ID O97193_LEIMA Unreviewed; 351 AA.
AC O97193;
DT 01-MAY-1999, integrated into UniProtKB/TrEMBL.
DT 01-MAY-1999, sequence version 1.
DT 27-MAR-2024, entry version 135.
DE RecName: Full=fructose-bisphosphatase {ECO:0000256|ARBA:ARBA00013093};
DE EC=3.1.3.11 {ECO:0000256|ARBA:ARBA00013093};
DE AltName: Full=D-fructose-1,6-bisphosphate 1-phosphohydrolase {ECO:0000256|ARBA:ARBA00032973};
GN Name=FBP {ECO:0000313|EMBL:CAC22660.1};
GN ORFNames=LMJF_04_1160 {ECO:0000313|EMBL:CAC22660.1};
OS Leishmania major.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5664 {ECO:0000313|EMBL:CAC22660.1, ECO:0000313|Proteomes:UP000000542};
RN [1] {ECO:0000313|EMBL:CAC22660.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=16020728; DOI=10.1126/science.1112680;
RA Ivens A.C., Peacock C.S., Worthey E.A., Murphy L., Aggarwal G.,
RA Berriman M., Sisk E., Rajandream M.A., Adlem E., Aert R., Anupama A.,
RA Apostolou Z., Attipoe P., Bason N., Bauser C., Beck A., Beverley S.M.,
RA Bianchettin G., Borzym K., Bothe G., Bruschi C.V., Collins M., Cadag E.,
RA Ciarloni L., Clayton C., Coulson R.M., Cronin A., Cruz A.K., Davies R.M.,
RA De Gaudenzi J., Dobson D.E., Duesterhoeft A., Fazelina G., Fosker N.,
RA Frasch A.C., Fraser A., Fuchs M., Gabel C., Goble A., Goffeau A.,
RA Harris D., Hertz-Fowler C., Hilbert H., Horn D., Huang Y., Klages S.,
RA Knights A., Kube M., Larke N., Litvin L., Lord A., Louie T., Marra M.,
RA Masuy D., Matthews K., Michaeli S., Mottram J.C., Muller-Auer S.,
RA Munden H., Nelson S., Norbertczak H., Oliver K., O'neil S., Pentony M.,
RA Pohl T.M., Price C., Purnelle B., Quail M.A., Rabbinowitsch E.,
RA Reinhardt R., Rieger M., Rinta J., Robben J., Robertson L., Ruiz J.C.,
RA Rutter S., Saunders D., Schafer M., Schein J., Schwartz D.C., Seeger K.,
RA Seyler A., Sharp S., Shin H., Sivam D., Squares R., Squares S., Tosato V.,
RA Vogt C., Volckaert G., Wambutt R., Warren T., Wedler H., Woodward J.,
RA Zhou S., Zimmermann W., Smith D.F., Blackwell J.M., Stuart K.D.,
RA Barrell B., Myler P.J.;
RT "The genome of the kinetoplastid parasite, Leishmania major.";
RL Science 309:436-442(2005).
RN [2] {ECO:0000313|EMBL:CAC22660.1, ECO:0000313|Proteomes:UP000000542}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MHOM/IL/81/Friedlin {ECO:0000313|Proteomes:UP000000542};
RX PubMed=22038252; DOI=10.1101/gr.122945.111;
RA Rogers M.B., Hilley J.D., Dickens N.J., Wilkes J., Bates P.A.,
RA Depledge D.P., Harris D., Her Y., Herzyk P., Imamura H., Otto T.D.,
RA Sanders M., Seeger K., Dujardin J.C., Berriman M., Smith D.F.,
RA Hertz-Fowler C., Mottram J.C.;
RT "Chromosome and gene copy number variation allow major structural change
RT between species and strains of Leishmania.";
RL Genome Res. 21:2129-2142(2011).
RN [3] {ECO:0007829|PDB:5OEY, ECO:0007829|PDB:5OEZ}
RP X-RAY CRYSTALLOGRAPHY (2.41 ANGSTROMS) IN COMPLEX WITH AMP; MN(2+) AND
RP BETA-D-FRUCTOSE 6-PHOSPHATE.
RX PubMed=28882541; DOI=10.1016/j.jmb.2017.08.010;
RA Yuan M., Vasquez-Valdivieso M.G., McNae I.W., Michels P.A.M.,
RA Fothergill-Gilmore L.A., Walkinshaw M.D.;
RT "Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-
RT Specific Differences in the Mechanism of Allosteric Inhibition.";
RL J. Mol. Biol. 429:3075-3089(2017).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-
CC phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11;
CC Evidence={ECO:0000256|ARBA:ARBA00001273};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the FBPase class 1 family.
CC {ECO:0000256|ARBA:ARBA00010941, ECO:0000256|RuleBase:RU000508}.
