ID A0A1T5CEE0_9MICC Unreviewed; 474 AA.
AC A0A1T5CEE0;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-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=SAMN05660473_01364 {ECO:0000313|EMBL:SKB57703.1};
OS Arthrobacter sp. 49Tsu3.1M3.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1279029 {ECO:0000313|EMBL:SKB57703.1, ECO:0000313|Proteomes:UP000189904};
RN [1] {ECO:0000313|EMBL:SKB57703.1, ECO:0000313|Proteomes:UP000189904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=49Tsu3.1M3 {ECO:0000313|EMBL:SKB57703.1,
RC ECO:0000313|Proteomes:UP000189904};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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; FUZD01000004; SKB57703.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5CEE0; -.
DR Proteomes; UP000189904; 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 Aminopeptidase {ECO:0000313|EMBL:SKB57703.1};
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 52..222
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 267..457
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT REGION 1..45
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 52276 MW; A735D02F6859B149 CRC64;
MSTSAPSSSG AAARGEISGE ISREISRATS PEAGAPDPYM PGHGTNAYRV TRYELDLDYR
VSSNRLAGHA VLHAITQLPT SAIVLDLAGL RATKIQLNGR RVRRFTQRAE QLVVYPDNPL
LATEAFTLDI RYEGYPAPRR GVWGEVGWEE LSDGVLVAGQ PNGAASWFPC NDHPRDKATY
LITVTTDANY RAVCNGVLLS RTSRASRETW VFEQAEPMAT YLATVQIGRY ELLTLNADRP
SGHVPQYVAV PASLQAGARA ALARQPDMMR TFTSCFGPYP FPEYTVVVTD DVLEIPLEAQ
TLSILGPNHL RQDWESQRMI AHELAHQWFG NSLTTATWKD IWLHEGFACY AEWIWSEEAG
IMSAAARARA AWRKLAAAPQ DLMVGDPGPE LMFDDRVYKR GALALHALRV RCGDLAFFAL
LHDWTDRFRH GTVTTADFIV AAAHTTGLDA EALLHPWLFA DALPPLPQAT PPKI
//
