ID   A0A1S1JD88_9FLAO        Unreviewed;       857 AA.
AC   A0A1S1JD88;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=BHE19_01595 {ECO:0000313|EMBL:OHT46233.1};
OS   Flavobacterium tructae.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=1114873 {ECO:0000313|EMBL:OHT46233.1, ECO:0000313|Proteomes:UP000180252};
RN   [1] {ECO:0000313|Proteomes:UP000180252}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MSU {ECO:0000313|Proteomes:UP000180252};
RA   Chen S., Walker E.;
RL   Submitted (SEP-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}.
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:OHT46233.1}.
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DR   EMBL; MIKE01000011; OHT46233.1; -; Genomic_DNA.
DR   RefSeq; WP_070906034.1; NZ_MUHG01000002.1.
DR   AlphaFoldDB; A0A1S1JD88; -.
DR   STRING; 1278819.BHE19_01595; -.
DR   OrthoDB; 100605at2; -.
DR   Proteomes; UP000180252; 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; 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; IPR001930; Peptidase_M1.
DR   InterPro; IPR014782; Peptidase_M1_dom.
DR   InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR   PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR   PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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   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          142..210
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          251..463
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   857 AA;  97897 MW;  60E47D295AAC2713 CRC64;
     MKISYSLLCF FVFTTIGFSQ SKQKEKLTLE DGVSEQLAHF RKKQISKLTY GLSFEIPEKK
     AQSINAELVL DLVIADGSES LYLDFKEKTQ NIKSVTANGK NIPIVHQKGH IIIPAEGLVK
     GKNTIAISFI AGDLSLNRND DFLYTLLVPD RASTLFPCLD QPDIKATYKL KLTVPKDWSV
     LAGAYVEEKF EKDDFTSYTF GESDKMSTYL FSFVAGKFKS ITEKPGLEMT MLYRENNAEK
     LKSSTDTIFK LHQQSLDFLE KYTHYKFPFQ KLDFASIPVF QYGGMEHVGA IQYKESTLFL
     DNSATDSEKL DRAKLIAHET SHMWFGDLVT MKWFDDVWMK EVFANFMADK IMNPIFPKVN
     HNLQFLTAHY PNAYGEDRSL GTHPIKQNLA NLKNAGSLYG AIIYNKAPIM MRQLEASMGK
     TAFQKGIEKY IKKYANDNAD WNNLVEILDA ETPLDMKKWS EVWVNKSGRA IFTDKIAYDA
     QNRISSFEIT QQAEDRSTNV WPQIFDIGLV YPNNVKVISA TIKDKSLSLK EAIGLEKPIA
     VIYNYNGFGY GVFPLDGNNL ESVLSLKDEV ARASTYINIY ENTLTGNIAP TKAFDCFVKG
     IQQEQNELVL KIITNQTSAV FWKYLTQKQQ NRAQKQLEEV VFDRLKTNLP SNIKKTLFNL
     FSSIAYSDSG KVKLYAIWSK ETVISGLKLN EDDYTNMAMN LAIFKHEKAD EILNKTKTSI
     SNPDKQKRFE FLLPSLSKDE GGRDAFVQSL KDDANREKEA WVSVGLANIN HPLRQESAQR
     YIRFSLDLVD EIQRTGDIFF PKDWLNNTIG KYSSKYAFDE VQRFLKENPN FSPILKRKLM
     QATDGLYRAQ NIKKETE
//