ID A0A1Y5T0K9_9RHOB Unreviewed; 850 AA.
AC A0A1Y5T0K9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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:SLN52461.1};
GN ORFNames=PEL8287_02763 {ECO:0000313|EMBL:SLN52461.1};
OS Roseovarius litorisediminis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=1312363 {ECO:0000313|EMBL:SLN52461.1, ECO:0000313|Proteomes:UP000193827};
RN [1] {ECO:0000313|EMBL:SLN52461.1, ECO:0000313|Proteomes:UP000193827}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8287 {ECO:0000313|EMBL:SLN52461.1,
RC ECO:0000313|Proteomes:UP000193827};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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; FWFL01000007; SLN52461.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5T0K9; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000193827; 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:SLN52461.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:SLN52461.1};
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:UP000193827};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 97..179
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 218..429
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 437..528
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 533..847
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 850 AA; 95026 MW; 084CBC74534EA57D CRC64;
MRDAAPQTIY LKDYTPFGYL VDNVHLTFAL SPGATRVTSR IAFRPNPKVT DRVFFLHGED
LKLHWAKIDG ADVSPQLTDR GLTCTVPDAP FIFEAEVEID PAANTALEGL YMSNGMYCTQ
CEAEGFRKIT YYPDRPDVMS VFTVRIEGDE NVMLSNGNPV ADGDGFAEWQ DPWPKPAYLF
ALVAGDLVNH PDRFTTRSGR EVELNIWVRP GDEGKCAFGM EALKKSMKWD EDVYGREYDL
DIFNIVAVDD FNMGAMENKG LNIFNSSAVL ASAETSTDAN FERIEAIIAH EYFHNWTGNR
ITCRDWFQLC LKEGLTVYRD SQFTSDMRSA PVKRISDVIA LRARQFREDN GPLAHPVRPD
SFVEINNFYT ATVYEKGAEL IGMLKTLVGD EAYYKALDLY FERHDGDAAT IEDWLNVFQD
ATGRDLTQFK CWYEEAGTPR LTVSDDFKDG TYTLNFEQKT PPTPGQDVKN PRVIPITVGL
LGPNGDEVRE STVLEMTEGK QSFSFDGLST RPIPSILRGF SAPVILERKT ANTERAFLLA
HDTDPFNKWE AGNALARDGL IAMVRDGAAP DGAYLDAVQT MARDDDLDPA FRALALGLPS
QDDLAQALFD LGHTPDPQAI WDALETLRQA RAQAMQDLAP RLYAQFQVNE AYSPDARQAG
ARALANAALG LITRLDGGSQ AQKQYDTADN MTQQLAAWSC LLQAKTGDAA TQAFYRQWQH
DRLVIDKWFM LQILHAEPEE AANTVKKLTK HTDFTMKNPN RFRATLGALS GSAAGFHHAR
GEGYKVLADW LIKLDPLNPQ TTARMCSAFE TWKRYDSGRQ ALIKAQLDRI LATPNLSRDT
TEMVSRIRGA
//
