ID A0A0P0M9S5_9BURK Unreviewed; 903 AA.
AC A0A0P0M9S5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
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:ALK89071.1};
GN ORFNames=L63ED372_01867 {ECO:0000313|EMBL:ALK89071.1};
OS Limnohabitans sp. 63ED37-2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK89071.1, ECO:0000313|Proteomes:UP000059510};
RN [1] {ECO:0000313|EMBL:ALK89071.1, ECO:0000313|Proteomes:UP000059510}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK89071.1,
RC ECO:0000313|Proteomes:UP000059510};
RA Ahn J.-H., Kim S.B.;
RT "Limnohabitans sp. 2 strains.";
RL Submitted (JUN-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}.
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DR EMBL; CP011774; ALK89071.1; -; Genomic_DNA.
DR RefSeq; WP_062405543.1; NZ_CP011774.1.
DR AlphaFoldDB; A0A0P0M9S5; -.
DR STRING; 1678128.L63ED372_01867; -.
DR KEGG; lih:L63ED372_01867; -.
DR PATRIC; fig|1678128.3.peg.1855; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000059510; Chromosome.
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:ALK89071.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ALK89071.1};
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:UP000059510};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 91..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..456
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 464..566
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 572..900
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 903 AA; 100023 MW; B1F592A7E66E747F CRC64;
MREGQPTAIH REAYAAPAFW IDTVDLTFDL DPAKTRVLNK MRLRRNPDVA AQPLRLDGED
LNLARVLVNG GGTSFKMDGA QLVLENLPDG HEPFDLEIFT TCNPEKNTQL MGLYVSNDSF
FTQCEAEGFR RITYFLDRPD VMASYTVTLR ADKAKYPVLL SNGNLVEQGA LEDGRHFAKW
VDPHKKPCYL FALVAGQLVA REQRILSRSG TEHLLQVFVR PGDLDKTEHA MNSLMASVAW
DEARFGLPLD LERFMIVATS DFNMGAMENK GLNIFNTKFV LANPNTATDL DFGNIESVVG
HEYFHNWTGN RITCRDWFQL SLKEGLTVFR DQEFSQDMAG VASARAVKRI EDVRVLRTVQ
FAEDAGPMAH PVRPDSYVEI NNFYTVTIYE KGSEVVRMMQ TLVASPADLQ GRDGFAKGMK
LYFERHDGQA VTCDDFAQAI ADANPGSALT QNLTAFKHWY SQAGTPRLQA SGVYSANERS
YTLTLRQSCP ATPDQADKKP FVIPVTLGLL SRDGTALPLQ LADAHHSALQ QTLVLTEESA
SFSFVNIDSE PVPSLLRGFS APVVLEDGLS AADLLILLAH DSDPFNQWEA GQRLMLQSAT
DAIQQNKDLT GQPVLSDALI GALRNVLRHP ELDAAFKDLA LTLPSENYIA DQLDVVDPQR
VHALRESMRL TLATALQADW QWAWDAHKHN GAYTPDTKSS GRRALAGLSM TMLCVAAVHN
GDAVTPGRVY QQFKDAGNMT DRFNALSALV VSGHALAQDA LALFHKMFQH EALVIDKWFA
LQAGAPDRAG DVLPRVRQLM QHPDFSLRNP NRARSLIFSY CSANPAGFHR ADAAGYVYWS
EQVLALDSIN PQVAARLARA MDRWSRLAEP YRSAARVAIE RVAAKADLSN DVREVVSRAL
SAA
//
