ID A0A1E4NDB1_9PROT Unreviewed; 894 AA.
AC A0A1E4NDB1;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=ABT21_09000 {ECO:0000313|EMBL:ODU89807.1};
OS Thiobacillus sp. SCN 65-179.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC Thiobacillaceae; Thiobacillus.
OX NCBI_TaxID=1660144 {ECO:0000313|EMBL:ODU89807.1, ECO:0000313|Proteomes:UP000094681};
RN [1] {ECO:0000313|EMBL:ODU89807.1, ECO:0000313|Proteomes:UP000094681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=26031303; DOI=10.1111/1462-2920.12936;
RA Kantor R.S., van Zyl A.W., van Hille R.P., Thomas B.C., Harrison S.T.,
RA Banfield J.F.;
RT "Bioreactor microbial ecosystems for thiocyanate and cyanide degradation
RT unravelled with genome-resolved metagenomics.";
RL Environ. Microbiol. 17:4929-4941(2015).
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:ODU89807.1}.
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DR EMBL; MEGN01000003; ODU89807.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1E4NDB1; -.
DR STRING; 1660144.ABT21_09000; -.
DR Proteomes; UP000094681; 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:ODU89807.1};
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 108..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 450..563
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 567..893
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 894 AA; 97481 MW; 04E2C7BF89364EA8 CRC64;
MRTETPVTLY LKDYTPPAWL IDAVDLHVSI LAGHATVRAR LTCRRNPAAA AGPLVLLGED
LVLESLALDG APLAPEAYVC TDDRLTLAGP LPESFVLDTQ VRIQPDQNTQ LSGLYKSKDG
YFTQCEAEGF RRITYYPDRP DVMAIFACTV EADRAQFPVL LSNGNPVTAG SCDDPARHWV
RWEDPFPKPA YLFALVAAKL DVLADTFVTA SGRSVQLEIL VEPGKLDQCD HAMAALKKSM
RWDETRFGLE YDLDRYMIVA VGDFNMGAME NKGLNIFNTK YVLARPDTAT DTDYQNIDRV
VAHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQEFGADV HSRAVTRIQE VRTLRAAQFP
EDAGPMAHPI RPVSYAEINN FYTATVYEKG AEVIRMIHTL LGEAGFQRGM QQYFERHDGQ
AVTCEDFVAA MQDASGVDLT QFRRWYARAG TPVLHAHGAY DAAAQTYTLT LTQTLVPTAY
EKRLADAGQA VDDGPLHIPV ALGLVLPNGR DTELCLAGET APAGTTRVLS LTSATQTFVF
ERVPQAPVVS LLRNFSAPVR LDFAQSDAEL THLMAHDADA FNRWEAGQRL ATRVLLAGIA
TGGQGSDWIP QTFIDACARV LDDGLTGDAA LAAEALMLPS ETVLADTVAA AGNVIDPDAI
FAARLTLRRT LSTALRTQFE AAWQALAPTG DYAPDGAQAG RRALRNACLA ILADAAPAAL
APQLAAQCAA HSNMTDVAAA LATLAQLDVP ERAPALAAFY DRWKDEALVV DKWLSIQATA
RVTTADTVRD LMRHPAFDLK NPNRVYALIR GFCGANPRHF HTADGSGYAL AADVISELQA
INPQVASRIA RSFDRWRQFD AGRQAHARAA LDRIAAIEGL AKDVAEVVGN ALKA
//
