ID I9C5N0_9SPHN Unreviewed; 883 AA.
AC I9C5N0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=WSK_2329 {ECO:0000313|EMBL:EIZ79142.1};
OS Novosphingobium sp. Rr 2-17.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=555793 {ECO:0000313|EMBL:EIZ79142.1, ECO:0000313|Proteomes:UP000004732};
RN [1] {ECO:0000313|EMBL:EIZ79142.1, ECO:0000313|Proteomes:UP000004732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RR2-17 {ECO:0000313|Proteomes:UP000004732};
RX PubMed=22933764; DOI=10.1128/JB.01159-12;
RA Gan H.M., Chew T.H., Hudson A.O., Savka M.A.;
RT "Genome Sequence of Novosphingobium sp. Strain Rr 2-17, a Nopaline Crown
RT Gall-Associated Bacterium Isolated from Vitis vinifera L. Grapevine.";
RL J. Bacteriol. 194:5137-5138(2012).
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:EIZ79142.1}.
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DR EMBL; AKFJ01000083; EIZ79142.1; -; Genomic_DNA.
DR RefSeq; WP_008995262.1; NZ_AKFJ01000083.1.
DR AlphaFoldDB; I9C5N0; -.
DR MEROPS; M01.005; -.
DR PATRIC; fig|555793.3.peg.2280; -.
DR eggNOG; COG0308; Bacteria.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000004732; 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:EIZ79142.1};
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:UP000004732};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 123..208
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 248..461
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 466..557
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 562..882
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 883 AA; 96894 MW; 7C46EFFCE886CD45 CRC64;
MDIVSTPAEP QNLQVADAAP PPPAPAVIKR EDYLPPAWLV PEITLDFRLG LEETRVASVL
QVRRNPAGNG TDTLRLNGDQ IAPASVKVDG VAIEDWRLDG PDLLVPLTGE AHEVAIETIV
NPAANSQLMG LYASNGMLCT QCEAEGFRRI TFFPDRPDVL STYTVRMSGP KAAFPILLAN
GNCTASGEGE DGTHWAEWHD PWPKPSYLFA LVAGDLVANN AHFTTMGGRE VELNIWVRPG
DEGRTQHAMD SLINSMKWDE EAFGREYDLD LFNIVAVSDF NMGAMENKGL NVFNTRYVLA
DPETATDGDY DAVEGVIGHE YFHNWSGNRV TCRDWFQLSL KEGFTVLRDQ LFSAAMGSEA
VKRIEDVRIL RSAQFPEDSG PLAHPIRPDS YQEISNFYTA TVYNKGAEVI RMMRTMAGPD
VFRKGTDLYF DRHDGEAATC EDFVTSIEEG TGLDLAQFRQ WYSQAGTPQL EVELVHEGTQ
ARLTLTQLVP PTPGQPTKAP MPIPLRVALF DRASGRHDGE QLIVLDKVSD TFVFDGFASA
PVISINRGFS APVSIQFERD PDDLVFLAAH DDDPFARYEA TQSLVVQHLV AAVGGSLSDA
QHRAGRAAIG EAFSAVLTDP ALDDLMRGEL MILPAGSYLA EQFALADPAR IQDEREALKA
WLGTECMAAL TALHDRAVAV PYGRDAAARG ARKIKTGALT FIAAADPAEG ARRAIAQYRA
ADNMTDRQGA VMVLASLDAP EREEALADFR QRYEGNALVI DKWFSLQAGS LHPRVLEHIR
SLANHPDFAL TNPNRARSLY MAAAVNPVAF HDASGEGYRL IGDLIRRLDP INPQTAARFV
PALGRWRRIE PVRAALMRAE LERIAAEPSL SRDVREQVSK SLG
//