(data stored in SCRATCH zone)

SWISSPROT: Q13QU5_PARXL

ID   Q13QU5_PARXL            Unreviewed;       345 AA.
AC   Q13QU5;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 90.
DE   RecName: Full=Fructose-1,6-bisphosphate aldolase {ECO:0000256|RuleBase:RU365019};
DE            Short=FBP aldolase {ECO:0000256|RuleBase:RU365019};
DE            EC=4.1.2.13 {ECO:0000256|RuleBase:RU365019};
GN   ORFNames=Bxe_B2447 {ECO:0000313|EMBL:ABE33544.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33544.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33544.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33544.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC       phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-
CC       phosphate (G3P) to form fructose 1,6-bisphosphate (FBP) in
CC       gluconeogenesis and the reverse reaction in glycolysis.
CC       {ECO:0000256|RuleBase:RU365019}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-
CC         phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729,
CC         ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776;
CC         EC=4.1.2.13; Evidence={ECO:0000256|RuleBase:RU365019};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU365019};
CC       Note=One is catalytic and the other provides a structural
CC       contribution. {ECO:0000256|RuleBase:RU365019};
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC       phosphate and glycerone phosphate from D-glucose: step 4/4.
CC       {ECO:0000256|RuleBase:RU365019}.
CC   -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC       family. {ECO:0000256|RuleBase:RU365019,
CC       ECO:0000256|SAAS:SAAS00836930}.
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; CP000271; ABE33544.1; -; Genomic_DNA.
DR   RefSeq; WP_011490909.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2447; -.
DR   EnsemblBacteria; ABE33544; ABE33544; Bxe_B2447.
DR   GeneID; 4007057; -.
DR   KEGG; bxb:DR64_4775; -.
DR   KEGG; bxe:Bxe_B2447; -.
DR   PATRIC; fig|266265.5.peg.5262; -.
DR   eggNOG; ENOG4105D2N; Bacteria.
DR   eggNOG; COG0191; LUCA.
DR   HOGENOM; HOG000227792; -.
DR   KO; K01624; -.
DR   OMA; VHFKYVS; -.
DR   OrthoDB; 827430at2; -.
DR   BioCyc; BXEN266265:BXE_RS24970-MONOMER; -.
DR   UniPathway; UPA00109; UER00183.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR   CDD; cd00947; TBP_aldolase_IIB; 1.
DR   Gene3D; 3.20.20.70; -; 1.
DR   InterPro; IPR013785; Aldolase_TIM.
DR   InterPro; IPR000771; FBA_II.
DR   InterPro; IPR006412; Fruct_bisP_Calv.
DR   Pfam; PF01116; F_bP_aldolase; 1.
DR   PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR   TIGRFAMs; TIGR00167; cbbA; 1.
DR   TIGRFAMs; TIGR01521; FruBisAldo_II_B; 1.
DR   PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13QU5.
DR   SWISS-2DPAGE; Q13QU5.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Glycolysis {ECO:0000256|RuleBase:RU365019};
KW   Lyase {ECO:0000256|RuleBase:RU365019, ECO:0000256|SAAS:SAAS00132197,
KW   ECO:0000313|EMBL:ABE33544.1};
KW   Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW   ECO:0000256|RuleBase:RU365019, ECO:0000256|SAAS:SAAS00132199};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|RuleBase:RU365019,
KW   ECO:0000256|SAAS:SAAS00132210}.
FT   REGION      233    235       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   REGION      275    278       Dihydroxyacetone phosphate binding.
FT                                {ECO:0000256|PIRSR:PIRSR001359-2}.
FT   ACT_SITE     83     83       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR001359-1}.
FT   METAL        84     84       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   METAL       105    105       Zinc 2. {ECO:0000256|PIRSR:PIRSR001359-
FT                                3}.
FT   METAL       142    142       Zinc 2. {ECO:0000256|PIRSR:PIRSR001359-
FT                                3}.
FT   METAL       198    198       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   METAL       232    232       Zinc 1; catalytic. {ECO:0000256|PIRSR:
FT                                PIRSR001359-3}.
FT   BINDING     199    199       Dihydroxyacetone phosphate; via amide
FT                                nitrogen. {ECO:0000256|PIRSR:PIRSR001359-
FT                                2}.
SQ   SEQUENCE   345 AA;  36830 MW;  7B9826FE2BAC4285 CRC64;
     MAFIALRQLL DHAAEHGYGV PAFNVNNMEQ IHAIMQAAEA TSSPVILQAS AGARKYAGEP
     YLRHLVLAAL EAHPDIPLVL HQDHGASPAV CQQAIRSGFT SVMMDGSLLP DQKTPAAYEY
     NVDVSRRVVE AAHAVGVSVE GELGCLGSLE TGTAGDEDGV GAEGQLSRDD LLTDPREAQI
     FVEATGVDAL AIAIGTSHGA YKFSRQPTGD ILAIDRIVEI HERIPNTHLV MHGSSSVPQE
     WLAVIREYGG EIPTTYGVPV EEIQRGIAHG VRKVNIDTDI RLAMSGAMRK SMANARAEFD
     PRAALKAATA AASAICVERF EAFGCAGQAS RIKPLPLDAM ARRYH
//

If you have problems or comments...

PBIL Back to PBIL home page