GenomeNet

Database: UniProt
Entry: A0A086BLI4_9FLAO
LinkDB: A0A086BLI4_9FLAO
Original site: A0A086BLI4_9FLAO 
ID   A0A086BLI4_9FLAO        Unreviewed;       217 AA.
AC   A0A086BLI4;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
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   ORFNames=IQ37_03850 {ECO:0000313|EMBL:KFF29798.1};
OS   Chryseobacterium piperi.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=558152 {ECO:0000313|EMBL:KFF29798.1, ECO:0000313|Proteomes:UP000028709};
RN   [1] {ECO:0000313|EMBL:KFF29798.1, ECO:0000313|Proteomes:UP000028709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTM {ECO:0000313|EMBL:KFF29798.1,
RC   ECO:0000313|Proteomes:UP000028709};
RA   Pipes S.E., Stropko S.J., Newman J.D.;
RT   "Genome of Chryseobacterium piperi CTM.";
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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:KFF29798.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JPRJ01000003; KFF29798.1; -; Genomic_DNA.
DR   RefSeq; WP_034681921.1; NZ_JPRJ01000003.1.
DR   AlphaFoldDB; A0A086BLI4; -.
DR   STRING; 558152.IQ37_03850; -.
DR   KEGG; cpip:CJF12_02645; -.
DR   eggNOG; COG0176; Bacteria.
DR   OrthoDB; 9807051at2; -.
DR   UniPathway; UPA00115; UER00414.
DR   Proteomes; UP000028709; Unassembled WGS sequence.
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:SF40; FRUCTOSE-6-PHOSPHATE ALDOLASE 1-RELATED; 1.
DR   PANTHER; PTHR10683; 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   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:UP000028709};
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        87
FT                   /note="Schiff-base intermediate with substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00494"
SQ   SEQUENCE   217 AA;  23593 MW;  579F118470FDBA12 CRC64;
     MKFFIDTANL EQIKEAKDLG ILDGVTTNPS LMAKEGIQGA EAIKNHYKAI CEIVDGDISA
     EVLSTTYDEM IKEGEELAAI HPNIVVKIPM IKDGIKALKY FSDKGIKTNC TLIFSPGQAL
     LAAKAGATYV SPFLGRLDDI STDGLNLIQE IRLIFDNYMY DTEILAASIR HSMHIIDCAK
     IGADVITSPL PPILSLLKHP LTDSGLAQFI SDSQKLA
//
DBGET integrated database retrieval system