ID A0A1H8KLB4_9RHOB Unreviewed; 857 AA.
AC A0A1H8KLB4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SAMN04489859_10233 {ECO:0000313|EMBL:SEN93712.1};
OS Paracoccus alcaliphilus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=34002 {ECO:0000313|EMBL:SEN93712.1, ECO:0000313|Proteomes:UP000199054};
RN [1] {ECO:0000313|EMBL:SEN93712.1, ECO:0000313|Proteomes:UP000199054}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8512 {ECO:0000313|EMBL:SEN93712.1,
RC ECO:0000313|Proteomes:UP000199054};
RA de Groot N.N.;
RL Submitted (OCT-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; FODE01000023; SEN93712.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8KLB4; -.
DR STRING; 34002.SAMN04489859_10233; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000199054; 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:SEN93712.1};
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:UP000199054};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 78..185
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 224..438
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 443..534
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 539..853
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 857 AA; 95196 MW; 7438B7B22E07199F CRC64;
MTIEATANEQ FLADYRPYPF DLKQVALEFD LAPAATRVLA ALDFQPRESG ADLVLDGGKQ
IKLLSLTIDG AVPDAAHVSR DDETLTIAAA ALPSGPFRLE TEVQIDPSAN TAFEGLYLSG
GMFCTQCEAE GFRHITFYPD RPDVMTTFRV LVRSDQPVLL SNGNPVRQEP GLAEWHDPWP
KPSYLFALVA GDLVAVSDHF TTRSGRDVAL NVWVRPGDQD RAGFAMESLI KSMKWDEDAY
GREYDLDVFN IVAVDDFNMG AMENKGLNIF NSKLVLASPD TATDADYERI ESVIAHEYFH
NWTGNRITCR DWFQLCLKEG LTVFRDQQFT ADMRSAAVKR ISDVQSLRAR QFREDQGPLA
HPPRPDHYEE INNFYTATVY EKGAEVIGML KRLVGDDGYR KSLDLYFQRH DGDAATIEDW
LQVFEDATGR DLTQFKRWYT DAGTPRLKMA EDWGDGRLTL RFTQNTPPTP GQPDKPARVI
PISVGLIGPN GDEVLPSQIL EMTEASQSFS FDGLGARPVV SALRGFSAPV ILEREIDDAT
RAFLLAHDSD PFARWEAGRD LALSALLQLA QGNMAGDDYI AAIGQLIADE NADPAFRALC
LNLPSEEEIA TRLSARGVVP DPDAIHAART DLARRIAETH EALLSNLYRL MAVPGAYSPD
ADAAARRSLR IAVLGLLSRI DGGDRAEVLF GTAGNMTERM AALVCLIRRG RGQTALRLLE
EEFGDNRLVM DKWFMIQPMV APVAESVQIA QTLAKRKDFD WKNPNRFRAL LGGLAANHAG
FHRADGAGYA FTADWLMKMD RANPQIAARM STAFETWTRY DAGRREKALA ALQRMAAMEG
ISRNLREMVS RMIAARK
//
