ID B4UA35_HYDS0 Unreviewed; 654 AA.
AC B4UA35;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 93.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN OrderedLocusNames=HY04AAS1_1311 {ECO:0000313|EMBL:ACG57996.1};
OS Hydrogenobaculum sp. (strain Y04AAS1).
OC Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae;
OC Hydrogenobaculum.
OX NCBI_TaxID=380749 {ECO:0000313|EMBL:ACG57996.1};
RN [1] {ECO:0000313|EMBL:ACG57996.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=Y04AAS1 {ECO:0000313|EMBL:ACG57996.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Kiss H., Brettin T.,
RA Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Resenback A.-L., Mead D.;
RT "Complete sequence of Hydrogenobaculum sp. Y04AAS1.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
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 ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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DR EMBL; CP001130; ACG57996.1; -; Genomic_DNA.
DR AlphaFoldDB; B4UA35; -.
DR STRING; 380749.HY04AAS1_1311; -.
DR KEGG; hya:HY04AAS1_1311; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_0; -.
DR OrthoDB; 8732661at2; -.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
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; PF02780; Transketolase_C; 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; PS00801; TRANSKETOLASE_1; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 345..516
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 654 AA; 73495 MW; E525EEE404A583D4 CRC64;
MNIDELVINS IRFLSIDAVE KANSGHPGMP LGTAHIGYIL FDKILRYNPE NPKWVNRDRF
VLSNGHGSML LYSLLYLYGF DLTLEDIKNF RQLGSKTPGH PESFLTKGVE ATTGPLGQGI
ANAVGMAIEQ KHLGAICNKL DEPILNYKVF CMVGDGDLME GISYEAAALA GHLNLDNLFI
IWDNNRITID GDTSLAWGED VLKRFENAGF TVRHIEDGYD IELLEKTIKE LLTNQSKPVF
LSVRTHIGYK SIKQDSAEAH GSPLGKEAIA KLRESLNWPY EPFHIPQEVL DYTRRKVEEG
KVLEQKWQEK LSKYKETHKD VVDILTKNIN LENVISHIPR FTEDMATRQA SGKVLNAIAP
HMPTLFGGSA DLHESNNTYI HNEGDFEATN YYGRNIHFGI REHVMGAIAN GMAYGGITTP
YVATFLIFSD YMRPSIRVAA LSKLHVIYIF THDSIGLGED GPTHQPVEHI PSLRLIPNLW
VMRPCDANET AYCWELALRR KDGPVALILS RQKLKTLDRT KYAKENMAKY GAYVLSGAPN
QEFTIIASGS EVGLALALQD KLAENGIQST VVSAPCLELF EMQDEAYKNE VIPKNTKHVV
IEAAKGDIWY KYVNKDALVI SMETFGKSGK GPDVMKHFGF HEEYIYQKVK EKWM
//
