ID A0A1Q4ZSW2_9ACTN Unreviewed; 838 AA.
AC A0A1Q4ZSW2;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=A6A27_34755 {ECO:0000313|EMBL:OKI49899.1};
OS Micromonospora sp. CB01531.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=1718947 {ECO:0000313|EMBL:OKI49899.1, ECO:0000313|Proteomes:UP000186700};
RN [1] {ECO:0000313|EMBL:OKI49899.1, ECO:0000313|Proteomes:UP000186700}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01531 {ECO:0000313|EMBL:OKI49899.1,
RC ECO:0000313|Proteomes:UP000186700};
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:OKI49899.1}.
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DR EMBL; LWLS01000104; OKI49899.1; -; Genomic_DNA.
DR RefSeq; WP_073838286.1; NZ_LWLS01000104.1.
DR AlphaFoldDB; A0A1Q4ZSW2; -.
DR STRING; 1718947.A6A27_34755; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000186700; 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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_C; 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 Aminopeptidase {ECO:0000313|EMBL:OKI49899.1};
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:UP000186700};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 224..436
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 519..825
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 838 AA; 90829 MW; AED31A0AF687F802 CRC64;
MPSLTRVEAT ARGALITVES YQVDLDLTGA GERFRSTVTI RFRATPGADT FAEVKPVNLL
GVRLNDRDLD PAVLDDNRLP LTGLAVENTL TVSAEMAYSN TGEGVHRFVD PADGETYLYA
MSFLDDVQRI FAAFDQPDLK APVILSVTAP PEWTVAANGR LAERPAPGRW EFAPTEPLAT
YFFTLIAGPW HVRHDEHDGI PLGLYCRRSL AAHLDADADE IFTVTRQCLD RFHQLFAERY
PFGKYDQAFM PEFNAGAMEN PGLVTLRDDY IFRSAVTDTQ RELRATTIAH EMAHMWFGDL
VTMRWWDDLW LNESFAEYLG TRVTAEATRF DRAWTTFAMR RKAWGYAADQ RPSTHPVAPA
EVPDAAQALL NFDGISYAKG ASVLRQLVAW VGDDAFLTGL NAHFAKHRFG NATLTDLLES
LSTASGRDLA DWAARWLRRP QVNTLRMVTA VDADGRWSEA AVVQTAPEAY PVLRPHRIGV
ARYAPDAPVH RFEVDLDPDA DGGRTELTEL IGQPAAGLLL PNAGDLTFAK IRLDPASADA
VPMLLAGLDD PLARALLWGE ALDAATDGER PVASVVSLIA AALPAETEVI IAEDVLTLSR
GLVDRYLEPL ARDAALLRIA EACAALLAGA PAGGSLQLAA ARGLIGATAD AGLLAGWLAG
DGVPEGLAVD ADLRWALLHR LVVLGAAGEP EIAAEAAADR SATGAERAAS CRAALPDADA
KRAAWEIITS STELSNRLVE ATAEGFWQPE QAELTAGYVE RYFADMPAAA RLRTPWMADR
VATLAFPRYA VARSTRDLAA ALLARDDLTP GLRRQVVDRD DDLRRALVAR TAVAAASA
//
