ID S2YB91_9ACTN Unreviewed; 456 AA.
AC S2YB91;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=HMPREF1211_04492 {ECO:0000313|EMBL:EPD61461.1};
OS Streptomyces sp. HGB0020.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1078086 {ECO:0000313|EMBL:EPD61461.1, ECO:0000313|Proteomes:UP000014410};
RN [1] {ECO:0000313|EMBL:EPD61461.1, ECO:0000313|Proteomes:UP000014410}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HGB0020 {ECO:0000313|EMBL:EPD61461.1,
RC ECO:0000313|Proteomes:UP000014410};
RG The Broad Institute Genomics Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Schmidt T.M., Dai D., Dover J.,
RA Kim K., Walker B., Young S., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Allen A.W., Alvarado L., Arachchi H.M., Berlin A.M.,
RA Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sisk P.,
RA Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Streptomyces sp. HGB0020.";
RL Submitted (APR-2013) 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:EPD61461.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AGER01000016; EPD61461.1; -; Genomic_DNA.
DR RefSeq; WP_016434427.1; NZ_KE150427.1.
DR AlphaFoldDB; S2YB91; -.
DR STRING; 1078086.HMPREF1211_04492; -.
DR MEROPS; M01.033; -.
DR PATRIC; fig|1078086.3.peg.4543; -.
DR HOGENOM; CLU_014298_2_0_11; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000014410; 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; cd09603; M1_APN_like; 1.
DR Gene3D; 1.10.390.10; Neutral Protease Domain 2; 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; IPR001930; Peptidase_M1.
DR InterPro; IPR014782; Peptidase_M1_dom.
DR InterPro; IPR027268; Peptidase_M4/M1_CTD_sf.
DR PANTHER; PTHR11533:SF303; AMINOPEPTIDASE N; 1.
DR PANTHER; PTHR11533; PROTEASE M1 ZINC METALLOPROTEASE; 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 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:UP000014410};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 26..195
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 238..429
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 456 AA; 50263 MW; 78BE8937E9A58544 CRC64;
MAVQQAAGSD PYFPDHGDAR YRVHRYELAL DYRPGPNRLA GTARINAIAG RSPLAEFVLN
LADFKIGRVR VDGRQPHYTH RGGRLRIRPA KPVRAGAAFT VEVQWSGNPK PVNSPWGGLG
WEELEDGALV ASQPVGAPSW YPCNDRPADK ASYQISVTTP SAYAVVASGR LLTRTTKAST
TTWVYEQSAP TSSYLVGLAI GKYQTVLLGD PGPGGVPQHG HIPAHLLPEF SRDFARQPQM
MDLFQEVFGP YPFGEYAVVV TEEELDVPVE AQGLSLFGAN HVDGARSSER LVAHELAHQW
FGNSVSIADW RHIWLNEGLA KYAEWLWSER SGGRDAQHFA AVAHRLLSAQ PQDLKLADPG
RKSMFDDRLY ERGGLTVHAV RCAMGDEAFF RMLRNWAVLH RDGAVTTKTF TAHVNRFADE
PLDDLFAAWV HGAQLPPLPT QFPARPTHPP TNAESA
//
