ID A0A1B9YLP3_9BRAD Unreviewed; 661 AA.
AC A0A1B9YLP3;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=LMTR3_32510 {ECO:0000313|EMBL:OCK55654.1};
OS Bradyrhizobium sp. LMTR 3.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=189873 {ECO:0000313|EMBL:OCK55654.1, ECO:0000313|Proteomes:UP000093220};
RN [1] {ECO:0000313|EMBL:OCK55654.1, ECO:0000313|Proteomes:UP000093220}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMTR 3 {ECO:0000313|EMBL:OCK55654.1,
RC ECO:0000313|Proteomes:UP000093220};
RA Ormeno-Orrillo E., Duran D., Rey L., Ruiz Argueso T., Imperial J.,
RA Martinez E.;
RL Submitted (JUL-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}.
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:OCK55654.1}.
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DR EMBL; MAXC01000043; OCK55654.1; -; Genomic_DNA.
DR RefSeq; WP_065747410.1; NZ_MAXC01000043.1.
DR AlphaFoldDB; A0A1B9YLP3; -.
DR STRING; 189873.LMTR3_32510; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000093220; 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:UP000093220};
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..523
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 661 AA; 70183 MW; 032E81C6CEF4CED2 CRC64;
MTQVDHTRMA NAIRGLAMDA VEKAKSGHPG LPMGAADIAT VLFTQFLKFD VAAPTWPDRD
RFVLSAGHGS MLLYALLYLT GNKDMTLDQI RNFRQLGSKT PGHPENFETS GVETTTGPLG
QGIATSIGMA LAEKMLAAEF GKKVVSHHTY VLASDGDLME GVSQEAIAMA GHWKLNKLIV
LYDNNGISID GPTSLADSVD QVKRFKSAGW AAELIDGQDP KAIAAAISRA QKSNKPSLIS
CKTTIGYGAP TRAGTAKAHG EALGADELKG AKEKLGISLD AFSVPDDVLK AWRAAGSRGA
AAREEWESVF AELGPRKRAE FERRMRHERP AALSKALRAH KKALLESPQN VATRKSSESA
IEAIAAAMPM EFLAGSADLT GSNNNKAKSA VAFSAKMPKG RFIHYGIREH GMAAAMNGIF
LHGGFAPNGA TFLVFTDYAR PAMRLAALMG AGVVYVMTHD SIGLGEDGPT HQPVEHLAAL
RAIPNMRVFR PCDAVEVAEC WELALNRVDG PTVLALTRQN LPQLRTNAPN DNPCAHGAYE
LVAAQGNAKV SLFASGSEVE IAVAAQKQLS ERGIPSRVVS VPSLELLLAQ PADRKAAIIG
DAPVKVAIEA AVRWGWDAVI GQDGEFIGMH GFGASAPAKD LFKHFGITAE AAVNAVLKRL
G
//
