ID A0A0P6SM27_9STRE Unreviewed; 661 AA.
AC A0A0P6SM27;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-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=AKK44_03905 {ECO:0000313|EMBL:KPJ22533.1};
OS Streptococcus phocae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=119224 {ECO:0000313|EMBL:KPJ22533.1, ECO:0000313|Proteomes:UP000049578};
RN [1] {ECO:0000313|EMBL:KPJ22533.1, ECO:0000313|Proteomes:UP000049578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51973 {ECO:0000313|EMBL:KPJ22533.1,
RC ECO:0000313|Proteomes:UP000049578};
RA Avendano-Herrera R.;
RT "Genome sequence of Streptococcus phocae subsp. phocae ATCC 51973T isolated
RT from liver specimen obtained from seal.";
RL Submitted (AUG-2015) 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:KPJ22533.1}.
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DR EMBL; LHQM01000012; KPJ22533.1; -; Genomic_DNA.
DR RefSeq; WP_054278605.1; NZ_LHQM01000012.1.
DR AlphaFoldDB; A0A0P6SM27; -.
DR STRING; 119224.AKK44_03905; -.
DR PATRIC; fig|119224.3.peg.310; -.
DR Proteomes; UP000049578; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 352..523
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 661 AA; 70901 MW; 43524A0AA6C69697 CRC64;
MTFDAVDQLA VNTVRTLSMD AIQAANSGHP GLPMGAAPMA YVLWNHFMNI NPKTSRNWSN
RDRFILSAGH GSAMLYSLLH LAGYDLSLDD LKNFRQWGSK TPGHPEVNHT DGVEATTGPL
GQGIANAVGM AMAEAHLAAT FNKPGYDIVD HYTFALNGDG DLMEGVSQEA ASLAGHLKLG
KLVLLYDSND ISLDGPTSMA FTEDVKGRFE AYGWQHILVK DGNDLDEIAA AIAAAKAETG
KPTIIEVKTI IGFGAEKQGT SSVHGAPLGA DGISFAKKAY AWEYPEFTVP AEVAERFATG
LKARGEKAEA AWNELFAAYE AEYPELAAQY KQAFSGEAAH VELEAHELGS AVASRVSSHK
AIQQISEQVP SFWGGSADLS ASNNTMIKAE TDFQPENYAG RNIWFGVREF AMAAAMNGIA
LHGGTRVYGG TFFVFSNYLL PAVRMAALQN LPTVYVMTHD SIAVGEDGPT HEPIEQLASV
RSMPNLNVIR PADGNETNAA WKRALVETDR PTLLVLTRQN LPVLEGTKEL AAVGVNKGAY
ILSEAKGDLD GIIIATGSEV KLALDTQAAL ETQGIHVRVV SMPSQNIFDE QSSEYKESIL
PATVTKRLAI EAGSSFGWAK YVGMSGQTLT IDTWGASAPG NRIFEEYGFT VANAVTLYKS
L
//
