ID C5B1R8_METEA Unreviewed; 950 AA.
AC C5B1R8;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 106.
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 OrderedLocusNames=MexAM1_META1p1862 {ECO:0000313|EMBL:ACS39702.1};
OS Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB
OS 9133 / AM1) (Methylobacterium extorquens).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylorubrum.
OX NCBI_TaxID=272630 {ECO:0000313|EMBL:ACS39702.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS39702.1, ECO:0000313|Proteomes:UP000009081}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1
RC {ECO:0000313|Proteomes:UP000009081};
RX PubMed=19440302; DOI=10.1371/journal.pone.0005584;
RA Vuilleumier S., Chistoserdova L., Lee M.-C., Bringel F., Lajus A., Zhou Y.,
RA Gourion B., Barbe V., Chang J., Cruveiller S., Dossat C., Gillett W.,
RA Gruffaz C., Haugen E., Hourcade E., Levy R., Mangenot S., Muller E.,
RA Nadalig T., Pagni M., Penny C., Peyraud R., Robinson D.G., Roche D.,
RA Rouy Z., Saenampechek C., Salvignol G., Vallenet D., Wu Z., Marx C.J.,
RA Vorholt J.A., Olson M.V., Kaul R., Weissenbach J., Medigue C.,
RA Lidstrom M.E.;
RT "Methylobacterium genome sequences: a reference blueprint to investigate
RT microbial metabolism of C1 compounds from natural and industrial sources.";
RL PLoS ONE 4:E5584-E5584(2009).
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}.
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DR EMBL; CP001510; ACS39702.1; -; Genomic_DNA.
DR RefSeq; WP_012752672.1; NC_012808.1.
DR AlphaFoldDB; C5B1R8; -.
DR STRING; 272630.MexAM1_META1p1862; -.
DR KEGG; mea:Mex_1p1862; -.
DR eggNOG; COG0166; Bacteria.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_013922_0_0_5; -.
DR OrthoDB; 140919at2; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000009081; 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; cd05015; SIS_PGI_1; 1.
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; IPR035476; SIS_PGI_1.
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, ECO:0000313|EMBL:ACS39702.1};
KW Pentose shunt {ECO:0000256|HAMAP-Rule:MF_00493};
KW Reference proteome {ECO:0000313|Proteomes:UP000009081};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493, ECO:0000313|EMBL:ACS39702.1}.
FT ACT_SITE 140
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 950 AA; 102358 MW; B2B53F142C1A6161 CRC64;
MNPLKALQDQ GQAVWLDFVA RGFMADGHLK KLVEEDGLRG VTSNPAIFEK AIAHSDEYDT
SLRSAEAGAD VPVIALFEQL AIEDIRNAAD VLRPVYDATD GADGFVSLEV SPYLALETED
TIAEGRRLWR EVGRENLMIK VPATQAGLPA IRHLIGEGIN VNVTLLFAQD VYEAVANAYI
EGLEALAAKG NVSRVASVAS FFVSRIDSAI DQRLDQKIRE ANDPDEKAAL ERLKGKVAIA
NAKLAYQRYK RLFATSRWNG LAVRGARPQR LLWASTGAKN KAYRDVLYVE ELIGPDAVNT
MPPATLDAFR DHGRVRPSLE EGVGEAQRAL VALARAGISL DEVTAGLVDD GVRLFVDAAD
KLLGAVASKR AAILGTRLNR QTLALGADLD REVGATIEQW RANAAARRLW RKDKSLWTGA
DEDRWLGWLD IIDRELGRVD AYRAFAEDVR REGFSDAVLL GMGGSSLGPE VLAETVGAAP
GFPRLRILDS TDPAQVRAME EAIDLHRTLF IVSSKSGSTL EPNIFKDYFF ERVASVVGPE
RAGQRFVAVT DPGSSMEQAA QAARFWRIFH GDPGIGGRYS VLSAFGLVPA AAAGLDVGRF
LESACLMARS CGPDVPPAEN PGVRLGLAMG LAARQGRDKV TVVAAPSIAA FGAWAEQLIA
ESTGKDGKGL IPVAAEPLGP PEIYGQDRFF IHLRLEGKRD DSQEAALGAL ETAGHPVARI
DLASPDGIVQ EFFRWEFATA VAGAVIGINP FDQPDVEASK VRTRELTAAY EKSGELPLEM
PLFSGEGVEV YADPRNADAL RELVRDDHLE GWLRAHLRRL TPGDYFALLA YVARTQEHTA
ALQNVRLAVR DARRVATCLG FGPRFLHSTG QAYKGGPNSG VFLQVTADGA EDLAIPGHAF
GFGTVKAAQA RGDFEVLADR GRRALRVHLK GGDVAAGLGS LGAALRRALA
//
