ID A0A076HRZ0_9BACT Unreviewed; 799 AA.
AC A0A076HRZ0;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=N008_11255 {ECO:0000313|EMBL:AII52550.1};
OS Hymenobacter sp. APR13.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC Hymenobacter.
OX NCBI_TaxID=1356852 {ECO:0000313|EMBL:AII52550.1, ECO:0000313|Proteomes:UP000028590};
RN [1] {ECO:0000313|EMBL:AII52550.1, ECO:0000313|Proteomes:UP000028590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APR13 {ECO:0000313|EMBL:AII52550.1,
RC ECO:0000313|Proteomes:UP000028590};
RA Li P., Jiang J., Kwok A.H.Y., Lou X., Xu D., Leung F.C.C.;
RT "Complete genome sequence assembly of Hymenobacter sp. APR13.";
RL Submitted (JUL-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 ---------------------------------------------------------------------------
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; CP006587; AII52550.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A076HRZ0; -.
DR STRING; 1356852.N008_11255; -.
DR KEGG; hym:N008_11255; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_014298_0_0_10; -.
DR Proteomes; UP000028590; Chromosome.
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; 1.25.10.10; Leucine-rich Repeat Variant; 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; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000357; HEAT.
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; PF02985; HEAT; 1.
DR Pfam; PF13646; HEAT_2; 1.
DR Pfam; PF01433; Peptidase_M1; 1.
DR Pfam; PF17900; Peptidase_M1_N; 1.
DR PRINTS; PR00756; ALADIPTASE.
DR SUPFAM; SSF48371; ARM repeat; 1.
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:UP000028590};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 15..202
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 240..448
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
SQ SEQUENCE 799 AA; 91039 MW; 413EA3347C2736DF CRC64;
MQPAATILHD LLDTKLDVRF DWAKQWLLGT ATLTVKPHFY PQTQLVLDAK GFDIKSVKLV
NGGKEKNLTY TYDKKKLTIT LDRTYARTEP CQVRIQYVAK PNELEVGGSA AITQDKGLYF
INPLGTDKTK PRQLWTQGET EGNSCWFPTI DRPNQRMTQE ISLTVDSELK TLSNGLLTSS
RKNSDGTRTD TWKQSLAHAP YLTMVAVGDF AVISDTWRGK PVDYYVDPKF SNTARAVFGN
TPQMLDYFSK KLGVDFPWEK YTQVAVHDFV SGAMENTTAV TFEQSLVQFA PRELADVGYD
AESTVAHELF HHWFGDYVTT ESWANLPLNE SFADYSELLW AEHKYGADAA GLVQQEKLNR
YLEEAQSKRE PLIRYRYAKQ EDMFDRHSYD KGGRVLHMLR NYVGDDAFFA SLNRYLTQNK
FSTSEIAKLR IAFEETTGED LMWFFDQWFM QRGHPELKVT HSFANGQVSM RVQQLQDSTF
TPIYRLPVTV TVWANNQPTD HRITVTKADQ TFRLPSSQRP GLVKFDSQAQ LLAEIEEERT
QDELMYQYTH AKNYLQRYEA VTQLKAKSAE LSVSTLLRNV LNDPFWAVRQ AAVQALRRYK
GPEGNAVRQD LQQVAMKDKS SQVRATALNA LASFSNENYS SAFLTALNDS SYKVVSAGIQ
ALAKTPTADS QEKVAAMQES QNAEVLTSIA TYYSLNGSST EQYQWFMRRL PDVSDADLYR
SYLPDFATFM LRMPPIERDK GIQRLESLAR TAPSTFVRLG AYRGLSILAS SMPTLKATLQ
DIRSKEKDEQ VKAYYAMMQ
//
