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
//