ID A0A091BYU3_9GAMM Unreviewed; 872 AA.
AC A0A091BYU3;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=P873_10250 {ECO:0000313|EMBL:KFN49525.1};
OS Arenimonas composti TR7-09 = DSM 18010.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Arenimonas.
OX NCBI_TaxID=1121013 {ECO:0000313|EMBL:KFN49525.1, ECO:0000313|Proteomes:UP000029391};
RN [1] {ECO:0000313|EMBL:KFN49525.1, ECO:0000313|Proteomes:UP000029391}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TR7-09 {ECO:0000313|EMBL:KFN49525.1,
RC ECO:0000313|Proteomes:UP000029391};
RA Chen F., Wang G.;
RT "Genome sequencing of Arenimonas composti.";
RL Submitted (SEP-2013) 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:KFN49525.1}.
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DR EMBL; AWXU01000033; KFN49525.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091BYU3; -.
DR STRING; 1121013.GCA_000426365_02832; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000029391; Unassembled WGS sequence.
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 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:UP000029391};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 108..191
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..443
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 449..552
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 557..869
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 872 AA; 96395 MW; F49F31FBF5BEAA7B CRC64;
MSPPRADGFV HLEDYAPPAW RIPHAELAFD LEREATVVEA TLRLEPDPGQ PGHAVVLDGE
ELELLDIEAD GAPLPADRWD YDGRHLRIDG FASAFTLRTR ARIRPADNTR LEGLYTSGPL
LLTQCEAEGF RRITFFADRP DVMPTWRIVL RADRAAFPVL LANGNPAGTR ELDGGRHEAT
WENPHPTPCY LFAIAAGQLR RVTHTLRTAE GREVELNVWA QGDDVVRCHY ALGAVERALR
WDEQRFGRCY DLEVFNVVAA QDFTMGAMEN KGLNIFNARY ILADEESATD EDFLAIESVV
AHEYLHNWSG NRVTLRDWFQ LSLKEGLTVF RDTEFSADLH SRALKRIEVV RLLRARQFAE
DAGALAHAVR PDRYREISNF YTLTIYEKGA EVVRVLQALV GEEAFRAGMD RYFADNDGRA
ATIEDFLAAH AAASGSDLSD FARWYAQAGT PELWITADYD EASGDYTLQV DQHTPPTPGQ
AHKEALPMPL RFVLFAPDGG VIDAAPETDA PALPGGGVAL TQATHVLRWR GLRARPLPAF
NQGFAAPVKL RFEYDAADLA ALARFESDPF NRWDLLQRLA SGALLHTLDP EQATVALGDA
LGALLDDDAA DPAFVAECLA LPDFDTLAEA CDVVDVDELV ARRESLLDRL AEEHVERLQR
RYESLAAAAG DGLTAPAMAA RALRNACLAW LTRLDPEATL AQAQFATATT MTARLGALRC
LVHFEAPGAA AALAEFRTRW AADPLVTDKW IACLASRPHP DTLDDIGELL ASSWWLPTNP
NRVRAVVGTF SRANPLGFHR RDGAGYRFVA AQVEKLDGIN PQVAARLLGA FETWRKLAEP
LRHQARLALA SLQGRLHSGD TRDLLQRLLD DA
//
