ID E6WCB1_PANSA Unreviewed; 871 AA.
AC E6WCB1;
DT 08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT 08-MAR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN OrderedLocusNames=Pat9b_1350 {ECO:0000313|EMBL:ADU68671.1};
OS Pantoea sp. (strain At-9b).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=592316 {ECO:0000313|EMBL:ADU68671.1, ECO:0000313|Proteomes:UP000001624};
RN [1] {ECO:0000313|EMBL:ADU68671.1, ECO:0000313|Proteomes:UP000001624}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=At-9b {ECO:0000313|EMBL:ADU68671.1,
RC ECO:0000313|Proteomes:UP000001624};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Davenport K., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Ovchinnikova G., Pinto A., Currie C., Woyke T.;
RT "Complete sequence chromosome of Pantoea sp. At-9b.";
RL Submitted (DEC-2010) 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; CP002433; ADU68671.1; -; Genomic_DNA.
DR RefSeq; WP_013508532.1; NC_014837.1.
DR AlphaFoldDB; E6WCB1; -.
DR STRING; 592316.Pat9b_1350; -.
DR MEROPS; M01.005; -.
DR KEGG; pao:Pat9b_1350; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000001624; 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:ADU68671.1};
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 23..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 225..439
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 444..545
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..870
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 871 AA; 98957 MW; 690F4CF2FB433C51 CRC64;
MTQQPQIKYR HDYRAPDFTI TDIDLTFDLN EVTTRVTAVS QVKRLGNSQA ELRLDGEDLT
LVSLAVDGHP WSHYREEEGA LVLSQLPDAF TLTIINDIHP DQNTALEGLY KSGEALCTQC
EAEGFRHITW YLDRPDVLAR FTTTIIADAA RYPFLLSNGN KLESGRHEDG RHWVKWQDPF
PKPCYLFALV AGDFDVLRDS FTTRSGRDVA LEIFVDRGNL DRADWAMTSL KNSMKWDEER
FGLEYDLDIF MIVAVDFFNM GAMENKGLNV FNSKYVLAKA ETATDKDYLG IEAVIGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RIDNVRVMRG AQFAEDASPM
AHPIRPDQVI EMNNFYTLTV YEKGSEVIRM MHTLLGEENF QKGMQLYFER HDGSAATCDD
FVQAMEDASN VDLSQFRRWY SQSGTPVLTV RDDYNPELEQ YTLHVTQHTP ATAEQKEKLP
LHIPLDIELY DGEGKVIPLQ HNGHPVHHVL NVTEEFQSFV FDKVYFQPVP SLLREFSAPV
KLDYKWSDAQ LTFLMRHARN DFSRWDAAQS LLATYIRLNV ARHQQGQPLS LPLHVADAFR
AVLLDEQGDP ALMALILSLP SENEIAELFE VIDPQAIADV REALVRTLAK ELSDEFLAVY
RANQSHEYRV EHAEIGKRAL KNVCLSYLAF GDAEQADKLV QAQYQHATNM TDALAALAAA
VAAQLPCRDA LLAAYDERWH QDGLVMDKWF VLQATSPASN VLSKVRELLH HRSFTMGNPN
RIRSLIGAFA SANPSAFHAK DGSGYQFLVE MLTDLNTRNP QVAARMIEPL IRLKRYDAGR
QALMRQALET LKGLDKLSGD LYEKITKALN A
//
