ID A8L204_FRASN Unreviewed; 851 AA.
AC A8L204;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN ORFNames=Franean1_5306 {ECO:0000313|EMBL:ABW14664.1};
OS Frankia sp. (strain EAN1pec).
OC Bacteria; Actinomycetota; Actinomycetes; Frankiales; Frankiaceae; Frankia.
OX NCBI_TaxID=298653 {ECO:0000313|EMBL:ABW14664.1};
RN [1] {ECO:0000313|EMBL:ABW14664.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=EAN1.pec {ECO:0000313|EMBL:ABW14664.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Hammon N.,
RA Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T.,
RA Bruce D., Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Kim E., Rawnsley T., Niemann J., Benson D.R., Huang Y.,
RA Mastronunzio J., Bassi C.A., Tisa L.S., Richardson P.;
RT "Complete sequence of Frankia sp. EAN1pec.";
RL Submitted (AUG-2007) 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; CP000820; ABW14664.1; -; Genomic_DNA.
DR AlphaFoldDB; A8L204; -.
DR STRING; 298653.Franean1_5306; -.
DR MEROPS; M01.012; -.
DR KEGG; fre:Franean1_5306; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_11; -.
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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_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:ABW14664.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 111..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 227..436
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..834
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 851 AA; 93992 MW; E7FD999AB401D1CD CRC64;
MPHNLTRDEA RERARLLAVS SYDVELDLTV GDETFLSSTT ASFTCAEPGA STFVELAAPA
VREVVLNGRS LDPAVVFDGG RIALPDLAAT NELRVVAECA YSRTGEGLHR FVDPVDSAVY
LYTQFETYDA HRMYTCFDQP DLKAAFTLAV TAPADWRIIS NSVVTGTTAA PDGATRTAFA
PTPVMSTYIT ALVAGPYHEV RDHHDGIDLG VYCRRSLAEF LDPDEILEIT KQGFDFYHRV
FDYRYPFGKY DQLFVPEFNA GAMENAGCVT FLEEYVFRAK VTEARRERRA ETILHEMAHM
WFGDLVTMRW WDDLWLNESF ATYMSVLAQV TSTRFTNGWT TFANAEKGWA YRQDQLSSTH
PIVADAPDMD AVRTNFDGIT YAKGASVLKQ LVAWVGQEEF LAGLRSYFRK YEYGNTSLKD
LLVELEKASG RDLSPWSADW LETTGANTLR PRFLTDSSGL FTSFDVVQEP ASAPATASRT
LRPHRVAIGL YDRDTTGALV RRERVELDVV GEITEVSKIV GARQPDLILL NDDDLTYAKV
RLDERSLRTL IDSIGTISSS LPRTLCWAAA WDMTRDAELA ARDYVRLVLS GIDAEDDIGV
VQSLVTKAAL TVDSYGDPAN RPAALRELTT RAEELMRSAE PGSDLQLVFA TAFAQTEEPE
QIARVMAIFE GSDVVQGLAL DTELRWALLI QLVARGVYGD AEIGAELARD NTATGEKRAA
TARSARPTAQ AKADAWSAVM DSDALSNHLA VATMGGFWIS DQLELTRPYV DRFFAEIGGI
WETRSFDTAQ TITQMLFPSG VIEQSTVDLT DAYLAERDPV PALRRALMEG RDGLVRALAA
RAKDTAGPVA G
//
