ID A0A126T2Q0_9GAMM Unreviewed; 880 AA.
AC A0A126T2Q0;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:AMK76360.1};
GN ORFNames=JT25_007620 {ECO:0000313|EMBL:AMK76360.1};
OS Methylomonas denitrificans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylomonas.
OX NCBI_TaxID=1538553 {ECO:0000313|EMBL:AMK76360.1, ECO:0000313|Proteomes:UP000030512};
RN [1] {ECO:0000313|EMBL:AMK76360.1, ECO:0000313|Proteomes:UP000030512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJG1 {ECO:0000313|EMBL:AMK76360.1,
RC ECO:0000313|Proteomes:UP000030512};
RX PubMed=25580993; DOI=10.1111/1462-2920.12772;
RA Kits K.D., Klotz M.G., Stein L.Y.;
RT "Methane oxidation coupled to nitrate reduction under hypoxia by the
RT Gammaproteobacterium Methylomonas denitrificans, sp. nov. type strain
RT FJG1.";
RL Environ. Microbiol. 17:3219-3232(2015).
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; CP014476; AMK76360.1; -; Genomic_DNA.
DR RefSeq; WP_036275337.1; NZ_CP014476.1.
DR AlphaFoldDB; A0A126T2Q0; -.
DR STRING; 1538553.JT25_007620; -.
DR KEGG; mdn:JT25_007620; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000030512; 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; 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:AMK76360.1};
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:UP000030512};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 60..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 452..553
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 558..880
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 880 AA; 99556 MW; 8E0A3AF6C35B81C8 CRC64;
MRDASPQTVF LKDYTPPEYL IDQVELNFDL HEQRTQVRSI LNLRRNPQSQ ERSAALTLLG
EELQLVSIAI DGQPLEQSQY LLDGEALIVH EVPQDRPFQI VIENIINPQA NTALEGLYLS
SSMLCTQCEA QGFRKITWFL DRPDVMSRFK TTLTGDKSKY PVLLSNGNKV GQGELENNRH
WVSWEDPFAK PCYLFALVAG QLECVADEFV TMSGRRIALE IFVEKHNVDK CAHAMQSLKN
AMRWDEETYG LEYDLDLYMI VAVDHFNMGA MENKGLNVFN TKFVLARPDT ATDSDYEHIE
GVIGHEYFHN WSGNRVTCRD WFQLSLKEGF TVFRDQQFSG DRTSPAVKRI EDVNALRTRQ
FAEDAGPLAH PIRPEAYIEI NNFYTLTVYE KGAEVVRMLH TLLGAAGFRK GCDLYFQRHD
GQAVTCEDFV KALEDANGVE LEQFRRWYSQ AGTPVLTVGQ QYDAESQQLH LTIQQSCPPT
PNQPVKAPLH IPVKLGLLAA DGSAATIHYN GSSQAEITLN VTEAEQTFSF AKLPQQPVVS
LLRGFSAPVT LKMERSLDEL AFLLRHDSDT FNRWEAGQQL AVQVIFKLID AIELSRPLQL
EPVIVDAYRS VLTDSGGDLS YQALLLALPE ESYLSGQMAI IDVEAIHQAR EFVKKTLAEQ
LHAEFKQLYV QHHLDESGIF DAGAVGRRRL KNACLSYLSK LENEDVYHIA EQQFYSARNM
TDQMAALSAI VNSNHPAKAR SLDSFYMQWR QEALVIDKWF TLQATSSMPN TFATVQALMK
HPAFDMKTPN RVRSLIGAFS QANPLHFHAI NGEGYRFLAD QVLALNTLNP QIASRMVTGL
AQWRRYDAAR QGLMKQQLQR IVATEHLSKD VYEIASKSLA
//
