ID A0A0U3LI06_9BURK Unreviewed; 953 AA.
AC A0A0U3LI06;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=DES44_4528 {ECO:0000313|EMBL:REG11926.1}, RD2015_1613
GN {ECO:0000313|EMBL:ALV06098.1};
OS Roseateles depolymerans.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=76731 {ECO:0000313|EMBL:ALV06098.1, ECO:0000313|Proteomes:UP000060699};
RN [1] {ECO:0000313|EMBL:ALV06098.1, ECO:0000313|Proteomes:UP000060699}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 42856 {ECO:0000313|EMBL:ALV06098.1,
RC ECO:0000313|Proteomes:UP000060699};
RA Kim K.M.;
RT "Complete genome of Roseateles depolymerans KCTC 42856.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:REG11926.1, ECO:0000313|Proteomes:UP000256283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11813 {ECO:0000313|EMBL:REG11926.1,
RC ECO:0000313|Proteomes:UP000256283};
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 (AUG-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}.
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DR EMBL; CP013729; ALV06098.1; -; Genomic_DNA.
DR EMBL; QUMT01000006; REG11926.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0U3LI06; -.
DR STRING; 76731.RD2015_1613; -.
DR KEGG; rdp:RD2015_1613; -.
DR PATRIC; fig|76731.3.peg.1653; -.
DR Proteomes; UP000060699; Chromosome.
DR Proteomes; UP000256283; 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:ALV06098.1};
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:UP000060699};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..188
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 228..440
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 455..558
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 563..888
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
FT REGION 925..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 104620 MW; 5B7922D8C23CA9A8 CRC64;
MREGTVTLIR REDYVAPIFW IRTVDLTFDL DPAKTLVTSK MQLERNAAVP HGPLRLHGEE
LNLLRVLING ESVSFRQEGH ELIIDNVPDA DFVLEIRNTC CPDKNTALSG LYTSGGGFFT
QCEAEGFRRI TYFLDRPDVM AVYTVTLRAD KSRFPVLLSN GNLLDTADLD NGRHMAKWHD
PFPKPSYLFA LVAGDLVARE QRIRTRAGKD HLLQVYVRRG DLEKTEHAMN SLIASVVWDE
ARFNLPLDLE RFMVVGVSDF NMGAMENKGL NIFNTSALLA SPATATDADF QRIESIVAHE
YFHNWTGNRV TCRDWFQLSL KEGLTVFRDQ EFSMDMAATP SARAVCRIQD VRALRSMQFP
EDAGAMAHPV RPDVYAEINN FYTPTVYEKG SEVVRMYQTL VGREGFGKGM ALYFERHDGQ
AVTCDDFAQA IADANPGSEL SKRLDTFKRW YSQAGTPRLQ ARGQYDAAAR TYTLSLQQVN
PPSPGQPDKL PQVIPVALGL LSRDGAALPL QLDGEAQAAG TDRVLVLDSA EQSFVFVNVD
SAPVPSLLRG FSAPVVLDDG LGDEELLVLL KHDSDAFNRW EASQRLALSR LLTSVRNGQP
LRLDDAYLDA MRAVLRHPDL DPAFKALALQ LPDEAYIAEQ LTVVDPQAIH AAVTQAQEQL
AAALQADWAW AFETHQVSGG YQPDPVQSGK RALTNLALSM LVLHATRSGD GVWPGRAYQR
FKDATNMTDR MGALSALVQA HAALAEPALE RFHAQFKGEA LVIDKWFALQ GRATELDGKT
FARVKQLAKH SDFTLKNPNR ARSLIFSLCM FNPAAFHRTD AAGYVFWAEQ VLALDAINPQ
VAGRLARVMD RWTTLATPYR SAAREAIARV AAKAELSNDV REIIDRQLAM DTPAAAPAAA
PAAAVAVTAV AAAPAVAAPV EPAAVEAPTQ PAPDLPPAAV IDVTASDPSA VQG
//
