ID A0A3G6ZN15_9MICO Unreviewed; 848 AA.
AC A0A3G6ZN15;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 22.
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:AZC14108.1};
GN ORFNames=DT073_10625 {ECO:0000313|EMBL:AZC14108.1};
OS Microbacterium sp. ABRD28.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=2268461 {ECO:0000313|EMBL:AZC14108.1, ECO:0000313|Proteomes:UP000280903};
RN [1] {ECO:0000313|EMBL:AZC14108.1, ECO:0000313|Proteomes:UP000280903}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ABRD_28 {ECO:0000313|EMBL:AZC14108.1};
RA Jin H.M.;
RT "Genome sequence of Microbacterium sp. ABRD28.";
RL Submitted (JUL-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; CP031015; AZC14108.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3G6ZN15; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000280903; 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:AZC14108.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:AZC14108.1};
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:UP000280903};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 102..189
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 230..445
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 527..838
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
SQ SEQUENCE 848 AA; 93835 MW; 2997FBF9B4FCC4FC CRC64;
MPGENLTRLE AQERRAVVDT DSYQVDLDLT RGAEIFGSRT VVRFRGQPGS STFIDLIARD
VREITLNGRS IDPATAFADS RIALDGLAED NELVIDADCV YTNTGEGLHR FVDPVDGEVY
LYSQFEVPDS RRMFAVFEQP DLKATFRFTV TAPEAWEVVS NSPTPEPARH GDGTATWDFE
PTPRISSYIT ALIAGPYEKT FSELTSASGR VIPLGVYARK SLWNHLDADY VFDKTRQGFA
YFEEKFDYPY PFAKYDQLFV PEFNAGAMEN AGAVTFTETY VFRSKVTDAV RERRVVTILH
ELAHMWFGDL VTMKWWNDLW LNESFAEWAS TIATAEATEW TEAWTTFNAM EKTWAYRQDQ
LPSTHPVVAE INDLEDVQVN FDGITYAKGG SVLKQLAAWV GIEAFFAGVA AYFMKHEWSN
TELSDLLTEL EATSGRELTT WSKKWLETAG VNTLSPVIDE SPDGTIRRFA IIQTAPADYP
TIRPHRLGVG FYTLQDGALV RTHAVELDVD GDRTEVPELA GLVRPDLVLL NDGDLAYAKI
RLDERSLQTA IDHLAGIADP LARSLVWGAA WDQTRDAEAS ATDYVDLVLR NIASETESTT
VRTTLAQLLL ASSSYVTPEK RDDTRRRVAG HLWALAQNAP AGSDSQLQFV TAFAAAACTQ
EQWAAVKSLR DGDVVLDGLQ IDTDLSWQLL VSLAAGGIAS IGDIETALAA DNTAKGGEFA
AQARAALPFP EAKRAAWASL VDRDDLPNTV VRSASLGFVN PAGRDLLADY VQPYFDMLLP
VWESRTYKIA EYLIAGLYPA PLANTALRDA TRAWLAEHAD APAALRRLVQ ENLAGVERAL
AVQERDAQ
//
