ID A0A0S8KQ05_9CHLR Unreviewed; 913 AA.
AC A0A0S8KQ05;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=AMJ93_04210 {ECO:0000313|EMBL:KPL23644.1};
OS Anaerolineae bacterium SM23_84.
OC Bacteria; Chloroflexota; Anaerolineae.
OX NCBI_TaxID=1703388 {ECO:0000313|EMBL:KPL23644.1, ECO:0000313|Proteomes:UP000052016};
RN [1] {ECO:0000313|EMBL:KPL23644.1, ECO:0000313|Proteomes:UP000052016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM23_84 {ECO:0000313|EMBL:KPL23644.1};
RX PubMed=25922666; DOI=10.1186/s40168-015-0077-6;
RA Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RT "Genomic resolution of linkages in carbon, nitrogen, and sulfur cycling
RT among widespread estuary sediment bacteria.";
RL Microbiome 3:14-14(2015).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KPL23644.1}.
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DR EMBL; LJUZ01000040; KPL23644.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0S8KQ05; -.
DR PATRIC; fig|1703388.3.peg.3788; -.
DR UniPathway; UPA00109; UER00181.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000052016; Unassembled WGS sequence.
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|HAMAP-Rule:MF_00493};
KW Schiff base {ECO:0000256|HAMAP-Rule:MF_00493};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00493}.
FT ACT_SITE 138
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00493"
SQ SEQUENCE 913 AA; 98596 MW; 2491670ADB79FB66 CRC64;
MTKLHELAEL GQAVWLDYIR RSFIVSGDLQ ALVDDGLRGV TSNPSIFEKA IAGSIDYDQH
LHRLVDDGRS VQEIYEALTL DDIRRAADGL RPVYDTTDRV DGYVSLEVSP TLAQDTGGTV
AEADRLFKAL DRPNIMIKVP ATPEGIPAIE RLIGEGINVN VTLMFSLAHY DAVAKAYLAG
LEKFMMAGGD LSRVASVASF FISRVDGVVD PQLEAAGNAE LQGKIAVANA KLAYARFRET
FSGKRWERLA AEGARVQRPL WASTSTKNPL YSDVLYVDSL IGPLTVNTMP PQTLNAFRDH
GTVAVTVDKE LDEARAQIDQ LAELGIDLDA ITEKLQDDGV AAFVKSFEGL MASIAEKRER
LLVGWQHITA TLGTYQPAVD AALAQMAKQK ITARIWAHDH TVWKSDPAEI TNRLGWLHIA
EAMLENVSRL HESAEQARAA GYTHALLLGM GGSSLAPEVF RNTFGVKEGH LDLTVLDSTD
PGAVLAHADL LQLSRTLFIV STKSGGTAET LSFFKFFYNR VAEVVGADHA GEHFVAITDP
GTQLVDLAKR YHFRATFLND PNIGGRYSAL SYFGLVPAAL IGANVKLLLQ RAQETDAACA
SCLADTENPG AWLGTILGVL ANLGRDKLTL VTTPAIASFG NWVEQLIAES TGKDGRGILP
VVGEPLAGAL AYGDDRLFVA LELAGEDLDK EALAVLEDIG HPVVRLYLRD LYDLGQQMLL
WEMATAAAGY HLGINPFDQP NVESAKALAR EAIAAYMDKG ALPRPESVPP TGETLLGFLD
QARAGDYVSL QAYVTPTAST DAALHELRTR LRDHLKLAAT SGYGPRFLHS TGQLHKGDAG
NGLFIQFTAN DARDVAIPDE AGSTASTMTF GVLKEAQVQG DYQALRKAGR RVIRFHLGDD
VVGGLRVLAN ALK
//
