ID A0A0N0JHV6_9SPHN Unreviewed; 869 AA.
AC A0A0N0JHV6;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, 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 Name=pepN {ECO:0000313|EMBL:KPF54326.1};
GN ORFNames=IP65_11430 {ECO:0000313|EMBL:KPF54326.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF54326.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF54326.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF54326.1,
RC ECO:0000313|Proteomes:UP000037880};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF54326.1}.
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DR EMBL; LJHO01000004; KPF54326.1; -; Genomic_DNA.
DR RefSeq; WP_054131787.1; NZ_LJHO01000004.1.
DR AlphaFoldDB; A0A0N0JHV6; -.
DR STRING; 1523413.IP65_11430; -.
DR PATRIC; fig|1523413.3.peg.3334; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000037880; 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:KPF54326.1};
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:UP000037880};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 82..191
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 449..541
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 547..867
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 869 AA; 94876 MW; 8015D5CAC01A1CB2 CRC64;
MKDSASQPPV VIQRADYRPP AWLVPDIALD FLLDLAATQV TATLDVERNA AGDGGPLRLN
GDGLVAQSVS VDGEPHSAWT MDGDDLVVEL PGDAHQVTIE TTIDPTANTQ LSGLYASGGL
LCTQCEAEGF RRITFFPDRP DVLSRYTVTL TADKAAFPVL LSNGNPMDSG EEDDGTHWAI
WHDPWPKPSY LFALVAGDLI ATRDRFTTMS GREVDLAIWV RAGDETRTAH AMRALIASMD
WDEKVYGREY DLDLFNIVAV SDFNAGAMEN KGLNIFNTRY ILADPETATD ADYDGVEGVV
AHEYFHNWSG NRVTCRDWFQ LSLKEGFTVL RDQQFSADQG SAPVKRIEDV RVLRSAQFPE
DSGPLAHPIR PDSYQEISNF YTATVYNKGA EVIRMMTVLA GPERFRAGTD LYFERHDGEA
ATCEDFVTAI EDGAGLDLKQ FRRWYEQAGT PQVDVGMTHD AASGTVTLAF KQTVPPTPGQ
PVKQPMVIPL RTALFDRATG RHGGEHLIVL ADAAQTFTFD GFAQAPVLSI NRGFSAPVAI
NAPQSVEDLV FLAGHDDDAF ARYEAMQQLV VQHLVAAVEG RLDDASREAG RAAIGGALGA
ILADTALDDL MRGELVMLPG EAYLAEQINP VDPARVHAER EALKAWLGRE LGDAWRGLHD
RCTAVPYGLD AAARGARKLK TQALVYLAAA DPVEAAQRAK TQYDAADNMT DRQGALMVLC
GLDVPARDEA LAHFHARFAE NRLVIDKWFS LQAGSLHPRA LDHVRALAQH ADFTLTNPNR
VRALYMAFAA NAQAFHAADG AGYALIADLI LALDPINGNV AARFVAPLGR WRRIEPVRAA
LMRAQLERIA AAPRLSRDVR EQVSKSLDG
//
