ID A0A1Q4WDE7_9ACTN Unreviewed; 575 AA.
AC A0A1Q4WDE7;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=A6A06_34540 {ECO:0000313|EMBL:OKI08143.1};
OS Streptomyces sp. CB02923.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1718985 {ECO:0000313|EMBL:OKI08143.1, ECO:0000313|Proteomes:UP000185893};
RN [1] {ECO:0000313|EMBL:OKI08143.1, ECO:0000313|Proteomes:UP000185893}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02923 {ECO:0000313|EMBL:OKI08143.1,
RC ECO:0000313|Proteomes:UP000185893};
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:OKI08143.1}.
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DR EMBL; LWKZ01000003; OKI08143.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q4WDE7; -.
DR STRING; 1718985.A6A06_34540; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000185893; 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; 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 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 ECO:0000313|EMBL:OKI08143.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000313|EMBL:OKI08143.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000185893};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 286..476
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 481..575
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 575 AA; 62159 MW; 271EF26B34C17326 CRC64;
MLAAASLVAA GLPDATPLGI GDRLYPHLGN PGYDVRAYDI ALTYSGHNDR PLDAVTKITA
RATARLERIN LDFAHGTVRS VEVDGRPAAH VTRGEDLIVT PHRTLRAGTP VRIVVRHTSD
PRPRKGGKDK EIGWLRTKDG LVMANQVDAA HRVFPGNDHP SDKALYTFRV TAPSGLTVVA
NGSRVARYPG ALPGRSAPAG LRGRAGQDVR QGRAAPAATT WVYRSAHPMA TEVAQVSIGR
SAVVRRTGPH GLPLRDVVPA ADRKRLEPWL AETPGQLAWM EKQVGRYPFE TYGVLLAQAE
TGFELETQTL SLFEERLFVT RQYPRWYIEA IMVHELAHQW FGNSVSPRIW SDAWLNESHA
TWYEELYAHE HAKMSMDERT RRAYSVSDRM RAEGGPPGAP KVPTPGNKTG IFRPVMYDGS
ALVLYALRAK IGHAAFDRLE RAWVARHRDG VAGTADFVAL ASRVAGRDLG GFFRRWLYDA
KTPPMPGHPD WRSHYRTPQP PARKPGAKPG GGQSGGKPAG KPAGKPASKP AGNAGNAGGQ
SAGKPAGKPA RGQAAGKPGA KPVKTRPATP HGKPG
//
