ID A0A0B4EB38_9RHOB Unreviewed; 850 AA.
AC A0A0B4EB38;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=GC1_13340 {ECO:0000313|EMBL:KID08173.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID08173.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID08173.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID08173.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
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:KID08173.1}.
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DR EMBL; AFCF02000008; KID08173.1; -; Genomic_DNA.
DR RefSeq; WP_019296838.1; NZ_AFCF02000008.1.
DR AlphaFoldDB; A0A0B4EB38; -.
DR STRING; 1002340.GC1_13340; -.
DR MEROPS; M01.005; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000031201; 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:KID08173.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 40..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..848
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 850 AA; 94650 MW; 9256D420D224A171 CRC64;
MAKDTPQTFY LKDYTPFGFD VESVHLTFRL APETTRVLSK IRFAPKPDAA NKTFFLHGED
LQLISAKIDG QAVTPELVEG GLKCDVPSAP FTWEAEVEIN PAGNTALEGL YMSNRMYCTQ
CEAEGFRKIT YYPDRPDVMS TFTVRIEGDE PVMLSNGNPM GQGEGWAEWH DPWPKPAYLF
ALVAGDLVNH PGSFTTKSGK EVELNIWVRP GDEGKCAFGM EALKKSMKWD EDVYGLEYDL
ELFNIVAVDD FNMGAMENKG LNIFNSSCVL ASPETSTDAN FERIEAIIAH EYFHNWTGNR
ITCRDWFQLC LKEGLTVFRD AQFTADMRSE PVKRIDDVIT LRARQFPEDN GPLAHPPRPE
AFQEINNFYT ATVYEKGAEV IGMLKRLVGD DNYYKALKLY FERHDGQACT IEDWLKVFED
ATGRDLSQFK LWYSQAGTPR VKVTEDYADG TYTLTFEQST PPTPGQPDKA PRVIPVAVGL
LSPNGDEIRA TEVLEVTEAK QSFTFGGLAS KPVPSILREF SAPVILERET TNAERAFLLA
HDTDPFNRWE AGNALAKETR VAMVLDGAAP DAAYLDALEK LVRDDDQDPA FRALVLSPPS
QADIAQTLHE RGYTPDPQKI YDAAETFAQT LAQQLETSLP RLYAATTVEG PYSPDAESSG
KRALNGRILS LLTRLDGGEQ AARQYASADN MTQQSAALAA LMKAENGETQ SQAFFDQWQD
DRLVMDKWFA LQIACAAPEK TAATAAALTK HPLFDMKNPN RFRAVMGALA GNHAGFHHSS
GEGYQLLADN LIALDRLNPQ TTARMCAAFQ TWKRYDAGRQ SMIRAQLTRI ADTEGLSRDT
NEMVTRILDA
//
