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TKTP_CUPNH
ID   TKTP_CUPNH              Reviewed;         670 AA.
AC   P21726;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   03-AUG-2022, entry version 149.
DE   RecName: Full=Transketolase, plasmid;
DE            Short=TK;
DE            EC=2.2.1.1;
GN   Name=cbbTP; OrderedLocusNames=PHG420;
OS   Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS   / H16 / Stanier 337) (Ralstonia eutropha).
OG   Plasmid megaplasmid pHG1.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8226680; DOI=10.1128/jb.175.22.7329-7340.1993;
RA   Schaeferjohann J., Yoo J.-G., Kusian B., Bowien B.;
RT   "The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus
RT   encode phosphoglycolate phosphatase.";
RL   J. Bacteriol. 175:7329-7340(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX   PubMed=12948488; DOI=10.1016/s0022-2836(03)00894-5;
RA   Schwartz E., Henne A., Cramm R., Eitinger T., Friedrich B., Gottschalk G.;
RT   "Complete nucleotide sequence of pHG1: a Ralstonia eutropha H16 megaplasmid
RT   encoding key enzymes of H(2)-based lithoautotrophy and anaerobiosis.";
RL   J. Mol. Biol. 332:369-383(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-77.
RX   PubMed=2559876; DOI=10.1016/0378-1119(89)90490-3;
RA   Kossmann J., Klintworth R., Bowien B.;
RT   "Sequence analysis of the chromosomal and plasmid genes encoding
RT   phosphoribulokinase from Alcaligenes eutrophus.";
RL   Gene 85:247-252(1989).
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:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250};
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+). {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250};
CC   -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}.
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DR   EMBL; M68905; AAA20194.1; -; Unassigned_DNA.
DR   EMBL; AY305378; AAP86169.1; -; Genomic_DNA.
DR   EMBL; M33562; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   PIR; C49934; C49934.
DR   RefSeq; WP_011154332.1; NZ_CP039289.1.
DR   AlphaFoldDB; P21726; -.
DR   SMR; P21726; -.
DR   STRING; 381666.PHG420; -.
DR   EnsemblBacteria; AAP86169; AAP86169; PHG420.
DR   GeneID; 39976481; -.
DR   KEGG; reh:PHG420; -.
DR   PATRIC; fig|381666.6.peg.348; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_4; -.
DR   OMA; YALQQTD; -.
DR   OrthoDB; 188169at2; -.
DR   UniPathway; UPA00116; -.
DR   Proteomes; UP000008210; Plasmid megaplasmid pHG1.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR   CDD; cd02012; TPP_TK; 1.
DR   Gene3D; 3.40.50.920; -; 1.
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   PANTHER; PTHR43522; PTHR43522; 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; SSF52518; 2.
DR   SUPFAM; SSF52922; SSF52922; 1.
DR   TIGRFAMs; TIGR00232; tktlase_bact; 1.
DR   PROSITE; PS00801; TRANSKETOLASE_1; 1.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Calcium; Calvin cycle; Magnesium; Metal-binding; Plasmid;
KW   Reference proteome; Thiamine pyrophosphate; Transferase.
FT   CHAIN           1..670
FT                   /note="Transketolase, plasmid"
FT                   /id="PRO_0000191892"
FT   ACT_SITE        417
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         32
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         120..122
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         161
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         162
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         191
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         193
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         267
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         364
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         391
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         443
FT                   /ligand="thiamine diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58937"
FT                   /evidence="ECO:0000250"
FT   BINDING         467
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         475
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         526
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            32
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
FT   SITE            267
FT                   /note="Important for catalytic activity"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   670 AA;  71474 MW;  A71583509327627A CRC64;
     MNAPERIDPA ARCANALRFL AADAVELARS GHPGAPMGMA EMAEVVWRRH LRHNPANPAW
     PDRDRFVLSN GHASMLQYAL LHLTGYDLPM SQLRQFRQLH AVTPGHPEVD VTPGVETTTG
     PLGQGLANAV GMALAEKLLA ATFNRPGFDI VDHHTYVFLG DGCLMEGLSH EACSLAGTLG
     LGKLICLYDD NGISIDGEVA GWFADDTPKR FAAYGWHVIA DVDGHDAHAL DAALHEAKAE
     RDRPTLICCR TVIGKGAPAK AGGHDVHGAP LGAPEIAAMR TALGWEAEPF TVPADVADAW
     DARAQGAARE AEWEARFVSY CAAHPELAEE FVRRANGRLP EGFDAELMAL LDAPSPLQGK
     IATRKASQLC LEALTPALPE LLGGSADLTG SNLTNVKASV WVNHAGHGNY VSYGVREFGM
     AAVMNGIALH GGLIPYGGTF MTFSDYSRNA IRMAALMRLR VVHVLTHDSI GLGEDGPTHQ
     PVEHAASLRL IPNNQVWRPC DGAETAYAWL AALQRENGPT CLVLSRQALM PFERDAAQRA
     DIARGGYVLR DVPAPRVVLI ATGSEVEIAA RAALDLADAG IAARVVSMPC VELFYAQDAA
     YRDSVLPPGL PRISVEAGAT WYWRGVVGEQ GLALGIDSFG ESAPAEALYQ HFGLTPAHVA
     AAARVLLEDA
 
 
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