ID R1D6Z5_EMIHU Unreviewed; 483 AA.
AC R1D6Z5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=fructose-bisphosphate aldolase {ECO:0000256|ARBA:ARBA00013068};
DE EC=4.1.2.13 {ECO:0000256|ARBA:ARBA00013068};
GN ORFNames=EMIHUDRAFT_418341 {ECO:0000313|EMBL:EOD30832.1};
OS Emiliania huxleyi (Coccolithophore) (Pontosphaera huxleyi).
OC Eukaryota; Haptista; Haptophyta; Prymnesiophyceae; Isochrysidales;
OC Noelaerhabdaceae; Emiliania.
OX NCBI_TaxID=2903 {ECO:0000313|EMBL:EOD30832.1};
RN [1] {ECO:0000313|EMBL:EOD30832.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|EMBL:EOD30832.1};
RG DOE Joint Genome Institute;
RA Read B., Kegel J., Klute M., Kuo A., Lefebvre S.C., Maumus F., Mayer C.,
RA Miller J., Allen A., Bidle K., Borodovsky M., Bowler C., Brownlee C.,
RA Claverie J.-M., Cock M., De Vargas C., Elias M., Frickenhaus S.,
RA Gladyshev V.N., Gonzalez K., Guda C., Hadaegh A., Herman E.,
RA Iglesias-Rodriguez D., Jones B., Lawson T., Leese F., Lin Y.-C.,
RA Lindquist E., Lobanov A., Lucas S., Malik S.-H.B., Marsh M.E., Mock T.,
RA Monier A., Moreau H., Mueller-Roeber B., Napier J., Ogata H., Parker M.,
RA Probert I., Quesneville H., Raines C., Rensing S., Riano-Pachon D.M.,
RA Richier S., Rokitta S., Salamov A., Sarno A.F., Schmutz J., Schroeder D.,
RA Shiraiwa Y., Soanes D.M., Valentin K., Van Der Giezen M., Van Der Peer Y.,
RA Vardi A., Verret F., Von Dassow P., Wheeler G., Williams B., Wilson W.,
RA Wolfe G., Wurch L.L., Young J., Dacks J.B., Delwiche C.F., Dyhrman S.,
RA Glockner G., John U., Richards T., Worden A.Z., Zhang X., Grigoriev I.V.;
RT "Genome variability drives Emilianias global distribution.";
RL Submitted (JUL-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000013827}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CCMP1516 {ECO:0000313|Proteomes:UP000013827};
RX PubMed=23760476; DOI=10.1038/nature12221;
RA Read B.A., Kegel J., Klute M.J., Kuo A., Lefebvre S.C., Maumus F.,
RA Mayer C., Miller J., Monier A., Salamov A., Young J., Aguilar M.,
RA Claverie J.M., Frickenhaus S., Gonzalez K., Herman E.K., Lin Y.C.,
RA Napier J., Ogata H., Sarno A.F., Shmutz J., Schroeder D., de Vargas C.,
RA Verret F., von Dassow P., Valentin K., Van de Peer Y., Wheeler G.,
RA Dacks J.B., Delwiche C.F., Dyhrman S.T., Glockner G., John U., Richards T.,
RA Worden A.Z., Zhang X., Grigoriev I.V., Allen A.E., Bidle K., Borodovsky M.,
RA Bowler C., Brownlee C., Cock J.M., Elias M., Gladyshev V.N., Groth M.,
RA Guda C., Hadaegh A., Iglesias-Rodriguez M.D., Jenkins J., Jones B.M.,
RA Lawson T., Leese F., Lindquist E., Lobanov A., Lomsadze A., Malik S.B.,
RA Marsh M.E., Mackinder L., Mock T., Mueller-Roeber B., Pagarete A.,
RA Parker M., Probert I., Quesneville H., Raines C., Rensing S.A.,
RA Riano-Pachon D.M., Richier S., Rokitta S., Shiraiwa Y., Soanes D.M.,
RA van der Giezen M., Wahlund T.M., Williams B., Wilson W., Wolfe G.,
RA Wurch L.L.;
RT "Pan genome of the phytoplankton Emiliania underpins its global
RT distribution.";
RL Nature 499:209-213(2013).
RN [3] {ECO:0000313|EnsemblProtists:EOD30832}
RP IDENTIFICATION.
RG EnsemblProtists;
RL Submitted (NOV-2023) to UniProtKB.
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 -!- 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 -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-
CC phosphate and glycerone phosphate from D-glucose: step 4/4.
CC {ECO:0000256|ARBA:ARBA00004714}.
CC -!- SIMILARITY: Belongs to the class II fructose-bisphosphate aldolase
CC family. {ECO:0000256|ARBA:ARBA00005812}.
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DR EMBL; KB864664; EOD30832.1; -; Genomic_DNA.
DR RefSeq; XP_005783261.1; XM_005783204.1.
DR STRING; 2903.R1D6Z5; -.
DR PaxDb; 2903-EOD30832; -.
DR EnsemblProtists; EOD30832; EOD30832; EMIHUDRAFT_418341.
DR GeneID; 17276106; -.
DR KEGG; ehx:EMIHUDRAFT_418341; -.
DR eggNOG; KOG4153; Eukaryota.
DR HOGENOM; CLU_036923_0_0_1; -.
DR OMA; WSYWEGI; -.
DR UniPathway; UPA00109; UER00183.
DR Proteomes; UP000013827; 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; 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 SUPFAM; SSF51569; Aldolase; 1.
DR PROSITE; PS00602; ALDOLASE_CLASS_II_1; 1.
PE 3: Inferred from homology;
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152};
KW Lyase {ECO:0000256|ARBA:ARBA00023239};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000013827};
KW Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT REGION 248..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 483 AA; 52065 MW; 9B891E088BED9BF6 CRC64;
MLTLSAAAAL AYSPTVAAPH ARTSAASVSS RASAPRLGLL QKLGLRRGAR FADDLGLPCV
DECAVASYPN LPPSVHPGVV TGQALVDLLQ HAKENRYAIP AVNCVTSSSV NTCLEAARKA
DAPIIIQFSS GGSQFYAGKG LDNTDYKAAI AGAVSGAYHV RAMAEQYGVP VILHTDHCAK
NLLPWLDGML AASERYYAAH REPLFSSHMI DLSEEPLEEN IDICVSYLQR MAKLDMLLEM
ELGSPRRRRA TGITGGEEDG VDNEDANPED LYSKPEEIWQ VYEKLSAVPN GRFTVAAAFG
NVHGVYAPGN AELDPPDTRN VKLDPEILGN AQTFIADKVS SSDAKPVSFV FHGGSGSDLK
DIKQANPATA GHLGRSRPDP AIDYGVVKMN IDTDTQWSYW DGIRAYYKKY EPYLNSQIGN
PDGADKPNKK FYDPRACLRS AEDSTNARLQ QCFEDLNCVG ILGLGDMPPP QNVLGPRRGA
LPC
//
