ID C5ASU4_METEA Unreviewed; 941 AA.
AC C5ASU4;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 108.
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_META1p4950 {ECO:0000313|EMBL:ACS42557.1};
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:ACS42557.1, ECO:0000313|Proteomes:UP000009081};
RN [1] {ECO:0000313|EMBL:ACS42557.1, 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; ACS42557.1; -; Genomic_DNA.
DR RefSeq; WP_003600150.1; NC_012808.1.
DR AlphaFoldDB; C5ASU4; -.
DR STRING; 272630.MexAM1_META1p4950; -.
DR KEGG; mea:Mex_1p4950; -.
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; cd05798; SIS_TAL_PGI; 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:ACS42557.1};
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:ACS42557.1}.
FT ACT_SITE 141
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 941 AA; 101063 MW; 4857AC1664DA1AA6 CRC64;
MNALNALFAE HEQAVWLDFV ARGFIAKGEL QALVEKDDLR GVTSNPAIFE KAIGHSAEYD
DSLKAVLSQG DARVIDLYEG LAIADIQAAA DVLRRVYDTS DGADGYVSLE VSPYLALDTE
ETLNEARRLH AAVGRDNLMV KVPATPAGLP AIRQLTAEGI SVNITLLFSQ SVYEEVANAF
IDGLTEFGAK GGDVSKVASV ASFFISRIDS LVDKKLDEVG GYEDLKGKVA IANAKLAYQR
YKRIFSGPKW EALEAKGAKA QRLLWASTGT KNKAYSDVLY VEELIGKNTV NTMPPATMDA
FRDHGRVRAT LEENIGEAET VMARLAEAGI DIEAVARQLV EEGVQLFVDA ADALLGAVAG
KRAALLDHRL DAQTFKFDEP LQAATDKAVE SWRASGAIRR LWAHDATVWT GRDEGKWLGW
LRIVEDELER VDLYESFAEE VRAEGFTDAV VLGMGGSSLG PEVISATYGH REGFPKLRIL
DSTDPDEVRA VEAAVNLETT LFIVASKSGS TLEPNVFRDY FLGRMKEVVG ADKAGRHFVA
VTDPGSAMEK AAKDDNFRKI FLGVPQIGGR YSVLSAFGLV PAAAAGVEIR EFLDSARMMV
RSCGPAVPPA VNPGVRLGAA MGVAAKDFGR DKITIIASPG IGTFGTWAEQ LIAESTGKEG
VGIIPVEGEP VGVPAVYGED RLFVYLRLTS QADARQDEAV KILESEAQPV VRIDLDKVEQ
LPQEFFRFEI ATAVAGAVLG INPFDQPDVE ASKIETKKLF ASAEETGALP AETPIFEDET
VALYADAANA EALRSGEGFE AIVAAHLARV KPCDYVAVLA YVERNEAHQA ALQEARLTVR
DARQVATCLE FGPRFLHSTG QAYKGGPASG VFLQITADPS ADLPIPGRKL GFKTVIAAQA
RGDFAVLSER KRRALRIHLK GGDVSGGVKR VAAAIKAAVA G
//
