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Database: UniProt
Entry: E3HVX7_ACHXA
LinkDB: E3HVX7_ACHXA
Original site: E3HVX7_ACHXA 
ID   E3HVX7_ACHXA            Unreviewed;       201 AA.
AC   E3HVX7;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   SubName: Full=Thiamine pyrophosphate enzyme, C-terminal TPP binding domain protein 11 {ECO:0000313|EMBL:ADP16290.1};
GN   OrderedLocusNames=AXYL_02970 {ECO:0000313|EMBL:ADP16290.1};
OS   Achromobacter xylosoxidans (strain A8).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=762376 {ECO:0000313|EMBL:ADP16290.1, ECO:0000313|Proteomes:UP000006876};
RN   [1] {ECO:0000313|EMBL:ADP16290.1, ECO:0000313|Proteomes:UP000006876}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A8 {ECO:0000313|EMBL:ADP16290.1,
RC   ECO:0000313|Proteomes:UP000006876};
RX   PubMed=21097610; DOI=10.1128/JB.01299-10;
RA   Strnad H., Ridl J., Paces J., Kolar M., Vlcek C., Paces V.;
RT   "Complete genome sequence of the haloaromatic acids-degrading bacterium
RT   Achromobacter xylosoxidans A8.";
RL   J. Bacteriol. 193:791-792(2011).
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DR   EMBL; CP002287; ADP16290.1; -; Genomic_DNA.
DR   AlphaFoldDB; E3HVX7; -.
DR   STRING; 762376.AXYL_02970; -.
DR   KEGG; axy:AXYL_02970; -.
DR   PATRIC; fig|762376.5.peg.2988; -.
DR   eggNOG; COG0028; Bacteria.
DR   HOGENOM; CLU_117492_0_0_4; -.
DR   OrthoDB; 6843902at2; -.
DR   Proteomes; UP000006876; Chromosome.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR000399; TPP-bd_CS.
DR   InterPro; IPR011766; TPP_enzyme_TPP-bd.
DR   PANTHER; PTHR42818:SF1; SULFOPYRUVATE DECARBOXYLASE; 1.
DR   PANTHER; PTHR42818; SULFOPYRUVATE DECARBOXYLASE SUBUNIT ALPHA; 1.
DR   Pfam; PF02775; TPP_enzyme_C; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR   PROSITE; PS00187; TPP_ENZYMES; 1.
PE   4: Predicted;
FT   DOMAIN          35..159
FT                   /note="Thiamine pyrophosphate enzyme TPP-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02775"
SQ   SEQUENCE   201 AA;  20477 MW;  19BA815F6458C7C5 CRC64;
     MPMTTLEACR AIHAARGDAV VVSTMSAMKA MDEVAPGAPL ALSSVPLMGG AAGLALGIAL
     AQPARAVLVL DGDASLLMEL GVLATVAGAA PRRYIHFVFA NGVQFNGNAN LGMPGGGRVD
     FAAAAMAAGY AAAFHIGDAR ELATSLPDIM AAASPVLVEL AITPCPPVLG KDNPFPEQPD
     KRFQRMGDEA ARLREQLGAD S
//
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