ID A0A1U7DJD9_9RHOB Unreviewed; 359 AA.
AC A0A1U7DJD9; A0A2M9DAK4;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=BV394_09970 {ECO:0000313|EMBL:APX90003.1}, CLV77_2531
GN {ECO:0000313|EMBL:PJJ82756.1};
OS Brevirhabdus pacifica.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Brevirhabdus.
OX NCBI_TaxID=1267768 {ECO:0000313|EMBL:APX90003.1, ECO:0000313|Proteomes:UP000187266};
RN [1] {ECO:0000313|EMBL:APX90003.1, ECO:0000313|Proteomes:UP000187266}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DY6-4 {ECO:0000313|EMBL:APX90003.1,
RC ECO:0000313|Proteomes:UP000187266};
RA Wang X.;
RT "Genomic analysis of Xuhuaishuia manganoxidans DY6-4.";
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:PJJ82756.1, ECO:0000313|Proteomes:UP000229573}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27767 {ECO:0000313|EMBL:PJJ82756.1,
RC ECO:0000313|Proteomes:UP000229573};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) 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 biosynthesis; Calvin cycle.
CC {ECO:0000256|ARBA:ARBA00005215}.
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}.
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DR EMBL; CP019124; APX90003.1; -; Genomic_DNA.
DR EMBL; PGFI01000013; PJJ82756.1; -; Genomic_DNA.
DR RefSeq; WP_076980024.1; NZ_PGFI01000013.1.
DR AlphaFoldDB; A0A1U7DJD9; -.
DR STRING; 1267768.BV394_09970; -.
DR OrthoDB; 9803995at2; -.
DR UniPathway; UPA00109; UER00183.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000187266; Chromosome.
DR Proteomes; UP000229573; 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 GO; GO:0019253; P:reductive pentose-phosphate cycle; 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; PS00806; ALDOLASE_CLASS_II_2; 1.
PE 3: Inferred from homology;
KW Calvin cycle {ECO:0000256|ARBA:ARBA00022567};
KW Glycolysis {ECO:0000256|RuleBase:RU365019};
KW Lyase {ECO:0000256|RuleBase:RU365019};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR001359-3,
KW ECO:0000256|RuleBase:RU365019};
KW Reference proteome {ECO:0000313|Proteomes:UP000187266};
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 359 AA; 38916 MW; 08FB803DF84E98BC CRC64;
MALITLRQLL DHGAEYGYGV PAFNINNMEQ GIAIMKAAEA VDAPVILQAS RGARSYAGDI
MLRHMVQALA EMFPNNPICM HQDHGNNEQT CLSAIGHGFT SVMMDGSLEA DMKTPASYEY
NVDITQRVSQ MAHWVGASVE GELGVLGSLE TGEAAEEDGS GAVGKLSMED LLTDPDQAAD
FVATTKVDAL AIACGTSHGA YKFSRKPDGE ILAMTRIAEI HKRIPTVHLV MHGSSSVPQS
LQDMINEFGG EMPQTYGVPV EEIEKGIKSG VRKVNIDTDC RMAMTAQFRK VATQNPKEFD
PRKFLIPAMQ EMEDLCRDRF ERFGTAGNAS KIKVIPMDDM ARRYADGSLD PVIGAAKAA
//
