ID A0A3L8PXA6_9GAMM Unreviewed; 850 AA.
AC A0A3L8PXA6;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=D5018_08970 {ECO:0000313|EMBL:RLV60036.1};
OS Parashewanella curva.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Parashewanella.
OX NCBI_TaxID=2338552 {ECO:0000313|EMBL:RLV60036.1, ECO:0000313|Proteomes:UP000281474};
RN [1] {ECO:0000313|EMBL:RLV60036.1, ECO:0000313|Proteomes:UP000281474}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C51 {ECO:0000313|EMBL:RLV60036.1,
RC ECO:0000313|Proteomes:UP000281474};
RA Wang G.;
RT "Phylogeny of the Shewanellaceae, and recommendation for two new genera,
RT Pseudoshewanella and Parashewanella.";
RL Submitted (SEP-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}.
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:RLV60036.1}.
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DR EMBL; QZEI01000022; RLV60036.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8PXA6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000281474; 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:RLV60036.1};
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:UP000281474};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 20..184
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 224..434
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 442..532
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 535..849
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 850 AA; 96270 MW; 9FEA840DD5FA690F CRC64;
MSELQAKYLK DYQQSDFTIN HLSLDFQLNI PTTKVVAISQ VERQSKQATE LVLDGEDLDL
VSVKVNSQPA SHQVKDKQLY IQADLDNFEL EIITHIKPAE NTALEGLYMS DGAYCTQCEA
EGFRRITYYL DRPDVLAKFD VRVEADKTEF PFLLSNGNLI SSGDAVNGRH FATWQDPFPK
PSYLFALVAG DFDLLEDQFT TRSGRDVKLQ VFVDKGNLHK AHHAMASLKK SMKWDEDRFD
LEYDLDIYMI VAVDFFNMGA MENKGLNVFN TKYVLADKES ATDDDYHGIE SVIGHEYFHN
WTGNRVTCRD WFQLSLKEGL TVFRDQEFSS DVGSRPVNRI QAIQVIRNHQ FAEDAGPMAH
PIRPESVIEM NNFYTVTVYN KGAEVIRMMH TLLGEKNFQA GMKLYFERHD GQAVTCDDFV
SAMEDASGVD LQQFRLWYSQ AGTPSVAVSE NFEDGQYQLT LTQSRPTVAG NNDLPMHIPF
DVELIDLDGK SITSKVLNFT ERQQTFTFDG LTQKPVVSLL QDFSAPVKLE YQYEDEHLAH
LMRYASSEVA RWEASVSLFS KSVWDNVKAL VAGKSMQLSD IVKDAFKGVI LDEKLDEELI
AEIMSVPSIS ALVEQTESVD LDSLITARSF VKDELALACE DEVVARYHTS KDKDIASARA
LKNECLSWAC VANEEHEALV NAQYESATNM TDSLGALKVA SDLNLSNRES LMTHFENRWV
DTPLVMDKWF TLQAIQDSEQ VIDKIKALTS HKAFSFNNPN RVRSLIGSFA AGNIKHFHKS
DGSGYQYLTD ILKKMNIINP QVAARIITPL IQFSKFDLAR QQKIKESLQE LIELPDLSKD
LYEKVSRALS
//