ID A0A1V4E3V8_9ACTN Unreviewed; 695 AA.
AC A0A1V4E3V8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B1R27_13055 {ECO:0000313|EMBL:OPG07605.1};
OS Streptomyces sp. GKU 895.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1662404 {ECO:0000313|EMBL:OPG07605.1, ECO:0000313|Proteomes:UP000190311};
RN [1] {ECO:0000313|EMBL:OPG07605.1, ECO:0000313|Proteomes:UP000190311}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GKU 895 {ECO:0000313|EMBL:OPG07605.1,
RC ECO:0000313|Proteomes:UP000190311};
RA Kruasuwan W.;
RT "Draft genome sequence of plant growth promoting endophytic Streptomyces
RT sp. GKU 895 isolated from root of sugarcane plants.";
RL Submitted (FEB-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}.
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:OPG07605.1}.
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DR EMBL; MWJO01000022; OPG07605.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4E3V8; -.
DR Proteomes; UP000190311; Unassembled WGS sequence.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
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"
FT COILED 318..345
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 695 AA; 75084 MW; B83E212F283212DA CRC64;
MSTKPTTTDL EWTELDQRAV DTARVLAADA VQKVGNGHPG TAMSLAPAAY TLFQKVMRHD
PADPEWVGRD RFVLSAGHSS LTLYTQLYLA GFGLELDDLK AFRTWGSKTP GHPEYGHTKG
VETTTGPLGQ GVANAVGMAM AARYERGLFD PEAPQGESPF DHFVYAIAGD GCLQEGISAE
ASSLAGHQKL GNLILLWDDN HISIEGDTET AVSEDTVKRY EAYGWHVQRI APKPDGDLDP
HAIYNAIEAA KQVTDKPSFI AMRSIIAWPA PNAQNTEAAH GSALGDDEVA ATKRVLGFDP
EKTFEVADEV IAHTRQALDR GREAKAEWEK QLQEWRDNNA ERAAEFDRIA AGELPKGWEE
KLPVFEPGKG VATRAASGKV LQALGAVIPE LWGGSADLAG SNNTTIDKAS SFLPADNPLP
EANPYGRTIH FGIREHSMAA EMNGIALHGN TRIYGGTFLV FSDYMRNAVR LSALMHLPVT
YVWTHDSIGL GEDGPTHQPV EHLASLRAIP GLNVVRPADA NETAIAWREI LKRWTKEFGK
GAPHGLALTR QGVPTYEPNE DAAKGGYVLF EASGGSPEVV LIATGSEVHV AVEAREALEA
DGVPTRVVSM PSVEWFEEQD QGYRDSVLPP AVRARVAVEA GIGLTWHKYV GDAGRIVSLE
HFGASADGKV LFEEFGFTAE NVAAKARESL ADAQR
//
