ID A0A110AZM2_9SPHI Unreviewed; 833 AA.
AC A0A110AZM2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN_1 {ECO:0000313|EMBL:BAU51990.1};
GN ORFNames=FHS11_004460 {ECO:0000313|EMBL:MBB3058014.1}, MgSA37_00140
GN {ECO:0000313|EMBL:BAU51990.1};
OS Mucilaginibacter gotjawali.
OC Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC Sphingobacteriaceae; Mucilaginibacter.
OX NCBI_TaxID=1550579 {ECO:0000313|EMBL:BAU51990.1, ECO:0000313|Proteomes:UP000218263};
RN [1] {ECO:0000313|EMBL:BAU51990.1, ECO:0000313|Proteomes:UP000218263}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SA3-7 {ECO:0000313|EMBL:BAU51990.1,
RC ECO:0000313|Proteomes:UP000218263};
RA Lee J.S., Lee K.C., Kim K.K., Lee B.W.;
RT "Genome sequence of Mucilaginibacter gotjawali.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB3058014.1, ECO:0000313|Proteomes:UP000539265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8628 {ECO:0000313|EMBL:MBB3058014.1,
RC ECO:0000313|Proteomes:UP000539265};
RA Whitman W.;
RT "Genomic Encyclopedia of Type Strains, Phase III (KMG-III): the genomes of
RT soil and plant-associated and newly described type strains.";
RL Submitted (AUG-2020) 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; AP017313; BAU51990.1; -; Genomic_DNA.
DR EMBL; JACHWX010000017; MBB3058014.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A110AZM2; -.
DR KEGG; mgot:MgSA37_00140; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000218263; Chromosome.
DR Proteomes; UP000539265; 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; IPR021133; HEAT_type_2.
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.
DR PROSITE; PS50077; HEAT_REPEAT; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000313|EMBL:BAU51990.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:BAU51990.1};
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:UP000218263};
KW Signal {ECO:0000256|SAM:SignalP}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..833
FT /note="Aminopeptidase N"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5033247302"
FT DOMAIN 52..242
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 280..488
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 833 AA; 93656 MW; 08395638647B31B6 CRC64;
MLTFKTLSTL IFSGLATGMA FSTAYAQAPA KADDPLMKIY RATPPKINDL VHTKLDVRFD
YKKCFMYGKE WVTLRPHFYP TDTLRLDAKG MDLNNISVVR NGKNYPLKFK YDDSLTVAIQ
LDKVYHNNET YTIYIDYTAK PNQLKTKGSA AINDAKGLYF INPDGAVKDK PVQIWTQGET
ESSSAWFPTI DKPEQKTTDE IIMTVPAKYV TLSNGRLAAQ KLNGDGTRTD DWKMELPHSP
YLFMMAVGDF KIYHDHWRNK EVNYYLEPKY APYAKQIFGM TPELIEFYSK TLDYPFAWNK
YSQIVVRDYV SGAMENTSAT LHGDYVQETP RELLDANYDA GRSTIAHELF HQWFGDLVTA
ESWSNLTVNE SFADFSEMLW AEHKYGKDEA DAHSYTALQN YLGSPDASTK DLVRFHYDDK
EDVFDVVTYQ KGGRILNMLR NYLGDAAFFK GLNIYLKTNQ FKNGEAQQLR LAEEEASGLD
LNWFFNQWYY GAGHPVLNIS YKWDEGSKTE TVYLQQTQEG QIFKLPFAVD IYAGGKKERH
KVWMNDKADT LTFTVASKPN LVNVDGDKVL LCAKTDNKSL EEFEFQYFNA PLYLDRFEAI
NAVSGRQSDK GAQKVLIAAL KDKYYGLRIK AIRALNMSND DIHNAALPVL TTLAQTDDNT
LVRAAAISAL GKLKASGNMN LFKQALSSQS YAVQGAALTA INLLDPKQAL PLAKGFEQDN
KGPLTQAIIT VYSTSGGSDE WPYVLKAFNE QGPQGKFGMA RNFAAMTGHV DNPTYAQQGI
AAFKDLGIKY KKFGVAPFVT GLLADIKAQR VKLKDDASAK AADDATQAIN DAK
//
