ID A0A069IL72_9BURK Unreviewed; 899 AA.
AC A0A069IL72;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:KDP89276.1};
GN ORFNames=CF70_009015 {ECO:0000313|EMBL:KDP89276.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP89276.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP89276.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP89276.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-2014) 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 -!- 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:KDP89276.1}.
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DR EMBL; JFJV02000018; KDP89276.1; -; Genomic_DNA.
DR RefSeq; WP_035859481.1; NZ_JFJV02000018.1.
DR AlphaFoldDB; A0A069IL72; -.
DR MEROPS; M01.005; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000023560; 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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:KDP89276.1};
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 83..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 226..440
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 448..560
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 565..898
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 899 AA; 99381 MW; FEED3A374934C3F9 CRC64;
MLRTDTPVTV HRKDYTPPAF AFEHVDLVLE LDPARTVVTN TLRFTRQGPG PLVLAGEELE
LVGVSLDGKP LDGARQEADS LTLPELPAQG TLEIVTACQP AANTSLSGLY VSNGNFFTQC
EAEGFRKITY YLDRPDVMST FRVTLRAQRA AYPVLLSNGN LIGERELPDG RHEAVWEDPF
KKPAYLFALV AGKLECIEER IASASGKEKL LQVWVEPQDL PKTRHAMDSL IHSIRWDERR
FGLELDLDRF MIVAVGDFNM GAMENKGLNI FNTKYVLANA QTATDADFGN IESVVGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SADMMGSESG RAVKRIEDVR MLRQVQFPED
AGPMAHPVRP DSYEEINNFY TVTVYEKGAE VVRMYQTLLG RDGFRKGMDL YFRRHDGQAV
TCDDFRAAMA DANGRDLTQF GRWYSQAGTP VVAVRTAWDG ANGSLTLTLS QSCPKVGIET
HPGTPDKLPF HIPFALGLID ADGKDLPLQL EGESQPGTTT RVLDFTEAEQ SFRFVNLPRG
AEPPLASLLR DFSAPVIVDA DYSEAQLTFL LAHDSDPFNR WEAGQRLTTR ALLQLVAQSQ
AGHELKLDPA LVAALRTVLN DAQLSPAFRE QTLTLPAEAY LAERMGVADP AAIHRARQFM
REALARALKA DWLAAFEANA TPGAYSPDAV SAGKRALRNL ALGYLADSGD AAMQALAEAQ
YQAADNMTDR FAALSAMVNT FAPGREAALA DFYQRFEQDA LVIDKWFSLQ GMQRGTVGPQ
AAGHAGKHTI DTVRALMQHP AFNLRNPNRA RSLIFSFCAA NPAQFHAEDG SGYAFWAEQV
LALGAINPQV ASRLARVMDR WQKYALPLRD RMRAALEQVA AASDLSRDVR EIVSKALAA
//
