ID A0A135I5B7_9GAMM Unreviewed; 869 AA.
AC A0A135I5B7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:KXF80631.1};
GN ORFNames=ATN88_08225 {ECO:0000313|EMBL:KXF80631.1};
OS Enterovibrio coralii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Enterovibrio.
OX NCBI_TaxID=294935 {ECO:0000313|EMBL:KXF80631.1, ECO:0000313|Proteomes:UP000070529};
RN [1] {ECO:0000313|EMBL:KXF80631.1, ECO:0000313|Proteomes:UP000070529}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 912 {ECO:0000313|EMBL:KXF80631.1,
RC ECO:0000313|Proteomes:UP000070529};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (NOV-2015) 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:KXF80631.1}.
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DR EMBL; LNTY01000050; KXF80631.1; -; Genomic_DNA.
DR RefSeq; WP_067419216.1; NZ_LNTY01000050.1.
DR AlphaFoldDB; A0A135I5B7; -.
DR STRING; 294935.ATN88_08225; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000070529; 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:KXF80631.1};
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:UP000070529};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 89..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 226..436
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 444..544
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..867
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 869 AA; 97568 MW; 4653E11461F4CE21 CRC64;
MAQQPQAKYR KDYKAPDFTI TDIDLDFDLG ATKTTVIAKS KVKQLTPGSD TLTLDGEGFI
LRRVEIDDNA WTHYEETAEG LVLSNLPSEF TLLIETELDP AANTSLEGLY LSDGAYCTQC
EAEGFRRITY YLDRPDVLAK FTTKITADKA AFPFLLSNGN KVGQGDLDAG RHWVQWEDPF
AKPSYLFALV AGDFDLLQDV FTTRSGRDVA LEIFVDKGNL DRATHAMTSL KNSMKWDEER
FDLEYDLDIY MIVAVDFFNM GAMENKGLNV FNSKFVLANS DTATDTDYLG IEAVIGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRIMRG PQFAEDCSPM
AHPIRPEKVI EMNNFYTLTV YEKGSEVIRM MHTLLGETNF QKGMKLYFER HDGTAATCED
FVKAMEDASG IDLGQFRLWY SQSGTPELTV SAEYQTDAKT LTLTINQKTP PTADQKEKAP
LLIPFDVELY AADGSVVELQ CNNKKVSSIL HVTEETQTFV FENVSEKPVI SMLREFSAPV
KLNFDYSDEE LAFLMVHARN EFARWDAGQM LLAKHIKQNV ARIQQGEAFV LPGDVVDAFR
GVLLDGKLDS ALIAEVLTLP SENEIGGWFD VVDVDAINTV RTAIKHRFAT DLSDELSAVY
HTLNQEDYSI EHDAIGKRSL RNVCLGYLAH IENGNDLVQA HFDGANNMTD TAAALGAANH
AELASRESLM KAFSDKWTHD GLVMDKWFML QGCNPATNAL ENVKAQMSHP AFSLKNPNRT
RSLVASFCNN NPVHFHAKDG SGYAFLTEIL TQLNTSNPQV ASRLIDPLLK FKRFDEDRQA
LMRSSLERLA SLDNLAKDLY EKINKALDA
//
