ID A0A1H3Z6K7_9BURK Unreviewed; 962 AA.
AC A0A1H3Z6K7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN05192564_101625 {ECO:0000313|EMBL:SEA19409.1};
OS Paraburkholderia sartisoli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=83784 {ECO:0000313|EMBL:SEA19409.1, ECO:0000313|Proteomes:UP000198638};
RN [1] {ECO:0000313|EMBL:SEA19409.1, ECO:0000313|Proteomes:UP000198638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24000 {ECO:0000313|EMBL:SEA19409.1,
RC ECO:0000313|Proteomes:UP000198638};
RA de Groot N.N.;
RL Submitted (OCT-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; FNRQ01000001; SEA19409.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H3Z6K7; -.
DR STRING; 83784.SAMN05192564_101625; -.
DR Proteomes; UP000198638; 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:SEA19409.1};
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:UP000198638};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 170..252
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 292..512
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 517..629
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 633..961
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 962 AA; 107104 MW; 6D0EC349873A8E74 CRC64;
MSCGVWQARR AIAPRPDITL TRAIGTKFET HDIKWLCTMA QLVGRSAPRA AVDRPALFNE
SAMSDIATPA VIRRADYAPP AFLIDTVALE FDLVPEHTVV RNTMRVRRNP DAARAPRFEL
MGEQLEFVSA TIDGKPHAAV HSHERGLTLD HVPDDFELTL VSACNPAENT TLSGLYVSGG
NFFTQCEAEG FRRITYFLDR PDVMATYTVT LRADKATYPV LLSNGNLIEE GDLPDGRHFA
RWEDPFRKPS YLFALVAGKL VALEERVKSG SGKEKLLQVW VEPHDLDKTQ HAMDSLKHSI
RWDEQRFGLE LDLDRFMIVA VSDFNMGAME NKGLNIFNTK YVLANPETAT DTDFANIEAV
VGHEYFHNWT GNRVTCRDWF QLSLKEGLTV FRDQEFSADM AGGATDEAAR ATKRIEDVRV
LRQMQFAEDA GPMAHPVRPE SYVEINNFYT MTVYEKGSEV VRMYQTLFGR DGFRRGMDLY
FERHDGHAVT CDDFRHALAD ANGRDLAQFE RWYSQAGTPR VSVKTAYDAA QRRYNVTLTQ
GYGDSTPAAR DTQKGPLLIP FAIGLIGKDG ADLPLRLEGE TAAAAAGTGT TRVLEFTATE
QTFTFVDVAD RPLPSLLRNF SAPVIVEYDY TNEELAFLLA HDSDPFNRWE AGQRLATREL
LALAARAATG EPLQLDDSVV AAFARVLRDE TLSPAFRELA LMLPSEAYLA EQMAESNPAA
VHQARQFVRN RLANALRADW LAIHARHQTP GAYEATPAAS GHRALKNLAL SYLAELDDPA
EAVRLAHAQY DAANNMTDRS AALSALLNAS SAAGGTLADA ALDDFYRRFE KEPLVIDKWF
ALQATQRGSA QRPVIDVVRK LMAHPAFTLK NPNRARSLIF SFCAANPSQF HAEDGSGYRF
WAEQVIALDA MNPQVAARLA RSLELWRRFT PTLRDGMRAA LETVAAKVKS RDVREIVEKA
LG
//
