ID A0A494SPD8_9NOCA Unreviewed; 448 AA.
AC A0A494SPD8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=D8W71_00305 {ECO:0000313|EMBL:AYJ47029.1};
OS Rhodococcus sp. P1Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=1302308 {ECO:0000313|EMBL:AYJ47029.1, ECO:0000313|Proteomes:UP000277147};
RN [1] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Belimov A., Safronova V.I., Ismailov T.;
RT "Complete genome sequence of the abscisic acid utilizing strain Rhodococcus
RT sp. P1Y.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000277147}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=P1Y {ECO:0000313|Proteomes:UP000277147};
RA Nikolaichik Y.A., Gogoleva N.E., Khlopko Y.A., Gogolev Y.V.;
RL Submitted (OCT-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}.
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DR EMBL; CP032762; AYJ47029.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A494SPD8; -.
DR KEGG; rhop:D8W71_00305; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000277147; Chromosome.
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:UP000277147};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 38..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 249..423
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 448 AA; 49945 MW; 0571FF3B1F8620F5 CRC64;
MKFAGSKLVT PTFDLDANDA PIDDYLPQNG NRGYRVSRYE LDLEYKVESN RLAGKAKITA
VTTATTSKFA FDLGPALTVS KVTVNGSRSV KFSQHRGKLK ITPAKQIASG AALVVVIQYA
GTPKPINGFW GEVGWDELTE GSIVASQPNG AASWFPCDDH PVSKASYGIT ITTDSPYYAV
ANGTLVRKQT RASRTTWVYE QPEPMATYLA TIQIGPYSQH TTSPGPVLMK AVLPHRLRAN
FDHDFGRQTE MMSTFERLYG PYPFAAYTVV ITDDDLEIPI EAQGLSIFGA NHCSGTRYFE
RLVAHELAHQ WFGNSLTLGK WKDIWLHEGF ACYSEWIWAE TSDGTSARDK ARRVHTMQRG
LPRDLILGDP GPAKMFDDRV YKRGALTLHA LRTTIGDEQF FGLIQEWTSK YRYSTVCTAD
FIDLATRFGC PRSLWEAWLE SPQLPALP
//
