ID A0A1H3F1V9_9GAMM Unreviewed; 882 AA.
AC A0A1H3F1V9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN05443545_107320 {ECO:0000313|EMBL:SDX84827.1};
OS Aidingimonas halophila.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Aidingimonas.
OX NCBI_TaxID=574349 {ECO:0000313|EMBL:SDX84827.1, ECO:0000313|Proteomes:UP000198500};
RN [1] {ECO:0000313|EMBL:SDX84827.1, ECO:0000313|Proteomes:UP000198500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19219 {ECO:0000313|EMBL:SDX84827.1,
RC ECO:0000313|Proteomes:UP000198500};
RA de Groot N.N.;
RL Submitted (OCT-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; FNNI01000007; SDX84827.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3F1V9; -.
DR STRING; 574349.SAMN05443545_107320; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000198500; 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:SDX84827.1};
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:UP000198500};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 107..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 450..553
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 558..880
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 882 AA; 99734 MW; AFB7C79551881501 CRC64;
MSASAPQPIY LNDYRPPAYR VTHTELKFDL VSSATRVIAR LHLERHPERQ EGELPLVLDG
EQLRLLHIAI DGQALEDDEY DVNESHLTVY RVPSTFVLDT EVEVDPEANT ALEGLYLSNG
MFCTQCEAEG FRRITFYPDR PDVMATFSTT VIGDKGSLPV LLSNGNPVEQ GDLPNGKHFV
TWDDPHPKPC YLFALVAGDL QKVEDHFTTM SGRDVTLQLW VEEENLSKTD HAMASLKRAM
KWDEETYGRE YDLDRFMIVA VNDFNMGAME NKGLNIFNSA AVLTHPQTAT DATFQRVEGI
VAHEYFHNWS GNRVTCRDWF QLSLKEGFTV FRDQCFSADT NSAPVKRIED VSFFRTAQFA
EDAGPTAHPV QPDHYIEIGN FYTLTIYEKG AEIVRMLRNL LGWEAFRQGS DLYFQRYDGQ
AVTIEDFVEC MAEVSGLDLG QFMRWYFQAG TPEIDAIGEY DYAKGEYRLT LRQRTPPTPD
QHEKLPLHIP VRMGLVGTKS GKDLSMTLEG ESLGTDAVIH LRDEEQEFVF TDIAEAPVPS
LLRGFSAPVK LRFPYGREDL AFLLQHDSDG FNRWDSGQRL ALLALDDLIA AHRNGVEKVM
DSRVTEAFRG LLTTDTDDKA VLAEMLTLPS EAYIAEQQPV VDVDAIHAAR TFVKQALALA
LRDEFMAVYR ANQSDAPYVP EPRQIAQRSL KNVALSYLMA IEDEEAVELA RNQFEDGHNM
TDVRTALTLL THSSRGDIAD PALKAFGEKW AHDPLVMDQW FSIQVTRPQS DALERVKFLM
DHPAFSLTNP NKVRALIGAF AGQNRVNFHR ADGEGYRLLA DVVIELNKLN PEIAARIITP
LTRWQRFDES RQALMKAELE RIRAEELSSN VYEVIEKALA TA
//
