ID A8BVD3_GIAIC Unreviewed; 719 AA.
AC A8BVD3;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:EDO76940.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:EDO76940.1};
GN ORFNames=GL50803_009704 {ECO:0000313|EMBL:KAE8302687.1}, GL50803_9704
GN {ECO:0000313|EMBL:EDO76940.1};
OS Giardia intestinalis (strain ATCC 50803 / WB clone C6) (Giardia lamblia).
OC Eukaryota; Metamonada; Diplomonadida; Hexamitidae; Giardiinae; Giardia.
OX NCBI_TaxID=184922 {ECO:0000313|EMBL:EDO76940.1};
RN [1] {ECO:0000313|EMBL:EDO76940.1, ECO:0000313|Proteomes:UP000001548}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50803 / WB clone C6 {ECO:0000313|Proteomes:UP000001548},
RC and WB C6 {ECO:0000313|EMBL:EDO76940.1};
RX PubMed=17901334; DOI=10.1126/science.1143837;
RA Morrison H.G., McArthur A.G., Gillin F.D., Aley S.B., Adam R.D.,
RA Olsen G.J., Best A.A., Cande W.Z., Chen F., Cipriano M.J., Davids B.J.,
RA Dawson S.C., Elmendorf H.G., Hehl A.B., Holder M.E., Huse S.M., Kim U.U.,
RA Lasek-Nesselquist E., Manning G., Nigam A., Nixon J.E., Palm D.,
RA Passamaneck N.E., Prabhu A., Reich C.I., Reiner D.S., Samuelson J.,
RA Svard S.G., Sogin M.L.;
RT "Genomic minimalism in the early diverging intestinal parasite Giardia
RT lamblia.";
RL Science 317:1921-1926(2007).
RN [2] {ECO:0000313|EMBL:KAE8302687.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=WB C6 {ECO:0000313|EMBL:KAE8302687.1};
RA Xu F., Jex A., Svard S.G.;
RT "New Giardia intestinalis WB genome in near-complete chromosomes.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
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 -!- 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|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:EDO76940.1}.
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DR EMBL; AACB02000051; EDO76940.1; -; Genomic_DNA.
DR EMBL; AACB03000003; KAE8302687.1; -; Genomic_DNA.
DR RefSeq; XP_001704614.1; XM_001704562.1.
DR AlphaFoldDB; A8BVD3; -.
DR STRING; 184922.A8BVD3; -.
DR EnsemblProtists; EDO76940; EDO76940; GL50803_9704.
DR GeneID; 5697492; -.
DR KEGG; gla:GL50803_009704; -.
DR VEuPathDB; GiardiaDB:GL50803_9704; -.
DR HOGENOM; CLU_009227_0_0_1; -.
DR InParanoid; A8BVD3; -.
DR OMA; ADYMRGS; -.
DR Proteomes; UP000001548; Chromosome 3.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
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; IPR049557; Transketolase_CS.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 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.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000001548};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EDO76940.1}.
FT DOMAIN 358..529
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 719 AA; 77564 MW; 529358E2C84424A0 CRC64;
MLDGIDGRCI NAIRCLSVDQ VNAANSGHPG TPIGFAPAAY ILFKEFLQFD PSDPLWINRD
RFVLSNGHAS PLIYSLLHLF GYNLSMDDLR HFRQLGSHTP GHPERDISRG IEITTGALGQ
GIGSAVGMAL ASKCAAAQYP GVFTNKVICV VGDGCLQEGV SAEASSLAGR LQLNNLIVLY
DDNGITIDGK TAISFTEDVA RRYQAYGWQV LEVKNGNTGL EELRSVIGKA YTSLLSCPTL
VIIKTTIGYG TAKQGTAAVH GAPLGESTRQ FKELIGVNPD LEFHVSDEVR NNFESIIAKK
KAAHAKWTKN VFERLAPDVR VTIERRFKGL EHRTLSELFA KADHEYEKLV AANVGKRLAS
RQMSQQILDL LATHVLGDSM LIGSADLASS NLTKVSAFTA VADGFTKGSN YVNYGVREHA
MAAISNGIGA HGGFVSFDAT FLMFFSYCCA GIRNGALSEV PAIHVFTHDS FFLGEDGGTH
HPIETVAWIR SMPRVIDWRP CSLAEVYGVY MTALADDVKI TIHGNGTGLQ AKDPHTYPMS
KLQHIVCLSR QALDDVPNSS ARAVLKGAYS VHETGGLGAF TTNITDGKHL ILLSSGSEVG
LCLKATDALV KQIPEASVRV VSMPSYTIFN SQPFSEQNAV LPCLTTPGIP CLSVEPYTSF
GIAGKYAHKS VSIEDFSFSG KPDDLARHFN MTVTNVVDIA QAMLAQNSSS PSPALMWMQ
//
