ID Q6FAV8_ACIAD Unreviewed; 329 AA.
AC Q6FAV8;
DT 19-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 19-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 140.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU004155};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|RuleBase:RU004155};
GN Name=tal {ECO:0000313|EMBL:CAG68805.1};
GN OrderedLocusNames=ACIAD1980 {ECO:0000313|EMBL:CAG68805.1};
OS Acinetobacter baylyi (strain ATCC 33305 / BD413 / ADP1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=62977 {ECO:0000313|EMBL:CAG68805.1, ECO:0000313|Proteomes:UP000000430};
RN [1] {ECO:0000313|EMBL:CAG68805.1, ECO:0000313|Proteomes:UP000000430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33305 / BD413 / ADP1 {ECO:0000313|Proteomes:UP000000430};
RX PubMed=15514110; DOI=10.1093/nar/gkh910;
RA Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L.,
RA Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N.,
RA Weissenbach J., Marliere P., Cohen G.N., Medigue C.;
RT "Unique features revealed by the genome sequence of Acinetobacter sp. ADP1,
RT a versatile and naturally transformation competent bacterium.";
RL Nucleic Acids Res. 32:5766-5779(2004).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518,
CC 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,
CC 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,
CC ECO:0000256|RuleBase:RU004155}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012, ECO:0000256|RuleBase:RU004155}.
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DR EMBL; CR543861; CAG68805.1; -; Genomic_DNA.
DR RefSeq; WP_004927298.1; NC_005966.1.
DR AlphaFoldDB; Q6FAV8; -.
DR STRING; 202950.GCA_001485005_00389; -.
DR GeneID; 45234342; -.
DR KEGG; aci:ACIAD1980; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_047470_0_1_6; -.
DR OrthoDB; 9809101at2; -.
DR BioCyc; ASP62977:ACIAD_RS09115-MONOMER; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000000430; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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 Pentose shunt {ECO:0000256|ARBA:ARBA00023126,
KW ECO:0000256|RuleBase:RU004155};
KW Reference proteome {ECO:0000313|Proteomes:UP000000430};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004155}.
SQ SEQUENCE 329 AA; 36449 MW; 79589AA327608B0A CRC64;
MTQSALDQLK KLTTVVADSS DIEAIRKFLP LDATTNPSLI TAAASIPENK ALIEDAFNQA
HQEGYENDLL IERTIDILTV KFGVEILKLI QGRVSTEVDA SLSYNTEATI EKARELSKLY
KEYGIDQSRI LIKIASTWQG IQAAKVLEAE GIPCNLTLLF GLHQAQACAD AKVTLISPFV
GRILDWYKKA ENVDHYPIEK DPGVVSVKKI FTYYKQQGTP TQVMGASFRS IDQVLGLAGS
DLLTISPALL SELEQDHRTV EATLTIEEAK QAEIIHRAAQ TEQSFKDELE HDLMAFQLLQ
SGIDGFIKAR EQLSTLLRQS YGIDAEIQP
//
