ID A0A0A8EQ29_9ACTN Unreviewed; 874 AA.
AC A0A0A8EQ29;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=GZL_05770 {ECO:0000313|EMBL:AJC58345.1};
OS Streptomyces sp. 769.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1262452 {ECO:0000313|EMBL:AJC58345.1, ECO:0000313|Proteomes:UP000031113};
RN [1] {ECO:0000313|EMBL:AJC58345.1, ECO:0000313|Proteomes:UP000031113}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=769 {ECO:0000313|EMBL:AJC58345.1,
RC ECO:0000313|Proteomes:UP000031113};
RA Du Q., Wang Q., Li Q., Wang L., Zhang Z., Ren J., Wang J., Wang M.;
RT "Complete Genome Sequence of Streptomyces gongzhulingensis.";
RL Submitted (DEC-2012) 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}.
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DR EMBL; CP003987; AJC58345.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A8EQ29; -.
DR MEROPS; M01.009; -.
DR KEGG; stre:GZL_05770; -.
DR HOGENOM; CLU_007335_1_1_11; -.
DR Proteomes; UP000031113; 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:AJC58345.1};
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 113..205
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 250..463
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 552..861
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 874 AA; 96011 MW; 1D3200C0483DECD6 CRC64;
MEGWPDEAMT TCEGEGRVPG TNLTREEAQE RARLLTVDAY DIELDLSGAQ DGGTFRSVTT
VRFDAVEDGA ASFIDLVAPT VHEVLLNGTA LDAAAVFQDS RIALSGLRAG RNELTVVADC
AYTNSGEGLH RFVDPVDQQA YLYTQFEVPD ARRVFASFEQ PDLKATFRFT VTAPQGWTVI
SNSPTPEPAD NVWRFAPTPR ISTYVTALIA GPYHSVHSTW EGADGRSVPL GIYCRPSLAE
HLDAEEIFAV TRQGFDWFEE KFDYPYPFAK YDQLFVPEFN AGAMENAGAV TIRDQYVFRS
KVTDAAYEVR AETILHELAH MWFGDLVTME WWNDLWLNES FATYTSIACQ AYAPGSKWPH
SWTTFANSMK TWAYRQDQLP STHPIMAEIR DLDDVLVNFD GITYAKGASV LKQLVAYVGM
DEFFQGVQAY FKAHAYGNTR LTDLLGALEK TSGRDLKTWS KKWLETAGIN VLRPEIEVAA
DGTVTAFAVR QEAPALPAGA TGEPVLRPHR IAIGYYDLQD GKLVRTGGVE LDVDGERTEV
PFPEGFRRPD VILLNDGDLS YAKVRLDEQS LKVVTEHLGD FTESLPRALS WASSWDMTRD
AELPTRDYLS LALSGIGKES DIGVVQSLHR QVKLAQDLYA APERRAAGLA AWTEAALAHL
RAAEPGSDHQ LAWARAFAAS ARTDEQLDLL QGLLDGTQEV PGLAVDTELR WALLERLAAT
GRADEPEIAA ELKRDATSAG ERHAVTARAA RPTAAAKAEA WASIVESDAL PNAVQEAVIG
GFVQPDQQEL LAPYTAKYFE AIKGVWDNRS HEMAQQIVVG LYPALQISQE TLDATDAWLA
QADPSPALRR LVTESRAGVE RALKARAADA AAGA
//
