ID A0A246JIQ2_9SPHN Unreviewed; 866 AA.
AC A0A246JIQ2;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=CDQ91_18315 {ECO:0000313|EMBL:OWQ92410.1};
OS Sphingopyxis witflariensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingopyxis.
OX NCBI_TaxID=173675 {ECO:0000313|EMBL:OWQ92410.1, ECO:0000313|Proteomes:UP000197097};
RN [1] {ECO:0000313|EMBL:OWQ92410.1, ECO:0000313|Proteomes:UP000197097}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 14551 {ECO:0000313|EMBL:OWQ92410.1,
RC ECO:0000313|Proteomes:UP000197097};
RX PubMed=12508864; DOI=10.1099/ijs.0.02217-0;
RA Kampfer P., Witzenberger R., Denner E.B., Busse H.J., Neef A.;
RT "Sphingopyxis witflariensis sp. nov., isolated from activated sludge.";
RL Int. J. Syst. Evol. Microbiol. 52:2029-2034(2002).
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:OWQ92410.1}.
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DR EMBL; NISJ01000013; OWQ92410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A246JIQ2; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000197097; 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:OWQ92410.1};
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:UP000197097};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 101..193
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..443
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 451..545
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 551..864
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 866 AA; 95328 MW; 0CA09D708E9FD914 CRC64;
MTDASSTPAI PVTIHRGDYR PPEWQVPDIA LDFALGIDET RVSARLSVVR HADAPAPLLL
RGDGITPAEV RVDGSVWNDW RMEGGDLIVD LGERTAAMVE VDTVINPATN TQLMGLYASN
AMLCTQCEAE GFRRITFHPD RPDVLSRYRV RMEGDKAAFP ILLSNGNCVE QGAGEGGRHW
ALWEDPWPKP SYLFALVAGD LVVNRDSFTT MSGRKVELGI WVRAGDEDRT GHAMQALKDS
MAWDERVYGR EYDLDLFNIV AVSDFNMGAM ENKGLNVFNT RYILADPDTA TDMDYDGVEG
VVAHEYFHNW SGNRVTCRDW FQLSLKEGFT VYRDQSFSAD MGSPPVKRIE DVRLLRAAQF
PEDAGPLAHP IRPDSFQEIS NFYTATIYNK GAEIIRMMAT MVGPERFRKG TDLYFDRHDG
EAATCEDFVK AIEDGAGIDL TQFRLWYSQA GTPRITARIA TDERNGERTL HLTQVVPATP
GQPEKAPMLI PLRIKAYDLD GGHGVEEEQL VLLDRTEMAV PLGHYRSPPM LSLNRGFSAP
VIVDFAREEG ELEWLAANDD DPFARYEALQ QLMLDTLVTA VSGKASDAGA VVDAIRQTLT
GSAADPAFVA EAVLLPSEAF IGDQMVIVDP DAIRRERLAL QAAIGTALES EWRAILGQLA
PAATLLTPLA KGRRRLRGVA LAYLAATGMG DASELAFGIF SGADGMTERQ AALATLAHGD
SKERAQALDI FYRRYRDNPL VLDKWFQVQA WSLRSDTVAA VAALAEHPDF TLTNPNRVRA
LYGALSANQA AFHQADGAGY RLIADLVLAL DPKNPQTAAR MIPPLGRWKR FGDARAAMMK
AELERILAQP GLSRDVTEQA SKSLLG
//
