ALF_HALVD
ID ALF_HALVD Reviewed; 330 AA.
AC D4GYE0;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Fructose-bisphosphate aldolase class 2;
DE Short=FBP aldolase;
DE Short=FBPA;
DE EC=4.1.2.13;
DE AltName: Full=Fructose-1,6-bisphosphate aldolase;
DE AltName: Full=Fructose-bisphosphate aldolase class II;
GN Name=fba; OrderedLocusNames=HVO_1494; ORFNames=C498_11261;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP INDUCTION, FUNCTION, DISRUPTION PHENOTYPE, SUBUNIT, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ACTIVITY REGULATION.
RC STRAIN=DS2 / DS70;
RX PubMed=22493022; DOI=10.1128/jb.00200-12;
RA Pickl A., Johnsen U., Schoenheit P.;
RT "Fructose degradation in the haloarchaeon Haloferax volcanii involves a
RT bacterial type phosphoenolpyruvate-dependent phosphotransferase system,
RT fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate
RT aldolase.";
RL J. Bacteriol. 194:3088-3097(2012).
CC -!- FUNCTION: Catalyzes the aldol condensation of dihydroxyacetone
CC phosphate (DHAP or glycerone-phosphate) with glyceraldehyde 3-phosphate
CC (G3P) to form fructose 1,6-bisphosphate (FBP) in gluconeogenesis and
CC the reverse reaction in glycolysis. Is required for the utilization of
CC fructose as a sole carbon and energy source. Plays a role in
CC gluconeogenesis during growth on acetate, D-xylose, and casamino acids.
CC {ECO:0000269|PubMed:22493022}.
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; EC=4.1.2.13;
CC Evidence={ECO:0000269|PubMed:22493022};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000250};
CC -!- ACTIVITY REGULATION: EDTA is an inhibitor of catalytic activity.
CC {ECO:0000269|PubMed:22493022}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.24 mM for D-fructose 1,6-bisphosphate
CC {ECO:0000269|PubMed:22493022};
CC Vmax=55 umol/min/mg enzyme {ECO:0000269|PubMed:22493022};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:22493022};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22493022}.
CC -!- INDUCTION: Expression is highly up-regulated in presence of fructose.
CC {ECO:0000269|PubMed:22493022}.
CC -!- DISRUPTION PHENOTYPE: Loss of growth on fructose, but growth on glucose
CC is slightly stimulated. Loss of growth on acetate, D-xylose, or
CC Casamino acids. {ECO:0000269|PubMed:22493022}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000305}.
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DR EMBL; CP001956; ADE02710.1; -; Genomic_DNA.
DR EMBL; AOHU01000090; ELY28268.1; -; Genomic_DNA.
DR RefSeq; WP_004043441.1; NZ_AOHU01000090.1.
DR AlphaFoldDB; D4GYE0; -.
DR SMR; D4GYE0; -.
DR STRING; 309800.C498_11261; -.
DR EnsemblBacteria; ADE02710; ADE02710; HVO_1494.
DR EnsemblBacteria; ELY28268; ELY28268; C498_11261.
DR GeneID; 8924997; -.
DR KEGG; hvo:HVO_1494; -.
DR PATRIC; fig|309800.29.peg.2146; -.
DR eggNOG; arCOG07500; Archaea.
DR HOGENOM; CLU_040088_0_1_2; -.
DR OMA; PRTWGKL; -.
DR OrthoDB; 81623at2157; -.
DR BRENDA; 4.1.2.13; 2561.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
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 Gene3D; 3.20.20.70; -; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
PE 1: Evidence at protein level;
KW Glycolysis; Lyase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..330
FT /note="Fructose-bisphosphate aldolase class 2"
FT /id="PRO_0000428981"
FT ACT_SITE 92
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT BINDING 53
FT /ligand="D-glyceraldehyde 3-phosphate"
FT /ligand_id="ChEBI:CHEBI:59776"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 115
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 191
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 192
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 226..228
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
FT BINDING 247..250
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000250"
SQ SEQUENCE 330 AA; 36302 MW; 6CF4C55B24F75CD1 CRC64;
MPFYGGEELA TVYDEALDEG FGLIASNIAE PNIMMGLMEG ADRMDSDLLL QMSGGACRFA
GDGDAVAGLK AMGNYIETIA ERYDIGVFLN MDHQTDLEFI EQQIELDIPS SIMIDASHEP
FDENVATSRE VVEMVEAAGS DVLIEAELGQ IKGVEDEIEA EEAFYTDPEQ AVEFVDKTGA
DLLAISVGTQ HGVAKGKDLE LRPDLANDIR QALRDHGLDT PLVLHGSSGV QPDQLQEMLK
HGICKVNKDT RYQYEYTRTA YDRYNEEPNA IVPPEGVADA RDTFFNETDW SPNKDVFDPR
VAGRDIRERI ADVHADLTEV SGSAGQSLFK
