ID F3ZX24_MAHA5 Unreviewed; 216 AA.
AC F3ZX24;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=Probable transaldolase {ECO:0000256|HAMAP-Rule:MF_00494};
DE EC=2.2.1.2 {ECO:0000256|HAMAP-Rule:MF_00494};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00494};
GN OrderedLocusNames=Mahau_0255 {ECO:0000313|EMBL:AEE95473.1};
OS Mahella australiensis (strain DSM 15567 / CIP 107919 / 50-1 BON).
OC Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacterales Family IV. Incertae Sedis; Mahella.
OX NCBI_TaxID=697281 {ECO:0000313|EMBL:AEE95473.1, ECO:0000313|Proteomes:UP000008457};
RN [1] {ECO:0000313|Proteomes:UP000008457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC {ECO:0000313|Proteomes:UP000008457};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Teshima H., Brettin T.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Pukall R.,
RA Steenblock K., Schneider S., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Mahella australiensis DSM 15567.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEE95473.1, ECO:0000313|Proteomes:UP000008457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15567 / CIP 107919 / 50-1 BON
RC {ECO:0000313|Proteomes:UP000008457};
RX PubMed=21886860;
RA Sikorski J., Teshima H., Nolan M., Lucas S., Hammon N., Deshpande S.,
RA Cheng J.F., Pitluck S., Liolios K., Pagani I., Ivanova N., Huntemann M.,
RA Mavromatis K., Ovchinikova G., Pati A., Tapia R., Han C., Goodwin L.,
RA Chen A., Palaniappan K., Land M., Hauser L., Ngatchou-Djao O.D., Rohde M.,
RA Pukall R., Spring S., Abt B., Goker M., Detter J.C., Woyke T., Bristow J.,
RA Markowitz V., Hugenholtz P., Eisen J.A., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Mahella australiensis type strain (50-1
RT BON).";
RL Stand. Genomic Sci. 4:331-341(2011).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|HAMAP-Rule:MF_00494}.
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_00494};
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_00494}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00494}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B subfamily.
CC {ECO:0000256|ARBA:ARBA00005740, ECO:0000256|HAMAP-Rule:MF_00494}.
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DR EMBL; CP002360; AEE95473.1; -; Genomic_DNA.
DR RefSeq; WP_013779906.1; NC_015520.1.
DR AlphaFoldDB; F3ZX24; -.
DR STRING; 697281.Mahau_0255; -.
DR KEGG; mas:Mahau_0255; -.
DR eggNOG; COG0176; Bacteria.
DR HOGENOM; CLU_079764_0_0_9; -.
DR OrthoDB; 9807051at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000008457; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016832; F:aldehyde-lyase activity; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniRule.
DR CDD; cd00956; Transaldolase_FSA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00494; Transaldolase_3b; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR022999; Transaldolase_3B.
DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase.
DR InterPro; IPR018225; Transaldolase_AS.
DR InterPro; IPR033919; TSA/FSA_arc/bac.
DR NCBIfam; TIGR00875; fsa_talC_mipB; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF36; TRANSALDOLASE-RELATED; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00494};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW Rule:MF_00494}; Reference proteome {ECO:0000313|Proteomes:UP000008457};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00494};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00494}.
FT ACT_SITE 83
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
SQ SEQUENCE 216 AA; 23550 MW; 9419929C30656CC2 CRC64;
MKLFIDTANV DEIKEANDWG VICGVTTNPS LVAKEGRDFM QVLKEICGIV DGPISAEVIS
TQHEGMVEEA KKLAAVHPNV IIKIPMLPEG LKAVKILSQQ GIKTNVTLIF SAAQALLAAR
AGATYVSPFV GRLDDVANEG MQVVKDIADI FLLHDIPTQI IAASIRHPMH VIEAAKAGSH
IATVPYKVLQ QMFSHPLTDI GIERFLKDWE GVKFKF
//
