ID A0A2S6NAZ6_RHOGL Unreviewed; 878 AA.
AC A0A2S6NAZ6;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=Aminopeptidase N {ECO:0000256|ARBA:ARBA00015611};
DE EC=3.4.11.2 {ECO:0000256|ARBA:ARBA00012564};
GN ORFNames=CCS01_16340 {ECO:0000313|EMBL:PPQ31788.1};
OS Rhodopila globiformis (Rhodopseudomonas globiformis).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Rhodopila.
OX NCBI_TaxID=1071 {ECO:0000313|EMBL:PPQ31788.1, ECO:0000313|Proteomes:UP000239724};
RN [1] {ECO:0000313|EMBL:PPQ31788.1, ECO:0000313|Proteomes:UP000239724}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 161 {ECO:0000313|EMBL:PPQ31788.1,
RC ECO:0000313|Proteomes:UP000239724};
RX PubMed=29423563;
RA Imhoff J.F., Rahn T., Kunzel S., Neulinger S.C.;
RT "New insights into the metabolic potential of the phototrophic purple
RT bacterium Rhodopila globiformis DSM 161(T) from its draft genome sequence
RT and evidence for a vanadium-dependent nitrogenase.";
RL Arch. Microbiol. 0:0-0(2018).
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:PPQ31788.1}.
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DR EMBL; NHRY01000182; PPQ31788.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S6NAZ6; -.
DR OrthoDB; 100605at2; -.
DR Proteomes; UP000239724; 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:PPQ31788.1};
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:UP000239724};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT DOMAIN 102..194
FT /note="Aminopeptidase N-like N-terminal"
FT /evidence="ECO:0000259|Pfam:PF17900"
FT DOMAIN 234..447
FT /note="Peptidase M1 membrane alanine aminopeptidase"
FT /evidence="ECO:0000259|Pfam:PF01433"
FT DOMAIN 452..555
FT /note="Peptidase M1 alanyl aminopeptidase Ig-like fold"
FT /evidence="ECO:0000259|Pfam:PF11940"
FT DOMAIN 560..878
FT /note="Peptidase M1 alanyl aminopeptidase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF17432"
SQ SEQUENCE 878 AA; 96135 MW; 15A3ECF345DF7E18 CRC64;
MPADSIRTDA APVEVRLADY APPAYLVDTV DLTFELGETA TMVVSKLSVR RNPAAPDDAP
LHLDGEALTL VDVTCNGAPV TPVETRDGLT ITDVPATAVL EITTSLTPIA NTEFSGLYVS
GGNYYTQCEA QGFRRITYFP DRPDVMSRYT TTIIADKAAC PVMLSNGNPG PVKDLGDGRH
GITWTDPHPK PCYLFALVAG DLVSVKDSFT TRSGRHVDLA IYVRRGDEDR CAHAMQALKT
SMAWDEQVFG LEYDLDVFNI AAVSDFNMGA MENKGLNVFN TKYVLARPET ATDVDYQGIE
TVIAHEYFHN WTGNRVTCRD WFQLSLKEGL TVYRDQEFSA DQSSRAVKRI GDVRGLRAAQ
FREDAGPLAH PVQPSAYMAI DNFYTATVYN KGAEVIRMMA TIIGRQAFRR GMDLYFARHD
NQAVTIDDFV QAMQDASGVD LTAFKRWYHQ AGTPDVSVED SYDAAAKRYT LTISQETKPT
PGQPEKLPLV IPVAMGLLDG NGQELATRLE GEAAAKPGTR VLLATQATNR FEFVDVASPP
VPSLLRDFSA PVKLSGLSPE RLRFLAAHDT DPFVRWDSGQ QVAASVLLDM VATFQQGRQP
GVDPALFEAV GSLLDQEPAF AAEALALPGE STLADKMTVV DVDAIHTARD RARTAIGQAL
YDRLRATYDR LSDTGPYRID GASIGRRSLR NGCLSYLVAS GDAAAVRLAK AQFDAGQNMT
DVLAALGILS GVDCPERLDA LAAFYQAWRH DPLVLDKWFA IQALSPLPDT VQAVQALKAH
ADFDLRNPNR IRALISSFAG NQVRFHDPSG AGYRLYADTI IQLDPTNGQV AARMVSPLGQ
WRRYDAARQA LMKQELQRIL DLPNLSRNTF EMASKSLA
//
