ID A0A1H8Z7J1_9BACI Unreviewed; 665 AA.
AC A0A1H8Z7J1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=SAMN05216362_101224 {ECO:0000313|EMBL:SEP60301.1};
OS Piscibacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Piscibacillus.
OX NCBI_TaxID=571933 {ECO:0000313|EMBL:SEP60301.1, ECO:0000313|Proteomes:UP000199427};
RN [1] {ECO:0000313|EMBL:SEP60301.1, ECO:0000313|Proteomes:UP000199427}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21633 {ECO:0000313|EMBL:SEP60301.1,
RC ECO:0000313|Proteomes:UP000199427};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOES01000001; SEP60301.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8Z7J1; -.
DR STRING; 571933.SAMN05216362_101224; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000199427; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000199427};
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 COILED 301..328
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 665 AA; 73016 MW; 7BB6EE9EAE29C4DF CRC64;
MSNNIEQMSI NTIRTLAIDA VEKANSGHPG MPMGAAPMAY TLWTKVMNHN PKNSSWFNRD
RFVLSAGHGS MLLYALLHLS GYKVSMDDLK NFRQWGSKTP GHPEFGHTDG VEATTGPLGQ
GIAMSVGMAM AERFLASKFN TDNHQVIDHY TYSICGDGDL MEGVSQEAAS LAGHLKLGKL
VVMYDSNDIS LDGDLNRSFS ESVEDRFKSY GWQVIRVEDG NDTEAIEKAL LDAKATEDQP
TLIEVKTVIG YGSPNKGGKS DAHGAPLGQE ERQLVREHYN WEHEDFHVPD EVAADFEEKT
IKRGQEAENN WNELLQQYKN EFPELAEEFE LAMKGELPAN WNADLPIYDE NSKALATRAA
SGEVLNGLAK NIPNLIGGSA DLAGSNKTML KDEDDFKYPD YSGRNIWFGV REFAMACALN
GMALHGGLKV YGGTFFVFSD YLRPAVRLSA LMGTPVTYVF THDSIAVGED GPTHEPIEQL
PSLRAMPNLN LVRPADANET KAAWEIAVQA EDAPTALVLT RQGLPVIPEI ADKASEGVRR
GAYALNKVEN PDILLLASGS EVQLIHKASE QLKEEGINAQ VVSMPSWYLF DQQDEAYKES
VLPKNVKARL AVEMASPFGW ERYTGIDGDV LGISTFGASA PGNKVIEEYG FTVENVVSRA
KELLK
//
