ID A0A3N1NJM2_9GAMM Unreviewed; 893 AA.
AC A0A3N1NJM2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, 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=EDC38_0607 {ECO:0000313|EMBL:ROQ20014.1};
OS Marinimicrobium koreense.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Marinimicrobium.
OX NCBI_TaxID=306545 {ECO:0000313|EMBL:ROQ20014.1, ECO:0000313|Proteomes:UP000273643};
RN [1] {ECO:0000313|EMBL:ROQ20014.1, ECO:0000313|Proteomes:UP000273643}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16974 {ECO:0000313|EMBL:ROQ20014.1,
RC ECO:0000313|Proteomes:UP000273643};
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 (NOV-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:ROQ20014.1}.
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DR EMBL; RJUK01000001; ROQ20014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N1NJM2; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000273643; 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:ROQ20014.1};
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:UP000273643};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 56..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 452..559
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 564..892
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 893 AA; 100750 MW; 11CF1EAA303A6B5D CRC64;
MSARDAQPKA IQLKDYRPPE YLIDRTELHF DLGADKTRVT STLTLRRNPD VTPTGKGLTL
HGQEIELVSV SIDGRTLSDN DYRLDDETLT LPEAPEQFEL TTVGDIDPKN NTSLEGLYRS
RTMYCTQCEA EGFRKITWYL DRPDVMSEFF TTVVADEKQF PVLLSNGNLI EQGSADNGRH
FATWHDPHKK PAYLFALVAG NLEHIEDTFT TMSGRDVTLK IFVEAKDLDK CGHAMTSLKN
AMRWDEEQYG REYDLDIFMI VAVDDFNMGA MENKGLNIFN TACVLAKPET TTDAGFQRVE
GVVAHEYFHN WSGNRVTCRD WFQLSLKEGF TVYRDATFSA DMGSPTFKRV EDVSMLRTLQ
FAEDAGPMAH PVRPDSYIEI SNFYTLTIYE KGNEVVRMLA NLLGPELFRK GTDLYFERHD
GQAVTTEDFV AALEAVSGRD LTQFKRWYDQ AGTPKLTVTD RWDEDAGEYH LTIAQTCPPT
PGQPEKQPFH IPVAMGLLGS AGSLPLKIKG QAPNPETDDN THTVLELTEA EHTFVFEQLP
EKPVPSLLRG FSAPVKLYYG YSRDDLMRLM SGDSDGFCRW DASQQLAIEV IEDVMVAYQK
GEDLSGITID GRLIEANRLL LQDDSLDKAM VALMLSLPSE AYLGEQQDEI QVEAIHHSRA
AVKRALAEAL KPELTQIYRA YDHGKPYRPT ADDIAERSLK NAALSYLMTL NEPEMIEACE
QQYRQANNMT DAIAAVGELV NSQASGAETV REQVLADFYQ TWKDEPLVVD QWLRVQATSS
RSNTLDVVHE LEQHPAFEPN NPNKIRALVG AFTNANPINF HRADGAGYRF LGDQILRLNS
VNPQIAARLV TPFTRWKRYP KAQQELMHAE LERIKAEPKL SKDVYEVVSK SLV
//