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Database: UniProt
Entry: I3TJW1_TISMK
LinkDB: I3TJW1_TISMK
Original site: I3TJW1_TISMK 
ID   I3TJW1_TISMK            Unreviewed;       887 AA.
AC   I3TJW1;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE            EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN   Name=pepN {ECO:0000313|EMBL:AFK53049.1};
GN   OrderedLocusNames=TMO_1210 {ECO:0000313|EMBL:AFK53049.1};
OS   Tistrella mobilis (strain KA081020-065).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Geminicoccaceae; Tistrella.
OX   NCBI_TaxID=1110502 {ECO:0000313|EMBL:AFK53049.1, ECO:0000313|Proteomes:UP000005258};
RN   [1] {ECO:0000313|EMBL:AFK53049.1, ECO:0000313|Proteomes:UP000005258}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KA081020-065 {ECO:0000313|EMBL:AFK53049.1,
RC   ECO:0000313|Proteomes:UP000005258};
RX   PubMed=22458477; DOI=10.1021/ja301735a;
RA   Xu Y., Kersten R.D., Nam S.J., Lu L., Al-Suwailem A.M., Zheng H.,
RA   Fenical W., Dorrestein P.C., Moore B.S., Qian P.Y.;
RT   "Bacterial biosynthesis and maturation of the didemnin anti-cancer
RT   agents.";
RL   J. Am. Chem. Soc. 134:8625-8632(2012).
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; CP003236; AFK53049.1; -; Genomic_DNA.
DR   RefSeq; WP_014744728.1; NC_017956.1.
DR   AlphaFoldDB; I3TJW1; -.
DR   STRING; 1110502.TMO_1210; -.
DR   MEROPS; M01.005; -.
DR   KEGG; tmo:TMO_1210; -.
DR   PATRIC; fig|1110502.3.peg.1246; -.
DR   eggNOG; COG0308; Bacteria.
DR   HOGENOM; CLU_007993_2_0_5; -.
DR   OMA; FKRWYSQ; -.
DR   Proteomes; UP000005258; Chromosome.
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:AFK53049.1};
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   Reference proteome {ECO:0000313|Proteomes:UP000005258};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          25..191
FT                   /note="Aminopeptidase N-like N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17900"
FT   DOMAIN          231..443
FT                   /note="Peptidase M1 membrane alanine aminopeptidase"
FT                   /evidence="ECO:0000259|Pfam:PF01433"
FT   DOMAIN          449..557
FT                   /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT                   /evidence="ECO:0000259|Pfam:PF11940"
FT   DOMAIN          561..887
FT                   /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF17432"
SQ   SEQUENCE   887 AA;  98475 MW;  07B777EB29B12322 CRC64;
     MKTDTPKTIL LSEYTPPAYL VPSIDLEFRL DPHATRVTAV SRMERTADTP ADAPLVLNGA
     GLKLVSVAID GAPVGPDRWL QEEERLVIRK VPAAFELTVV TEIDPAGNTA LEGLYLSNGI
     FCTQCEAEGF RKITYFPDRP DVMARYRTTI IGDPAVLPVM LSNGNPVADE IGEDGLRHIT
     WEDPFPKPSY LFALVAGDLA LCESPFTTMS GRDVSLRLYV EPRNADKCEH AMASLKKAMV
     WDEQAYGREY DLDIYMIVAV DDFNMGAMEN KGLNVFNSKY ILARPDTATD SDYGGIEAVV
     AHEYFHNWTG NRITCRDWFQ LSLKEGLTVF REQQFVADHQ SAAVSRIHDV RVLRAAQFPE
     DAGPTAHPVR PDSYIEISNF YTSTVYNKGA EVIRMLHTLI GPEAFARGMD LYFERHDGQA
     VTCEDFVRAH ADANELDLGD FFRWYVQAGT PEVSVETRHD PESRSFELTF TQTLKPTPGQ
     PVKKPMVIPV RTALIGADGA PLALRLANEA ADAPEADQTE RVLVLEDRVT RFTFADVAER
     PVPSLLRGFS APVKLETRAE DADLAFLMGH DDDAFNRWEA AQTYAIRVIH RLIADAAAGR
     PLVLPADFRD AFARTIGDDS LDPALIAEAL TLPGESYLAE TMTRIDVEGI TAARQFVRRE
     IGRSLEGLLL EVFDRLAAED AGKPYSFDPA SVGRRSLANL CLAYLGAPGG TAGLERARRR
     FETADNMTDA LGGLLVLADQ EDALSQPAFD AFYARWKDEP LVVDKWFMVQ ATASRANALD
     HVLKLMEHPA FSMRNPNRVR SLIGAFAASN PRGFHEASGR GYDFLADQII TLDASNPQIA
     ARLVGPFKRW RRYDDQRQAL MRQALERIAA RQGLSRDVYE MVSKSLA
//
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