ID   R4WL29_9AQUI            Unreviewed;       270 AA.
AC   R4WL29;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:BAN18917.1};
DE   Flags: Fragment;
GN   Name=tkt {ECO:0000313|EMBL:BAN18917.1};
OS   Persephonella sp. MT-32.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Hydrogenothermaceae;
OC   Persephonella.
OX   NCBI_TaxID=1274994 {ECO:0000313|EMBL:BAN18917.1};
RN   [1] {ECO:0000313|EMBL:BAN18917.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=MT-32 {ECO:0000313|EMBL:BAN18917.1};
RX   PubMed=23630523; DOI=10.3389/fmicb.2013.00107;
RA   Mino S., Makita H., Toki T., Miyazaki J., Kato S., Watanabe H., Imachi H.,
RA   Watsuji T., Nunoura T., Kojima S., Sawabe T., Takai K., Nakagawa S.;
RT   "Biogeography of Persephonella in deep-sea hydrothermal vents of the
RT   Western Pacific.";
RL   Front. Microbiol. 4:107-107(2013).
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=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; AB774144; BAN18917.1; -; Genomic_DNA.
DR   AlphaFoldDB; R4WL29; -.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
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   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
FT   DOMAIN          1..174
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          189..270
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02779"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:BAN18917.1"
FT   NON_TER         270
FT                   /evidence="ECO:0000313|EMBL:BAN18917.1"
SQ   SEQUENCE   270 AA;  30178 MW;  7825DDB27660EB95 CRC64;
     ISSEAAALAG RLKLGKLIYL YDDNHITIDG PTDITWNEDI ELRFKAHGWH VITVPDGEDL
     DAIYGAIKAA QDEKEKPSLI RVRTHIGWHS PKQDDPAVHG APLSEEEARK TKRALGFPED
     KNFYIPEEAL NHFRKAIDRG AEIERQWRDM FEEYRKSYPE LAEQFERFVK GELPEGWEED
     LPVYTDTTKK VATRSASGET LNVLADKIPN LIGGSADLAH SNKVFLKGKG EFYCDTPSGR
     NIHFGIREHA MGAAVNGMAL HGGIIPFGAT
//