ID A0A2A7NGI7_MYCAG Unreviewed; 442 AA.
AC A0A2A7NGI7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-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=CQY20_00165 {ECO:0000313|EMBL:PEG43054.1}, MAGR_60150
GN {ECO:0000313|EMBL:GFG54574.1};
OS Mycolicibacterium agri (Mycobacterium agri).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=36811 {ECO:0000313|EMBL:PEG43054.1, ECO:0000313|Proteomes:UP000220914};
RN [1] {ECO:0000313|EMBL:PEG43054.1, ECO:0000313|Proteomes:UP000220914}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG37673 {ECO:0000313|EMBL:PEG43054.1,
RC ECO:0000313|Proteomes:UP000220914};
RA Tortoli E., Trovato A., Cirillo D.M.;
RT "The new phylogeny of genus Mycobacterium.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:GFG54574.1, ECO:0000313|Proteomes:UP000465302}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG54574.1,
RC ECO:0000313|Proteomes:UP000465302};
RX PubMed=31287781;
RA Matsumoto Y., Kinjo T., Motooka D., Nabeya D., Jung N., Uechi K., Horii T.,
RA Iida T., Fujita J., Nakamura S.;
RT "Comprehensive subspecies identification of 175 nontuberculous mycobacteria
RT species based on 7547 genomic profiles.";
RL Emerg. Microbes Infect. 8:1043-1053(2019).
RN [3] {ECO:0000313|EMBL:GFG54574.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCM 6377 {ECO:0000313|EMBL:GFG54574.1};
RA Matsumoto Y., Motooka D., Nakamura S.;
RL Submitted (FEB-2020) 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:PEG43054.1}.
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DR EMBL; BLKS01000001; GFG54574.1; -; Genomic_DNA.
DR EMBL; PDCP01000001; PEG43054.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2A7NGI7; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000220914; Unassembled WGS sequence.
DR Proteomes; UP000465302; 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:UP000220914};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 30..201
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 240..433
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 442 AA; 49483 MW; 06728840C71FF300 CRC64;
MTRTKKAARK IPVIDPYLPH NGNFGYRVSR YELDLEYKVA INRLAGSATI TAVTLAQLRT
FTLDLSDALS VSKVTVNGRK PASFGCSHDK LHIALPSPLP AGAAMTVSVR YGGAPRPIRS
HWGDVGFEEL TEGALVAGQP NGAASWFPCD DHPSAKASFR IQISTENPYR VIANGELISR
RTRAAMTTWT YELAEPTSTY LITLQIGMYE IYRLQKSPVL MQAALPARLK RNFDHDFGRQ
PEMMKVFAKR FGPYPLPTGY TVVVTDDDLE IPLEAQGISI FGANHCDGTG SSERLIAHEL
AHQWFGNSVT ARRWRDIWLH EGFACYAEWL WSEESGGRSA DEWARHYHAR LTKSPQDLLL
SDPGPRDMFD DRVYKRGALT LHALRRCIGD ANFFTLLQDW AARYRHATAV TDDFTGLAAN
YADVSLRSLW DGWLYSKDVP AL
//
