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Database: UniProt
Entry: G8PTX4_PSEUV
LinkDB: G8PTX4_PSEUV
Original site: G8PTX4_PSEUV 
ID   G8PTX4_PSEUV            Unreviewed;       380 AA.
AC   G8PTX4;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
DE   SubName: Full=NUDIX hydrolase {ECO:0000313|EMBL:AEV38726.1};
GN   OrderedLocusNames=PSE_4222 {ECO:0000313|EMBL:AEV38726.1};
OS   Pseudovibrio sp. (strain FO-BEG1).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Stappiaceae; Pseudovibrio.
OX   NCBI_TaxID=911045 {ECO:0000313|EMBL:AEV38726.1, ECO:0000313|Proteomes:UP000005634};
RN   [1] {ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|Proteomes:UP000005634};
RA   Bondarev V., Richter M., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile and symbiotically
RT   interacting bacteria.";
RL   Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEV38726.1, ECO:0000313|Proteomes:UP000005634}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FO-BEG1 {ECO:0000313|EMBL:AEV38726.1,
RC   ECO:0000313|Proteomes:UP000005634};
RX   PubMed=23601235; DOI=10.1111/1462-2920.12123;
RA   Bondarev V., Richter M., Romano S., Piel J., Schwedt A., Schulz-Vogt H.N.;
RT   "The genus Pseudovibrio contains metabolically versatile bacteria adapted
RT   for symbiosis.";
RL   Environ. Microbiol. 15:2095-2113(2013).
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DR   EMBL; CP003147; AEV38726.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8PTX4; -.
DR   STRING; 911045.PSE_4222; -.
DR   KEGG; psf:PSE_4222; -.
DR   eggNOG; COG0454; Bacteria.
DR   HOGENOM; CLU_727350_0_0_5; -.
DR   Proteomes; UP000005634; Chromosome.
DR   GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   CDD; cd04301; NAT_SF; 1.
DR   CDD; cd02883; Nudix_Hydrolase; 1.
DR   Gene3D; 3.40.630.30; -; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   PANTHER; PTHR43877; -; 1.
DR   PANTHER; PTHR43877:SF2; AMINOALKYLPHOSPHONATE N-ACETYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51186; GNAT; 1.
DR   PROSITE; PS51462; NUDIX; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:AEV38726.1}.
FT   DOMAIN          1..149
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000259|PROSITE:PS51186"
FT   DOMAIN          234..380
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   380 AA;  42190 MW;  D4ADF3482BE42331 CRC64;
     MRPAEKSQAI ALTNIMHTAK GHWGYDPQDM QEFRDHWKIT PEMIDKDPIL VISEEDHPIG
     FARVLKESTE VALLDCLFVL PEAHGKGHGA WLLEGAEEIA KRMQCTQLRL ESDANAAPFY
     AHHGYHSTSN RPSAFQGAGP IEHMQKDLTP QIHKVSEIDL KLDMAATWDF ATNNSEAIKA
     NWQTLISDNP DLWDGKVLSL YQYSFDNAQF TGELVEINYS EFLAWRDWGF PDRSAKNLFG
     CAVLRSREGH LVFGKMAGNT ATAGQVYPPG GNLDLNDITP SGEVDIFGSI ARELEEETGL
     TLDQGDLGEV LAIEDGPRLA IARILTLQLS SDEILSKISH FNANQEKPEL EEAVIITSPE
     DLKAYSVPPY AIALTAHLLN
//
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