ID A0A2I1DMF9_9PROT Unreviewed; 665 AA.
AC A0A2I1DMF9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=B1757_06480 {ECO:0000313|EMBL:PKY11053.1};
OS Acidithiobacillus marinus.
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=187490 {ECO:0000313|EMBL:PKY11053.1, ECO:0000313|Proteomes:UP000234329};
RN [1] {ECO:0000313|EMBL:PKY11053.1, ECO:0000313|Proteomes:UP000234329}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SH {ECO:0000313|EMBL:PKY11053.1,
RC ECO:0000313|Proteomes:UP000234329};
RA Sharmin S., Tokuhisa M., Kanao T., Kamimura K.;
RT "Draft genime sequence of the acidophilic sulfur-oxidizing bacterium
RT Acidithiobacillus sp. SH, isolated from seawater.";
RL Submitted (MAR-2017) 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:PKY11053.1}.
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DR EMBL; MXAV01000026; PKY11053.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I1DMF9; -.
DR InParanoid; A0A2I1DMF9; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000234329; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000234329};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 418..439
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 356..527
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 665 AA; 72143 MW; C897F28F10DA34A3 CRC64;
MTVTRTDLAN AIRVLAMDAV EKAKSGHPGM PMGMADIAEV LWNDFLVHNP ANPHWPGRDR
FILSNGHGSM LQYALLHLSG YDLSIEDLQQ FRQWHSKTPG HPEYRDAPGV ETTTGPLGQG
VANGVGMALA ERMLAAQFNR PDHEIVNNYT YVFLGDGCLM EGVSHEACSL AGVWGLNKLV
CFYDDNNISI DGHVDDWFGD DTPARFEAYG WHVIRHVDGH DPEAIKKAIA QAHKQTTQPT
LICCKTVIGH GSPNKAGTHD VHGAALGAEE VALTRKNLGW SGAPFEIPEA IYHGYNAKAK
GEAAESAWKE KFAQYKANFP KEAAEFERRL TGEASPEFDA AIARLISEFR TENPKIATRV
ASGKTIQGIA ASLPEFLGGS ADLTPSNNTR WKEAIDIGKH RLMGNYIHYG VREFGMSAIM
NGVSLYGGFL PFGGTFLIFS DYSRNAIRMS ALMGIRVVYV MTHDSIGLGE DGPTHQPVEQ
VNSLRLIPNL NVWRPADAVE TTIAWESSVK LQRTPSLLAL SRQNLPALPH TDETVANARR
GGYVLKDAEG DKAQGILIAT GSEVELALAA QAKLAEQGHA VRVVSMPCMD IFAAQDAAYQ
ESVLPAGISK RVAIEAGTTG LWYKYVGLQG AVVGIDHFGA SAPAPTLFAK FGFTVDNIVA
QYQSL
//
