ID A0A0N8HIY7_9GAMM Unreviewed; 883 AA.
AC A0A0N8HIY7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:KPM79592.1};
GN ORFNames=AOG28_09685 {ECO:0000313|EMBL:KPM79592.1};
OS Cobetia sp. UCD-24C.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Cobetia.
OX NCBI_TaxID=1716176 {ECO:0000313|EMBL:KPM79592.1, ECO:0000313|Proteomes:UP000050261};
RN [1] {ECO:0000313|EMBL:KPM79592.1, ECO:0000313|Proteomes:UP000050261}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCD-24C {ECO:0000313|EMBL:KPM79592.1,
RC ECO:0000313|Proteomes:UP000050261};
RA Krusor M., Coil D.A., Lang J.M., Eisen J.A., Alexiev A.;
RT "Draft Genome of Cobetia sp. UCD-24C.";
RL Submitted (SEP-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:KPM79592.1}.
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DR EMBL; LJTD01000005; KPM79592.1; -; Genomic_DNA.
DR RefSeq; WP_054556284.1; NZ_LJTD01000005.1.
DR AlphaFoldDB; A0A0N8HIY7; -.
DR STRING; 1716176.AOG28_09685; -.
DR PATRIC; fig|1716176.3.peg.2696; -.
DR Proteomes; UP000050261; 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:KPM79592.1};
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:UP000050261};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 57..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..446
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 451..555
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 560..883
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 883 AA; 98083 MW; CC3E5229CD34BEDB CRC64;
MSQPAAIHLA DYQAPAWRVL DTRLTFDLAP SATRVTTVLT LEANPDAAVG SDATPPLVLN
GEHLMLESVR VDGRALASDE YKLDETHLTL AGLPANCELE TVVVIDPAAN TALEGLYVSS
GMFCTQCEAE GFRRITYYPD RPDVMSVFTT TIIADKDSYP ILLSNGNPIE RGEREGGRHF
VTWQDPHPKP CYLFALVAGD LVKHDDSFTT MSGRDVALEI WVEPENLDKT QHAMNSLKAS
MKWDEEVYGR EYDLDIFMIV AVNDFNMGAM ENKGLNIFNS ACVLANPDTT TDAAFQRVEG
VVAHEYFHNW SGNRVTCRDW FQLSLKEGFT VYRDQTFSAD MNSAPVKRIE DVAMLRTAQF
AEDAGPTAHP VRPASYIEIS NFYTLTIYEK GSEVVRMVAN LLGEEAFRRG SDLYFARNDG
SAATIEDFIS AMSEASGRDF SQFMRWYSQA GTPNIAASGT FDAQAGTYSL TLRQSTPPSP
GQAEKLPLVI PVRMGLVGAD GSDLTLTLDG EALGTETVLE LTEAEQTFVF TGLAGDAEPV
PSLLRGFSAP VKLAFDYSRE QLAFLMQHDS DGFNRWDAGQ RLAMAALEDL MAAWQRGEQE
AQLDERLLAA YRFLLQSEAS DRAVLAEMLT LPSEAYIAEQ QSVVDVDAIH WARKTAKAQL
ASALRDDFVA LYHANAQQGD YAPTFEQMAR RSLKNAALSY LMSIEDEEGV RLAQTQLAAA
HNMTDVRAAL TMLVHSSRTD LGDPALKSFA ERWSHDPLVM DQWFSIQVTR PQADVLDRVR
FLMEHPAFSL TNPNKVRALI GAFAGQNRVN FHRLDGEGYR LLADVVIELN RLNPEIAARI
ITPLTRYNRF DAKRQDLMKA ELERIRGEKL SNNLYEVVEK ALA
//
