ID Q1YEL1_AURMS Unreviewed; 882 AA.
AC Q1YEL1;
DT 02-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 02-MAY-2006, sequence version 1.
DT 24-JAN-2024, entry version 72.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=SI859A1_01064 {ECO:0000313|EMBL:EAS48580.1};
OS Aurantimonas manganoxydans (strain ATCC BAA-1229 / DSM 21871 / SI85-9A1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Aurantimonadaceae; Aurantimonas.
OX NCBI_TaxID=287752 {ECO:0000313|EMBL:EAS48580.1, ECO:0000313|Proteomes:UP000000321};
RN [1] {ECO:0000313|EMBL:EAS48580.1, ECO:0000313|Proteomes:UP000000321}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SI85-9A1 {ECO:0000313|EMBL:EAS48580.1,
RC ECO:0000313|Proteomes:UP000000321};
RX PubMed=18344346; DOI=10.1128/AEM.01656-07;
RA Dick G.J., Podell S., Johnson H.A., Rivera-Espinoza Y., Bernier-Latmani R.,
RA McCarthy J.K., Torpey J.W., Clement B.G., Gaasterland T., Tebo B.M.;
RT "Genomic insights into Mn(II) oxidation by the marine alphaproteobacterium
RT Aurantimonas sp. strain SI85-9A1.";
RL Appl. Environ. Microbiol. 74:2646-2658(2008).
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:EAS48580.1}.
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DR EMBL; AAPJ01000008; EAS48580.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1YEL1; -.
DR MEROPS; M01.005; -.
DR HOGENOM; CLU_007993_2_0_5; -.
DR BioCyc; AURANTIMONAS:SI859A1_01064-MONOMER; -.
DR Proteomes; UP000000321; 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:EAS48580.1};
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:UP000000321};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 95..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 233..444
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 452..554
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 559..882
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 882 AA; 97640 MW; 2FA65A2CEAB9B3D2 CRC64;
MLRIEDGQTI RLEDYRPTDF ILHCVDMTVR LFEGRAEIDT RLVLERREGV AEDAPLVLDG
DELTLTGLAL DGAVLEADAY TATPDRLTIR QAPARDRFLL DIATRTVPEE NTKLMGLYRS
NGIWCTQCEA EGFRRITYFL DRPDVLAPYR VRIEADRTAA PVLLSNGNPT ESGDLGDGRH
YAVWDDPFNK PAYLFALVAG DLDSIREPFT TASGKPVELA VYTEKGRAGQ AGYAMDALKR
SMVWDERRFG REYDLDVFNI VAIADFNMGA MENKGLNVFN HKYVLLDPQT ATDADYAGVE
TVIAHEYFHN WTGNRITCRD WFQLCLKEGL TVYRDQEFSA DERSATVQRI GAVRRLKAHQ
FPEDQGPLQH PVRPTEYKEI NNFYTATIYD KGAEIVRMLA TILGEDGFRK GMDLYFERHD
GDAATIEDYL ACFEAATGVD LSHLAVWYNQ AGTPTLSVHE DYDAGTDRLT VTLRQSLEPG
AAGTRTDPVH IPIRFGLVGS NGQDKDAVPT QGPDVEGDVI HLTEAETTLV FENLGERPYL
SILRDFSAPV NLDFAQSEAD RLALARLDPN LFNRWSVLND LIGEAMVRAC RAGGKETASP
LPAEIVDAVL ATAADPALEP AFRAQALALP AEPDVARMLG RDVDPQIVHD VVDAARRAIS
TAGVQVFERL AAEMATVQAF SPDAESAGRR ALANAALAYL TAATNDPAAA EAQYASASNM
TDRLAALGIL VHRFPDAPAS QAALDDFYRR FETDELVLDK WFALQATVPR PATLETVIAL
TGHARFSMRN PNRVRAVIGT FAAGNQLAFH RPDGAGYRWV AERLVELDRL NPQIAARIAT
TFRSWRSFEP TRRGQAEATL RQLLETEHLS TDLGDILGRS LK
//
