ID   W5XYH8_9CORY            Unreviewed;       455 AA.
AC   W5XYH8;
DT   16-APR-2014, integrated into UniProtKB/TrEMBL.
DT   16-APR-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   ORFNames=B843_01715 {ECO:0000313|EMBL:AHI21735.1};
OS   Corynebacterium vitaeruminis DSM 20294.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1224164 {ECO:0000313|EMBL:AHI21735.1, ECO:0000313|Proteomes:UP000019222};
RN   [1] {ECO:0000313|EMBL:AHI21735.1, ECO:0000313|Proteomes:UP000019222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10234 {ECO:0000313|Proteomes:UP000019222};
RA   Ruckert C., Albersmeier A., Kalinowski J.;
RT   "The complete genome sequence of Corynebacterium vitaeruminis DSM 20294.";
RL   Submitted (FEB-2013) 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; CP004353; AHI21735.1; -; Genomic_DNA.
DR   RefSeq; WP_025251802.1; NZ_CP004353.1.
DR   AlphaFoldDB; W5XYH8; -.
DR   STRING; 1224164.B843_01715; -.
DR   MEROPS; M01.033; -.
DR   KEGG; cvt:B843_01715; -.
DR   PATRIC; fig|1224164.3.peg.331; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_014298_2_0_11; -.
DR   Proteomes; UP000019222; Chromosome.
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; cd09603; M1_APN_like; 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:SF303; 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   Reference proteome {ECO:0000313|Proteomes:UP000019222};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          30..207
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          249..444
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
SQ   SEQUENCE   455 AA;  50998 MW;  3A30018CF3E49894 CRC64;
     MIRSRLRKTP VPGTRDSYTG IDFNLGYHIR HYRLELDYKV APNHLRAVAT LSLDNYQELK
     QLTLDLASHL RVTEVSARGI GAVEVTVARF RHANAKLRIT FDDPIPVDQE FELTIRYSGN
     PRPVRSTWGT IGWEELSNGS LVASQPCGAH SWFPCDDTPD EKATYEFLIT ADSPYTVVAN
     GALDSKSVKG SRTTWRYHTN HPMASYLATV QVGQYKLIEL DGSKTPIHAY VPPAVIPGFR
     NDFADQGAML ELYSKLYGPY PFASYTVVVT EDELEIPLEA QGLSIFGANH AKGDKDWERL
     IAHELSHQWF GNSLGLAQWD DIWLNEGFAC YSEWLWFEHS TGKTAAESAR EHYDVLASKP
     QDLLLAAPGA KDMFDDRVYK RGALTVHALR VLLGDEAFFA MVRSYVAAGR HSVVEPIDLL
     REARRAAEAA GVAVDKLDAL WDAWLKKTAL PEFPQ
//