ID A0A1N6ETQ1_9RHOB Unreviewed; 849 AA.
AC A0A1N6ETQ1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN05444002_1088 {ECO:0000313|EMBL:SIN86334.1};
OS Vannielia litorea.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Vannielia.
OX NCBI_TaxID=1217970 {ECO:0000313|EMBL:SIN86334.1, ECO:0000313|Proteomes:UP000184932};
RN [1] {ECO:0000313|Proteomes:UP000184932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 29440 {ECO:0000313|Proteomes:UP000184932};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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; FSRL01000001; SIN86334.1; -; Genomic_DNA.
DR RefSeq; WP_074255196.1; NZ_FSRL01000001.1.
DR AlphaFoldDB; A0A1N6ETQ1; -.
DR STRING; 1217970.SAMN05444002_1088; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000184932; 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; 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:SIN86334.1};
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:UP000184932};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 45..162
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 218..432
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 437..528
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 534..848
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 849 AA; 94965 MW; FF281CF90C4D9DF8 CRC64;
MKDAAPQPVR PVRLAEYTPF PFVVEHVELW FTLAGAETRV RSRIRFAPNP AAEPAREIFL
HGKALALQWA RIDGADVQPE TTPKGLTCPV PSGPFTWEAE VQIDPTTNTS LDGLYTSGGM
YCTQCEAEGF RKITYYPDRP DVMAPFRVHI DSDMPVKLSN GNPLGDGTWD DPWPKPAYLF
ALVAGDLRAF SSDFTTLSGR HVDLNIWVRP GDEPRAEYAM DALIRSMKWD EETYGREYDL
DVFNIVAVDD FNMGAMENKG LNIFNSKYVL ASPDTATDSD YDLIEGIIAH EYFHNWTGNR
ITCRDWFQLC LKEGLTVFRD QQFSSDMRGA AVKRITEVMQ LRARQFREDQ GPLAHPVRPE
EYIEINNFYT ATVYEKGAEV IHMLKHLVGD DGYSKALDLY FDRHDGDAAT IEDWLKVFED
ATGRDLTQFS RWYSQAGTPR LSLTERFNDG TLTLDFKQET RPTPGQPTKL PQVIPIAVGL
IGPNGDEVLP TTVLEMSEAE QSFEFTGLSA RPVASVLRGF SAPVVLDRPL DNATRAFLLA
HDTDPFNRWE AGRVLGKEVL TRMITEGAAP APDLLTGLHR LVADASLEPA YRALMLGLPS
EDDLAQTLFD SGHVPDPAAI HAARERLLDA MAAEMEPTLA RLYDEMETPA PYSPDAEAAG
KRALRSACLA LLSRRDGCAR AQALFAAADN MTEEMAALAT LVRHDQGAEA VQAFYDKWRH
DRLVMDKWFM LQVVHARHEI MAETAAALTA HPDFDWKNPN RFRSVLGGMQ ANPAGFHRAD
GAAYRLYADW LIKLDPVNPQ TTARMSTAFE TWARYDADRQ AMMREQLERI AALEGLSENT
GEMVGRILG
//
