(data stored in ACNUC7421 zone)

SWISSPROT: A0A0H2ZKT8_PSEAB

ID   A0A0H2ZKT8_PSEAB        Unreviewed;       665 AA.
AC   A0A0H2ZKT8;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   07-JUN-2017, entry version 17.
DE   RecName: Full=Transketolase {ECO:0000256|RuleBase:RU004996};
DE            EC=2.2.1.1 {ECO:0000256|RuleBase:RU004996};
GN   Name=tktA {ECO:0000313|EMBL:ABJ15511.1};
GN   OrderedLocusNames=PA14_07130 {ECO:0000313|EMBL:ABJ15511.1};
OS   Pseudomonas aeruginosa (strain UCBPP-PA14).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208963 {ECO:0000313|EMBL:ABJ15511.1, ECO:0000313|Proteomes:UP000000653};
RN   [1] {ECO:0000313|EMBL:ABJ15511.1, ECO:0000313|Proteomes:UP000000653}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCBPP-PA14 {ECO:0000313|EMBL:ABJ15511.1,
RC   ECO:0000313|Proteomes:UP000000653};
RX   PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90;
RA   Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S.,
RA   Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L.,
RA   Grills G., Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.;
RT   "Genomic analysis reveals that Pseudomonas aeruginosa virulence is
RT   combinatorial.";
RL   Genome Biol. 7:R90.1-R90.14(2006).
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; CP000438; ABJ15511.1; -; Genomic_DNA.
DR   RefSeq; WP_003110216.1; NC_008463.1.
DR   ProteinModelPortal; A0A0H2ZKT8; -.
DR   SMR; A0A0H2ZKT8; -.
DR   EnsemblBacteria; ABJ15511; ABJ15511; PA14_07130.
DR   KEGG; pau:PA14_07130; -.
DR   KO; K00615; -.
DR   OMA; FADYMRG; -.
DR   Proteomes; UP000000653; 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; A0A0H2ZKT8.
DR   SWISS-2DPAGE; A0A0H2ZKT8.
KW   Calcium {ECO:0000256|RuleBase:RU004996};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000653};
KW   Magnesium {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651250};
KW   Metal-binding {ECO:0000256|RuleBase:RU004996,
KW   ECO:0000256|SAAS:SAAS00651225};
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       12     32       TRANSKETOLASE_1. {ECO:0000259|PROSITE:
FT                                PS00801}.
SQ   SEQUENCE   665 AA;  72220 MW;  9D3D8836AF99CA52 CRC64;
     MPSRRERANA IRALSMDAVQ KANSGHPGAP MGMADIAEVL WRDYMQHNPS NPQWANRDRF
     VLSNGHGSML IYSLLHLTGY DLGIEDLKNF RQLNSRTPGH PEYGYTAGVE TTTGPLGQGI
     ANAVGMALAE KVLAAQFNRD GHAVVDHYTY AFLGDGCMME GISHEVASLA GTLRLNKLIA
     FYDDNGISID GEVHGWFTDD TPKRFEAYGW QVIRNVDGHD ADEIKTAIDT ARKSDQPTLI
     CCKTVIGFGS PNKQGKEECH GAPLGADEIA ATRAALGWEH APFEIPAQIY AEWDAKETGA
     AQEAEWNKRF AAYQAAHPEL AAELLRRLKG ELPADFAEKA AAYVADVANK GETIASRKAS
     QNALNAFGPL LPELLGGSAD LAGSNLTLWK GCKGVSADDA AGNYVFYGVR EFGMSAIMNG
     VALHGGFIPY GATFLIFMEY ARNAVRMSAL MKQRVLYVFT HDSIGLGEDG PTHQPIEQLA
     SLRLTPNLDT WRPADAVESA VAWKHAIERA DGPSALIFSR QNLPHQARDV AQVADIARGG
     YVLKDCEGEP ELILIATGSE VGLAVQAYDK LSEQGRKVRV VSMPCTSVYE QQDESYKQSV
     LPVEVGARIA IEAAHADYWY KYVGLDGRII GMTSFGESAP APALFEHFGF TLDNVLAVAE
     ELLED
//

If you have problems or comments...

PBIL Back to PBIL home page