ID Q6N0W8_RHOPA Unreviewed; 361 AA.
AC Q6N0W8;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 108.
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 Name=cbbA {ECO:0000313|EMBL:CAE30082.1};
GN OrderedLocusNames=RPA4642 {ECO:0000313|EMBL:CAE30082.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE30082.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE30082.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572607; CAE30082.1; -; Genomic_DNA.
DR RefSeq; WP_011160174.1; NZ_CP116810.1.
DR AlphaFoldDB; Q6N0W8; -.
DR STRING; 258594.RPA4642; -.
DR GeneID; 66895794; -.
DR eggNOG; COG0191; Bacteria.
DR HOGENOM; CLU_040088_0_0_5; -.
DR PhylomeDB; Q6N0W8; -.
DR UniPathway; UPA00109; UER00183.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000001426; Chromosome.
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 Reference proteome {ECO:0000313|Proteomes:UP000001426};
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 361 AA; 39341 MW; 3CC7C699321B8035 CRC64;
MARITLRQLL DHAAEHGYGV PAFNINNMEQ GLAIMEAAAL VDAPVIIQAS RGARSYANDI
MLAKMIDALA EMYPDIPLCM HQDHGNDEAT CATAIRYGFT SVMMDGSLKA DAKTAADYQY
NVDITRRVVD MAHWVGASVE GELGVLGSLE HGGGEQEDGH GVEGKVSREQ LLTDPDQAVE
FVRATKVDAL AIAMGTSHGA YKFSRKPDGD VLAMKVVEEI HRRLPNTHLV MHGSSSVPQD
LQDIFNEFGG AMPQTFGVPV EEIVRGIKHG VRKVNIDTDC RLAMTGVFRK VATQNKAEFD
PRKFLKPAMD AMRDICKLRF EQFGTAGNAS KIKVVPMAEM AKRYKSGALD PQIGQVARAA
E
//
