ID A0A0L6CYQ2_9RHOB Unreviewed; 850 AA.
AC A0A0L6CYQ2;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
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:KNX42917.1};
GN ORFNames=ROTO_05640 {ECO:0000313|EMBL:KNX42917.1};
OS Roseovarius tolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=74031 {ECO:0000313|EMBL:KNX42917.1, ECO:0000313|Proteomes:UP000037046};
RN [1] {ECO:0000313|Proteomes:UP000037046}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EL-164 {ECO:0000313|Proteomes:UP000037046};
RA Voget S., Bruns H., Wagner-Doebler I., Schulz S., Daniel R.;
RT "Draft Genome Sequence of Roseovarius tolerans EL-164, a producer of N-
RT Acylated Alanine Methyl Esters (NAMEs).";
RL Submitted (JUL-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}.
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:KNX42917.1}.
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DR EMBL; LGVV01000004; KNX42917.1; -; Genomic_DNA.
DR RefSeq; WP_050661502.1; NZ_LGVV01000004.1.
DR AlphaFoldDB; A0A0L6CYQ2; -.
DR STRING; 74031.SAMN04488077_11083; -.
DR PATRIC; fig|74031.6.peg.579; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000037046; 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:KNX42917.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KNX42917.1};
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:UP000037046};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 79..179
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 218..432
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; 94830 MW; 9871B708206C6D75 CRC64;
MKDASPQTIY LADYTPPAFL VEKVHLTFRL SPEKTRVLSK IEFRPNPASS SRTFFLHGEN
LRLIGAKIDG AAITPQVTAE GLTADVPDAP FTFEAEVEID PAGNTALEGL YMSNGMYCTQ
CEAEGFRKIT YYPDRPDVMS VFTVRIEGDM PVMLSNGNPV AEGDGWAEWH DPWPKPAYLF
ALVAGDLVNH ADRFTTRSGR KVDLNIWVRP GDEGKCAFGM EALKKSMTWD EEVYGREYDL
DLFNIVAVDD FNMGAMENKG LNIFNSSCVL ASPETSTDAN FERIEAIIAH EYFHNWTGNR
ITCRDWFQLC LKEGLTVYRD SEFTADMRSA PVKRIGDVIA LRARQFREDN GPLAHPVRPE
SFVEINNFYT ATVYEKGAEL IGMLKRLVGD DAYGRALDLY FERHDGQACT IEDWLQVFED
ATGRDLAQFK RWYTQAGTPR LRVSEDYEGG TYTLHFEQHT PPTPGQEVKD PRVIPIAVGL
LGPNGDEIKE TQLLEMTEAR QSFTFDGLAA KPVPSILRDF SAPVILDRET SNEERAFLLA
HDTDPFNKWE AGRALARNGL LAMIREGAAP DAAYLDAVHT MARDETLDPA FRALAHGLPS
EDDLAQSLHD AGHTPDPQAI WEALETLRDA RAVTMEATAR ALYDRHQVTA PYRPDPEQTG
ARALANAALA ILTRRDGGAQ AQAQYDAADN MTQQLAGLSC LLQAGKGAAA VQAFYEQWQH
DRLVIDKWFS LQILQAAPQD TADTTARLTE HRDFTIRNPN RFRATLGALA MSPAGFHHAS
GKGYKTLADW LIALDPLNPQ TTARMCSAFE TWRRYDADRR ALIAEQLDRI LASPNLSRDT
TEMVSRIRGG
//
