ID A0A0D0QC85_9RHOB Unreviewed; 850 AA.
AC A0A0D0QC85;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=Wenmar_02834 {ECO:0000313|EMBL:KIQ68563.1};
OS Wenxinia marina DSM 24838.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Wenxinia.
OX NCBI_TaxID=1123501 {ECO:0000313|EMBL:KIQ68563.1, ECO:0000313|Proteomes:UP000035100};
RN [1] {ECO:0000313|EMBL:KIQ68563.1, ECO:0000313|Proteomes:UP000035100}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24838 {ECO:0000313|EMBL:KIQ68563.1,
RC ECO:0000313|Proteomes:UP000035100};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (JAN-2013) 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:KIQ68563.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AONG01000013; KIQ68563.1; -; Genomic_DNA.
DR RefSeq; WP_018303932.1; NZ_KN848374.1.
DR AlphaFoldDB; A0A0D0QC85; -.
DR STRING; 1123501.Wenmar_02834; -.
DR MEROPS; M01.005; -.
DR PATRIC; fig|1123501.6.peg.2949; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000035100; 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:KIQ68563.1};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:KIQ68563.1};
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:UP000035100};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 105..179
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 218..429
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 437..528
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 532..848
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 850 AA; 94165 MW; B10B57C49BA0BE3C CRC64;
MKDAAPQTIH LADYAPPPWL VERVELTFRL APTATRVLSR IRFVPNPATS DRRFFLHGEG
LKTLSARIDG AEVTPREVPG GIEADVPDGA FTWEAEVEVD PAGNTALEGL YMSNGMYCTQ
CEAEGFRKIT WYPDRPDVMA PFRVRIESDL PVLLSNGNPA GSGDGWAEWD DPWPKPAYLF
ALVAGDLVAH RDTFVTMSGR EVALGIWVRA GDEDRCAFAM EALKASMRWD EEVYGREYDL
DVFNIVAVDD FNMGAMENKG LNIFNSALVL ASPDTATDAT FERIEAVIAH EYFHNWTGNR
VTCRDWFQLC LKEGLTVYRD QQFTSDMRSA AVKRIEDASL MRTRQFREDG GPLAHPVRPE
SFVEINNFYT ITVYEKGAEL IGMLKRLVGD DGYRKAVDLY FQRHDGEAAT IEDWLAAFEE
ATGRDLSQFK LWYSQAGTPR LTVSEQWEDG TYTLTFRQET PPTPGQTDKQ PLVIPLAVGL
LNPNGDEVVP TTVLEMTKEE QSFTFDGLAS RPVPSILRNF SAPVRLDRAT TDAERAFLLA
HDTDPYNKWD AGRALAMSAL TAAATDGTAP GADYLDGLGR TLRDETLDPA FRALVLSLPS
EDEIAQALHA AGTTPDPDAI HAGRRAVQEA IAGAHEATLA DLHERMQPTG PYRPDADDAG
RRSLANAALA LLTRIDGGAR ARTQFAAADN MTQSVAALAA LLAIGAGEDQ SQTYHDRWQG
ERLVMDRWFG LRAGLAPAEQ ALDTTQELAR HPAFHWKTPN RFRALVGGFA NNHAGFHRAD
GRGYEFVTDW LLKLDPLNPQ TAAGMSKVFE TWGRYDAERQ GKIRACLRRI AGTDRLSRDL
GEMVQRMLGD
//
