ID A0A1H2R3S5_9BACI Unreviewed; 661 AA.
AC A0A1H2R3S5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
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=SAMN05421781_0563 {ECO:0000313|EMBL:SDW13534.1};
OS Marinococcus luteus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Marinococcus.
OX NCBI_TaxID=1122204 {ECO:0000313|EMBL:SDW13534.1, ECO:0000313|Proteomes:UP000199488};
RN [1] {ECO:0000313|EMBL:SDW13534.1, ECO:0000313|Proteomes:UP000199488}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23126 {ECO:0000313|EMBL:SDW13534.1,
RC ECO:0000313|Proteomes:UP000199488};
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; FNNC01000001; SDW13534.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H2R3S5; -.
DR STRING; 1122204.SAMN05421781_0563; -.
DR Proteomes; UP000199488; 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:UP000199488};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 351..522
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 661 AA; 71294 MW; 131591CA66CC352C CRC64;
MAISTEQLAI NTIRTLSIES IEKAQSGHPG LPMGAAPMAY ALWTKAMNHN PGNPSWFNRD
RFVLSAGHGS MLLYSMLHLS GYDLSLEELK NFRQWGSQTP GHPEYGHTAG VEATTGPLGQ
GLAMGTGMAM AERHLAAKYN TDDHAVVDHF TYVLCGDGDL MEGVASESAS LAGHLKLGNL
VVLYDSNDVS LDGALHQSFS ENVLQRYEAY GWHTVFIEDG NDVDALEAAI EEAKQSPKPS
MIEVKTVIGY GAPNKGGTNA AHGAPIGEDE YNLVKEAYQW EYDAFHVPPE VTELFDEVKK
AGAKAEQEWN ELFDAYKQAN PELAEELEQA IAGRLPEGWD AKLPVFTDEK VATRAASGDA
LQEVAAAVPS LFGGSADLAG SNKTLIKAEN DFSRNDYTGR NIWFGVREFA MAAAVNGIQL
HGGLKPFGST FLVFSDYLRP ALRLSALMEL PLTQVFTHDS IAVGEDGPTH EPVEQLAALR
AIPNLNVIRP ADGNETVAAW RVAMESEKTP TALVLTRQGV PTLEDTKEKA VEGVRKGAYV
IGEQAENPDL LLVAAGSEVS LAVDAKAQLQ KDGLTVNIVS MPNFHAFDHQ SEDYRRSVLP
DGVPAMAVEM GSSFGWYKYV GAHGSVYGID RFGASAPGGE VVEKYGFTPD KVAQAARQLI
K
//
