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Database: UniProt
Entry: E1V9X0_HALED
LinkDB: E1V9X0_HALED
Original site: E1V9X0_HALED 
ID   E1V9X0_HALED            Unreviewed;       276 AA.
AC   E1V9X0;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 57.
DE   SubName: Full=Transketolase_Nterm domain protein {ECO:0000313|EMBL:CBV43858.1};
GN   OrderedLocusNames=HELO_3974 {ECO:0000313|EMBL:CBV43858.1};
OS   Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS   / 1H9).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV43858.1, ECO:0000313|Proteomes:UP000008707};
RN   [1] {ECO:0000313|Proteomes:UP000008707}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC   {ECO:0000313|Proteomes:UP000008707};
RX   PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA   Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA   Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA   Kunte H.J.;
RT   "A blueprint of ectoine metabolism from the genome of the industrial
RT   producer Halomonas elongata DSM 2581(T).";
RL   Environ. Microbiol. 13:1973-1994(2011).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; FN869568; CBV43858.1; -; Genomic_DNA.
DR   AlphaFoldDB; E1V9X0; -.
DR   STRING; 768066.HELO_3974; -.
DR   KEGG; hel:HELO_3974; -.
DR   eggNOG; COG3959; Bacteria.
DR   HOGENOM; CLU_009227_4_1_6; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000008707; Chromosome.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR47514; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   PANTHER; PTHR47514:SF1; TRANSKETOLASE N-TERMINAL SECTION-RELATED; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
PE   4: Predicted;
FT   DOMAIN          17..256
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
SQ   SEQUENCE   276 AA;  30251 MW;  935F98F55345FE68 CRC64;
     MTLRPLGPDE LAQQCREMRK TIIKTIGNAN MGHIGGDLSV IDILGTLYFN VLKVNPDEPT
     APERDRFIMS KGHCAVALYT TMAHAGYFPV EELSTFVQPQ SRLNGHPCNE KLPGVETSTG
     PLGHGLPVGV GAAIGAKLQK QDWEVFVVVG DGEIQEGSNW EAAMTAAHKK LDNLTLIIDR
     NRLQQGDRTH DVTSLEPLAE RFSAFGWDAL EVDGHDYAAL IEALTAPRVA DKPRCLVANT
     FKGKGVSFIQ DRVEWHHKVP SPEQVEEALN ELERGA
//
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