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DR EMBL; FR796400; CAC22660.1; -; Genomic_DNA.
DR RefSeq; XP_888627.1; XM_883534.1.
DR PDB; 5OEY; X-ray; 2.80 A; A/B/C/D=1-351.
DR PDB; 5OEZ; X-ray; 2.41 A; A/B/C/D=1-351.
DR PDB; 5OFU; X-ray; 2.62 A; A/B/C/D=1-351.
DR PDBsum; 5OEY; -.
DR PDBsum; 5OEZ; -.
DR PDBsum; 5OFU; -.
DR AlphaFoldDB; O97193; -.
DR SMR; O97193; -.
DR STRING; 5664.O97193; -.
DR EnsemblProtists; CAC22660; CAC22660; LMJF_04_1160.
DR GeneID; 3684922; -.
DR KEGG; lma:LMJF_04_1160; -.
DR VEuPathDB; TriTrypDB:LmjF.04.1160; -.
DR VEuPathDB; TriTrypDB:LMJFC_040018600; -.
DR VEuPathDB; TriTrypDB:LMJLV39_040017200; -.
DR VEuPathDB; TriTrypDB:LMJSD75_040017500; -.
DR eggNOG; KOG1458; Eukaryota.
DR HOGENOM; CLU_039977_2_2_1; -.
DR InParanoid; O97193; -.
DR OMA; YIPENCP; -.
DR BRENDA; 3.1.3.11; 2950.
DR Proteomes; UP000000542; Chromosome 4.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0020015; C:glycosome; IDA:GeneDB.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IDA:GeneDB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006000; P:fructose metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IMP:GeneDB.
DR GO; GO:0005986; P:sucrose biosynthetic process; IBA:GO_Central.
DR CDD; cd00354; FBPase; 1.
DR Gene3D; 3.40.190.80; -; 1.
DR Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
DR HAMAP; MF_01855; FBPase_class1; 1.
DR InterPro; IPR044015; FBPase_C_dom.
DR InterPro; IPR000146; FBPase_class-1.
DR InterPro; IPR033391; FBPase_N.
DR InterPro; IPR028343; FBPtase.
DR InterPro; IPR020548; Fructose_bisphosphatase_AS.
DR PANTHER; PTHR11556; FRUCTOSE-1,6-BISPHOSPHATASE-RELATED; 1.
DR PANTHER; PTHR11556:SF1; FRUCTOSE-BISPHOSPHATASE; 1.
DR Pfam; PF00316; FBPase; 1.
DR Pfam; PF18913; FBPase_C; 1.
DR PIRSF; PIRSF500210; FBPtase; 1.
DR PIRSF; PIRSF000904; FBPtase_SBPase; 1.
DR PRINTS; PR00115; F16BPHPHTASE.
DR SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR PROSITE; PS00124; FBPASE; 1.
PE 1: Evidence at protein level;
KW 3D-structure {ECO:0007829|PDB:5OEY, ECO:0007829|PDB:5OEZ};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU000508};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000508};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0007829|PDB:5OEY};
KW Nucleotide-binding {ECO:0007829|PDB:5OFU};
KW Reference proteome {ECO:0000313|Proteomes:UP000000542}.
FT DOMAIN 11..204
FT /note="Fructose-1-6-bisphosphatase class I N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00316"
FT DOMAIN 208..333
FT /note="Fructose-1-6-bisphosphatase class 1 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF18913"
FT BINDING 16
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 25
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 26
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 27
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 28
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 29
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 74
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 98
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 113
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 118
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 120
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 121
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5OEY"
FT BINDING 121
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 122
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 218
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 247
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 248
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 252
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 268
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 278
FT /ligand="beta-D-fructose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:57634"
FT /evidence="ECO:0007829|PDB:5OFU"
FT BINDING 284
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0007829|PDB:5OEY"
SQ SEQUENCE 351 AA; 38826 MW; 87E93847978DE87B CRC64;
MDVRRTPTPT TLTQYIIKSQ PPHSRGDFTL LMMAIQTSVK VIEKNIRRAG MKGMLGYIAG
QSANATGDHQ AKLDVISNIA FKAYLLSSTS VCVLGSEEEE QMIIAESGRR GDYLIFFDPL
DGSSNIDANV SVGSIWGVWR LPKDTTINSV EDANAVIRML KGTDMVSAGY AVYGSATNLV
LTSGHGVDGF TLDPNIGEFI LTHPHISIPK KRSIYSVNEG NYGKWEPWFK EYIDYLKMNK
TTRYSARYIG SMVGDIHRTL LYGGIFCYPK DANQVEGKLR LLYEAAPMAM IVEQAGGKAV
GSNGRILEQS ITRLHQRTPV YFGSRQEVDL CMAFRDRNVK TEALAPTSSK L
//
