ID A0A158AN62_9BURK Unreviewed; 906 AA.
AC A0A158AN62;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=AWB75_02413 {ECO:0000313|EMBL:SAK59183.1};
OS Caballeronia catudaia.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1777136 {ECO:0000313|EMBL:SAK59183.1, ECO:0000313|Proteomes:UP000054870};
RN [1] {ECO:0000313|EMBL:SAK59183.1, ECO:0000313|Proteomes:UP000054870}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29318 {ECO:0000313|EMBL:SAK59183.1};
RA Oliw E.H.;
RL Submitted (JAN-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; FCOF02000009; SAK59183.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A158AN62; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000054870; 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:SAK59183.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 110..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..457
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 462..570
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 574..905
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 906 AA; 101018 MW; 4A8C51F8153BCA11 CRC64;
MSTTTASAVI RRQDYTPPAF LIDSVALEFD LVPARTVVKN TMKLRRNPDA GGDAPRLELM
GEQLEFVKAV IDGVAHADVH VHENGLSIGT IPAADTFELS IESICNPAEN TTLSGLYVSS
GNFFTQCEAE GFRRITYFLD RPDVMSTYTV TLRADKTAYP VLLSNGNLIE EGELPGGRHF
AKWEDPFKKP SYLFALVAGK LVCIEEKIKS GSGKEKLLQV WVEPHDLDKT RHAMDSLIHS
IRWDEKRFGL ELDLDRFMIV AVSDFNMGAM ENKGLNIFNT KYVLANPETA TDTDFSNIEA
VVGHEYFHNW TGNRVTCRDW FQLSLKEGLT VFRDQEFSAD MAAGDVEGSA SAAARATKRI
EDVRVLRQMQ FAEDAGPMAH PVRPESYVEI NNFYTMTVYE KGSEVVRMYQ TLFGRDGFRR
GMDLYFQRHD GQAVTCDDFR HALADANHRD LAQFERWYSQ AGTPRVSVRA AYDAAKKRYT
LTLAQGYGDA SEAARDTQKG PLLIPFSVGL IGQNGADLPL RLEGEKEPNG TTRVLEFTER
EQSFTFVDVS EAPLPSLLRN FSAPVIVEYD YTNDELAFLL AHDSDPFNRW EAGQRLATRE
LLGLAERAAK GETLSLDDQV IAAFARVLDD TTLTPAFREL ALMLPSESYL AEQMTVSDPA
AVHAARVFMS RRLASQLREK WIATYQANRT PGDYRPTPED AGKRGLKNLA LAYLSQLDDP
REAVKLAQAQ YDAADNMTDR SAALAALLLS SATKGADASV ADAALADFYR RFENEALVID
KWFALQATQR GGPERNVIEI VRKLMQHQAF NIKNPNRARS LIFSFCSGNP AQFHAPDGSG
YAFWAEQVIA LDALNPQVAA RLARGLELWR RFTPKLREKM HAALSEVASK AKSRDVREVV
EKALAA
//
