ID A0A1G7PRG8_9RHOB Unreviewed; 671 AA.
AC A0A1G7PRG8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN04489759_103419 {ECO:0000313|EMBL:SDF88793.1};
OS Sulfitobacter delicatus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Sulfitobacter.
OX NCBI_TaxID=218672 {ECO:0000313|EMBL:SDF88793.1, ECO:0000313|Proteomes:UP000199399};
RN [1] {ECO:0000313|EMBL:SDF88793.1, ECO:0000313|Proteomes:UP000199399}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16477 {ECO:0000313|EMBL:SDF88793.1,
RC ECO:0000313|Proteomes:UP000199399};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FNBP01000003; SDF88793.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G7PRG8; -.
DR STRING; 218672.SAMN04489759_103419; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000199399; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 357..528
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 671 AA; 72842 MW; 6BACFD223AC1FFF3 CRC64;
MDLQALAQAN PDHWSKATAI RALTLDAVAA ANSGHSGMPM GMADVATVLF EKHLKFDAAN
PLWPDRDRFI LSAGHGSMLI YSLLHLTGYE QFPIEELKNF RQMGARTAGH PENFLADAIE
TTTGPLGQGI ANSVGFAMAE EMLRAQYGQK VVDHHTYVIA GDGCLMEGVS QEAITLAGRH
KLSKLIVMWD NNSITIDGPV SLSDNTDQVA RFKAAQWHVI EIDGHNPDEI DAALTEAKAT
DLPTMIACKT HIALGHAAQD TSKGHGALTD ADQMAEAKKA YGWTSGPFEV PADVKSAWEE
IGKRGADARR EWEERFDKMP RHKRETFNRA LALDAPKKMS ATVKAFKKQI SESAPKMATR
AASEKALEVL NPILPETVGG SADLTGSNNT KTSDLGVFDV DNRGGRYVYW GIREHGMAAA
MNGMALHGGL RPYGGTFMCF TDYARPSMRL AALMQIPTAF VMTHDSIGLG EDGPTHQPVE
HLAISRSTPN TYVFRPADAV ETAEAWEIAF TSKTTPSVLS LTRQGLPTVR LEHKNNNLTE
KGAYVLADAE GKRQVILIAT GSEVHVAMEA RDLLQAEGIG TRVVSMPCME LFAAQDDAYR
KRVLPGGAVR VGIEAGVRQG WDQWLLGERG KFGKADFVGM DRFGASAPAE ELFERFGFTA
QNVADKAKAL L
//
