ID B0VRM3_ACIBS Unreviewed; 329 AA.
AC B0VRM3;
DT 08-APR-2008, integrated into UniProtKB/TrEMBL.
DT 08-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 108.
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:CAP01541.1};
GN OrderedLocusNames=ABSDF2217 {ECO:0000313|EMBL:CAP01541.1};
OS Acinetobacter baumannii (strain SDF).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=509170 {ECO:0000313|EMBL:CAP01541.1, ECO:0000313|Proteomes:UP000001741};
RN [1] {ECO:0000313|EMBL:CAP01541.1, ECO:0000313|Proteomes:UP000001741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SDF {ECO:0000313|EMBL:CAP01541.1,
RC ECO:0000313|Proteomes:UP000001741};
RX PubMed=18350144; DOI=10.1371/journal.pone.0001805;
RA Vallenet D., Nordmann P., Barbe V., Poirel L., Mangenot S., Bataille E.,
RA Dossat C., Gas S., Kreimeyer A., Lenoble P., Oztas S., Poulain J.,
RA Segurens B., Robert C., Abergel C., Claverie J.-M., Raoult D., Medigue C.,
RA Weissenbach J., Cruveiller S.;
RT "Comparative analysis of Acinetobacters: three genomes for three
RT lifestyles.";
RL PLoS ONE 3:E1805-E1805(2008).
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; CU468230; CAP01541.1; -; Genomic_DNA.
DR AlphaFoldDB; B0VRM3; -.
DR KEGG; abm:ABSDF2217; -.
DR HOGENOM; CLU_047470_0_1_6; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000001741; 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 Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004155}.
SQ SEQUENCE 329 AA; 36335 MW; 8377316436DF623E CRC64;
MTHTALDQLK TLTTVVADSS DLEAIRKFRP LDATTNPSLI TAAAEQPESK ELIEDAYYQA
KEEGYKNDEL IERTIDILTV KFGVEILKLI EGRVSTEVDT ALSYDTEATI QKAHELCELY
KGYGIDQSRI LIKIASTWEG IQAAKVLEAE GIACNLTLLF GLHQAQACAD AKVTLISPFV
GRILDWYKKA EGVDSYPIEK DPGVVSVKKI YTYYKQQNIP TQVMGASFRS IDQVLGLAGC
DLLTISPSLL TQLEQDTRTV DAALDANKAK QAEAIVRPAQ DEQSFKDELN HDLMAFQLLQ
GGVDGFIKAR DQLSLLLRQS FGIDAEIKS
//
