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Database: UniProt
Entry: A0A089WMI1_9PSED
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ID   A0A089WMI1_9PSED        Unreviewed;       665 AA.
AC   A0A089WMI1;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=LK03_03505 {ECO:0000313|EMBL:AIR88364.1};
OS   Pseudomonas cremoricolorata.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=157783 {ECO:0000313|EMBL:AIR88364.1, ECO:0000313|Proteomes:UP000029493};
RN   [1] {ECO:0000313|EMBL:AIR88364.1, ECO:0000313|Proteomes:UP000029493}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND07 {ECO:0000313|EMBL:AIR88364.1,
RC   ECO:0000313|Proteomes:UP000029493};
RA   Chan K.-G.;
RL   Submitted (SEP-2014) 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}.
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DR   EMBL; CP009455; AIR88364.1; -; Genomic_DNA.
DR   RefSeq; WP_038411082.1; NZ_CP009455.1.
DR   AlphaFoldDB; A0A089WMI1; -.
DR   STRING; 157783.LK03_03505; -.
DR   KEGG; psw:LK03_03505; -.
DR   eggNOG; COG0021; Bacteria.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000029493; Chromosome.
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; 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|ARBA:ARBA00022837, 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:UP000029493};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          12..32
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   665 AA;  72241 MW;  D9D16A8BC0CD5492 CRC64;
     MPSRRERANA IRALSMDAVQ KANSGHPGAP MGMADIAEVL WRDYLKHNPS NPHFADRDRF
     VLSNGHGSML IYSLLHLTGY DLSIDDLKGF RQLHSRTPGH PEFGYTAGVE TTTGPLGQGL
     ANAVGFAIAE KVMAGQFNRE GHDIVDHHTY VFLGDGCMME GVSHEVASLA GTLGLNKLIA
     FYDDNGISID GEVHGWFTDD TPKRFEAYNW QVIRNVNGHD ADEIKTAIET ARKSDRPTLI
     CCKTIIGFGS PNKQGKEESH GAALGADEIV LTRNGLNWSH EAFQIPAEIY AEWDAKDAGA
     KAEAEWNQRF DAYAQAHPEL AAEFKRRSSG ELPADFAEKA AAYVQQVAEK GETIASRKAS
     QNTLNAFGPL LPELLGGSAD LAASNLTLWK GCKGVEATDA SGNYLFYGVR EFGMTAIMNG
     LALHGGLVPY GATFLMFMEY ARNAVRMSAL MKQRVIHVYT HDSIGLGEDG PTHQPIEQLT
     SLRTTPNLDT WRPADAVESA VCWQQALLRN DGPSALIFSR QNLQHQARSA EQIAQISQGG
     YVLRDCAGEP ELILIATGSE VGLAVQAFDA LSAQGRKVRV VSMPCTSVFD AQDAAYKQSV
     LPVEVGARIA IEAAHADYWY KYVGLDGRII GMTTYGESAP ASALFEAFGF TLDNVLAVAE
     ELLED
//
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