ID A0A1G9PWD9_9FLAO Unreviewed; 356 AA.
AC A0A1G9PWD9; A0A4U8WD71;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
DE Short=FBP aldolase {ECO:0000256|RuleBase:RU366023};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068, ECO:0000256|RuleBase:RU366023};
GN Name=fba {ECO:0000313|EMBL:VFB04302.1};
GN ORFNames=NCTC12078_02325 {ECO:0000313|EMBL:VFB04302.1},
GN SAMN05216273_11118 {ECO:0000313|EMBL:SDM02791.1};
OS Chryseobacterium taihuense.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1141221 {ECO:0000313|EMBL:SDM02791.1, ECO:0000313|Proteomes:UP000199242};
RN [1] {ECO:0000313|Proteomes:UP000199242}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10941 {ECO:0000313|Proteomes:UP000199242};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SDM02791.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10941 {ECO:0000313|EMBL:SDM02791.1};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:VFB04302.1, ECO:0000313|Proteomes:UP000290013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3012STDY6944375 {ECO:0000313|EMBL:VFB04302.1,
RC ECO:0000313|Proteomes:UP000290013};
RG Pathogen Informatics;
RL Submitted (FEB-2019) 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|RuleBase:RU366023}.
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:RU366023};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR001359-3,
CC ECO:0000256|RuleBase:RU366023};
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 ECO:0000256|RuleBase:RU366023};
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:RU366023}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00005812, ECO:0000256|RuleBase:RU366023}.
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DR EMBL; FNHD01000011; SDM02791.1; -; Genomic_DNA.
DR EMBL; LR215974; VFB04302.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G9PWD9; -.
DR STRING; 1141221.SAMN05216273_11118; -.
DR KEGG; ctai:NCTC12078_02325; -.
DR OrthoDB; 9803995at2; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000199242; Unassembled WGS sequence.
DR Proteomes; UP000290013; Chromosome.
DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IEA:UniProtKB-EC.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00946; FBP_aldolase_IIA; 1.
DR Gene3D; 3.20.20.70; Aldolase class I; 1.
DR InterPro; IPR013785; Aldolase_TIM.
DR InterPro; IPR000771; FBA_II.
DR InterPro; IPR006411; Fruct_bisP_bact.
DR NCBIfam; TIGR00167; cbbA; 1.
DR NCBIfam; TIGR01520; FruBisAldo_II_A; 1.
DR PANTHER; PTHR30559:SF0; FRUCTOSE-BISPHOSPHATE ALDOLASE; 1.
DR PANTHER; PTHR30559; FRUCTOSE-BISPHOSPHATE ALDOLASE CLASS 2; 1.
DR Pfam; PF01116; F_bP_aldolase; 1.
DR PIRSF; PIRSF001359; F_bP_aldolase_II; 1.
DR SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|RuleBase:RU366023};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU366023};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR001359-3};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR001359-3}.
FT ACT_SITE 106
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-1"
FT BINDING 107
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 141
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 171
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-3"
FT BINDING 223
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 224
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 261
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 262..264
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
FT BINDING 283..286
FT /ligand="dihydroxyacetone phosphate"
FT /ligand_id="ChEBI:CHEBI:57642"
FT /evidence="ECO:0000256|PIRSR:PIRSR001359-2"
SQ SEQUENCE 356 AA; 39224 MW; 6690CD3A5357B221 CRC64;
MSRIFPAGVA TGQLVTDIFQ YAKENKFALP AVNVIGSSNV NAVMETAAKL NSPVIIQFSN
GGAAYNAGKG LSNDAQKSAI LGGIAGAKHI HTLAEAYGAT VILHTDHAAK KLLPWIDGLM
EANEEFYKQT GKSLYSSHML DLSEESLEEN LEISAQYFEK MAKMQMTLEV EIGVTGGEED
GVDNSDVDNS KLYTQPEDVA YTYEKLKAIS DNFTIAAAFG NVHGVYKPGN VVLTPKILDN
SQKFVQEKFG TAEKPINFVF HGGSGSTLEE IREAIDYGVI KMNIDTDLQF AYTEGIRNYM
TENIEYLKTQ IGNPDGDDKP NKKFYDPRVW IRKGEETFSK RLVQAFEDLN NVNTLK
//
