ID A0A1M3HJB1_9SPHI Unreviewed; 531 AA.
AC A0A1M3HJB1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=BGO55_25250 {ECO:0000313|EMBL:OJW58586.1};
OS Sphingobacteriales bacterium 50-39.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX NCBI_TaxID=1895841 {ECO:0000313|EMBL:OJW58586.1, ECO:0000313|Proteomes:UP000184242};
RN [1] {ECO:0000313|EMBL:OJW58586.1, ECO:0000313|Proteomes:UP000184242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=50-39 {ECO:0000313|EMBL:OJW58586.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-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:OJW58586.1}.
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DR EMBL; MKTZ01000009; OJW58586.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M3HJB1; -.
DR STRING; 1895841.BGO55_25250; -.
DR Proteomes; UP000184242; 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; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670}; Signal {ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..531
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012521919"
FT DOMAIN 30..204
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 251..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 531 AA; 60609 MW; 696B11B10DD384E3 CRC64;
MALRLPFLAL LLVFFSVSFG QPYNPAVDVQ NYEFALRVSD TSDMIQGTAF IHIKFRQHAD
SFLLDLKNVD GQGKGMYVFA VEQEMHPLTF SKNFKQTKDH LIIYDTADSE EQRLYVIEYK
GIPSDGLIIS KNKYGHRGFF GDNWPNRAHN WLPCIDDPSD KATVTFDVVA PAHYTVVANG
ALQKEEKLDN GMKVTSWIES APLSPKIMMV GISDFAVDHP GDVEGVPVYN YVYPEDKTVG
FHSYANALKI LPFYIHRIGP YPFEKCGNVQ SKTRFGGLEN ASAICYYENS VSSPGVESLM
AHEIAHQWFG DAVTETQWRH LWLSEGFATY MTHCYLESRY GADTLKAGLR KDRITVLHFE
KKRMTPVVDS SVHHDYMVLL NPNSYQKGGW VLHMLRRKIS DSLFWKAIST YYNTYRNGNA
STEDFEKIVE TASGQDLHTF FHQWLYTPGH PSVRLQWHYD DANSALFITT TQLQPIPFEF
PLELSIDGKP YTIQLTTKTN FLRIPLIAEP TTIVPDPNVD LLADFKMPEH H
//
