ID   A0A1C4DNA1_9ENTR        Unreviewed;       870 AA.
AC   A0A1C4DNA1;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=GA0061070_101745 {ECO:0000313|EMBL:SCC32846.1};
OS   Kosakonia oryziphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Kosakonia.
OX   NCBI_TaxID=1005667 {ECO:0000313|EMBL:SCC32846.1, ECO:0000313|Proteomes:UP000198515};
RN   [1] {ECO:0000313|Proteomes:UP000198515}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=REICA_142 {ECO:0000313|Proteomes:UP000198515};
RA   Varghese N., Submissions Spin;
RL   Submitted (AUG-2016) 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; FMBC01000017; SCC32846.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C4DNA1; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000198515; 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:SCC32846.1};
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          25..186
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          225..439
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          444..545
FT                   /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF11940"
FT   DOMAIN          548..870
FT                   /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17432"
SQ   SEQUENCE   870 AA;  98859 MW;  44A81A36C0F50458 CRC64;
     MTQQPQAKYR HDYRAPDYLI SDIDLTFDLD AAKTIVTALS TVSRHSASAT PLRLDGGELK
     LISIHVNDEP WTNYKEEGSQ LVLDGLPERF TLRIVNEISP AANTALEGLY QSGEALCTQC
     EAEGFRHITW YLDRPDVLAR FTTKLIADKS RYPFLLSNGN RVAQGELENG RHWVQWQDPF
     PKPCYLFALV AGDFDVLRDT FTTRSGREVA LELYVDRGNL DRAPWAMTSL KNSMKWDEQR
     FGLEYDLDIY MIVAVDFFNM GAMENKGLNI FNSKYVLART DTATDKDYLD IERVIGHEYF
     HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RINNVRTMRG LQFAEDASPM
     AHPIRPDKVI EMNNFYTLTV YEKGAEVIRM MHTLLGEANF QKGMQLYFER HDGSAATCDD
     FVQAMEDASN VDLSHFRRWY SQAGTPIVTV SDDYNPNTEQ YTLTISQRTP PTAEQQEKQP
     LHIPFDIELY DNEGKVIPLQ KDGHPVHHVL NVTQAEQTFI FDNVYFQPVP SLLREFSAPV
     KLEYKWSDQQ LTFLMRHASN DFSRWDAAQS LLATHIKLNV ARHQQGQALS LPLHVADAFR
     AILLDELIDP ALAAEILTLP SANEIAELFD IIDPLAIAAV REALTRTLAT ELADEFLAIY
     YANKLDSYQV EHADIGKRSL RNTALRYLAF GDAQLADKLV RQQYHDADNM TDALAALSAA
     VAAQLPCRDA LMQEYDDKWH QDGLVMDKWF ILQATSPANN VLEMVRSLLK HRSFSLSNPN
     RIRSLIGAFA GSNPAAFHAQ DGSGYQFLVE MLTELNSRNP QVASRLIEPL IRLKRYDSKR
     QVLMRAALEQ LKALPNLSGD LFEKVSKALA
//