ID A0A316HUX2_9GAMM Unreviewed; 883 AA.
AC A0A316HUX2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=C7456_11715 {ECO:0000313|EMBL:PWK82108.1};
OS Fulvimonas soli.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Fulvimonas.
OX NCBI_TaxID=155197 {ECO:0000313|EMBL:PWK82108.1, ECO:0000313|Proteomes:UP000245812};
RN [1] {ECO:0000313|EMBL:PWK82108.1, ECO:0000313|Proteomes:UP000245812}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14263 {ECO:0000313|EMBL:PWK82108.1,
RC ECO:0000313|Proteomes:UP000245812};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWK82108.1}.
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DR EMBL; QGHC01000017; PWK82108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316HUX2; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000245812; 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:PWK82108.1};
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:UP000245812};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 112..196
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 454..558
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 563..880
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 883 AA; 97031 MW; 803C2C11129F0948 CRC64;
MPARNDAAPL PIRLRDYAPP PWRVVQAELD FELGIDASEV GARLHLARDP AQDAPLRLDG
EELELLAIAL DGAPLPAGRW RYADGVLEVD GARDGSVLET RVRVRPAENT ALEGLYLSGS
REAGFLLTQC EAEGFRRITF FPDRPDVLAR FTVTLRADRA RFPVLLAGGN PDGAGELPGG
RHWARFVDPH PKPSYLFALV AGRLEKIERD YRTADGRAVK LAIWSEADAI GRCRYALGAL
ERAMRWDEET YGRNYDLDVF HVVATHDFNM GAMENKGLNI FNAKYLLADP DTTTDDEYRA
VEAVVAHEYF HNWSGNRVTC RDWFQLSLKE GLTVFREQQF SARMNSPALK RIEDVALLRR
AQFPEDAGPL AHPVRPAEYR EINNFYTATV YEKGAELVRM LAGRLGEAGF RRGMDLYFAR
HDGRAATLED FLAALGEANG LDLSPYLAWY AQAGTPRLTA RGRHDAAART YTLTLAQHTP
PTPGQPDKRP LPIPVKLALF DRAGRMLPLR LDGQTSAAST ERVVVLAQAE QDFVFRGVDA
PPVPSLLRGF SAPVILECDY APEELALLLA HDPDGFNRWE AGQQLALRAY AALRDGGGEA
AVEGWCAALA ALFDDAALDP ALLADLLTPP GEIELAERER EVDPARIHAL RQELQRRLAA
ALGGERLERH HRKLAADAGA QPDAAAQARR RLKRRVLELL ALHDPAAALP LAQRQYESAA
GMTDRLAALA VLVRHEAPQA LNALAAFRAR HAQDPLALDK WFAVQAQIPG EPALARVRAL
EADPAFTLKN PNRVRALLGS YASGNPSGFH RADGAGYRLL AERLAQLDAL NPQVAARLAT
AFNGWQRLEP VRREQARQAL AALAGHGALS RNLAEIVGHL LPA
//
