ID A0A291Q7N3_9ACTN Unreviewed; 855 AA.
AC A0A291Q7N3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=KY5_2782 {ECO:0000313|EMBL:ATL27800.1};
OS Streptomyces formicae.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1616117 {ECO:0000313|EMBL:ATL27800.1, ECO:0000313|Proteomes:UP000221011};
RN [1] {ECO:0000313|EMBL:ATL27800.1, ECO:0000313|Proteomes:UP000221011}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KY5 {ECO:0000313|EMBL:ATL27800.1,
RC ECO:0000313|Proteomes:UP000221011};
RA Holmes N.A., Devine R., Qin Z., Seipke R.F., Wilkinson B., Hutchings M.I.;
RT "Complete Genome Sequence of Streptomyces formicae KY5, the formicamycin
RT producer.";
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP022685; ATL27800.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291Q7N3; -.
DR KEGG; sfk:KY5_2782; -.
DR Proteomes; UP000221011; 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; 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:ATL27800.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ATL27800.1};
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:UP000221011};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 92..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 231..446
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 537..846
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 855 AA; 94300 MW; DD9ED303EED0D858 CRC64;
MPGTNLTREE AQQRAKLLTV DSYEIELDLS GAQEGGTYRS VTTVRFDSAE ANAETFIDLV
APAVHEVVLN GHALEVGAVF RDSRIALRHL EAGPNELKVV ADCEYTNTGE GLHRFVDPVD
QQAYLYTQFE VPDARRVFAS FEQPDLKATF QFTVKAPSGW TVISNSPTPE PKDDVWHFEP
TQRMSTYVTA LIVGPYHSVH SSYEGPNGQS VPLGIYCRPS LAEFLDSDAI FEVTRQGFDW
FQEKFDYAYP FPKYDQLFVP EFNAGAMENA GAVTIRDQYV FRSKVTDAAY EVRAATILHE
LAHMWFGDLV TMEWWNDLWL NESFATYAEA ACQAYAPGSK WPHSWTTFAN SMKTWAYRQD
QLPSTHPIMA DIRDLDDVLV NFDGITYAKG ASVLKQLVAY VGEDEFFQGV QAYFKRHAFG
NTRLSDLLGA LEETSGRDLK TWSKKWLETA GINVLRPVVD VDTAGVITSF AVKQEAPALP
EGAKGEPTLR PHRIAIGLYD LDDESGKLLR TDRVELDVDG ELTAVDALVG KHRPAVILLN
DDDLSYAKVR LDSESLAFVT DHIGDFEASL PRALSWASAW DMTRDAELPT SAYLSLVLSG
IAKESDIGVV QSLHRQVKLA LDLYAAPAGR DAALARWTEA TLEHLRAAEP GSDHQLAWAR
AFAATARTDA DLALLEALLD GSESIEGLAV DTELRWALVA RLAATGRLDE AGIEAELARD
RTAAGERHAA YARAARPTEE TKAAAWASVV ESDSLPNAIQ EAVISGFVQV DQRELLAPYT
EKFFSSVKTA WDSRSHEMAQ QIATGLYPSL QVSQATLDAT DAWLASSDPS AALRRLVTES
RAGVERALRA RSADV
//
