ID A0A0A0MBC0_9GAMM Unreviewed; 662 AA.
AC A0A0A0MBC0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=N791_04655 {ECO:0000313|EMBL:KGO99567.1};
OS Lysobacter defluvii IMMIB APB-9 = DSM 18482.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=1385515 {ECO:0000313|EMBL:KGO99567.1, ECO:0000313|Proteomes:UP000030003};
RN [1] {ECO:0000313|EMBL:KGO99567.1, ECO:0000313|Proteomes:UP000030003}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IMMIB APB-9 {ECO:0000313|EMBL:KGO99567.1,
RC ECO:0000313|Proteomes:UP000030003};
RA Wang Q., Wang G.;
RT "Genomic analysis of Lysobacter defluvii.";
RL Submitted (AUG-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=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|ARBA:ARBA00001941};
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:KGO99567.1}.
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DR EMBL; AVBH01000010; KGO99567.1; -; Genomic_DNA.
DR RefSeq; WP_027069372.1; NZ_AVBH01000010.1.
DR AlphaFoldDB; A0A0A0MBC0; -.
DR STRING; 1385515.GCA_000423325_00906; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000030003; 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:UP000030003};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 357..529
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 662 AA; 71847 MW; A893E6D0886D233C CRC64;
MPTPTRRDLA NAIRFLAIDA VQAANSGHPG MPMGMADIAE VLWNDYLSHN PANPGWLNRD
RFVLSNGHGS MLQYALLHLA GYDLPIEELK NFRQLGSKTP GHPENFVTTG VETTTGPLGQ
GFANAVGFAL AEKLLAQRFN RDGHEIVDHR TWVFMGDGCL MEGISHEAAS LAGTWGLNKL
VAFWDDNSIS IDGDVAGWFT DDTPARFEAY GWNVVRGIDG HDPESIKAGI EQALACSDRP
TLICCRTTIG YGSPKHAGKE SSHGAPLGLE DIAACRTGLC WEHEPFHVPQ DIYDAWNATG
AGREREEAWN QAMAAYREAF PEQAAEFERR MRGELPADFA THADEYIAKL QAEGPKVASR
KASQMAIEAY APRLPELVGG SADLAGSNLT LWSGSKTVAS TDPDANYIYF GVREFAMSAI
SNGLALHGGF IPYDATFLVF SDYARNAVRM SALMGARAVH VYTHDSIGLG EDGPTHQPIE
HLASLRYIPH NDVWRPCDAV ESAVAWKAAV ERADGPSCLV FSRQNLDPQQ REPGQVADIA
RGGYVLKDSA GEPELILIAT GSEVGLAMQA AQELGDSVRV VSMPSTDVFD RQDQAYRESV
LPRACRKRVA IEAGVSDFWR KYVGLDGAVI GIDRFGASAP AGDLFKHFGF TVDNVVEAAR
SL
//
