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Database: UniProt
Entry: A0A222SKG3_9CHLB
LinkDB: A0A222SKG3_9CHLB
Original site: A0A222SKG3_9CHLB 
ID   A0A222SKG3_9CHLB        Unreviewed;       668 AA.
AC   A0A222SKG3;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 28.
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   Name=tkt {ECO:0000313|EMBL:ASQ91222.1};
GN   ORFNames=CHL67_10135 {ECO:0000313|EMBL:ASQ91222.1};
OS   Prosthecochloris sp. GSB1.
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC   Prosthecochloris.
OX   NCBI_TaxID=281093 {ECO:0000313|EMBL:ASQ91222.1, ECO:0000313|Proteomes:UP000201322};
RN   [1] {ECO:0000313|Proteomes:UP000201322}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TY Vent \ GSB1 \ Ty-1 {ECO:0000313|Proteomes:UP000201322};
RA   Bryant D.A., Liu Z., Li T., Zhao F., Garcia Costas A.M.;
RL   Submitted (JUL-2017) 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=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; CP022571; ASQ91222.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A222SKG3; -.
DR   KEGG; pros:CHL67_10135; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000201322; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000201322};
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        413..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          15..35
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
FT   REGION          98..117
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   668 AA;  72759 MW;  099D8C9E9603D02B CRC64;
     MHTDQIDRLA IDTIRLLAVD MVEKAQSGHP GMPMGAAPMA YVLWTKIMKH NPENPHWLNR
     DRFVLSAGHG SALLYALLHL TGYDLSMEDL KEFRQWGSKT PGHPEYGHTP GVETTTGPLG
     QGLSNAVGMA IAERYCAERL NKKDFDLIDY HTYVICGDGD LMEGVTSEAA SIAGHLKLDK
     LVCLYDHNRI SIEGSTDLAF TESVHQRFEA YGWDVENVDG NDPEAVETAI LRAKKISGKP
     SLIIARTNIG FGSPNKQDSA SSHGSPLGAE EAAMVRKIFG FPEHSSFHVP ESVAAHMKNV
     LEKGREQETA WNELRRSFGE RHPDSASMLD AMHGHRLPDG WETLLPVFSP DEKLATRQAS
     SKVLHALVGK LPFLIGGSAD LAPSTGTAVR HAVDFTAENY GGENFRFGVR EHAMGAILNG
     MALSGMIIPY GATFLVFSDY MKPALRLSAL MNVPSVFIFT HDSIAVGEDG PTHQPIEHLA
     MLRSIPGLTV IRPADAQETK SAWRTTLMSR KPTALVFSRQ GLPVLDAEKY PVAEGAPKGA
     YILCDWSGAS GGGNRPVILV ATGAEVHLAL EAREQLEDEG IPARVVSMPS WELFEAQPAS
     YREEVLPSGM RRRVIVEAAS TFGWHRYATD EGTVLGIDRF GSSAPGGTVL KEYGFTVEHV
     VQAAKNLP
//
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