ID G3IUY8_METTV Unreviewed; 887 AA.
AC G3IUY8;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=Mettu_1608 {ECO:0000313|EMBL:EGW22784.1};
OS Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylobacter.
OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW22784.1, ECO:0000313|Proteomes:UP000004664};
RN [1] {ECO:0000313|EMBL:EGW22784.1, ECO:0000313|Proteomes:UP000004664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1195 / DSM 17260 / SV96
RC {ECO:0000313|Proteomes:UP000004664};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA Woyke T.;
RT "Genomic sequence of Methylobacter tundripaludum SV96.";
RL Submitted (JUN-2011) 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; JH109152; EGW22784.1; -; Genomic_DNA.
DR RefSeq; WP_006890752.1; NZ_JH109152.1.
DR AlphaFoldDB; G3IUY8; -.
DR STRING; 697282.Mettu_1608; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000004664; 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:EGW22784.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EGW22784.1};
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:UP000004664};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 453..555
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 561..882
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 887 AA; 100491 MW; 8DC6CE23FBC4DF73 CRC64;
MRDPNPQTIY LKDYTVPEYL IHSVALNFTL DDENTLVSSR LTLSRNPASQ SRDTSLTLSG
ENLKLMRINL DDGNDLSKDQ YLQTQDSLII NAVPQQQRFV LSIENAINPK ANTALEGLYL
SNGMLCTQCE AEGFRKITYF LDRPDVMTLF TTTLVGDKDR YPVLLSNGNK IAQGELSDNR
HWVTWEDPFN KPCYLFALVA GQLECIADRF TTQSGRDIDL QIFVEKHDID KCDHAMESLK
NAMHWDEQVY GREYDLDLYM IVAVSHFNMG AMENKGLNVF NTKFVLARPD TATDFDYEHI
EAVIGHEYFH NWTGNRITCR DWFQLSLKEG FTVFRDQEFT GDRTSKAVKR IEDVNMLRTR
QFAEDAGPLA HPIRPDAYIE INNFYTLTVY EKGAEVVRMI RTLVGAEGFR KGSDLYFERH
DGQAVTCDDF VSAMEAANDI DLTQFRRWYA QAGTPLLTAR QHYDPSAQTL TLTISQSCPP
TPGQAVKEPL HIPVTVGLLN KDGSVAPCKL QDGDQACDEV ILQLTQSEQA FIFEGLAEQP
VVSILRGFSA PVKLVMERSL EESAFLLSYD SDTFNRWEAG QQLAGQIIMG LIADLQNGRG
MHVNPIMINA FKQVLEQPWD DLSYFSLLLN LPSETYLAEQ MQVVDVEAIH AAREFVTLAL
AEQLQTQLQA LYLNNHRDES GKFDAGAIGR RRIKNTCLSY LSKLENKDIH HLSQQQFNTA
KNMTDQMAAL TVIVNNPHPA KQQCLDSFYR QWQAEALVID KWFTLQASNS MPDTFATVQA
LMQHPAFDLK NPNRVRSLIG AFSQSNPLHF HASNGQGYQF LTDQIIALNT LNPQIASRMV
GALTAWRRYD EGRQALMKAQ LERIITTEAI SKDVYEVASK SLIYKAD
//
