ID N6X3M9_9RHOO Unreviewed; 354 AA.
AC N6X3M9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 44.
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=C664_14803 {ECO:0000313|EMBL:ENO76301.1};
OS Thauera sp. 63.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=497321 {ECO:0000313|EMBL:ENO76301.1, ECO:0000313|Proteomes:UP000013007};
RN [1] {ECO:0000313|EMBL:ENO76301.1, ECO:0000313|Proteomes:UP000013007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63 {ECO:0000313|EMBL:ENO76301.1,
RC ECO:0000313|Proteomes:UP000013007};
RA Liu B., Shapleigh J.P., Frostegard A.H.;
RT "Draft Genome Sequences of 6 Strains from Genus Thauera.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00002181,
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; EC=4.1.2.13;
CC Evidence={ECO:0000256|ARBA:ARBA00000441,
CC ECO:0000256|RuleBase:RU365019};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3};
CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic and the other
CC provides a structural contribution. {ECO:0000256|PIRSR:PIRSR001359-3};
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 contribution.
CC {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|ARBA:ARBA00004714, ECO:0000256|RuleBase:RU365019}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|RuleBase:RU365019}.
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:ENO76301.1}.
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DR EMBL; AMXC01000020; ENO76301.1; -; Genomic_DNA.
DR RefSeq; WP_004262984.1; NZ_AMXC01000020.1.
DR AlphaFoldDB; N6X3M9; -.
DR eggNOG; COG0191; Bacteria.
DR OrthoDB; 9803995at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000013007; 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 CDD; cd00947; TBP_aldolase_IIB; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006412; Fruct_bisP_Calv.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01521; FruBisAldo_II_B; 1.
DR PANTHER; PTHR30304; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30304:SF0; D-TAGATOSE-1,6-BISPHOSPHATE ALDOLASE SUBUNIT GATY-RELATED; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|RuleBase:RU365019};
KW Lyase {ECO:0000256|RuleBase:RU365019, ECO:0000313|EMBL:ENO76301.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW ECO:0000256|RuleBase:RU365019};
KW Zinc {ECO:0000256|PIRSR:PIRSR001359-3, ECO:0000256|RuleBase:RU365019}.
FT ACT_SITE 83
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 84
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 105
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 142
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 198
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 199
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 232
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 233..235
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 275..278
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 354 AA; 38322 MW; DCCA5754C2EE61E8 CRC64;
MPLVSMRQLL DHAAEHSYGL PAFNVNNLEQ VQAIMEAAAE CDSPVIMQAS AGARKYAGEA
FLRHLIDAAV EAYPNIPIVM HQDHGQSPAI CMGAIRSGFS SVMMDGSLLE DGKTPSSYEY
NVAVTREVVK FSHAIGVSVE GELGCLGSLE TGQAGEEDGV GAEGTLDHSQ MLTDPDQAAD
FVKQTDCDAL AIAIGTSHGA YKFSRKPTGD ILAIERIKQI HARIPNTHLV MHGSSSVPQE
LLEIIRQYGG DMKETYGVPV EEIVQGIKYG VRKINIDTDI RLAMTGAVRK FLAENPSKFD
PREFNKPARE AAKLVCRARF EAFGCAGMAS KIKPVSLEKM AARYKAGDLT QIVR
//
