ID A0A2S7UXF5_9GAMM Unreviewed; 861 AA.
AC A0A2S7UXF5;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=BTO11_14100 {ECO:0000313|EMBL:PQJ54667.1};
OS Psychrosphaera saromensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Psychrosphaera.
OX NCBI_TaxID=716813 {ECO:0000313|EMBL:PQJ54667.1, ECO:0000313|Proteomes:UP000239007};
RN [1] {ECO:0000313|EMBL:PQJ54667.1, ECO:0000313|Proteomes:UP000239007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA4-48 {ECO:0000313|EMBL:PQJ54667.1,
RC ECO:0000313|Proteomes:UP000239007};
RA Yoshizawa S., Kogure K.;
RT "Diversity of luminous bacteria.";
RL Submitted (DEC-2016) 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:PQJ54667.1}.
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DR EMBL; MSCH01000003; PQJ54667.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7UXF5; -.
DR Proteomes; UP000239007; 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:PQJ54667.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000239007};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 46..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 232..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 450..540
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 545..860
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 861 AA; 98187 MW; 009D86143A1ECEEA CRC64;
MIVMTTEAKY LKDYQTPDFF IPETELFFNL DDEHTLVRSK LQMKRNGEHT RGLVLDCQVK
QVLRVLINGN QTDFNVEQEQ LKIDVDLAEF ELEIEVTVDP INNTALEGLY KSAGVFCTQC
EAESFRRITP YLDRPDVLSV FTVTIFADAE LYPHMLSNGN LIDSGLVTED DDSNKQLRWV
KWRDPHPKPS YLFALVAGDF DLLTDTFVTQ SGRTVDLELF VDKGNLHLGH HAMASLVKSM
AWDEQRYGLE YDLDKYMVVA VDFFNMGAME NKGLNVFNSK YVLADLNTAT DIDYHGIEAV
IGHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQQFSADM GSEVIERISH ANVMRTMQFA
EDSGPMAHPI RPEKVIEMNN FYTVTVYDKG AEVIRMMHSL LGESGFRAGM DLYFKRHDGN
AVTCDDFVSA MADANNKDLT QFQNWYSQAG TPSVVVSEKQ TDTALELTLS QSLPTRPAAE
QNKPLVIPVK YELLANSDGR SLERGTVIFD KTEQMFTFNC SEPVTLVLFE NFSAPVKVQR
TLTQEQLIHI VKYASDAFCR WDSMQSLWLQ QINGASDTIL DKSRQGLIEV IEYVLNNDDI
ETSIKAELLT IPSYTSIAET FDVINPSHIL KVKAEITQQI IESLFETINA LVQNLTNIED
GYIQSSVAQR RLKHILLTYL SHSKNSDVER LIRQVYLDST NMTEKVSALE SARVYSVALL
DDLLKDMDTQ FTDNVLVFDK MTSAVARIPH AEVYGKMALW AEHKLFSDKN PNRVRSLFGA
FIMNNPEQFH DESGKGYQFL ADFLKKMDKL NPQLASRMIS PLLSWQRYEP ARKDLMKQQL
TQLSKLELSK DLYEKVSSAL G
//
