ID A0A2U9NYX9_STRAS Unreviewed; 695 AA.
AC A0A2U9NYX9;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=DMT42_08960 {ECO:0000313|EMBL:AWT42433.1};
OS Streptomyces actuosus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1885 {ECO:0000313|EMBL:AWT42433.1, ECO:0000313|Proteomes:UP000247634};
RN [1] {ECO:0000313|EMBL:AWT42433.1, ECO:0000313|Proteomes:UP000247634}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25421 {ECO:0000313|EMBL:AWT42433.1,
RC ECO:0000313|Proteomes:UP000247634};
RA Liu W., Sun F., Hu Y.;
RT "The complete genome sequence of a nosiheptide producer Streptomyces
RT actuosus ATCC 25421: deducing the ability of producing a new class III
RT lantibiotics.";
RL Submitted (JUN-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=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; CP029788; AWT42433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2U9NYX9; -.
DR KEGG; sact:DMT42_08960; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000247634; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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:UP000247634};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 371..555
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 695 AA; 75258 MW; 0B76A60662B11C25 CRC64;
MSTKPTTTDL EWTELDQRAV DTARVLAADA VQKVGNGHPG TAMSLAPAAY TLFQKVMRHD
PSDPDWVGRD RFVLSAGHSS LTLYTQLYLA GFGLELDDLK AFRTWGSKTP GHPEYGHTKG
VETTTGPLGQ GVANAVGMAM AARYERGLFD PEAPQGESPF DHFVYCIAGD GCLQEGISAE
ASSLAGHQKL GNLILLWDDN HISIEGDTET AVSEDTVKRY EAYGWHVQRV APKPDGDLDP
HAIYDAIEEA KKVTDRPSFI AMRSIIAWPA PNAQNTEAAH GSALGDEEVA ATKRVLGFDP
EQSFEVADEV IAHTRKALER GAQAKAEWEK SLQQWRDANP ERAAEFDRIA AGELPAGWEE
KVPVFEPGKG VATRAASGKV LQALGAVIPE LWGGSADLAG SNNTTIDKTS SFLPEGNPLP
EASPYGRTIH FGIREHSMGA EMNGIALHGN TRIYGGTFLV FSDYMRNAVR LSALMHLPVT
YVWTHDSIGL GEDGPTHQPV EHLASLRAIP GLNIVRPADA NETAIAWREI LKRWTKEFGK
GQPHGLALTR QGVPTYEPDE NAARGGYVLF EADGGEPQVL LIATGSEVHV AVEAREQLQA
AGIPTRVVSM PCVEWFEQQD QGYRDSVLPP SVRARVAVEA GVGLTWHKYV GDAGRIVSLE
HFGASADAKV LFREFGFTAE NVAAKARESL EAAQR
//
