(data stored in ACNUC7421 zone)

SWISSPROT: D6ZBX6_SEGRD

ID   D6ZBX6_SEGRD            Unreviewed;       373 AA.
AC   D6ZBX6;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 59.
DE   RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118670};
DE            EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000256|SAAS:SAAS00118670};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN   OrderedLocusNames=Srot_0466 {ECO:0000313|EMBL:ADG96953.1};
OS   Segniliparus rotundus (strain ATCC BAA-972 / CDC 1076 / CIP 108378 /
OS   DSM 44985 / JCM 13578).
OC   Bacteria; Actinobacteria; Corynebacteriales; Segniliparaceae;
OC   Segniliparus.
OX   NCBI_TaxID=640132 {ECO:0000313|EMBL:ADG96953.1, ECO:0000313|Proteomes:UP000002247};
RN   [1] {ECO:0000313|EMBL:ADG96953.1, ECO:0000313|Proteomes:UP000002247}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-972 / CDC 1076 / CIP 108378 / DSM 44985 / JCM 13578
RC   {ECO:0000313|Proteomes:UP000002247};
RX   PubMed=21304703; DOI=10.4056/sigs.791633;
RA   Sikorski J., Lapidus A., Copeland A., Misra M., Glavina Del Rio T.,
RA   Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Jando M.,
RA   Schneider S., Bruce D., Goodwin L., Pitluck S., Liolios K.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chertkov O., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Brettin T., Detter J.C., Han C., Rohde M., Goker M.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P.;
RT   "Complete genome sequence of Segniliparus rotundus type strain (CDC
RT   1076).";
RL   Stand. Genomic Sci. 2:203-211(2010).
CC   -!- FUNCTION: Transaldolase is important for the balance of
CC       metabolites in the pentose-phosphate pathway. {ECO:0000256|HAMAP-
CC       Rule:MF_00493}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-
CC         phosphate = beta-D-fructose 6-phosphate + D-erythrose 4-
CC         phosphate; Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897,
CC         ChEBI:CHEBI:57483, ChEBI:CHEBI:57634, ChEBI:CHEBI:59776;
CC         EC=2.2.1.2; Evidence={ECO:0000256|HAMAP-Rule:MF_00493,
CC         ECO:0000256|SAAS:SAAS01126537};
CC   -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-
CC       glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-
CC       ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative
CC       stage): step 2/3. {ECO:0000256|HAMAP-Rule:MF_00493,
CC       ECO:0000256|SAAS:SAAS00118684}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493,
CC       ECO:0000256|SAAS:SAAS00118691}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_00493}.
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DR   EMBL; CP001958; ADG96953.1; -; Genomic_DNA.
DR   RefSeq; WP_013137409.1; NC_014168.1.
DR   STRING; 640132.Srot_0466; -.
DR   EnsemblBacteria; ADG96953; ADG96953; Srot_0466.
DR   KEGG; srt:Srot_0466; -.
DR   eggNOG; ENOG4107QQX; Bacteria.
DR   eggNOG; COG0176; LUCA.
DR   HOGENOM; HOG000226074; -.
DR   KO; K00616; -.
DR   OMA; ATECYYQ; -.
DR   OrthoDB; 417261at2; -.
DR   BioCyc; SROT640132:G1GLH-466-MONOMER; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000002247; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR   CDD; cd00955; Transaldolase_like; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   HAMAP; MF_00493; Transaldolase_2; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004732; Transaldolase_2.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   PANTHER; PTHR10683; PTHR10683; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   PIRSF; PIRSF036915; Trnald_Bac_Plnt; 1.
DR   TIGRFAMs; TIGR00876; tal_mycobact; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6ZBX6.
DR   SWISS-2DPAGE; D6ZBX6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002247};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00476608};
KW   Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118654};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002247};
KW   Schiff base {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118695};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00493,
KW   ECO:0000256|SAAS:SAAS00118651, ECO:0000313|EMBL:ADG96953.1}.
FT   ACT_SITE    144    144       Schiff-base intermediate with substrate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00493}.
SQ   SEQUENCE   373 AA;  39771 MW;  DE32B6F59B4DB69D CRC64;
     MSGQQNANLK ALSEAGVSVW LDDLSRDRLR TGNLAELIAT RSVVGVTTNP TIFQGALSKG
     EAYEAQISEI VARGADVEAV ITALTTDDVR AACDVFAPVY ERSGGVDGRV SIEVDPRLAH
     DTEGTVAQAL ELWKIVDRPN LLVKIPATKA GLPAITRVIA EGVSVNVTLI FSIERHSAVI
     DAYIAGVQAA AAAGRDLSKI HSVASFFISR VDSEVDERLG KVGTDAAKAL LGKAALANGV
     LAYELYQQKF SSDEFAELKA AGANPQRALW ASTGTKNPNY PDTLYVSDLV APNTVNTMPE
     KTLEAFADHG EVRLHSVVGK VQNAHDVFDQ LAEAGVDMDD VFEVLETQGV EKFIASWQEL
     LDATAEKLNG LRG
//

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