ID A0A0N1BQG1_9PROT Unreviewed; 859 AA.
AC A0A0N1BQG1;
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:KPF79720.1};
GN ORFNames=IP88_01395 {ECO:0000313|EMBL:KPF79720.1};
OS alpha proteobacterium AAP81b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria.
OX NCBI_TaxID=1523432 {ECO:0000313|EMBL:KPF79720.1, ECO:0000313|Proteomes:UP000037971};
RN [1] {ECO:0000313|EMBL:KPF79720.1, ECO:0000313|Proteomes:UP000037971}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP81b {ECO:0000313|EMBL:KPF79720.1,
RC ECO:0000313|Proteomes:UP000037971};
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:KPF79720.1}.
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DR EMBL; LJHX01000010; KPF79720.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1BQG1; -.
DR STRING; 1523432.IP88_01395; -.
DR PATRIC; fig|1523432.3.peg.54; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000037971; 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:KPF79720.1};
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:UP000037971};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 113..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 235..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 453..544
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 551..858
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 859 AA; 93687 MW; 00C3AC68431C0B10 CRC64;
MSNARSHTPA GQPQLPGAIR LADYAPPDWL VPDVELDFRL GADETEVRAR LHVRRNGDHD
RPLVLDGQLL ATRSVAVDGV PVNVAPDGDR LTLGLPGDEA IVETIVSIAP ARNTRLMGLY
ASQGRLVTQC EAEGFRAITW FPDRPDVLSR YHVRLEGDRR LYPVLLSNGD AGEAIDLGGR
HAVEWRDPWP KPCYLFALVA GNLEARRDRF VTRSGRAVDL AIWTAAADVS KSEHAMAALK
AAMAWDEAVY GREYDLGVFN IVAVADFNAG AMENKGLNIF NSKFILADCE TATDADFDSV
AGVVAHEYFH NWTGNRVTCR DWFQLSLKEG LTVFRDQQFM ADQGSPAVKR IDDVRALRAV
QFPEDAGPLA HPIRPDHYVE IANFYTATVY NKGAEVIRML HSLLGPEGFR RGADLYFDRH
DGEAVTCEDW LRAMEDATGR SLHQFRRWYE QAGTPRVAVR AVEANGRVAV TLTQSQAPTP
GQSIKLPMHL PFRLALIGRH TGRRIGDEHV LEISDAETRI VFDGLDEPVL LSLNRGFSAP
VIVDAPATRG ELAFLAGHDD DPFARWEAMQ RLALDVLAGD DPGDLVEAIG ATLGHDGLDP
AFVAEAVLLP SESFIGDQAA IVDVEGIHAR REAARRAIAS GLEAQWWAAW RRHSGSGTAL
TPAAKASRRL ANVALNYLTA TGSAEAIAAA RAQYDGAATM TDRMGALTAL VAGHSEARDA
ALADFHARFA GNADVIDKWF TVQALSTRGD TLARVRALLG HPDFSLANPN RLRALVGAFG
ANQRHFHDAS GDGYRLLADQ LLAVDRINPQ SAARLAVPLG RWRRFDPRRA ALMKAELERI
VGTPGVSKDV LEMAGRALG
//
