ID A0A0C9MNC8_SPHPI Unreviewed; 695 AA.
AC A0A0C9MNC8;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:GAN12226.1};
GN ORFNames=SP6_07_00120 {ECO:0000313|EMBL:GAN12226.1};
OS Sphingomonas paucimobilis NBRC 13935.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1219050 {ECO:0000313|EMBL:GAN12226.1, ECO:0000313|Proteomes:UP000032025};
RN [1] {ECO:0000313|EMBL:GAN12226.1, ECO:0000313|Proteomes:UP000032025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 13935 {ECO:0000313|EMBL:GAN12226.1,
RC ECO:0000313|Proteomes:UP000032025};
RA Hosoyama A., Hashimoto M., Hosoyama Y., Noguchi M., Uohara A., Ohji S.,
RA Katano-Makiyama Y., Ichikawa N., Kimura A., Yamazoe A., Fujita N.;
RT "Whole genome shotgun sequence of Sphingomonas paucimobilis NBRC 13935.";
RL Submitted (AUG-2014) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:GAN12226.1}.
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DR EMBL; BBJS01000007; GAN12226.1; -; Genomic_DNA.
DR RefSeq; WP_037568866.1; NZ_BBJS01000007.1.
DR AlphaFoldDB; A0A0C9MNC8; -.
DR GeneID; 78526600; -.
DR Proteomes; UP000032025; Unassembled WGS sequence.
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; 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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 383..553
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 125..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 695 AA; 74849 MW; 4D4D91FADC95A233 CRC64;
MTDATTHAVA DTHLHEDGSI ERLTIDTIRT LSMDAVQQAN SGHPGTPMAL APVGHTIWSK
FLRYDPAHAD WPNRDRFVLS VGHASMLLYS LIHLAGIEEI DANGNKSGKP ALSLEDLKGF
RQLNSKTPGH PEYRHTTGVE TTTGPLGAGC GNSVGMAIAE RWLAAHFNRE GFPIFDHDVY
VVCGDGDMME GVASEAASTA GHLKLSNLCW IYDSNHISIE GGTDLAFDED VGKRFEAYGW
NVIHVDDAND VAALTAALDD FKATQDKPTF IVVKSVIGYG SPKAGSEKAH GEPLGEDAIR
ATKKAYGWPE DAKFLVPDGV REAFQGAIET RGKPLRDEWV AMVERYRAEY PELAAQLDAM
LSDTLPEGWD SEIPVFEADA KGVASRDSGG KVQNAIAAKV PWLVGGSADL APSTKTLIKD
GGSFQAGSYD GRNLHFGVRE HSMGAIVDGM ALSHLRSYGA TFLVFSDYMR APIRLAAIME
LGAIFVFTHD SIGVGEDGPT HQPIEHLATL RAIPGLDTIR PGDANEVAEA WRCAAESADH
PTALIFSRQA LPTLDRSKYA AASGLKKGGY VLADCEGTPD VILIATGSEL SLVTDAYETL
TADGIKARVV SLPSWYRFEM QDAAYKESVL PRAVTARLAV EQAGSIGWDR YVGFEGRTIT
MSTFGASAPI SKLQDKFGFT LDNVVKVARE LVETK
//