ID A0A196QND4_9RHOB Unreviewed; 853 AA.
AC A0A196QND4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=A8B74_17070 {ECO:0000313|EMBL:OAN93186.1};
OS Sulfitobacter geojensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=1342299 {ECO:0000313|EMBL:OAN93186.1, ECO:0000313|Proteomes:UP000078317};
RN [1] {ECO:0000313|Proteomes:UP000078317}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EhN01 {ECO:0000313|Proteomes:UP000078317};
RA Rosana A., Orata F., Boucher Y., Case R.;
RL Submitted (MAY-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}.
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:OAN93186.1}.
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DR EMBL; LXYM01000015; OAN93186.1; -; Genomic_DNA.
DR RefSeq; WP_064223546.1; NZ_LXYM01000015.1.
DR AlphaFoldDB; A0A196QND4; -.
DR STRING; 1342299.Z947_3098; -.
DR eggNOG; COG0308; Bacteria.
DR Proteomes; UP000078317; 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:OAN93186.1};
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:UP000078317};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 108..182
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 222..435
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 440..531
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 535..850
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 853 AA; 94608 MW; 9051E004EE5915E7 CRC64;
MRDAAPKTIF LSDYTPYPWT VDSVDLHFTL DPHATRVRSV IRFAPNPAFT GETPKTMFLH
GEQIKLISAQ IDATAVDPDL TGEGLTCAVP GGPFTWESEV EIDPANNTAL EGLYMSNGMY
CTQCEAEGFR KITFYPDRPD VMSVFTVTVE GPHPVLLSNG NPVVTENHLA KWHDPWPKPA
YLFALVAGDL VAHSDSFTTM SGRHVDLNLY VRPGDEGKCA FGMQALKASM KWDEDVYGRE
YDLDLFNIVA VDDFNMGAME NKGLNIFNSS AVLASPETST DLNFERIEAI IAHEYFHNWT
GNRITCRDWF QLCLKEGLTV YRDSQFTSDM RSAPVKRISD VIDLRGRQFA EDQGPLAHPV
RPESFQEINN FYTATVYEKG AEVIGMLKTL VGDEAYYKAL DLYFTRHDGD AATIEDWLKV
FEDSTGRDLA QFKRWYSQAG TPRLSVAYSF ELDTLTLTFT QHTPPSAATP DPQPQVIPIA
VGLIYPDGTE ALETRVLEMT KATQSFRFTG LEDEPVPSIL RGFSAPVVLT HDLSDADRAH
LLAHDTDPFN RWEQGRMLAR KSLLAMITEG ADPDPAYLAG IHKVATDTTL DPATRALMLD
MPSEAELATV LHEAGTTPDP AAIYAAREAM AEARADAFAD VAADIYAANT VTEAYQPNAD
QAGRRVLGNA MLAMITRRDA GAQAAAQYDS ADNMNQQLVA LALLVGAGKG DEKLQAFEKQ
WQDDRLVMDK WFGLQVSKAK PEDAAAKARR LTEHPAFTHT NPNRFRAVFG ALVMHHAGFH
HASGDAYTLL ADWLITLDPL NPQTTARMCS AFQTWKRYDS DRQAKMLTEI TRILATPNLS
RDTTEMLTRI KGA
//
