ID A0A1Q5JJR0_9ACTN Unreviewed; 850 AA.
AC A0A1Q5JJR0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=AMK29_03835 {ECO:0000313|EMBL:OKJ69557.1};
OS Streptomyces sp. CB02261.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1703940 {ECO:0000313|EMBL:OKJ69557.1, ECO:0000313|Proteomes:UP000186742};
RN [1] {ECO:0000313|EMBL:OKJ69557.1, ECO:0000313|Proteomes:UP000186742}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB02261 {ECO:0000313|EMBL:OKJ69557.1,
RC ECO:0000313|Proteomes:UP000186742};
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:OKJ69557.1}.
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DR EMBL; LIVX01000001; OKJ69557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q5JJR0; -.
DR Proteomes; UP000186742; 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; IPR045357; Aminopeptidase_N-like_N.
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 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:0000313|EMBL:OKJ69557.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 117..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 239..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..837
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 850 AA; 94186 MW; 4E1EC4A69B762AEA CRC64;
MTVPGENLSR DEAQERAALL SVDGYEVVLD LRSAVGDSTE AVRTFRSETT IRFRRTGEGT
STFVDLIAPA VDAVTLNGRS LDPAVVFDGS RITLDGLADE NTLVVDARCA YSRTGEGLHR
FVDPEDGEVY LYTQYEPADA RRVYANFEQP DLKAPYRFTV TAPEGWTVWS NGAGEQDAEG
VWRFAETAPI STYITCVVAG PYHYVTDTYT RGDLVIPLGA MCRKGLAKHF DADDVFLITK
QGLDFFHDNF DYPYPFGKYD QAFVPEYNLG AMENPGMVTF REEYVYRGKV TQAAYESRAN
VILHEMAHMW FGDLVTMVWW DDLWLKESFA DFMGSFANAE ATRFTNSWVT FANNRKAWAY
RADQLPSTHP ITADIRDLED AKLNFDGITY AKGAAVLKQL VAYAGRDAFM EGARRYFKRH
AYGNTRLDDL LTILEETSGR DMRAWAKSWL QTSGVNTLTP VVTHDAEGRI TELAVVQEGD
ALRPHRAAVG LYRVSGGELV RYARAEADIT GARTVVTDLT GEERPDLVLV NDDDLTYCKI
RFDEASLATL RAHLGDITDP LARALCWSAL WNLTRDGLMP ARDFVAVALA FAGRETDIGV
LQMVHAWTRS AVTLYAAPEW REEGGRLLAE GGLRELRVAE PGSEHQLTWG RFLAATASTE
ADFQLLEGLL DGTAKIDGLD VDQELRWALL SPLAAHGRAD EARIGAELAR DDTATGKRHQ
VRLLASRPSA AVKAQAWAQV VESDTLSNAL VEATIAGFVQ PSQRELIAPY AERYFAAIER
VWAERSIQIG IHVVRGLFPG LQDDEATLTA TDTWLSAHAS AAPALRRLVL EARDDLARAL
RAQACDRLAA
//
