ID A0A193G9J4_9BORD Unreviewed; 947 AA.
AC A0A193G9J4;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=Transaldolase {ECO:0000256|HAMAP-Rule:MF_00493};
DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00493};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00493};
GN ORFNames=BAU07_05550 {ECO:0000313|EMBL:ANN76657.1};
OS Bordetella flabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN76657.1, ECO:0000313|Proteomes:UP000091926};
RN [1] {ECO:0000313|EMBL:ANN76657.1, ECO:0000313|Proteomes:UP000091926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10664 {ECO:0000313|EMBL:ANN76657.1,
RC ECO:0000313|Proteomes:UP000091926};
RA LiPuma J.J., Spilker T.;
RT "Complete genome sequences of Bordetella bronchialis and Bordetella
RT flabilis.";
RL Submitted (JUN-2016) 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_00493}.
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_00493};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate;
CC Xref=Rhea:RHEA:11816, ChEBI:CHEBI:57634, ChEBI:CHEBI:58225;
CC EC=5.3.1.9; Evidence={ECO:0000256|RuleBase:RU000612};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 2/4.
CC {ECO:0000256|RuleBase:RU000612}.
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_00493}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00493}.
CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000256|RuleBase:RU000612}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 2 subfamily.
CC {ECO:0000256|ARBA:ARBA00008426, ECO:0000256|HAMAP-Rule:MF_00493}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP016172; ANN76657.1; -; Genomic_DNA.
DR RefSeq; WP_066654843.1; NZ_CP016172.1.
DR AlphaFoldDB; A0A193G9J4; -.
DR STRING; 463014.BAU07_05550; -.
DR KEGG; bfz:BAU07_05550; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000091926; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0097367; F:carbohydrate derivative binding; IEA:InterPro.
DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IEA:UniProtKB-EC.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00955; Transaldolase_like; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00493; Transaldolase_2; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001672; G6P_Isomerase.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004732; Transaldolase_2.
DR InterPro; IPR018225; Transaldolase_AS.
DR NCBIfam; TIGR00876; tal_mycobact; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF31; TRANSALDOLASE; 1.
DR Pfam; PF00342; PGI; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR PRINTS; PR00662; G6PISOMERASE.
DR SUPFAM; SSF51569; Aldolase; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00493};
KW Gluconeogenesis {ECO:0000256|RuleBase:RU000612};
KW Glycolysis {ECO:0000256|RuleBase:RU000612};
KW Isomerase {ECO:0000256|RuleBase:RU000612};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW Rule:MF_00493};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00493}; Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT ACT_SITE 145
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 947 AA; 100901 MW; E4F92CCD31F6569F CRC64;
MNQTAKNPLG RLAEAGQAIW LDFLSREFLA AGGLDKLVRE DSLTGVTSNP SIFEKAMGHG
EVYDEQLHAI LYQADAEPGD VYERLAVHDI RTAADALRPV YDRLQGKDGY VSLEVSPYLA
YDTEGTLAEA RRLWQAVDRP NLMIKVPGTP AGVPAIRQLI EEGINVNVTL LFSRQAYREV
ALAYIDGLEA RVRAGKPVDR LASVASFFVS RIDTRIDKKI DDALQRPGAD SGALSALKGK
VAIANAKLAY QDYLALIGEE RWKALAQRGA QPQRLLWAST GTKNPAYPPT LYIDELIGPD
TVNTMPAGTM DAFRDGGKVK ASLTADIDAA RRVLDDAERL GLDLDAVTRE LVEDGTRQFS
DAFDALLGAV GAKRLAYLGD RINGAAYELP AALSEAVERT LDRARVDGWA RRVWQGDATL
WTGQQEDRWV GWLAAGQGRQ IDADAIAALA RDLQAERYAH AVLLGMGGSS LGPEVLGQTL
GEAGQGLALH ALDSTSPDEI CAVERGIDIA RTLFIVSSKS GSTLEPEILN AYFHAAAVAA
LGAEQAGSHF VAITDPGSKL EAAAQQAGYR AIFHGDPTIG GRYSVLSVFG MVPLGVMGHN
VAHFMDGTQP MVRACGPSSP PAINPGLRLG AILGEAAKAG RDKVTVFASP TVASIGSWLE
QLLAESTGKQ GKGIVPVDLE PIGAPDVYGQ DRVFAYVRCA TDDTTQLDAK VQALAAAGHP
VIRITLPRAT AIGQEFFRWE IATAIAGAVI GIDPFDQPDV EASKVKTRAL TDAYEKTGKL
PPETPIAEDG ELAFFGDAAL AGDGTVEGVV GAHLARLRPG DYAAVLAYIA RNAAHERQLA
ALRTALRDRR KVATVGGFGP RFLHSTGQAY KGGPNSGVFL QITADPAHDL QVPGRKISFG
TVQAAQALGD LQVLAERGRR YLRVHIRGGD VESGLARLAK AVKQVLN
//
