ID A0A0D6MGP9_9PROT Unreviewed; 577 AA.
AC A0A0D6MGP9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:GAN52696.1};
GN ORFNames=Tasa_001_011 {ECO:0000313|EMBL:GAN52696.1};
OS Tanticharoenia sakaeratensis NBRC 103193.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Tanticharoenia.
OX NCBI_TaxID=1231623 {ECO:0000313|EMBL:GAN52696.1, ECO:0000313|Proteomes:UP000032679};
RN [1] {ECO:0000313|EMBL:GAN52696.1, ECO:0000313|Proteomes:UP000032679}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 103193 {ECO:0000313|EMBL:GAN52696.1,
RC ECO:0000313|Proteomes:UP000032679};
RA Azuma Y., Hadano H., Hirakawa H., Matsushita K.;
RT "Genome sequencing of Tanticharoenia sakaeratensis NBRC 103193.";
RL Submitted (OCT-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAN52696.1}.
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DR EMBL; BALE01000001; GAN52696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6MGP9; -.
DR STRING; 1231623.Tasa_001_011; -.
DR OrthoDB; 7231069at2; -.
DR Proteomes; UP000032679; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
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; 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 SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000032679}.
FT DOMAIN 280..438
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 432..452
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 577 AA; 61221 MW; 93F7C1920041B485 CRC64;
MTDFPFPWTD LAARDSAPTE GLLQAAQALW GQALRFDPSD PLWPDRDRVV VSQPGLMDRL
RDMTGDVDAG LDMSRAPPGQ AIGTAVGLAL AEARLSARFG RSLVDHRTWV LCDGADLETG
VALEAAALAG MLGLARLCVI AGVAQSDTSG ADRFAASGWS VRRVSCEVPG PDGQMDREAV
RNAVVAAIAA TVRARRPMLI ICTQAAGIGS GRPTTDDAAV PAWAAVAARG RTARRGWQRR
AFRHRLRAEF TRWQNGAAPP LWEVDWARAW RTNVGSGTPA SPLAAAGHAL DQIAQLRPEL
TCLTLAPPDH DPQYTALAIA CGTRDHGMAA LLNGLGLHGA LLPFGVISAV SIDRLRPALR
LAAVMRQQVV HLLCDEGAAL QGADMIWLPV EQLASLRAMP NVFLFRPCDP VETRAAFTSA
LARTDGPSVI VLDGRPDTRR PDTEAAPHGG TLPLGIGPEQ GAYVRSGPNV ARDVTLIASG
HEVAVAEALR RRLAGHGIEA CVVSLPCWKQ FARTDATYRE AVLGTAPRIG LERASGFGWE
RWLGTEGLFL GAEAIANGCD DALLARVRAH LAAITTA
//
