ID A0A1I5TNM5_9SPHN Unreviewed; 860 AA.
AC A0A1I5TNM5;
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=SAMN04488241_108130 {ECO:0000313|EMBL:SFP83926.1};
OS Sphingomonas rubra.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=634430 {ECO:0000313|EMBL:SFP83926.1, ECO:0000313|Proteomes:UP000199586};
RN [1] {ECO:0000313|EMBL:SFP83926.1, ECO:0000313|Proteomes:UP000199586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.9113 {ECO:0000313|EMBL:SFP83926.1,
RC ECO:0000313|Proteomes:UP000199586};
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; FOXP01000008; SFP83926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5TNM5; -.
DR STRING; 634430.SAMN04488241_108130; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199586; 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:SFP83926.1};
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:UP000199586};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 76..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 228..441
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 446..540
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 545..860
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 860 AA; 94150 MW; 85770421810C2F15 CRC64;
MDIQHAVAQP TVIHRADYRP PAWSVPDVAL AFDLDAAATR VRAALSVVRN GAGDLRLDHE
GPPPLSVAVD GVAADWRMED GQLVIALPGD AHLVETEVEI APDRNTQLMG LYASKGILCT
QCEAEGFRRI TPFPDRPDVL SRYRVRMTAD KARYPVLLAN GDPVGAGELD DGRHWAEWHD
PFPKPCYLFA LVAGDLRVNA DTFTTGSGRE VTLGIWVRAA DLPRTAHALD ALKLAMAWDE
RVYGREYDLD VFNIVAVDDF NFGAMENKGL NIFNSRYVLA DPDTATDVDY DGVAAVVAHE
YFHNWSGNRV TCRDWFQLSL KEGFTVYRDQ GFSADQGSAA VKRIEDVRTL RAAQFSEDAG
PLAHPVRPDA YQEISNFYTA TIYNKGAELV RMMATIVGPV AFRAATDLYF DRFDGTAATC
EDFVACMEEA SGCDLARFRR WYGQAGTPRV SASIDHEAGS GRATLRLAQH VPATPGQPDK
QPMVLPLRLR LFGAATGRPL TDERLVILDD ATDTLVFDGV GERPVLSINR GFSAPVIVES
DRDAADLAFL SAHDDDPFAR YEAMQQLMLD TLVAAVVEGR AEHDAVLAAV ATTLDAAGLD
RTFVAEAVLL PSDAFVGDQL ARVDPDAVFA AREALHRDLG VRLAARWRAA YAERPAVPYA
YTPAEKGKRR LRNAALAYLA ASGAPDAASL AFGQFEAADN MTDRLAALQT LISLDADEGE
AALDIFYNRY AGDPLVIDKW FQAQALSPRA DTTDRVTELA RHPDFAPANP NRARSLLGAF
GVNQRAFHRA DGAGYRFLAD QLIGLDKLNP QTAARLLPPF GRWRRFDETR GAMMRAELER
IIAVPGVSKD LFEQASKSLN
//
