ID C7D8K8_9RHOB Unreviewed; 909 AA.
AC C7D8K8;
DT 22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 22-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 52.
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:EET47079.1};
GN ORFNames=TR2A62_1218 {ECO:0000313|EMBL:EET47079.1};
OS Thalassobium sp. R2A62.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Thalassobium.
OX NCBI_TaxID=633131 {ECO:0000313|EMBL:EET47079.1, ECO:0000313|Proteomes:UP000004701};
RN [1] {ECO:0000313|EMBL:EET47079.1, ECO:0000313|Proteomes:UP000004701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R2A62 {ECO:0000313|EMBL:EET47079.1,
RC ECO:0000313|Proteomes:UP000004701};
RA Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL Submitted (MAY-2009) 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; GG697169; EET47079.1; -; Genomic_DNA.
DR AlphaFoldDB; C7D8K8; -.
DR STRING; 633131.TR2A62_1218; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_5; -.
DR Proteomes; UP000004701; 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:EET47079.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EET47079.1};
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:UP000004701};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 163..238
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 277..488
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 496..587
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 591..907
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 909 AA; 100580 MW; E2142463AA9C5D2F CRC64;
MKFHAPSIAF LGRSKIFKNA LGPVIASHNC CVYCGIKQSA ELTKAAICQI NQAKKRATNM
TQTPPETIYL ADYTPPNYLI DTVHLTFRLA PDATRVISRI QFRPNPKAEN DQFFLHGEGL
TLISATIDGA AVTPQPVDGG LTCPVPNAPF VWETEVEIDP AANTALEGLY MSNGMYCTQC
EAEGFRKITY YPDRPDVMAV FTVRIEGDAP VLLSNGNPGD TGKGWAEWHD PWPKPAYLFA
LVAGDLVAHP DAFTTSEGRQ VALNIWVRPG DEDKCAFGMD ALKRSMVWDE EVYGRAYDLD
LFNIVAVDDF NMGAMENKGL NIFNSSCVLA SADTSTDADF ERIEAIIAHE YFHNWTGNRI
TCRDWFQLCL KEGLTVFRDQ QFTGDMRGHA VKRIDDAIVL RARQFREDQG PLAHPVRPAS
FVEINNFYTA TVYEKGAELI GMLKRLVGDE AYDRALELYF ARHDGDAATV EDWLAVFEET
TGRDLSQFKG WYELAGTPQV RVSETWENGV YTLHFEQETQ PTPGQSDKVP MVVPIVIGLL
DETGVEVVES HVFEMTESVQ STSFNGLKNK PIPSILRDFS APVSVHRDTT DAERTLLLAH
DTDPFNRWES GRILVGQTLA KMATDGASPS TQMLDALLAV ARDDTLDPAF RALVLSLPSQ
EDTSASIAAS GRVPDSLAIH RAHETLRQAI AQHMQDILPR LYATMQIEGA YAPTAVDGGK
RALGNTVMRL LSQLDGGTTA QAQFAAANNM TQQVTALNCL VEIDKGADAL AAFEAQWSHD
RLVMNKWFGV QVQMAQPQHA AQVAQRLTEH PQFDWKNPNR FRAVMGALAA NSAGFHSEDG
ASYDLLADWL IRLDPINPQT TARMTAAFET WKRFDVDRQA RIKSALNRIQ SSANLSRDTG
EMVGRILSA
//
