ID A0A222SKG3_9CHLB Unreviewed; 668 AA.
AC A0A222SKG3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 28.
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:ASQ91222.1};
GN ORFNames=CHL67_10135 {ECO:0000313|EMBL:ASQ91222.1};
OS Prosthecochloris sp. GSB1.
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=281093 {ECO:0000313|EMBL:ASQ91222.1, ECO:0000313|Proteomes:UP000201322};
RN [1] {ECO:0000313|Proteomes:UP000201322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TY Vent \ GSB1 \ Ty-1 {ECO:0000313|Proteomes:UP000201322};
RA Bryant D.A., Liu Z., Li T., Zhao F., Garcia Costas A.M.;
RL Submitted (JUL-2017) 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=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}.
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DR EMBL; CP022571; ASQ91222.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A222SKG3; -.
DR KEGG; pros:CHL67_10135; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000201322; Chromosome.
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; 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; 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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Reference proteome {ECO:0000313|Proteomes:UP000201322};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 413..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 15..35
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|PROSITE:PS00801"
FT REGION 98..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 668 AA; 72759 MW; 099D8C9E9603D02B CRC64;
MHTDQIDRLA IDTIRLLAVD MVEKAQSGHP GMPMGAAPMA YVLWTKIMKH NPENPHWLNR
DRFVLSAGHG SALLYALLHL TGYDLSMEDL KEFRQWGSKT PGHPEYGHTP GVETTTGPLG
QGLSNAVGMA IAERYCAERL NKKDFDLIDY HTYVICGDGD LMEGVTSEAA SIAGHLKLDK
LVCLYDHNRI SIEGSTDLAF TESVHQRFEA YGWDVENVDG NDPEAVETAI LRAKKISGKP
SLIIARTNIG FGSPNKQDSA SSHGSPLGAE EAAMVRKIFG FPEHSSFHVP ESVAAHMKNV
LEKGREQETA WNELRRSFGE RHPDSASMLD AMHGHRLPDG WETLLPVFSP DEKLATRQAS
SKVLHALVGK LPFLIGGSAD LAPSTGTAVR HAVDFTAENY GGENFRFGVR EHAMGAILNG
MALSGMIIPY GATFLVFSDY MKPALRLSAL MNVPSVFIFT HDSIAVGEDG PTHQPIEHLA
MLRSIPGLTV IRPADAQETK SAWRTTLMSR KPTALVFSRQ GLPVLDAEKY PVAEGAPKGA
YILCDWSGAS GGGNRPVILV ATGAEVHLAL EAREQLEDEG IPARVVSMPS WELFEAQPAS
YREEVLPSGM RRRVIVEAAS TFGWHRYATD EGTVLGIDRF GSSAPGGTVL KEYGFTVEHV
VQAAKNLP
//