ID A0A060NPF3_9BURK Unreviewed; 321 AA.
AC A0A060NPF3;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=transaldolase {ECO:0000256|ARBA:ARBA00013151};
DE EC=2.2.1.2 {ECO:0000256|ARBA:ARBA00013151};
GN ORFNames=SMCB_1022 {ECO:0000313|EMBL:BAO83250.1};
OS Serpentinimonas maccroryi.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Serpentinimonas.
OX NCBI_TaxID=1458426 {ECO:0000313|EMBL:BAO83250.1, ECO:0000313|Proteomes:UP000066014};
RN [1] {ECO:0000313|EMBL:BAO83250.1, ECO:0000313|Proteomes:UP000066014}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B1 {ECO:0000313|EMBL:BAO83250.1,
RC ECO:0000313|Proteomes:UP000066014};
RX PubMed=24845058; DOI=10.1038/ncomms4900;
RA Suzuki S., Kuenen J.G., Schipper K., van der Velde S., Ishii S., Wu A.,
RA Sorokin D.Y., Tenney A., Meng X.Y., Morrill P.L., Kamagata Y., Muyzer G.,
RA Nealson K.H.;
RT "Physiological and genomic features of highly alkaliphilic hydrogen-
RT utilizing Betaproteobacteria from a continental serpentinizing site.";
RL Nat. Commun. 5:3900-3900(2014).
CC -!- FUNCTION: Transaldolase is important for the balance of metabolites in
CC the pentose-phosphate pathway. {ECO:0000256|ARBA:ARBA00003518}.
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};
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}.
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transaldolase family. Type 1 subfamily.
CC {ECO:0000256|ARBA:ARBA00008012}.
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DR EMBL; AP014569; BAO83250.1; -; Genomic_DNA.
DR RefSeq; WP_045535536.1; NZ_AP014569.1.
DR AlphaFoldDB; A0A060NPF3; -.
DR STRING; 1458426.SMCB_1022; -.
DR KEGG; cbab:SMCB_1022; -.
DR HOGENOM; CLU_047470_0_1_4; -.
DR OrthoDB; 9809101at2; -.
DR UniPathway; UPA00115; UER00414.
DR Proteomes; UP000066014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004801; F:transaldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR CDD; cd00957; Transaldolase_TalAB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 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.
PE 3: Inferred from homology;
KW Pentose shunt {ECO:0000256|ARBA:ARBA00023126};
KW Schiff base {ECO:0000256|ARBA:ARBA00023270};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ SEQUENCE 321 AA; 35189 MW; D943BFFDF48853CF CRC64;
MNQLEALKQH STVVADTGDF LQLAQFQPQD ATTNPSLILK SVQKPDYAPL LAQTVARFGG
RPSDEIVDRL LVRFGCEILA IVPGRVSTEV DARLSFDTAA TIERAERLMA LYQAEGVPSD
RVLIKIAATW EGIEAAAQLE RRGIRTNLTL LFAFCQALAC AQARVQLISP FVGRIYDWHK
KQAGSQWDEA ARAGEHDPGV QSVRRIFEYY KRFGIGTEIM GASFRNCGQI VALAGCDLLT
ISPELLAQLA QPVASTDALP RALDADAARE LDLQPLQHDQ ASFRLALNED AMASEKLAEG
IRAFCADSVR LEQLIAARQG R
//
