEPTIDASE-RELATED; 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 Aminopeptidase {ECO:0000256|ARBA:ARBA00022438};
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:UP000185643};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..511
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012592372"
FT DOMAIN 49..218
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 308..454
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 465..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 511 AA; 55288 MW; 322887B729CB9FEE CRC64;
MHRKVIAPSV LAASLLLVIP ASAASAGPGA PGIGDPYYPA SGNGGYDVSH YDLRLQYQPK
TDLLEGTATL LATAKQDLSR FNLDFGLQVS EIRVNGAKAK FAVSGAHELE VTPAKPLARN
TPLSVVVKYA GKPSEFKVDG WSAWARTPDG AVAAQEPDSA AWWFPSNDHP LDKATFDVSV
NVPDGLQAIS NGVLQSQSSK LGWTRYNWRS NKPQATYLTT LAVGRFDITT DTTANGLPVL
NAYSKDLGDN AGAARASVER TTEVAEWLEG VFGPYPFNAL GGYVPNVTSG FALETQTRPF
YSPRQFQNGT NVSVVVHELA HQWYGDSVSV DGWKDIWINE GFARYSQWLW SEKEGEGTAR
ELADWTYATR PAEDPFWQVK PGDPGPDNQF HGAVYDRGAL AIQALRNEVG DETFFRILKG
WPTERALGNA KVGDFVRYAE KASGKPLAQL FETWLYTPGK PDASALNRPA PAAKSPSARS
GQAAPAAGQA EPKSWKKIAA TNSIHDDDHG H
//