(data stored in SCRATCH zone)

SWISSPROT: C3MIA2_SINFN

ID   C3MIA2_SINFN            Unreviewed;       663 AA.
AC   C3MIA2;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   07-JUN-2017, entry version 62.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   Name=cbbT {ECO:0000313|EMBL:ACP24450.1};
GN   OrderedLocusNames=NGR_c06570 {ECO:0000313|EMBL:ACP24450.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP24450.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP24450.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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: Sedoheptulose 7-phosphate + D-glyceraldehyde
CC       3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
CC       {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:SAAS00651207}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001389; ACP24450.1; -; Genomic_DNA.
DR   RefSeq; WP_012707235.1; NC_012587.1.
DR   RefSeq; YP_002825203.1; NC_012587.1.
DR   ProteinModelPortal; C3MIA2; -.
DR   STRING; 394.NGR_c06570; -.
DR   EnsemblBacteria; ACP24450; ACP24450; NGR_c06570.
DR   GeneID; 7791883; -.
DR   KEGG; rhi:NGR_c06570; -.
DR   PATRIC; fig|394.7.peg.3470; -.
DR   eggNOG; ENOG4105CV1; Bacteria.
DR   eggNOG; COG0021; LUCA.
DR   HOGENOM; HOG000225953; -.
DR   KO; K00615; -.
DR   OMA; LCFIRTS; -.
DR   OrthoDB; POG091H02B4; -.
DR   Proteomes; UP000001054; Chromosome.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008152; P:metabolic process; IEA:InterPro.
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;
DR   PRODOM; C3MIA2.
DR   SWISS-2DPAGE; C3MIA2.
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651225};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Thiamine pyrophosphate {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651235};
KW   Transferase {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651241}.
FT   DOMAIN       14     34       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   663 AA;  71175 MW;  E6B67E5E80FF6C52 CRC64;
     MTAVSVRDLA NAIRVLSIDG VEAANSGHPG MPMGMADAAA VLFGKHLKFD ASEPGWPDRD
     RFVLSNGHGS MLLYSLLHLT GYKEMTIEEI RNFRQWDSKT PGHPEYGHTA GVETTTGPLG
     QGIASAVGMA IAERRLGAEF GTALVDHHTY VFCGDGCLME GVGQEAASLA GHLQLGKLIV
     LYDDNSITID GSTAIAFSED VLARFDAYGW HTQRVDGHDA EAIDAAISNA KAETSRPSLV
     ALKTIIGFGS PSKAGKSSVH GAPLGASEAA ATKTAYGWTA DPFEIPTPIL ETWRAIGAKG
     AKSRREWQAR LEAAEPDVKS EFERRTAGSL PPHYEETVNA AKANLLDRPQ SVATRKASQI
     ALEALTELLP EMIGGSADLT HSNLTRVPAV DSDFTAVRSG RYVSYGVREF AMAAAMNGMA
     VHGGFIPYGG TFLVFSDYCR NAIRVAALMG ARSIFVMTHD SIGLGEDGPT HQPVEHLASL
     RAMPNLHVFR PADTIETLEC WDIAITSKNT PSVLALSRQN VPQLRSERDG SNRCARGAYV
     LREASRERAV TLIATGTEVV LAIQAAEELE ARNIPAAVVS MPSWDLFEKQ ARDYRHAVLG
     DAPRIAVEAL SKFGWTRYVD SEDDVIGMSG FGASAPAETL YEKFGITRDA IVARAVARVR
     GEE
//

If you have problems or comments...

PBIL Back to PBIL home page