ID A0A1N6IW54_9BACT Unreviewed; 875 AA.
AC A0A1N6IW54;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, 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=SAMN04488055_3402 {ECO:0000313|EMBL:SIO36278.1};
OS Chitinophaga niabensis.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=536979 {ECO:0000313|EMBL:SIO36278.1, ECO:0000313|Proteomes:UP000185003};
RN [1] {ECO:0000313|EMBL:SIO36278.1, ECO:0000313|Proteomes:UP000185003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24787 {ECO:0000313|EMBL:SIO36278.1,
RC ECO:0000313|Proteomes:UP000185003};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-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}.
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DR EMBL; FSRA01000002; SIO36278.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6IW54; -.
DR STRING; 536979.SAMN04488055_3402; -.
DR Proteomes; UP000185003; 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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
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; PF13646; HEAT_2; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF48371; ARM repeat; 1.
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:SIO36278.1};
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:UP000185003};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 66..271
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 309..518
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 875 AA; 98663 MW; B0E94BF36FB60843 CRC64;
MGRAYFCLKQ QFMHLQLKNT FSILLAGFAV IGLCAPVLAQ SGEQSKEDPA LQIYRSSPTK
INNLVHTKLD VRFDYAKRQL NGKAWITLQP HFYPTDSLTL DAKGMDIKQV SLVQTSGAAV
LKFPSEAMLK TAKTSPLKYE YDGKELRLKL NKTYKSSESY TVFVEYTAKP DEAEVKGSAA
ITDAKGLYFI NPDGKDPKKP IQIWTQGETE SSSVWFPTID KTNQKTTSEI SMTVDKKYVS
LSNGKLVSQK PNADGTRTDT WRMELPHAPY LFMMAVGDFA VIKDQWRGKE VNYYVEKEYA
PHAKAIFGNT PEMMTFYSKI LGYDYPWVKY SQIIVRDYVS GAMENTTATI HGDFLQKTDR
ELLDDDDRQG EAVIAHELFH HWFGDLATCE SWSNLTMNES FADYSEYLWF EHKFGKDAAD
EHAYSAMNNY MESAEYQGDH HLVRFHYHDK ENMFDAITYQ KGGRILNMLR NYVGDEAFFK
ALNLYLKQNA FKSTEAHQLR LAMEEVTGQD MNWFFNQWYF GEGYPTLDIN YDYSQSGTAK
VIISQKGDKV WDLPIAIDVY AGGKKERHNV RVTEKENTFS FPVSAKPDFI NIDADKVLIV
KKTDRRDLGT YVFQYKNAPN YLDRREAIEA CLKQQTSNPA ARATVIAALK DKYEGLRSLA
IGGLKLDNND IKTAALPILT DLAKSDAHSQ VRAAAIKQLG RLKDVQYTSL FEGALKDRSY
LVEGTALNAL AELDIKKAYQ LAKSMEKDAR GLLGSGIASV YAKNGDVSDV PFFAQKLEES
TGQDKIGAAI MYLNILGSVD DTQIVTKGID EVVAVVENFN NSWVNNYIIN LLTPMAKKKQ
EKAATASGDA KAALNKQAAY IQQAAQKIKE NTKEE
//
