ID   U5VUG6_9ACTN            Unreviewed;       405 AA.
AC   U5VUG6;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=AFR_04960 {ECO:0000313|EMBL:AGZ39281.1};
OS   Actinoplanes friuliensis DSM 7358.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1246995 {ECO:0000313|EMBL:AGZ39281.1, ECO:0000313|Proteomes:UP000017746};
RN   [1] {ECO:0000313|EMBL:AGZ39281.1, ECO:0000313|Proteomes:UP000017746}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 7358 {ECO:0000313|EMBL:AGZ39281.1,
RC   ECO:0000313|Proteomes:UP000017746};
RX   PubMed=24637369; DOI=10.1016/j.jbiotec.2014.03.011;
RA   Ruckert C., Szczepanowski R., Albersmeier A., Goesmann A., Fischer N.,
RA   Steinkamper A., Puhler A., Biener R., Schwartz D., Kalinowski J.;
RT   "Complete genome sequence of the actinobacterium Actinoplanes friuliensis
RT   HAG 010964, producer of the lipopeptide antibiotic friulimycin.";
RL   J. Biotechnol. 178:41-42(2014).
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; CP006272; AGZ39281.1; -; Genomic_DNA.
DR   AlphaFoldDB; U5VUG6; -.
DR   STRING; 1246995.AFR_04960; -.
DR   MEROPS; M01.032; -.
DR   KEGG; afs:AFR_04960; -.
DR   PATRIC; fig|1246995.3.peg.1002; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_014298_2_0_11; -.
DR   Proteomes; UP000017746; Chromosome.
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:UP000017746};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          9..166
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          259..396
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   405 AA;  43757 MW;  AE68D7E8BAA4381E CRC64;
     MRYDPASGEL GGTATISATA TQDLARFNFD LARLKASKVT VDGQAATSAA DGDELVVTPA
     AGIRTGTAFT VVVDYSGKPE ALNNEALGVG GWLRTKDGAF ALGQPESAST WFPVNDHPSD
     KATLALSMTV PDGTEAIGNG VPGPRETAGG WTTWTWKEQK PLASYLAFVA IGQYRVQTST
     HKGKPMVIAI PESLPPTSNA ARAMARTGEV ADYLETQFGP YPFDAYGGVV LDDDRVGYAL
     ETQSRPVYGN TFFKGGADVS VVAHELAHQW YGDSVALDRW QHIWLNEGFA TYAEWLWSEH
     EGGRTVQQSF DRVYAAFDWS TPPGDPGAKR LFSDAVYIRG AMTVHALRKA MGDKAFFALL
     KSWPADNRDG TVTTEDFIAA AEKASGKDLG DLFEQWLFGK TRPTY
//