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Database: UniProt
Entry: L0KDN7_HALHC
LinkDB: L0KDN7_HALHC
Original site: L0KDN7_HALHC 
ID   L0KDN7_HALHC            Unreviewed;       652 AA.
AC   L0KDN7;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   OrderedLocusNames=Halha_2324 {ECO:0000313|EMBL:AGB42198.1};
OS   Halobacteroides halobius (strain ATCC 35273 / DSM 5150 / MD-1).
OC   Bacteria; Bacillota; Clostridia; Halanaerobiales; Halobacteroidaceae;
OC   Halobacteroides.
OX   NCBI_TaxID=748449 {ECO:0000313|EMBL:AGB42198.1, ECO:0000313|Proteomes:UP000010880};
RN   [1] {ECO:0000313|Proteomes:UP000010880}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35273 / DSM 5150 / MD-1
RC   {ECO:0000313|Proteomes:UP000010880};
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Gu W.,
RA   Kyrpides N., Mavromatis K., Ivanova N., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P.,
RA   Woyke T., Wu D., Tindall B., Pomrenke H., Brambilla E., Klenk H.-P.,
RA   Eisen J.A.;
RT   "The complete genome of Halobacteroides halobius DSM 5150.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC         Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC         ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC         Evidence={ECO:0000256|ARBA:ARBA00001027};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; CP003359; AGB42198.1; -; Genomic_DNA.
DR   RefSeq; WP_015327912.1; NC_019978.1.
DR   AlphaFoldDB; L0KDN7; -.
DR   STRING; 748449.Halha_2324; -.
DR   KEGG; hhl:Halha_2324; -.
DR   PATRIC; fig|748449.3.peg.2243; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_9; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000010880; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR005478; Transketolase_bac-like.
DR   InterPro; IPR049557; Transketolase_CS.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   NCBIfam; TIGR00232; tktlase_bact; 1.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010880};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          350..521
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   652 AA;  72130 MW;  8E29F0CA05F4905A CRC64;
     MLNKVADIVR GLSADTVEQA GSGHPGMAIG CADIGAALYG EIMNYDPTQP NWPNRDRFIL
     SAGHGSVWLY SFLHLSGYDV SLEDLKRFRQ LHSKTPGHPE YGHTSGVETT TGPLGQGFAN
     AVGMAISEKM LAERYNTKEY EIIDHYTYTL LGDGCMMEGV TSEAASLAGH LGLDKLIAIY
     DSNDISIGGN VDITFTESVP DRFKAYDWHV IDEVDGHDIA SIKEAIAEAK EVTDKPTLII
     ANTHIAYGAP TKQDSNSAHG APLGKEELTG LKENFGLPTD KEFYVSNEVR EFFATRQEKL
     QKIRQDWEDR FTKWAKANPE LKTQWDQAHN LELPNDLERV VADIELDTPL ATRKASGSIL
     RKIADQVPYL VGGSADLAPS NKTYLDKYEE IQKESFSGRN FRFGVREHAM GAIANGISLH
     GGVRPFTATF LVFSDYMRPA IRMAALMKQP SIYVFTHDSI YIGEDGPTHQ PVEHVESLRL
     IPNLEVIRPA DEEETKAAWL EAMKRQDGPT ALILTRQNLP HLKKDKKINM DKGGYVVQEG
     NDPQVVLMAS GSEVSLAVEV AEKLDVETRV VSIPDRNKFI AQGQDYIKEV LGEDTFRVAL
     EAGVGQGWYQ LLGDKHHLVS VEDFGASGSG EKVGKYFGFV AEEITEQIIN RL
//
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