ID A0A387BS04_9MICO Unreviewed; 700 AA.
AC A0A387BS04;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-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=D7I44_15910 {ECO:0000313|EMBL:AYG04864.1};
OS Gryllotalpicola protaetiae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Gryllotalpicola.
OX NCBI_TaxID=2419771 {ECO:0000313|EMBL:AYG04864.1, ECO:0000313|Proteomes:UP000275069};
RN [1] {ECO:0000313|EMBL:AYG04864.1, ECO:0000313|Proteomes:UP000275069}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2DFW10M-5 {ECO:0000313|EMBL:AYG04864.1,
RC ECO:0000313|Proteomes:UP000275069};
RA Heo J., Kim S.-J., Kwon S.-W.;
RT "Genome sequencing of strain 2DFW10M-5.";
RL Submitted (SEP-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; CP032624; AYG04864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A387BS04; -.
DR KEGG; gry:D7I44_15910; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000275069; 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:UP000275069};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 367..548
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 700 AA; 75069 MW; F1BC79EF32E0F019 CRC64;
MAALQWDSID NKAVDTVRVL AADAVEKVGN GHPGTAMSLA PAAYLLWQKI MRRDPSDDQW
IGQDRFILSV GHSSLTQYIQ LYLGGWGLEL SDIEALRTWG SLTPGHPEYR HTKGVEITTG
PLGQGLASAV GFAFAQRYER GLFDPETPAG ESPFDHHVYV IAGDGDIEEG VTSEAGQLAG
TQQLGNLVVI YDKNHISIED NTDIALSEDT AKRYEAYGWD VHTVDWFKSG SYHEDVQELF
DTIEAAKAVT DKPSIIILKT LIGYPSPTKQ GTGKVHGAKL GAEEVAGVKK ALGFDPEKSF
DVDPEVLAHT RGAIERGKAQ RAEWQVGFDA WAAANPERKA LFDRLEAGEL PEGLEAALPV
FEAGKDVSTR AASGKAINAL AAQLPELWGG SADLAESNLT TIEGGGSFLP SSITTPEWGQ
GNPYGRILHF GIREHAMGSI LNGITLHGKT RSYGGTFLQF ADYMRPAVRL AALMDIPSIF
VWTHDSVALG EDGPTHQPVE HLAALRAIPN LAIVRPGDAN ETAYAWLETL SRRGGPVGLA
LSRQNLPVFE RGAGEASGDT FASAKFVGKG AYVLAEAPNG TPDIILIATG SELQIAVEAR
QVLAGEGINA RVVSVPSQEW FAEQSAEYKE SVLPASVTAR VAVEAGIALP WHTWVGDRGR
IVSIEHFGAS ADYKTLFEKF GMTTESVVAA AKESLAANEK
//
