ID A0A1C3EBR3_9GAMM Unreviewed; 869 AA.
AC A0A1C3EBR3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=A8L45_19610 {ECO:0000313|EMBL:ODA30681.1};
OS Veronia pacifica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Veronia.
OX NCBI_TaxID=1080227 {ECO:0000313|EMBL:ODA30681.1, ECO:0000313|Proteomes:UP000094936};
RN [1] {ECO:0000313|EMBL:ODA30681.1, ECO:0000313|Proteomes:UP000094936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 1920 {ECO:0000313|EMBL:ODA30681.1,
RC ECO:0000313|Proteomes:UP000094936};
RA Gomez-Gil B., Enciso-Ibarra J.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (MAY-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}.
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:ODA30681.1}.
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DR EMBL; LYBM01000049; ODA30681.1; -; Genomic_DNA.
DR RefSeq; WP_068905052.1; NZ_LYBM01000049.1.
DR AlphaFoldDB; A0A1C3EBR3; -.
DR STRING; 1080227.A8L45_19610; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000094936; 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:ODA30681.1};
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:UP000094936};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 22..186
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 225..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..868
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 869 AA; 98430 MW; DF20EDE7FD9A616B CRC64;
MTQQPQAKYR KDYQAPEFTI SHIDLTFDLK DKETRVVARS QVKQNLAGAT ALTLDGEGLK
LIRIEVDGQD WSDYRVEEST LTVNGVPSTF ELLIETEIDP QANTSLEGLY KSDGAYCTQC
EAEGFRRITY YLDRPDVLAK FTTKVIADKE AYPYLLSNGN KIGTGDLENG RHWVQWEDPF
AKPCYLFALV AGDFDCLRDN FVTVSGRDVA LEIFVDKGNL DRADYAMESL KNSMKWDEER
FGLEYDLDIY MIVAVDFFNM GAMENKGLNV FNSKFVLANS KTATDSDYHG IERVIGHEYF
HNWSGNRVTC RDWFQLSLKE GLTVFRDQEF SSDLGSRAVN RISNVRKVRS VQFAEDRSPM
AHPIRPEKVI EMNNFYTMTV YEKGSEVIRM LHTLLGENTF QKGIQLYFER HDGTAATCDE
FIQAMQDASG FDLTQFSLWY SQSGTPELTV VSDYDENAQT LSLTVSQITP PAADQADKQA
LLIPLDIELY AADGSVIELQ RNGEPVHNVL QVTQTEQLFT FDKVTEKPVL SLLREFSAPV
HLHYEYSDTE LVFLMVHARN EFARWDASQM LLAKHIKENV ARIQQGEAFT LPDSIVDAFR
GVLLDDNLDR SLIAEVLSLP TEVEVAGWYE TIDVDAIESV LESIRKTFAI EMADELSAVY
AACKASHYEL SHQAAADRRL KNVCLSYLAE VESGEHIVIE QFNSSDNMTD TFAALLAANI
ALLPSREQMM QSFSDKWHQD GLVMDKWFAL QGSSKMQGAL NNVKAQMNHP SFSIKNPNRL
RSLIGAFVMG NSVNFHAKDG SGYAFLTDIL IQLNEINPQI ASRLVDPLLK LKYFDEHRQG
LIREQLTRLS KIENLANDLF EKVNKALEV
//
