ID A0A1H1H194_9MICC Unreviewed; 470 AA.
AC A0A1H1H194;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, 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=SAMN04489742_4492 {ECO:0000313|EMBL:SDR19194.1};
OS Arthrobacter crystallopoietes.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=37928 {ECO:0000313|EMBL:SDR19194.1, ECO:0000313|Proteomes:UP000181917};
RN [1] {ECO:0000313|EMBL:SDR19194.1, ECO:0000313|Proteomes:UP000181917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20117 {ECO:0000313|EMBL:SDR19194.1,
RC ECO:0000313|Proteomes:UP000181917};
RA de Groot N.N.;
RL Submitted (OCT-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; FNKH01000002; SDR19194.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1H194; -.
DR STRING; 37928.SAMN04489742_4492; -.
DR KEGG; acry:AC20117_16935; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000181917; 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; 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:UP000181917};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 44..215
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 272..437
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 470 AA; 51104 MW; 19D15EFCA7ADF04F CRC64;
MTCLSSTPAD ATTDGPAAVL PAAVSAPLPD RYLPGRGTGD LLITHYDLDL ECKLASNRLA
GRAVLTGRTL KDTSRLEFDL TGLQAGRVQV NGQRPRKTSQ RNGKLVLSLK EPLPAETGLV
LDIRYEGTPA PINGDWGEVG WEELTDGVLV AGQPDGASSW FPCNDHPSQK ATFRISTTTD
AGYRAVANGE LVSHRKKASR ETWVYEMNEP MATYLATLQI GRYVLRDLVP AGPAGAGGDA
AVVQQVAAPA PLLTDAVVAL SRQEDMMAVF VRSFGPYPFA RYTVVVAEDE LEIPLEAQSL
SIIGRNHLDS GWEAQRLIAH ELSHQWFGNS LTAASWQDIW LHEGFACYSE WIWSEASGSL
PAAGRAKAAW QMLAALEQDI TVGDPGPELM FDDRVYKRGA LALHALRTEL GDERFFRLLR
RWCADYRHGS VSTSQFIGLA DTEAGRPGFS AATLLEPWLF SAALPEFPGK
//
