ID C9PQU1_9PAST Unreviewed; 869 AA.
AC C9PQU1;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN Name=pepN {ECO:0000313|EMBL:EEX49842.1};
GN ORFNames=HMPREF0621_1365 {ECO:0000313|EMBL:EEX49842.1};
OS Pasteurella dagmatis ATCC 43325.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=667128 {ECO:0000313|EMBL:EEX49842.1, ECO:0000313|Proteomes:UP000005519};
RN [1] {ECO:0000313|EMBL:EEX49842.1, ECO:0000313|Proteomes:UP000005519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43325 {ECO:0000313|EMBL:EEX49842.1,
RC ECO:0000313|Proteomes:UP000005519};
RA Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA Petrosino J., Highlander S., Gibbs R.;
RL Submitted (OCT-2009) 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:EEX49842.1}.
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DR EMBL; ACZR01000014; EEX49842.1; -; Genomic_DNA.
DR RefSeq; WP_005762134.1; NZ_GG704810.1.
DR AlphaFoldDB; C9PQU1; -.
DR STRING; 667128.HMPREF0621_1365; -.
DR MEROPS; M01.005; -.
DR HOGENOM; CLU_007993_2_0_6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000005519; 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:EEX49842.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEX49842.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 23..187
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 226..438
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 445..545
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 550..869
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 869 AA; 100256 MW; 6BEA6DA46F9F0CA6 CRC64;
MQAKAKYRKD YKAPDFTVSN IFLDFQLNSK KTIVTATSQY KRLNPEAIKL RLDGHSFQFS
TIKLNGKDFK HFKQDSESLT LDLSQLKENQ FELEIVTILH PEKNTSLQGL YQSGEGICTQ
CEAEGFRQIT YMLDRPDVLA RYTTRITAEK SKYPYLLSNG NRITSGELPD GRHWVEWNDP
FPKPSYLFAL VAGDFDLLKD TFITKSGREV ALELYVDRGN LDRAAWAMQS LKRSMKWDEE
RFGLEYDLDI YMIVAVDFFN MGAMENKGLN IFNSKFVLAN PSTATDEDYL AVESVIAHEY
FHNWTGNRIT CRDWFQLSLK EGLTVFRDQE FTSDLWSRSG KRIEDVRLLR TAQFAEDASP
MSHPIRPEKV IEMNNFYTMT VYEKGAEVIR MMHTLLGEEG FQKGMRLYVE EQDGKAATCE
DFVSAMERAS GIDLTQFRHW YSQSGTPELT ISDSYDEQKA VYSLHVSQMT PPTSDQMEKV
NLHIPLKIAL YDKSGIPLTL ENEGKEVNPV LDVKQTEQTF TFTNIHSKPV PALLCDFSAP
VKLNYEYSTA QLVTLLRHAE NHFVRWDVAQ MLYSMELRRN LTRHQQSKTL EFSAEILSEL
YQVLDHYQQD PELATLILTL PKVTEFAELF KTIDPEGITF VRDFMVRTIA ESLKQTLLKV
YNEIRLDEYR VTAEDITLRA LRNLCVSYLA YTTVGNNIVN KHYSYANNMT DTLAALSAAT
KAQLPCRDSL LADFESKWQH DGLVMDKWFA LQATRPDEDV LLNVMKLMDH PSFNFNNPNR
LRALVGSFAN QNLKAFHAID GSGYRFLTDV LIRLNESNPQ VASRLIEPLI RFSRYDGQRQ
TLMKRGLERI SELEKVSRDL YEKIEKALQ
//
