ID A0A2J6MNE7_9BURK Unreviewed; 896 AA.
AC A0A2J6MNE7;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=CY652_17785 {ECO:0000313|EMBL:PLZ01134.1};
OS Burkholderia sp. WAC0059.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=2066022 {ECO:0000313|EMBL:PLZ01134.1, ECO:0000313|Proteomes:UP000243676};
RN [1] {ECO:0000313|EMBL:PLZ01134.1, ECO:0000313|Proteomes:UP000243676}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAC0059 {ECO:0000313|EMBL:PLZ01134.1,
RC ECO:0000313|Proteomes:UP000243676};
RA Cho S.-T., Yang Y., Chen C.-L., Wang T.-F., Kuo C.-H.;
RT "Genome Sequence of Burkholderia sp. WAC0059.";
RL Submitted (DEC-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}.
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:PLZ01134.1}.
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DR EMBL; PNEO01000017; PLZ01134.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J6MNE7; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000243676; 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; cd09600; M1_APN; 1.
DR Gene3D; 2.60.40.1840; -; 1.
DR Gene3D; 3.30.2010.30; -; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 1.
DR Gene3D; 1.25.50.10; Peptidase M1, alanyl aminopeptidase, C-terminal domain; 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; IPR038438; PepN_Ig-like_sf.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR012779; Peptidase_M1_pepN.
DR InterPro; IPR024601; Peptidase_M1_pepN_C.
DR InterPro; IPR037144; Peptidase_M1_pepN_C_sf.
DR InterPro; IPR035414; Peptidase_M1_pepN_Ig-like.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02414; pepN_proteo; 1.
DR PANTHER; PTHR46322; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46322:SF1; PUROMYCIN-SENSITIVE AMINOPEPTIDASE; 1.
DR Pfam; PF11940; DUF3458; 1.
DR Pfam; PF17432; DUF3458_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:PLZ01134.1};
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:UP000243676};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 107..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..450
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 455..563
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 566..896
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 896 AA; 99739 MW; 8FA8C24A824C7D86 CRC64;
MTDTATSTAI RRADYTPPAF LIDTVALEFD LVPERTVVRS TLRIRRNPAA AHAPHLELVG
EQLEFLGATL DGAPYAAVRA HEHGLSVENV PDRFELTLTG ACDPSANTTL SGLYVSGGNF
FTQCEAEGFR RITWFLDRPD VMATYTVTLR ADKAAYPVLL SNGNLVEEGV LPDGRHYARW
EDPFRKPCYL FALVAGKLVA LEERIRSGSG KEKLLQVWVE PHDLDKTRHA MDSLIHAIRW
DERRFGLELD LDRFMIVAVS DFNMGAMENK GLNIFNTKYV LANPETATDT DFANIEAVVG
HEYFHNWTGN RVTCRDWFQL SLKEGLTVFR DQEFSADMAG GETDEAARAT KRIEDVRVLR
QVQFAEDAGP MAHPVRPESY VEINNFYTVT VYEKGAEVVR MYQTLFGRDG FRKGMDLYFQ
RHDGEAVTCN DFRAAMADAN GRDLAQFERW YSQAGTPRVT VTTRYDEAAR RYSVSVAQSY
GPTSPAARET QNGPLLIPFA IGLIGPDGAD LPLRLEGERE AQGTTRVLDV TGSQQTFTFV
DVPAKPLPSL LRNFSAPVIV EYDYSDDELA FLLAHDSDPF NRWEAGQRLA TRELLALAAH
AATGRTLQLD DAVVGAFRRV LTDETLSPAF RELALMLPSE TYLAEQMAES DPAAVHAARQ
FVRRRLAQAL KADWLAVYER HRTPGAYEAT STAAGHRALK NLALSYLAEL DDPADAVRLA
SAQYDAADNM TDRAAALSAL LNAAAGSGSD FAQGPLDDFY RRFEKEPLVI DKWFALQATQ
RGRKGRPVIA EVRRLMAHPA FNLKNPNRAR SLIFSFCAAN PAQFHAPDGS GYAFWAEQVI
ALDALNPQVA ARLARSLELW RRFTPALREP MRAALEKVAA QVKSRDVREI VEKALA
//
