ID E8QVB3_HELPW Unreviewed; 643 AA.
AC E8QVB3;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
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 OrderedLocusNames=HPSA_01815 {ECO:0000313|EMBL:ADU84384.1};
OS Helicobacter pylori (strain SouthAfrica7).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=907239 {ECO:0000313|EMBL:ADU84384.1, ECO:0000313|Proteomes:UP000007467};
RN [1] {ECO:0000313|Proteomes:UP000007467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica7 {ECO:0000313|Proteomes:UP000007467};
RA Kersulyte D., Segal I., Mistry R., Berg D.E.;
RT "Genome sequence of Helicobacter pylori strain SouthAfrica7.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADU84384.1, ECO:0000313|Proteomes:UP000007467}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SouthAfrica7 {ECO:0000313|EMBL:ADU84384.1,
RC ECO:0000313|Proteomes:UP000007467};
RX PubMed=24072860;
RA Duncan S.S., Bertoli M.T., Kersulyte D., Valk P.L., Tamma S., Segal I.,
RA McClain M.S., Cover T.L., Berg D.E.;
RT "Genome Sequences of Three hpAfrica2 Strains of Helicobacter pylori.";
RL Genome Announc. 1:e00729-13(2013).
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}.
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DR EMBL; CP002336; ADU84384.1; -; Genomic_DNA.
DR RefSeq; WP_001177254.1; NC_017361.1.
DR AlphaFoldDB; E8QVB3; -.
DR KEGG; hes:HPSA_01815; -.
DR PATRIC; fig|907239.3.peg.362; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_7; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000007467; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
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};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 407..428
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 344..510
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 643 AA; 70927 MW; 04A3F758085526A6 CRC64;
MQLSNADLER LKSMANTLRF LCADMIDKAN SGHPGVCLGL ADVMVVLSLH LNLNPTNPKW
LNRDRLVFSG GHASALAYSL LHLWGFDLSL EDLKHFRQLH SKTPGHPELH HTEGIEITTG
PLGQGFANAV GFSMASQYAQ TLLNKETISH KVYCLCGDGD LQEGISYESA SLAGHLRLDN
LIVIYDSNQI SIEGAINISF SEHVKMRFLA QNWEVLECDG HDYQAINDAL ETAKKATKPT
LLIAHTIIGK GAIGLEGSEK THGSPLNKEV LKQSKENACI NPNESFIISP KNKMHFEEVK
VRGISLEALW EKSLSPKIKE KIHALKNFDF NTIHYPTFKQ GESLATRVSN GMILNAIAKE
CEGFLGGSAD LAPSNNTHLK HSSDFPLGQN LHFGIREHAM GAITNALAAY GLFLPFCATF
FVFSDYLMPS MRLSALMRLK ALFIFTHDSI GVGEDGATHQ PIEQLSHLRA LPNFYAFRPS
DAFENTACMQ AALNLNAPSA FILSRQNLPV LDEVSKEQVL KGAYVKHPSK DPIITLVASG
SEVSLALESA KILERENIPT QVISAPCFDL LIEQDESYLK ELFKGKVLVV EASRAIEWYR
FADKIICMDS FGSSAKGDKL FEKFGFSVEN ITNQAKRLLN ACI
//
