ID A0A0N0UMI8_9ACTN Unreviewed; 861 AA.
AC A0A0N0UMI8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=ISGA_13415 {ECO:0000313|EMBL:KOY48948.1};
OS Gordonia sp. NB41Y.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=875808 {ECO:0000313|EMBL:KOY48948.1, ECO:0000313|Proteomes:UP000011989};
RN [1] {ECO:0000313|EMBL:KOY48948.1, ECO:0000313|Proteomes:UP000011989}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB4-1Y {ECO:0000313|EMBL:KOY48948.1,
RC ECO:0000313|Proteomes:UP000011989};
RX PubMed=23744905; DOI=10.1099/mic.0.068932-0;
RA Van Hamme J.D., Bottos E.M., Bilbey N.J., Brewer S.E.;
RT "Genomic and proteomic characterization of Gordonia sp. NB4-1Y in relation
RT to 6 : 2 fluorotelomer sulfonate biodegradation.";
RL Microbiology 159:1618-1628(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KOY48948.1}.
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DR EMBL; APHK02000136; KOY48948.1; -; Genomic_DNA.
DR RefSeq; WP_053778767.1; NZ_CP132196.1.
DR AlphaFoldDB; A0A0N0UMI8; -.
DR STRING; 1241906.ISGA_13415; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000011989; 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; 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:KOY48948.1};
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:UP000011989};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 106..192
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 236..443
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 531..850
FT /note="ERAP1-like C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11838"
FT REGION 723..742
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 861 AA; 93862 MW; 53999936D8854B6B CRC64;
MTAPNLTRDQ ARERAAILDV STYTIDLDLT DGNGRPGVDT FRSTTTVAFT ATAGSSTFID
LVAPRLLSAT LNGVALDVSG FDESVGIALP DLTAENELTV VADCAYSNTG EGLHRFVDPT
DSSVYLYTQF ETADAKRMFA CFDQPDLKAT YTLTVAAPED WKVISNAALV QNVAATPGVF
RFRETAVMST YLVALIAGPY AEWTDTYTDE HGTIPLGIYC RGSLAEFMDA DRLFTETKQG
FAFYHKNFGT PYAFGKYDQL FVPEFNAGAM ENAGAVTFLE DYVFRSRVTK YLYERRAETV
LHEMAHMWFG DLVTMQWWDD LWLNESFATF ASVLCQAEAT EYTSAWTTFA NVEKSWAYRQ
DQLPSTHPVA ADIPDLAAVE VNFDGITYAK GASVLKQLVS YVGLEPFLAG LRDYFATHRF
GNATFADLLA ALEKSSGRDL SDWGGQWLKT TGINVMRPDF ELDADGAFTR FTIVQDGAAP
GAGERRAHRL RVGVYDDTAT GTLERTHSVE LDVDGERTDV AELVGVPRGK LVLINDDDLT
YASVRLDPDS LATATARIGD ITDSMPRTLV WSAAWEMTRQ AEMRARDFVE LVQRGIAAET
EIGVVQRVLL QATTAIEAYA DPQWAAQTGR PGFSARLLEL ARGAEAGSDH QLAFVNTLLA
GRLTEDQVPV AQGLLDGDDP AAHGLSGLTV DADLRWKLVR ALATAGAIDT DPASTPVIDA
EAERDNTAAG TRQAAAARSS RPLPEAKADA WARAIDDDSL SNIYTRTMIE GFARPGQSDL
LDAYVTKYFE AVPGVWSRRS SEVAQTVVVG LYPSWAMTDE AIAAADEFLA ADHPPALKRL
ISEGRDSVAR SQRARIFDAG A
//
