ID A0A2J9E1R4_9GAMM Unreviewed; 867 AA.
AC A0A2J9E1R4;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=A6J60_012945 {ECO:0000313|EMBL:PNK61683.1};
OS Psychrobacter sp. FDAARGOS_221.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Psychrobacter.
OX NCBI_TaxID=1975705 {ECO:0000313|EMBL:PNK61683.1, ECO:0000313|Proteomes:UP000217719};
RN [1] {ECO:0000313|Proteomes:UP000217719}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FDAARGOS_221 {ECO:0000313|Proteomes:UP000217719};
RA Hoffmann M., Allard M., Evans P., Brown E., Tallon L., Sadzewicz L.,
RA Sengamalay N., Ott S., Godinez A., Nagaraj S., Vavikolanu K.,
RA Aluvathingal J., Nadendla S., Sichtig H.;
RT "FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS):
RT Supporting development and validation of Infectious Disease Dx tests.";
RL Submitted (DEC-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 -!- 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:PNK61683.1}.
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DR EMBL; NWFK02000001; PNK61683.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J9E1R4; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000217719; 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 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:PNK61683.1};
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 54..199
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 239..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 455..553
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 557..864
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 867 AA; 98057 MW; E495ADFE8BB4B93A CRC64;
MTTETLETTA THVEKIYLKD YTPPSYSVDS VALDIKMFDD HATVDSELHM TRQHPGDLVL
FGQNMSLTAI SINDEPLDDS RYQLDDSQLV IADAPDDVVL KISVRHQPQK NTELEGLYIA
GEGDEVMFVT QCEPEGFRKI TYYPDRPDVL SVFTTRLEAD KKFPTLLANG DLIESGDVEG
DSSRHYAIWH DASKKPSYLF ACVFANLSVL EDSYTTIEGR EVALEIYTQD YDIDKCHLAM
QALKDAMHWD EVNYGRAYDL DRYMIVAVKQ FNMGAMENKG LNIFNTSCVL SSPETTTDAR
SFSVKSIIAH EYFHNWTGNR VTCRDWFQLC LKEGLTVFRD QSFSADHQSP AVQRIDDVSR
LRAFQLTEDA GPLAHPPRPS SFVEINNFYT ATVYEKGAEV VRMLANTLGD EYRQGTDTYF
ERYDGQAVTV EDWLSALSAN GKSVERFIDW YTQPGTPEVS GSQQFDSATG TLTVSLSQQT
RHVEGYDAPK ALPIPIATAI FDRSSGELIE ERLLMLDKWQ QDFVFENVKT VDSQEPVVSL
LRDFSAPVQL KYNHSEQDLA FLLAHETSGF NQWQSAQALV NQVLIQNKPA DTYLQAVKKA
FLDLTETDAM LAARILDIPA ERELASSVNA DYQPEQMQQK WQQLKQQVAD SMVDKWADIY
QQLPINEYED TPEARGKRAL RNVVLDMALT AGIEEAQQWA KAQYEMASCM TERLGALSAM
VNHQHPQKDE MLADFYQRFN KQALVMDLWF SVQAADVNAN VDDIQALIER DDFDWGTPNR
IRAVVSSFAA QPTKLWTKKG VQTYISVVQK LDSTNPVLAS RLLQALSRWY TLAEPMRAEA
KQQLQQLGTQ VTSKNVTESL QTLLQAG
//
