ID I4Z5X2_9BURK Unreviewed; 321 AA.
AC I4Z5X2;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=Transaldolase {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151, ECO:0000256|HAMAP-Rule:MF_00492};
GN Name=tal {ECO:0000256|HAMAP-Rule:MF_00492};
GN ORFNames=LepocDRAFT_00003460 {ECO:0000313|EMBL:EIM31614.1};
OS Leptothrix ochracea L12.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Leptothrix.
OX NCBI_TaxID=735332 {ECO:0000313|EMBL:EIM31614.1, ECO:0000313|Proteomes:UP000053899};
RN [1] {ECO:0000313|EMBL:EIM31614.1, ECO:0000313|Proteomes:UP000053899}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EIM31614.1,
RC ECO:0000313|Proteomes:UP000053899};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA Kyrpides N., Ivanova N., Pagani I., Stepanauskas R., Masland D.,
RA Poulton N., Emerson D., Fleming E., Woyke T.;
RT "Improved High-Quality Draft sequence of Leptothrix ochracea L12.";
RL Submitted (APR-2012) 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_00492, ECO:0000256|RuleBase:RU004155}.
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_00492, ECO:0000256|RuleBase:RU004155};
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_00492, ECO:0000256|RuleBase:RU004155}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012, ECO:0000256|HAMAP-Rule:MF_00492,
CC ECO:0000256|RuleBase:RU004155}.
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DR EMBL; JH660673; EIM31614.1; -; Genomic_DNA.
DR RefSeq; WP_009453271.1; NZ_JH660673.1.
DR AlphaFoldDB; I4Z5X2; -.
DR HOGENOM; CLU_047470_0_1_4; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000053899; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR HAMAP; MF_00492; Transaldolase_1; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR001585; TAL/FSA.
DR InterPro; IPR004730; Transaldolase_1.
DR InterPro; IPR018225; Transaldolase_AS.
DR NCBIfam; TIGR00874; talAB; 1.
DR PANTHER; PTHR10683; TRANSALDOLASE; 1.
DR PANTHER; PTHR10683:SF18; TRANSALDOLASE; 1.
DR Pfam; PF00923; TAL_FSA; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS01054; TRANSALDOLASE_1; 1.
DR PROSITE; PS00958; TRANSALDOLASE_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00492};
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126, ECO:0000256|HAMAP-
KW Rule:MF_00492}; Reference proteome {ECO:0000313|Proteomes:UP000053899};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270, ECO:0000256|HAMAP-
KW Rule:MF_00492};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00492}.
FT ACT_SITE 126
FT /note="Schiff-base intermediate with substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00492"
SQ SEQUENCE 321 AA; 34833 MW; 25BD3ECBFD349B9C CRC64;
MPTQLEHLKQ FTTVVADTGN FRQLAQFAPH DATTNPSLIL KAVQQPEYAP LLAECVATHR
GKPLPDIVDQ VLVRFGCEIL ALIPGRVSTE VDARLSFDTA ATVARAHRLM ALYQHAGVPR
ERVLIKVAAT WEGIQAARVL EREGIHCNLT LLFSFCQAVA CGEAGVTLIS PFVGRIYDWY
KKSAGLGWDE LAHAGLNDPG VRSVTQIYTY YKHFGISTEV MGASFRNVGQ ILALAGCDLL
TISPDLLALL QSADVEAAPV VRILDPEAAK VAHMPAISYH EAAFRYALND DAMATEKLAE
GIRAFAGDAV KLDKMIELAL G
//
