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Database: UniProt
Entry: A0A1W9I444_9PROT
LinkDB: A0A1W9I444_9PROT
Original site: A0A1W9I444_9PROT 
ID   A0A1W9I444_9PROT        Unreviewed;       655 AA.
AC   A0A1W9I444;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
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=A4S15_04425 {ECO:0000313|EMBL:OQW54463.1};
OS   Proteobacteria bacterium SG_bin8.
OC   Bacteria; Pseudomonadota.
OX   NCBI_TaxID=1827387 {ECO:0000313|EMBL:OQW54463.1, ECO:0000313|Proteomes:UP000192872};
RN   [1] {ECO:0000313|EMBL:OQW54463.1, ECO:0000313|Proteomes:UP000192872}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SG_bin8 {ECO:0000313|EMBL:OQW54463.1};
RX   PubMed=28390307; DOI=10.1016/j.watres.2017.03.042;
RA   Wang Y., Ma L., Mao Y., Jiang X., Xia Y., Yu K., Li B., Zhang T.;
RT   "Comammox in drinking water systems.";
RL   Water Res. 116:332-341(2017).
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:OQW54463.1}.
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DR   EMBL; LWDL01000003; OQW54463.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9I444; -.
DR   STRING; 1827387.A4S15_04425; -.
DR   Proteomes; UP000192872; 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; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW   ECO:0000256|RuleBase:RU004996};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT   DOMAIN          6..26
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   655 AA;  69207 MW;  AEBD71AB3F6539E0 CRC64;
     MASAVRALAI DGVEAAKSGH PGLPLGAADI ATVLFTSFLR YDASNPSWPD RDRFILSAGH
     GSMLVYALLH LLDFPGMSME EIRRFRQKGS KTPGHPEFGH TAGIEMTTGP LGQGLASAVG
     MAIAETSLAA RFGSDLVDHR TVVLCSDGDL MEGISQEAIA LAGHLRLNKL IVLWDDNNIS
     IDGPLSLSDS TDQLARFAAS NWATDRVDGH DPNAILAALE RARASERPTL IACRTIIGYG
     APKKAGTSKA HGEPLGADEL TATKAALGWT AESFTVPDDV RAAWREAGKR AAATHVAWQA
     RLAATDEATR NEFIRSIAGT LPAGLSVALD AVKASALANP QSVATRKASE IVLEAINAVL
     PETIGGSADL SPSNLTRTKT LTPYSATGRA GRYIHFGIRE HAMAAAMNGM ALHGGIIPYA
     GTFLVFADYC RPSLRLAALM GVRVVHVMTH DSIGVGEDGP THQPVEHLAA LRAIPNLLVF
     RPCDTVEAAE AWLSALSHQH APSIIALSRQ AVPQSRSKSS ADNQVSRGAY EISPSSKPAA
     VTLFASGTEV SLALAAQKMI EAEGYGARVV SVPCFELFEA QDATYRRTVI GEAGVRIAIE
     AAIRQGWDRF IGEAGIFVGM SGFGMSAPYA EIYDHFAITP TAVTAKALDA LRRND
//
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