ID A0A1Y6C721_9ALTE Unreviewed; 889 AA.
AC A0A1Y6C721;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN02745866_02593 {ECO:0000313|EMBL:SMF40103.1};
OS Alteromonadaceae bacterium Bs31.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae.
OX NCBI_TaxID=1304903 {ECO:0000313|EMBL:SMF40103.1, ECO:0000313|Proteomes:UP000192901};
RN [1] {ECO:0000313|EMBL:SMF40103.1, ECO:0000313|Proteomes:UP000192901}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bs31 {ECO:0000313|EMBL:SMF40103.1,
RC ECO:0000313|Proteomes:UP000192901};
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 (APR-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; FXAI01000006; SMF40103.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6C721; -.
DR STRING; 1304903.SAMN02745866_02593; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000192901; 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:SMF40103.1};
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:UP000192901};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 99..190
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..443
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 448..550
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 556..889
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 889 AA; 101061 MW; A6FF5CBF9F987E6F CRC64;
MSNSQPKTIY LKDYKAPAFQ ISSTELVFDL FEDYADVHAR LNIERVSPGQ KGALVLHGLD
LELLAIKLDG TQLGDEQYTV EEACLSIHEV PDSFQLDTTT RIKPQENTSL EGLYKSQKMF
CTQCEAEGFR KITYYLDRPD VLSEFTCKVI ADKNRYPVLL SNGNKIAEGS EQEGRHWVQW
HDPFKKPCYL FALVAGDLQA IDDSYTTMSG REVLLRIFVE DKDKDKCAHA MNSLKKAMKW
DEDVYGREYD LDIFMIVAVD DFNMGAMENK GLNIFNTSCV LAHQKTTTDD SFQAVEAVVA
HEYFHNWSGN RVTCRDWFQL SLKEGFTVFR DSEFSADMGS RSVKRVEDVN LLRTLQFAED
AGPMAHPVQP SSFIEISNFY TLTIYEKGAE VVRMVHSLLG PELFRKGSDL YFERHDGHAV
TIEDFIRAMA DVSGRDFTQF MRWYQQAGTP HVSVSGIYHP EEQKFVLSFE QSCPPSPEAK
EQLPFHIPIS VGLLGETGPL AFRLEHEQGL IETCTLEITK KQQTINFFDV KEQVVPSLLR
NFSAPVKLKY CYSMADLQRI ISLDSDGFNR WDASQQLAVK ATENVRVALA ISPAPAVQGE
LLSSHEALLK QALATLDGED QQDLQMLAYT LALPSEEYLF EQQTQIDVEG THHARQRVKR
KLANSHFDLY LRIYQALNSN AVFSVDAQSI ARRRLKNTVL GYLVCSGKAQ AIELCIQQFN
SADNMTDELS ALSELVHSGS GEAQAYKSES LERFFEKWKH EALVVNRWFS LQATNPDPAT
LGRVEALMQH SYFDASNPNK LRALVGGFCN RNAICFHDRS GDGYRFLKER IVELNEKNPQ
IASRLLTPLT RWKRFDESRQ ILMRQELESI QALNNLSKDV FEVVSKSLN
//
