ID A0A1I5J2A3_PARPN Unreviewed; 359 AA.
AC A0A1I5J2A3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 33.
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=BDE18_1316 {ECO:0000313|EMBL:RKS52021.1}, HYQ43_12150
GN {ECO:0000313|EMBL:QLH15002.1};
OS Paracoccus pantotrophus (Thiosphaera pantotropha).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=82367 {ECO:0000313|EMBL:RKS52021.1, ECO:0000313|Proteomes:UP000273626};
RN [1] {ECO:0000313|EMBL:RKS52021.1, ECO:0000313|Proteomes:UP000273626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35512 / DSM 2944 / CIP 106514 / LMD 82.5 / NBRC 102493 /
RC NCCB 82005 / GB17 {ECO:0000313|Proteomes:UP000273626}, and DSM 2944
RC {ECO:0000313|EMBL:RKS52021.1};
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 (OCT-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:QLH15002.1, ECO:0000313|Proteomes:UP000509322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACCC10489 {ECO:0000313|EMBL:QLH15002.1,
RC ECO:0000313|Proteomes:UP000509322};
RA Si Y.;
RT "The complete genome of Paracoccus pantotrophus ACCC 10489.";
RL Submitted (JUL-2020) 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; CP058690; QLH15002.1; -; Genomic_DNA.
DR EMBL; RBLI01000001; RKS52021.1; -; Genomic_DNA.
DR RefSeq; WP_024844390.1; NZ_RBLI01000001.1.
DR AlphaFoldDB; A0A1I5J2A3; -.
DR GeneID; 51371987; -.
DR OrthoDB; 9803995at2; -.
DR UniPathway; UPA00109; UER00183.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000273626; Unassembled WGS sequence.
DR Proteomes; UP000509322; 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 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; PS00602; ALDOLASE_CLASS_II_1; 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 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; 38666 MW; 2535383DD989AC3F CRC64;
MALITLRQLL DHAAEHGYGV PAFNINNMEQ GLAIVKAAAE VDAPVILQAS RGARSYAGDI
MLRRMVEALA EMNPTIPICL HQDHGNNLAT CMSAIRHGFT SVMMDGSLHE DMKTPADYDY
NVAVTAKVSE AAHAVGASVE GELGVLGSLE TGEAAAEDGS GAEGKLDHSQ LLTDPDQAVD
FVARTHCDAL AIACGTSHGA YKFSRKPDGD ILAMHVIEAI HERLPGTHLV MHGSSSVPQY
LQDLINEAGG QMPQTYGVPV EEIERGIRHG VRKVNIDTDC RMAMTGQFRK IARDKPDEFD
PRKFLIPAMK ELTALCRDRF ERFGTAGHAS KIRVIPMDEM AKRYASGALD PAITGAKAA
//
