ID A0A1M6E2U1_9VIBR Unreviewed; 869 AA.
AC A0A1M6E2U1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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:SHI79568.1};
GN ORFNames=VA7868_04387 {ECO:0000313|EMBL:SHI79568.1};
OS Vibrio aerogenes CECT 7868.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1216006 {ECO:0000313|EMBL:SHI79568.1, ECO:0000313|Proteomes:UP000184608};
RN [1] {ECO:0000313|EMBL:SHI79568.1, ECO:0000313|Proteomes:UP000184608}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 7868 {ECO:0000313|EMBL:SHI79568.1,
RC ECO:0000313|Proteomes:UP000184608};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQXZ01000046; SHI79568.1; -; Genomic_DNA.
DR RefSeq; WP_073605964.1; NZ_FQXZ01000046.1.
DR AlphaFoldDB; A0A1M6E2U1; -.
DR STRING; 1216006.VA7868_04387; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000184608; 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:SHI79568.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SHI79568.1};
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:UP000184608};
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 230..436
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 444..544
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..867
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 869 AA; 99583 MW; 1EB18939CDD2616D CRC64;
MASELQAKYR KDYQSPSHTI TDIDLTFYLH EEKTRVVAIS QVRQLDSTNQ LVLDGENLEL
ASLHINDQAW TAFKVTDTGL ELSALPDGEF ELRVETMINP STNTALEGLY ISGQAYCTQC
EAEGFRRITY YMDRPDVLAR YTTTIVADRE KYPYLLSNGN KIEEGVTEDG ESWVRWQDPH
PKPAYLFALV AGDFDMIQEQ YKTKSGRMVT LEVFVDKGNR DRATHAMLSL INAMQWDEER
FGLEYDLDVY MVVAVDFFNM GAMENKGLNI FNSKFVLAND QTATDYDYQA IESIIGHEYF
HNWTGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRSVK RIQSVRLIRG PQFAEDASPM
SHPIRPEKVI EMNNFYTLTV YEKGSEVIRM IHTLLGETNF QKGMQLYFER HDGTAATCED
FVSAMEDASG IDLKQFRLWY SQSGTPVLTV SGEYSEADKQ FALHVSQHTS STVDQEEKQA
LHIPLKMSLY DSEGNRIELR CNGEKVSDIL NVTESEQTFI FENVFEKPVP SLLEEFSAPV
KLFYDYSDEE LIFLMVHAKN DFARWDAGQM LLGKYIRQNV EKVRDNQETT ISEGVIQAFK
DLLLDKSADP AFIAEMFALP NFNEVSEWFD EVDVDSITTV LKSMKVELAT ALKPELLSVY
HQLKQSDYTI DHESIGQRAL RNMCLSYLAF TDQGNELVQN QYQQALSMTD VIAAMTAANL
AGLSCRESLM QDYSKQWKHD GLVMDKWFVL QGQNPSENAL SMIYDSMEHE AFTMKNPNRI
RSLIGAFLNY NPKRFHDKSG SGYQFAGKIL QQLNTINPQV ASRMVDPLLK FKRYDKDRQA
LMKKELEALL NMDNLAKDLY EKVTKALDI
//
