UniProt: A0A1S1NQD6

Database: UniProt
Entry: A0A1S1NQD6_9GAMM

LinkDB:  A0A1S1NQD6_9GAMM 
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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (7)   
   InterPro (4)   
   Pfam (1)   
   PROSITE (2)   
All databases (16)   

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ID   A0A1S1NQD6_9GAMM        Unreviewed;       323 AA.
AC   A0A1S1NQD6;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
DE            EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
GN   Name=tal {ECO:0000256|HAMAP-Rule:MF_00492,
GN   ECO:0000313|EMBL:QEL10199.1};
GN   ORFNames=BH688_16065 {ECO:0000313|EMBL:OHV07703.1}, FY550_02990
GN   {ECO:0000313|EMBL:QEL10199.1};
OS   Kushneria phosphatilytica.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Kushneria.
OX   NCBI_TaxID=657387 {ECO:0000313|EMBL:OHV07703.1, ECO:0000313|Proteomes:UP000179907};
RN   [1] {ECO:0000313|EMBL:OHV07703.1, ECO:0000313|Proteomes:UP000179907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:OHV07703.1,
RC   ECO:0000313|Proteomes:UP000179907};
RA   Wang C., Qu L.;
RT   "The draft genome suquence of Kushneria sp. YCWA18.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:QEL10199.1, ECO:0000313|Proteomes:UP000322553}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YCWA18 {ECO:0000313|EMBL:QEL10199.1,
RC   ECO:0000313|Proteomes:UP000322553};
RA   Du G.-X., Qu L.-Y.;
RT   "Complete genome sequence of Kushneria sp. YCWA18, a halophilic phosphate-
RT   solubilizing bacterium isolated from Daqiao saltern in China.";
RL   Submitted (AUG-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC       the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518,
CC       ECO:0000256|HAMAP-Rule:MF_00492, ECO:0000256|RuleBase:RU004155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC         beta-D-fructose 6-phosphate + D-erythrose 4-phosphate;
CC         Xref=Rhea:RHEA:17053, ChEBI:CHEBI:16897, ChEBI:CHEBI:57483,
CC         ChEBI:CHEBI:57634, ChEBI:CHEBI:59776; EC=2.2.1.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00001469, ECO:0000256|HAMAP-
CC         Rule:MF_00492, ECO:0000256|RuleBase:RU004155};
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 stage):
CC       step 2/3. {ECO:0000256|ARBA:ARBA00004857, ECO:0000256|HAMAP-
CC       Rule:MF_00492, ECO:0000256|RuleBase:RU004155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492}.
CC   -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC       {ECO:0000256|ARBA:ARBA00008012, ECO:0000256|HAMAP-Rule:MF_00492,
CC       ECO:0000256|RuleBase:RU004155}.
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DR   EMBL; MKZT01000024; OHV07703.1; -; Genomic_DNA.
DR   EMBL; CP043420; QEL10199.1; -; Genomic_DNA.
DR   RefSeq; WP_070981580.1; NZ_MKZT01000024.1.
DR   AlphaFoldDB; A0A1S1NQD6; -.
DR   STRING; 657387.BH688_16065; -.
DR   KEGG; kuy:FY550_02990; -.
DR   OrthoDB; 9809101at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000179907; Unassembled WGS sequence.
DR   Proteomes; UP000322553; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004801; F:transaldolase 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; cd00957; Transaldolase_TalAB; 1.
DR   Gene3D; 3.20.20.70; Aldolase class I; 1.
DR   HAMAP; MF_00492; Transaldolase_1; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR001585; TAL/FSA.
DR   InterPro; IPR004730; Transaldolase_1.
DR   InterPro; IPR018225; Transaldolase_AS.
DR   NCBIfam; TIGR00874; talAB; 1.
DR   PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR   PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR   Pfam; PF00923; TAL_FSA; 1.
DR   SUPFAM; SSF51569; Aldolase; 1.
DR   PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR   PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492};
KW   Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW   Rule:MF_00492}; Reference proteome {ECO:0000313|Proteomes:UP000179907};
KW   Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW   Rule:MF_00492};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00492}.
FT   REGION          257..285
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        134
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ   SEQUENCE   323 AA;  36032 MW;  0E8D74E8E1FBDCAB CRC64;
     MATQLESLKA LSKVVADTGD LEAIKKYQPY DSTTNPSLLL KAFDLEGYQE LIDKTLAEVK
     KETEGQSREA RLEHAVDRLS VVVGTEITKL VPGRVSTEVA SKLSFDQQAS IDKARKLVEL
     YEKADVSRDR ILIKLASTWE GIRAAEILQK EGINCNLTLL FSDAQARACF EAGVFLISPF
     VGRVTDWYKQ RDGVEHYAPD DDPGVKFVRG VADYSNRYGY ETVVMGASFR NTDQIKALAG
     LNRLTISPNL LEELANSEGE VERKLTDNAT SGGGSEQRGE KMTEAQFRWE HNQDAMANDK
     LAEGIRKFAE DQEKLEGLIE KRM
//

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