ID A0A3G2G3Z6_9FLAO Unreviewed; 637 AA.
AC A0A3G2G3Z6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=EAG08_03185 {ECO:0000313|EMBL:AYM99476.1};
OS Chryseobacterium sp. 3008163.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=2478663 {ECO:0000313|EMBL:AYM99476.1, ECO:0000313|Proteomes:UP000273471};
RN [1] {ECO:0000313|EMBL:AYM99476.1, ECO:0000313|Proteomes:UP000273471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3008163 {ECO:0000313|EMBL:AYM99476.1};
RA Bekkelund A.K., Hansen B.R., Stokken H., Eriksen B.F., Kashulin N.A.;
RT "Effects of UV and annual dynamics of microbial communities in freshwater
RT RAS systems.";
RL Submitted (OCT-2018) 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; CP033070; AYM99476.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G2G3Z6; -.
DR KEGG; chrs:EAG08_03185; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000273471; Chromosome.
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 InterPro; IPR026444; Secre_tail.
DR NCBIfam; TIGR04183; Por_Secre_tail; 1.
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 Pfam; PF18962; Por_Secre_tail; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000273471};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..637
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018315911"
FT DOMAIN 53..228
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 310..465
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 574..634
FT /note="Secretion system C-terminal sorting"
FT /evidence="ECO:0000259|Pfam:PF18962"
SQ SEQUENCE 637 AA; 71279 MW; DCF0E094EEAE20B3 CRC64;
MKKFYLLILG VLVCQTVLAQ ENIEMKGLMA KEMKSFTAKM NAGNTNPNTL NYDLQYQRMD
VSLNPSVAQI SGSVTSHFKP TQAMSSIYFD LTNQLTVSQV TFHGQPLAFQ QLATKEVKID
FTSSLPANVL DSLTIQYSGN PPTNNNAFFT NSQGGTPVLS TLNEPYGAQD WFPTKQSLND
KIERFDIKVT TPSQYSVASN GRLMSETILG SGQKLTFWRT QYPTAAYLVA LSITNFVKLN
DTMGNPPFPF VNYIYPGTST NVGSMANIEW TKTVMNTFET YFGPYPFRNE KYGHMEFTAG
GGMEHQTMSS MGSWSKQLIA HELAHQWFGD KVTCGAWNDI WLNEGFATFG EHVAYEKLLM
TNTEFLNYLL SEKNYITSAT GGSVYVADAN LGSVGTIFSG RLSYSKGGYV VRMIKWILGE
TVFYQALKDY HARPNLAYNY VKTSDLNASL LQSTGRDFTG FFNDWIYGQG YPTYDIRWKQ
TGNQVTFKAG QTQSHASVSF FDMPLPIKVN GTGGQVAYFA LNNTSNNQYF TETVSFPVAS
VQFNYEYQIL EKNSTVAQDN TLSTSEAVLD QLSIYPNPAK DELFISGLKK QTDYNIVTAD
GRLVKKGNTE KKIDISALEK GVYFITIQQL NLKFIKE
//
