FBSB_SYNY3
ID FBSB_SYNY3 Reviewed; 345 AA.
AC P73922;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=D-fructose 1,6-bisphosphatase class 2/sedoheptulose 1,7-bisphosphatase;
DE Short=FBPase class 2/SBPase;
DE EC=3.1.3.11;
DE EC=3.1.3.37;
GN OrderedLocusNames=slr2094;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(1996).
CC -!- FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate (Fru
CC 1,6-P2) and sedoheptulose 1,7-bisphosphate (Sed 1,7-P2) to fructose 6-
CC phosphate and sedoheptulose 7-phosphate, respectively. {ECO:0000250}.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=D-sedoheptulose 1,7-bisphosphate + H2O = D-sedoheptulose 7-
CC phosphate + phosphate; Xref=Rhea:RHEA:17461, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57483, ChEBI:CHEBI:58335; EC=3.1.3.37;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FBPase class 2 family. {ECO:0000305}.
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DR EMBL; BA000022; BAA17988.1; -; Genomic_DNA.
DR PIR; S75126; S75126.
DR PDB; 3ROJ; X-ray; 2.30 A; A/B/C/D=2-345.
DR PDB; 3RPL; X-ray; 2.40 A; A/B/C/D=2-345.
DR PDBsum; 3ROJ; -.
DR PDBsum; 3RPL; -.
DR AlphaFoldDB; P73922; -.
DR SMR; P73922; -.
DR IntAct; P73922; 1.
DR MINT; P73922; -.
DR STRING; 1148.1653071; -.
DR PaxDb; P73922; -.
DR PRIDE; P73922; -.
DR EnsemblBacteria; BAA17988; BAA17988; BAA17988.
DR KEGG; syn:slr2094; -.
DR eggNOG; COG1494; Bacteria.
DR InParanoid; P73922; -.
DR OMA; AVFYMDK; -.
DR PhylomeDB; P73922; -.
DR BioCyc; MetaCyc:FBPSBP-MON; -.
DR BRENDA; 3.1.3.11; 382.
DR BRENDA; 3.1.3.37; 382.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000001425; Chromosome.
DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0050278; F:sedoheptulose-bisphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0030388; P:fructose 1,6-bisphosphate metabolic process; IBA:GO_Central.
DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central.
DR GO; GO:0006071; P:glycerol metabolic process; IEA:InterPro.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd01516; FBPase_glpX; 1.
DR InterPro; IPR004464; FBPase_class-2/SBPase.
DR PANTHER; PTHR30447; PTHR30447; 1.
DR Pfam; PF03320; FBPase_glpX; 1.
DR PIRSF; PIRSF004532; GlpX; 1.
DR TIGRFAMs; TIGR00330; glpX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calvin cycle; Carbohydrate metabolism; Hydrolase; Manganese;
KW Metal-binding; Reference proteome.
FT CHAIN 1..345
FT /note="D-fructose 1,6-bisphosphatase class 2/sedoheptulose
FT 1,7-bisphosphatase"
FT /id="PRO_0000342735"
FT BINDING 33
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 57
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 100..102
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 176..178
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 198..200
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 225
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT HELIX 5..21
FT /evidence="ECO:0007829|PDB:3ROJ"
FT TURN 22..25
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:3ROJ"
FT TURN 60..62
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 87..89
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 90..100
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 102..107
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 131..137
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:3ROJ"
FT TURN 142..144
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 151..161
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 177..179
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 180..189
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 192..198
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 216..222
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 223..236
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 239..245
FT /evidence="ECO:0007829|PDB:3ROJ"
FT TURN 248..250
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 260..269
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3ROJ"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 287..298
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 307..309
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 312..321
FT /evidence="ECO:0007829|PDB:3ROJ"
FT TURN 322..325
FT /evidence="ECO:0007829|PDB:3ROJ"
FT STRAND 326..335
FT /evidence="ECO:0007829|PDB:3ROJ"
SQ SEQUENCE 345 AA; 37075 MW; A6DA0D2E16724179 CRC64;
MDSTLGLEII EVVEQAAIAS AKWMGKGEKN TADQVAVEAM RERMNKIHMR GRIVIGEGER
DDAPMLYIGE EVGICTREDA KSFCNPDELV EIDIAVDPCE GTNLVAYGQN GSMAVLAISE
KGGLFAAPDF YMKKLAAPPA AKGHVDIDKS ATENLKILSD CLNRSIEELV VVVMDRPRHK
ELIQEIRNAG ARVRLISDGD VSAAISCAFS GTNIHALMGI GAAPEGVISA AAMRCLGGHF
QGQLIYDPEV VKTGLIGESR EGNLERLASM GIKNPDQVYN CEELACGETV LFAACGITPG
TLMEGVRFFH GGVRTQSLVI SSQSSTARFV DTVHMKESPK VIQLH