ID C0DRT5_EIKCO Unreviewed; 889 AA.
AC C0DRT5;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 24-JAN-2024, entry version 58.
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:EEG25231.1};
GN ORFNames=EIKCOROL_00050 {ECO:0000313|EMBL:EEG25231.1};
OS Eikenella corrodens ATCC 23834.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Eikenella.
OX NCBI_TaxID=546274 {ECO:0000313|EMBL:EEG25231.1, ECO:0000313|Proteomes:UP000005837};
RN [1] {ECO:0000313|EMBL:EEG25231.1, ECO:0000313|Proteomes:UP000005837}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23834 {ECO:0000313|EMBL:EEG25231.1,
RC ECO:0000313|Proteomes:UP000005837};
RA Fulton L., Clifton S., Chinwalla A.T., Mitreva M., Sodergren E.,
RA Weinstock G., Clifton S., Dooling D.J., Fulton B., Minx P., Pepin K.H.,
RA Johnson M., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-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:EEG25231.1}.
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DR EMBL; ACEA01000002; EEG25231.1; -; Genomic_DNA.
DR RefSeq; WP_003821719.1; NZ_EQ973316.1.
DR AlphaFoldDB; C0DRT5; -.
DR MEROPS; M01.005; -.
DR GeneID; 60770786; -.
DR eggNOG; COG0308; Bacteria.
DR HOGENOM; CLU_007993_2_0_4; -.
DR Proteomes; UP000005837; 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:EEG25231.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:EEG25231.1};
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 89..187
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 227..437
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 445..553
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 558..886
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 889 AA; 99640 MW; 19BECAF91AA5CA93 CRC64;
MPQQTAHYLK DYRAPEYLVP HIRLNFDVYD DHIAVTAELS IQPQPDAGGT LVLQGSAELV
SLELNGQRLP ETTYTLENNT LSIPNVPAQP FKLSVATRLY PHQNKSLMGL YASGGNLYTQ
CEPEGFRKIT YHPDRPDVMG IYTTRISADR ARFPVLLSNG NRIGHGTLPD NRHWAEWHDP
FAKPSYLFAL VAGDLVCTRD SFTTRSGRQV ALEFFTRAED AGKVRFGIES LKHAMRWDET
RFGLEYDLDI FMVVAVGDFN MGAMENKGLN IFNTACVLAD SRTATDADFE RVEGVIAHEY
FHNWTGNRVT CRDWFQLSLK EGLTVFRDQE FSADRASREV RRIENVSFLR AHQFPEDAGP
TSHPVRPASY VEMNNFYTLT VYEKGAEVVR MYHTFLGEEG FQKGMKLYFQ RHDGQAVTCD
DFRAAMADAN GFDFEQFALW YSQAGTPVLD VSGSLQTGNR FVLNIRQSIP PTPDMAAKQP
MMIPLKIALF SADEDTFGQP VPFRLPENGH TQTEAVLTLR QAEESVALQF EGNYQQVVPS
LLRGFSAPVN LHYAYSEHEL SVLLACDSDP FSRWEAAQTL YRRAIAANEA ALLSGSPLPE
HHALLQAIDY VLRADISAAF QAALLAIPNE AELWAGRQNI DPLIVHRARE ALLDLIAAHF
ADQFAALNTE ARHMEEEQSG LAEPYEYRPQ QAGWRALRNA CRAFILRARP GHIEQVAANY
NQMARNMTHE WGILSAVNHN DRPERNRLLE QFAAKFHSDD LVMCKYFSLV AASHRADTPA
QVAAALEHPA FSLENPNKAR ALLGSFSRNV PHFHAADGSG YAFLAGQIGC IDRFNPQIAA
RLAQAFNICA QLEPQRRSLM RAELQKLAEN LALSKDSGEI IGKILQASA
//
