ID A0A1H6ZNJ9_9BACT Unreviewed; 841 AA.
AC A0A1H6ZNJ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-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=SAMN05216327_11294 {ECO:0000313|EMBL:SEJ53724.1};
OS Dyadobacter sp. SG02.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Spirosomataceae;
OC Dyadobacter.
OX NCBI_TaxID=1855291 {ECO:0000313|EMBL:SEJ53724.1, ECO:0000313|Proteomes:UP000199631};
RN [1] {ECO:0000313|EMBL:SEJ53724.1, ECO:0000313|Proteomes:UP000199631}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG02 {ECO:0000313|EMBL:SEJ53724.1,
RC ECO:0000313|Proteomes:UP000199631};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNYL01000012; SEJ53724.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6ZNJ9; -.
DR STRING; 1855291.SAMN05216327_11294; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199631; 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; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF304; 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:SEJ53724.1};
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}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..841
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5011599286"
FT DOMAIN 46..209
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 252..463
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 841 AA; 95664 MW; F90C0ACE94C23513 CRC64;
MTFTRSLIFI LAAICVAFAC TRPQSPGPEK GVSFALNQYR KQHIDSIHYQ IELDIPAGKT
GKIEGKETIT FLLNALDSAL VLDFNADAGH LKEVRVDGEK VEYQFVNEHI VIDAKHLNKG
KNEIGIDFTA GDQSLNRSDD YLYTLFVPDR ASTCFPLFDQ PNLKASYQLS LKTPEGWEAV
SNGKLTAQTV ENGKRVYKFG ETKPVSSYLF AFAVGKFFKE TRMLDGREMT MYYRETDTSK
VNRNRDEVFK LHAQSLAWLE DYTAIDYPFG KFDFVLLPSF QYGGMEHPGA IFYNEPALFL
DENASVNRRM ARASVIAHES AHMWFGDLVT MDWFNDVWLK EVFANFMAAK IVHPSFPEIN
HDLRFLLAHY PNAYEVDRTA GTNPILQQLG NLKNAGTLYG AIIYMKAPIV MRQLERKIGE
KLMRESLREY LKTYSFGNAR WDDLIGIIDK RTTEDIATWS NVWVKTPGMP EYSVEKLKIV
QAKDSVSGRV WEQPLVSLAQ QCPEILVCPN SDGTGYGYFK MDTAAKAWFF EHYDDMDVSD
PVFKGAMLVN IWEGLLRGDG PAPEKLINYT LNALPKEQNP LLVDYLLGNL QSSWWVFLNA
NQRAAHQQRI EQALWQLLNG TKDKGIQTSY FRAFKAVALT DDGWQKMHGL WTGKLEVKGL
VLSEEDKISL AYELALKGKG DGKAILSEQL NATKNPDRKA RMQFVIPALS ASETARDAFF
ETLKKEQNRE KEAWVLDALT YLHHPLRAQS ALKYLHPSLD LLQEIQLTGD IFFPTRWLHN
TFAGHSSPEA AEIAQTFLKD HPDYPYFLKN KILQATDLLD RSVKLSETYA QKEHSPALSQ
Q
//
