ID N4WCJ9_9BACI Unreviewed; 666 AA.
AC N4WCJ9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN ORFNames=J416_07792 {ECO:0000313|EMBL:ENH96964.1};
OS Gracilibacillus halophilus YIM-C55.5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX NCBI_TaxID=1308866 {ECO:0000313|EMBL:ENH96964.1, ECO:0000313|Proteomes:UP000012283};
RN [1] {ECO:0000313|EMBL:ENH96964.1, ECO:0000313|Proteomes:UP000012283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM-C55.5 {ECO:0000313|EMBL:ENH96964.1,
RC ECO:0000313|Proteomes:UP000012283};
RA Sugumar T., Polireddy D.R., Antony A., Madhava Y.R., Sivakumar N.;
RT "Draft genome sequence of Gracibacillus halophilus YIM-C55.5, a moderately
RT halophilic and thermophilic organism from the Xiaochaidamu salt lake.";
RL Submitted (MAR-2013) 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:ENH96964.1}.
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DR EMBL; APML01000025; ENH96964.1; -; Genomic_DNA.
DR RefSeq; WP_003467744.1; NZ_APML01000025.1.
DR AlphaFoldDB; N4WCJ9; -.
DR STRING; 1308866.J416_07792; -.
DR PATRIC; fig|1308866.3.peg.1573; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000012283; Unassembled WGS sequence.
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; 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:UP000012283};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 355..526
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 97..116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 666 AA; 72162 MW; 778080AC1A63B63C CRC64;
MSNETAQKSI NSIRTLSIDA IENASSGHPG LPMGAAPMAY TLWTEHMKHN PGHSKWFDRD
RFVLSAGHGS MLLYSLLHLS GYDVSIDDLK GFRQWDSKTP GHPEAHHTDG VEATTGPLGQ
GIAMSVGMAM AEKHLSGKYN TDKHEIIDHN TYALVSDGDL MEGISHESAS LAGHLGLGKL
IALYDSNDIS LDGDLHKSFS EDIEGRFQSY GWQVLRVEDG NDIEAISKAI SEAKANTDQP
TLIEVKTVIG YGSPNKSASA ASHGAPLGED EVALTKEFYN WEHEPFHVPD EVYKDFETKI
QKRGQEAEQA WNQAFEEYKK ANPELGQDLE NAINNKLPEG WDKDLPVFEA GKDEAATRAA
SGKVLNALAD SVPSLFGGSA DLAGSNKTNL NAFDDFSKDT PAEKNVWFGV REHAMAAALN
GMTLHGGLKV FGGTFFVFSD YLRPSVRLSA IQNLPVTYVL THDSIAVGED GPTHEPVEQL
AAFRAMPNAS VIRPADGNEV QAAWRLAMEA TSHPTLLVLT RQGLPTLEST AEKAYEGVKK
GGYVVSPASK DTPDAILIAT GSEVQLAVKA QEALKEQGKD VSVVSLPSWD RFDQQDVAYK
ESVLPSAVTK RVGIEMAASL GWERYVGING KVISIDRFGA SANGGKIIDE YGFNVDNVVN
HVNELF
//
