ID A0A1X3CKM2_9NEIS Unreviewed; 876 AA.
AC A0A1X3CKM2;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=BWD10_11590 {ECO:0000313|EMBL:OSI08113.1};
OS Neisseria zoodegmatis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=326523 {ECO:0000313|EMBL:OSI08113.1, ECO:0000313|Proteomes:UP000193466};
RN [1] {ECO:0000313|EMBL:OSI08113.1, ECO:0000313|Proteomes:UP000193466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21643 {ECO:0000313|EMBL:OSI08113.1,
RC ECO:0000313|Proteomes:UP000193466};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OSI08113.1}.
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DR EMBL; MTBM01000023; OSI08113.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X3CKM2; -.
DR STRING; 326523.BWD10_11590; -.
DR Proteomes; UP000193466; 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:OSI08113.1};
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 Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 85..183
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 222..433
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 441..545
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 548..876
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 876 AA; 98225 MW; 6466009A34F60DE4 CRC64;
MTQTVHYLKD YQAPAYSVAN TDLYFDIHDR YMVVRADLHI QPQQPGAPLV LDGSAELLSV
NINGTEVEDY TLADEKLVLA QVPSEPFTLS VETLIRPSEN KSLMGLYASG GNLFTQCEPE
GFRKITFYPD RPDVMSVFTV TITADAARYP VMLSNGNKVD GGTLSDGRHW VKWADPFAKP
SYLFALVAGD LSLTRDTFTT ASGREVAIEF YTRAEDAGKV DFAVQSLKHA MKWDETRFGL
EYDLDIYMVV AVGDFNMGAM ENKGLNIFNT KYVLADSRTA TDADFAGIES VIAHEYFHNW
TGNRVTCRDW FQLSLKEGLT VFRDQEFSAD RIDHGTCRID NVAMLRQHQF PEDAGPTAHP
VRPAFYEEMN NFYTMTVYEK GAEVVRMYHT FLGEAGFQKG MKLYFERHDG QAVTCDDFRA
AMADANGFDF SRFALWYSQA GTPVLDVTGR LKDNGDYVLN VKQTVPPTPD MADKQPMMMP
LKIALFDAQT GRPVAFRRPE SDTAQTEAVL AVTQAEQEFV LHGVGVPVVP SLLRGFSAPV
HLNYDYSDEE LSVLLSADTD PFARWEAGQT LYRRAIAANE AALREGRPLP QHATLLKAFE
YVLDADISAG FKAMLLQVPP ETELWADGEN IDPLLVHRAR EALLDKLAVQ FKQHFMALNE
QSAAKEQAAD EAVRYEYSPE LAGWRSLRNI CRAFVLRADP DHIRVVAERY AAMVKNMTHE
WGILSAVNHN PHDTRNQLLA AFAEKFSEDA LVMDKYFALI ASSHRNDTPE QIQTALAHPK
FSLENPNKAR ALLGAFTRNV PHFHAQDGSG YAFIAAKVME IDRFNPQVAS RLVQAFNICN
KLEPTRRELM KAQLQQIQQQ SGLSKDVSEI VGKILA
//
