ID A0A076N1B7_AMYME Unreviewed; 843 AA.
AC A0A076N1B7;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
DE AltName: Full=Alanine aminopeptidase {ECO:0000256|ARBA:ARBA00029811};
DE AltName: Full=Lysyl aminopeptidase {ECO:0000256|ARBA:ARBA00031533};
GN Name=pepN {ECO:0000313|EMBL:AIJ24625.1};
GN ORFNames=AMETH_4533 {ECO:0000313|EMBL:AIJ24625.1};
OS Amycolatopsis methanolica 239.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis; Amycolatopsis methanolica group.
OX NCBI_TaxID=1068978 {ECO:0000313|EMBL:AIJ24625.1, ECO:0000313|Proteomes:UP000062973};
RN [1] {ECO:0000313|EMBL:AIJ24625.1, ECO:0000313|Proteomes:UP000062973}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=239 {ECO:0000313|EMBL:AIJ24625.1,
RC ECO:0000313|Proteomes:UP000062973};
RA Tang B.;
RT "Whole Genome Sequence of the Amycolatopsis methanolica 239.";
RL Submitted (JUL-2014) 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; CP009110; AIJ24625.1; -; Genomic_DNA.
DR RefSeq; WP_017983455.1; NZ_CP009110.1.
DR AlphaFoldDB; A0A076N1B7; -.
DR STRING; 1068978.AMETH_4533; -.
DR KEGG; amq:AMETH_4533; -.
DR PATRIC; fig|1068978.7.peg.4866; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007335_1_1_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000062973; 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; cd09602; M1_APN; 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; IPR024571; ERAP1-like_C_dom.
DR InterPro; IPR012778; Pept_M1_aminopeptidase.
DR InterPro; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR NCBIfam; TIGR02412; pepN_strep_liv; 1.
DR PANTHER; PTHR11533:SF304; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 1.
DR Pfam; PF11838; ERAP1_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:AIJ24625.1};
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:UP000062973};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 110..196
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..449
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 522..824
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 843 AA; 92249 MW; 3BBD090198221A10 CRC64;
MTVEHRTAAK RALTRDEAAV RAAEVGELHY TFTLDLARGD REFATSTVAR FHVRTGAAPV
FLDFTGEVDA VECDGSPVPG SAHDGTRVRL DVGPGAHTVR VTGRAQYSRT GEGLHRFRDP
LDGRVYLHTK FEPFAAHTVF ACFDQPDLKA TVELTVTAED GWVVIANAEP ADPDPPAAGG
RRVWRFRPTP PLPPYLVAFA AGPFRRIGSR HGPVPMGLYA RDSLAAELTA DAPEIFDVVA
KGLDFFASLF GVPYPFGKYD QVFAPEYAFG GMEHPGCVTL NERFLFRHRV TADTRRRRAE
VLLHEMAHMW FGDYVTMRWW DDLWLNESFA EAMSVAAQAE VTPYGDGWTP YAHHALPAAR
HAERLPTSHP IRAVTGDTDA ARVNFGPIVY KRGAAVLHDL AEHLGWVTFT AGVRAYLRAH
AWGNATLDDF VAALRRVSGA DVDRWVAEWV LRRGINTVEV SRTGNGARVT QTADRDGGRR
HLTVRCAGFD DRDGALVLRD QVTVPLTPDR PAASEIPAAD LLVPNADAVC HVAVRLDPES
RRAALRALST VEDARTRAVV WGALWDDVLD ARLAARDYAT AVLTHAQAEP DAGVVEALGQ
RAVQALREYA DPADRDELLA AWADGVRDRL ARAAPGSDQQ FVLARVLVDA LPGHDDLLTM
IARGRPPWPG LRVDPGLRWR AVLRLAVTGR LVDELVDETL DADPGDSGRR NALTARAARP
TVPAKEDAWA ELLGDGLSLA EKKAVMAGWR HPEQATVLTP FASWYPRTLV NLCRTARPEF
TVAFARALYP RFTTAEQRVL AETDELVREA ALPGAVCKAV AEERAELVLL RAARACDGTS
ALS
//
