ID A0A316GQA1_9RHOB Unreviewed; 671 AA.
AC A0A316GQA1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=C7455_101938 {ECO:0000313|EMBL:PWK62899.1};
OS Roseicyclus mahoneyensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseicyclus.
OX NCBI_TaxID=164332 {ECO:0000313|EMBL:PWK62899.1, ECO:0000313|Proteomes:UP000245708};
RN [1] {ECO:0000313|EMBL:PWK62899.1, ECO:0000313|Proteomes:UP000245708}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16097 {ECO:0000313|EMBL:PWK62899.1,
RC ECO:0000313|Proteomes:UP000245708};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWK62899.1}.
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DR EMBL; QGGW01000001; PWK62899.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316GQA1; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000245708; 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 Reference proteome {ECO:0000313|Proteomes:UP000245708};
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; 72339 MW; 27034AE4832B2E84 CRC64;
MDLTALATAH PDHWRRAACI RTLTLDAVAA ANSGHSGMPM GMADVATVLF DKHLSFDASA
PDWPNRDRFI LSAGHGSMLL YALLYLTGSP DMTLEQVKNF RQLGAITAGH PEYGHAQGIE
TTTGPLGQGI ANAVGFAMAE EFLRAKWGKR VIDHYTWCIA GDGCLMEGVS QEAIALAGRQ
ELSRLIVMWD DNGITIDGKV SISDRTDQKA RFAASGWDVF EVDGHDPVAI DGAITAAKAS
PRPAMIACKT HIALGHAAQD TAKGHGALTD AKQLQAAKDA YGWPHGPFEI PADLKSWWES
VGAKGREARK EWETQFALLS DGKKAEFTRA FALELPKKLS ATIKALKKQH SDNAPKVATR
QASQMALEVI NPILGEHLGG SADLTGSNNT DTADLGVFSP EDRKGRHVHY GIREHGMAAA
MNGMALHGGV RPYGGTFMVF TDYARPAMRL ASLMGLPVTY VMTHDSIGLG EDGPTHQPVE
HLTMMRATPN LLVMRPADAV ETAEAWEVAL MQKTTPSVLA LSRQALPTLR TEHKAKNMVA
QGAYVLAEAT GKRQAILLAT GSEVAIAMEA RALLEAEGIG TRVVSMPCWE IFEETDEAYR
KRVLPAGPVR VAVEAAIRFG WDRWLFGERG RREKSGFVGM HGFGASAPAG DLYKHFGITA
EAVAEKVKSL L
//