ID A0A0Q4GTB7_9MICO Unreviewed; 439 AA.
AC A0A0Q4GTB7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=ASE68_17235 {ECO:0000313|EMBL:KQM81493.1};
OS Agromyces sp. Leaf222.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Agromyces.
OX NCBI_TaxID=1735688 {ECO:0000313|EMBL:KQM81493.1, ECO:0000313|Proteomes:UP000050813};
RN [1] {ECO:0000313|EMBL:KQM81493.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM81493.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQM81493.1, ECO:0000313|Proteomes:UP000050813}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf222 {ECO:0000313|EMBL:KQM81493.1,
RC ECO:0000313|Proteomes:UP000050813};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQM81493.1}.
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DR EMBL; LMKQ01000002; KQM81493.1; -; Genomic_DNA.
DR RefSeq; WP_055862453.1; NZ_LMKQ01000002.1.
DR AlphaFoldDB; A0A0Q4GTB7; -.
DR STRING; 1735688.ASE68_17235; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000050813; 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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 27..198
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 238..429
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 439 AA; 48407 MW; 2F3E367C1E2BDBAD CRC64;
MSNPAPDAAA AAHRYLPRSG TDAFRVDSYD LDLRYKVSTN RLDAAAVISG RAVTGLTSIA
LDLVNLRARK VRLDGDRRTR FTQTATHLVV QTPRPIAPGT EFAIEVEYAG MPAPRRSRWG
TVGWEELTDG VLVASQPSGA PTWFPCNDRP SDKARYRIRI TTEQAYTVIA NGVLVDHSVA
SGRGSWTYVQ NEPTATYLAT VQIGRYAVER HSIAGVDAVL AYPPALELDV HADFAALSAM
LEVFQSAFGP YPFPTYTVVV TDDELEIPIE AQGMATFGAN HADGHGGSER LIAHELSHQW
FGNSVGVAGW RDIWLNEGFA CYAEWIWSEA SGGRTADRHA RAHHFALRLK PHDLVLDDPG
VEQMFDDRVY KRGACTLHAL RLTIGDERFF ALLRSWVEEH RGGVVTTAEF RAHAARYSPA
PLDELFDAWL SSKKLPALP
//
