(data stored in SCRATCH zone)

SWISSPROT: Q2IMN0_ANADE

ID   Q2IMN0_ANADE            Unreviewed;       665 AA.
AC   Q2IMN0;
DT   07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT   07-MAR-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   OrderedLocusNames=Adeh_0289 {ECO:0000313|EMBL:ABC80065.1};
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397 {ECO:0000313|EMBL:ABC80065.1, ECO:0000313|Proteomes:UP000001935};
RN   [1] {ECO:0000313|Proteomes:UP000001935}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2CP-C {ECO:0000313|Proteomes:UP000001935};
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from
CC       a ketose donor to an aldose acceptor, via a covalent intermediate
CC       with the cofactor thiamine pyrophosphate.
CC       {ECO:0000256|RuleBase:RU004996}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-
CC         phosphate; Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57737, ChEBI:CHEBI:58273, ChEBI:CHEBI:59776;
CC         EC=2.2.1.1; Evidence={ECO:0000256|RuleBase:RU004996};
CC   -!- SUBUNIT: Homodimer. {ECO:0000256|RuleBase:RU004996}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|RuleBase:RU004996, ECO:0000256|SAAS:SAAS01133303}.
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DR   EMBL; CP000251; ABC80065.1; -; Genomic_DNA.
DR   RefSeq; WP_011419348.1; NC_007760.1.
DR   STRING; 290397.Adeh_0289; -.
DR   EnsemblBacteria; ABC80065; ABC80065; Adeh_0289.
DR   KEGG; ade:Adeh_0289; -.
DR   eggNOG; ENOG4105CV1; Bacteria.
DR   eggNOG; COG0021; LUCA.
DR   HOGENOM; HOG000225954; -.
DR   KO; K00615; -.
DR   OMA; FADYMRG; -.
DR   BioCyc; ADEH290397:G1G5W-296-MONOMER; -.
DR   Proteomes; UP000001935; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; PTHR43522; 1.
DR   Pfam; PF02779; Transket_pyr; 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;
DR   PRODOM; Q2IMN0.
DR   SWISS-2DPAGE; Q2IMN0.
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001935};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460037};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460052};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001935};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS01133301};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00460013, ECO:0000313|EMBL:ABC80065.1}.
FT   DOMAIN       17     37       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   665 AA;  71201 MW;  95DE4E940483A708 CRC64;
     MPNARPELVE KAVNTIRMLA ADGVQQANSG HPGMPMGAAD MAFVLWTRHL RFDPAEPRWL
     GRDRFLLSAG HGSMLLYSLL HLAGFDCTLD DLKKFRQLHS RTPGHPEYGH LPGVEITSGP
     LGQGFANGVG FALGHAMLSA KLGPANPVAD AFVYAIVSDG DLMEGVSAEA ASFAGHHKLG
     RLVYLYDDNG ITIDGKTSIT FSGEDVTKRF EAYGWHVQSV DGRDLDGIDR AIQAAKAELG
     RPSLVRVHTT IGFGSPGKAG KSSVHGAPLG EAELEATKKA LGWPLEPRFL VPDDVRAYWA
     EVRAEKAAQK QAWSAAEHAW RAANPEQAAL LDAHVERWVP ERILDRARAE LPAPDATRKV
     SQAILQKIAP LVPCLVGGSA DLAESNLTEI KGAGSVAPGS FAGRNVHFGI REHAMGAIAN
     GLAYDGLFVP FVGTFLQFAD YMRPPVRLAA LSKLQAIYVW THDSIFLGED GPTHQPIEHL
     TALRAIPNLH VCRPADPEET AAAWAHALQR RDGPTALVLT RQKLAPVKRS VPLDPEAILR
     GGYLVDAPAG ATFTLAATGS EVPLAQAALE ALAKQGVVGR LASIPCLECF LAQPKAWRDE
     VVPPGQRVAV VEAARGTEWW QLAGRDGLVL GIERFGSSAP EKALAEDYGF TPAQVAGRVA
     RWLAG
//

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