ID Q2L1X8_BORA1 Unreviewed; 219 AA.
AC Q2L1X8;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=Glutathione S-transferase {ECO:0000313|EMBL:CAJ47668.1};
GN OrderedLocusNames=BAV0077 {ECO:0000313|EMBL:CAJ47668.1};
OS Bordetella avium (strain 197N).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=360910 {ECO:0000313|EMBL:CAJ47668.1, ECO:0000313|Proteomes:UP000001977};
RN [1] {ECO:0000313|EMBL:CAJ47668.1, ECO:0000313|Proteomes:UP000001977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=197N {ECO:0000313|EMBL:CAJ47668.1,
RC ECO:0000313|Proteomes:UP000001977};
RX PubMed=16885469; DOI=10.1128/JB.01927-05;
RA Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D., King N.D.,
RA Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D., Goble A., Lord A.,
RA Murphy L., Quail M.A., Rutter S., Squares R., Squares S., Woodward J.,
RA Parkhill J., Temple L.M.;
RT "Comparison of the genome sequence of the poultry pathogen Bordetella avium
RT with those of B. bronchiseptica, B. pertussis, and B. parapertussis reveals
RT extensive diversity in surface structures associated with host
RT interaction.";
RL J. Bacteriol. 188:6002-6015(2006).
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; AM167904; CAJ47668.1; -; Genomic_DNA.
DR RefSeq; WP_012415780.1; NC_010645.1.
DR AlphaFoldDB; Q2L1X8; -.
DR STRING; 360910.BAV0077; -.
DR GeneID; 41392007; -.
DR KEGG; bav:BAV0077; -.
DR eggNOG; COG0625; Bacteria.
DR HOGENOM; CLU_070658_0_0_4; -.
DR OrthoDB; 9799538at2; -.
DR Proteomes; UP000001977; Chromosome.
DR CDD; cd03194; GST_C_3; 1.
DR CDD; cd03043; GST_N_1; 1.
DR Gene3D; 1.20.1050.10; -; 1.
DR Gene3D; 3.40.30.10; Glutaredoxin; 1.
DR InterPro; IPR036282; Glutathione-S-Trfase_C_sf.
DR InterPro; IPR040079; Glutathione_S-Trfase.
DR InterPro; IPR004045; Glutathione_S-Trfase_N.
DR InterPro; IPR036249; Thioredoxin-like_sf.
DR PANTHER; PTHR42673; MALEYLACETOACETATE ISOMERASE; 1.
DR PANTHER; PTHR42673:SF4; MALEYLACETOACETATE ISOMERASE; 1.
DR Pfam; PF13410; GST_C_2; 1.
DR Pfam; PF13409; GST_N_2; 1.
DR SFLD; SFLDS00019; Glutathione_Transferase_(cytos; 1.
DR SFLD; SFLDG00358; Main_(cytGST); 1.
DR SUPFAM; SSF47616; GST C-terminal domain-like; 1.
DR SUPFAM; SSF52833; Thioredoxin-like; 1.
DR PROSITE; PS50404; GST_NTER; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000001977}.
FT DOMAIN 2..82
FT /note="GST N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS50404"
SQ SEQUENCE 219 AA; 24555 MW; E2DF6473504D4627 CRC64;
MYTLWIGNKN YSSWSLRAWL ALRVAGIAFQ EQKLALFTDS FSQHLGSLTP AGLVPVLRDG
DLVIWDSLAI CEYAAEQHPD RHLWPACSRA RARARSLASQ MHSGFTTLRT LLPMNIEAHL
PNIDIEAAKP EIARVQTLWQ NTRAEFGDGG PFLFGRFSIA DAFFAPVVSR FTTYGVAANG
PVRNYMDAIQ ALPAMREWTR DALAEATFVA QDEPYRSHR
//
