ID A0A0X3WK70_9ACTN Unreviewed; 854 AA.
AC A0A0X3WK70;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, 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};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=ADL30_12630 {ECO:0000313|EMBL:KUL56566.1};
OS Streptomyces sp. NRRL S-1521.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1609100 {ECO:0000313|EMBL:KUL56566.1, ECO:0000313|Proteomes:UP000053420};
RN [1] {ECO:0000313|EMBL:KUL56566.1, ECO:0000313|Proteomes:UP000053420}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL S-1521 {ECO:0000313|EMBL:KUL56566.1,
RC ECO:0000313|Proteomes:UP000053420};
RA Gilbert D.G.;
RL Submitted (OCT-2015) 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:KUL56566.1}.
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DR EMBL; LLZK01000155; KUL56566.1; -; Genomic_DNA.
DR RefSeq; WP_062773932.1; NZ_LLZK01000155.1.
DR AlphaFoldDB; A0A0X3WK70; -.
DR Proteomes; UP000053420; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_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:KUL56566.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000053420};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 118..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 240..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 533..843
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 854 AA; 94852 MW; B01E2454E5FFA402 CRC64;
MPGENLSRDE AHERAALLSV DGYEVFLDLR SAVGESGQEP RTFRSVTTIR FRAEPGAASF
ADLIAPSVTA LSLNGRDLDP AEVFDGTRIA LEDLAEENEL VVDAQCAYSR TGEGMHRFVD
PEDGEVYLYT QYEPADSRRV YANFEQPDLK APYRFQVQAP EGWTVWSNGV GELSDGVWRF
AETKPISTYI TTVVAGPYHY VEDRYERVLA DGTRLEIPLG AMCRKGLAPH FDADDVFLVT
KQGLDFFHDN FDYPYPFGKY DQAFVPEYNL GAMENPGLVT FREEFIFRGK VTQASYERRA
NVILHEMAHM WFGDLVTMRW WDDLWLKESF ADFMGSFSMV EATRFTNGWI TFANNRKAWA
YRADQLPSTH PVTADIRDLE DAKLNFDGIT YAKGASVLKQ LVAYVGRDAF LEGARRYFKR
HAYGNTVLGD LLSVLEETSG RDMAAWSRSW LQTAGVNSLT PQVILNAEGR VTELSVLQEA
AESHPELRPH RVAVGLYRRA AGGALERYAR AEVDVEGPRT VVAELAGEQA PELVLVNDDD
LTYCKIRFDE NSLVTLREHL GDITDPLARA LCWSALWSLT RDALMPARDF IGLVLRFAGR
ESDIGVLQML HAWTNSALTH YAAPEWREEG SRALAEGALR ELRIAEPGSQ HQLTWARFLA
AVASSPADLQ LLQGLLDGTA KIDGLDIDQE MRWALLAPLA AHGAADEEVL AAELARDDTA
SGKRHQVRCL AARPSAAVKA QAWASVVESS ALSNALVEAT ISGFSQPSQR ELTAPYVAKY
FDAIERVWAE RSIQIGMDVV RGLFPHLQSD EATLAAADAW LSAHEAAAPA LRRLVLEARD
DLARALRAQA CDAS
//
