ID A0A429BNU7_9ACTN Unreviewed; 457 AA.
AC A0A429BNU7;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DMB42_06760 {ECO:0000313|EMBL:RSN14235.1};
OS Nonomuraea sp. WAC 01424.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2203200 {ECO:0000313|EMBL:RSN14235.1, ECO:0000313|Proteomes:UP000286861};
RN [1] {ECO:0000313|EMBL:RSN14235.1, ECO:0000313|Proteomes:UP000286861}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC 01424 {ECO:0000313|EMBL:RSN14235.1,
RC ECO:0000313|Proteomes:UP000286861};
RA Waglechner N., Wright G.D.;
RT "Evolution of GPA BGCs.";
RL Submitted (MAY-2018) 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:RSN14235.1}.
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DR EMBL; QHHZ01000002; RSN14235.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A429BNU7; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000286861; 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; 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 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:UP000286861};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..457
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5019097808"
FT DOMAIN 307..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 457 AA; 49283 MW; E9C809ECB6BE9979 CRC64;
MKRLLALAAA AFISLPLTPA VALGGSPGAP GAGDPYFPDQ GNGGYDAGHY DLALDYDPSS
NVLTGVAAVT ARATQALSRF DLDLVATLSV RSVTVDGRAA AFTRSGSELI VTPAATLASG
RTFSVVVRYD GRPTYVLDPD GSRDGWIRTG DGVFNANEPQ GAMTWYPGNH HMTDKATYRF
AVTVPSTRVA VANGDLVSRT TAGGRTTYVW DAREPMASYL ATVTIGKFRL TDTRVGGYRV
ITAVDPKLAD KATDFAERHA PVLDYFSSLF GPYPFSSTGG IVDHAPNVGY ALETQTRPIY
PVAPSDSLLA HELAHQWFGD SVTPTLWRDI WLNEGFATYA EWLWLEKIGS RTVQTSFDGV
YAKPADDEFW QTPTADPGDA AGLFHDPVYD RGAATLHVLR RTVGDEAFFT ILRTWASEHR
YGNADTAAFV ALAERVSGKR LGPLFDAWLF QPGKPAL
//
