ID A0A243SAG6_9ACTN Unreviewed; 695 AA.
AC A0A243SAG6;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 32.
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=CA983_03445 {ECO:0000313|EMBL:OUD04608.1};
OS Streptomyces swartbergensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=487165 {ECO:0000313|EMBL:OUD04608.1, ECO:0000313|Proteomes:UP000195105};
RN [1] {ECO:0000313|EMBL:OUD04608.1, ECO:0000313|Proteomes:UP000195105}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMC13 {ECO:0000313|EMBL:OUD04608.1};
RA Le Roes-Hill M., Prins A., Durrell K.A.;
RT "Biotechnological potential of actinobacteria isolated from South African
RT environments.";
RL Submitted (MAY-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:OUD04608.1}.
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DR EMBL; NGFN01000010; OUD04608.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A243SAG6; -.
DR Proteomes; UP000195105; 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; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 24..44
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|PROSITE:PS00801"
SQ SEQUENCE 695 AA; 75034 MW; 01106607484CFD2B CRC64;
MSTKPTTTDL EWTELDQRAV DTARVLAADA VQKVGNGHPG TAMSLAPAAY TLFQKVMRHD
PADADWVGRD RFVLSAGHSS LTLYTQLYLA GFGLELDDLK SFRTWGSKTP GHPEYGHTTG
VETTTGPLGQ GVANAVGMAM AARYERGLFD PEAPEGESPF DHFIYCIAGD GCLQEGISAE
ASSLAGHQKL GNLILLWDDN HISIEGDTET AVSEDTALRY EAYGWHVQRV EPQANGDLDP
AAIFEAIQKA KAVTDKPSFI AMRSIIAWPA PNAQNTEAAH GSALGEDEVA ATKRVLGFDP
EQSFEVAGEV IEHTRKALER GQAARAVWEK AYQQWRDNNP ERAAEYDRVA KGELPTGWEE
KIPVFEVGKG VATRAASGKV LQALGAVVPE LWGGSADLAG SNNTTIDKTS SFLPADNPLP
EADPYGRTIH FGIREHAMAA EMNGIALHGN TRIYGGTFLV FSDYMRNAVR LSALMHLPVT
YVWTHDSIGL GEDGPTHQPV EHLASLRAIP GLNIVRPADA NETAIAWREI LRRWTKEFGK
GQPHGLALTR QGVPTYEPDD DAAKGGYVLF EADGGEPDVI LIATGSEVHV AVEAREQLQG
AGVPTRVVSM PCVEWFEQQD QGYRDSVLPP SVKARVAVEA GVGLTWHKYV GDAGRIVSLE
HFGASADGKV LFREFGFTAE NVAAAARESI AAAQR
//