ID A0A372DR12_9GAMM Unreviewed; 668 AA.
AC A0A372DR12;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN Name=tkt {ECO:0000313|EMBL:RFP61989.1};
GN ORFNames=D0Y53_02745 {ECO:0000313|EMBL:RFP61989.1};
OS Luteimonas weifangensis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Luteimonas.
OX NCBI_TaxID=2303539 {ECO:0000313|EMBL:RFP61989.1, ECO:0000313|Proteomes:UP000262917};
RN [1] {ECO:0000313|EMBL:RFP61989.1, ECO:0000313|Proteomes:UP000262917}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WF-2 {ECO:0000313|EMBL:RFP61989.1,
RC ECO:0000313|Proteomes:UP000262917};
RA Zhao H.;
RT "Lysobacter weifangensis sp. nov., a new member of the family
RT 'Xanthomonadaceae', isolated from soil in a farmland.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
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 ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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:RFP61989.1}.
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DR EMBL; QVPD01000002; RFP61989.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372DR12; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000262917; 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; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Reference proteome {ECO:0000313|Proteomes:UP000262917};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 357..533
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 668 AA; 72330 MW; 25E646DE06C7E803 CRC64;
MSTPTRRDLA NALRFLAIDA VEAAKSGHPG MPMGMADIAE VLWNDYLQHN PGNPKWFNRD
RFVLSNGHGS MLQYALLHLS GYELPLEELK RFRQLGSKTP GHPENHLTPG VETTTGPLGQ
GFANAVGMAL AEKLLAQRFN RPEFEIVDHR TWVFLGDGCL MEGISHEAAS LAGTWGLHKL
IAFWDDNRIS IDGDTGGWFT DDTPARFEAY GWSVIREVDG QDSESIKAAI EAALRAQDRP
TLICCRTTIG FGSPHKAGKE SSHGAPLGQD EVAATRAALG WPYPPFEIPQ PIRDAWRAGS
AGQVREHQWG QLFDAYAARY PAQAEELVRR SHGELPAGFG ADADAFIARL QADGPVIASR
KASQLAIEAY APLLPELVGG SADLAHSNLT LWKGSKSIVG DCTPEESREA NYVHYGVREF
AMTAISNGLA LHGCFVPYDA TFLVFSDYAR NAVRMSALTG ARAIHVYTHD SIGLGEDGPT
HQPVEHLAAL RYIPGNDVWR PCDAVESAVA WKAAIERADG PSCLVFSRQN LPHQARTPQQ
LAAIARGGYI LKDSVGAPEL ILIATGSEVG LAMQAAQQLG DGVRVVSMPS TEVFERQDAA
WRESVLPQAC RKRVAIEAGV TGFWYRYTGL DGAVIGIDSF GASAPAEALF PHFGFTVEHV
LDAARALA
//
