PSK_SYNE7
ID PSK_SYNE7 Reviewed; 426 AA.
AC Q31KC7;
DT 28-FEB-2018, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=D-ribulose kinase {ECO:0000305|PubMed:27223615};
DE Short=D-ribulokinase {ECO:0000305};
DE EC=2.7.1.47 {ECO:0000269|PubMed:27223615};
DE AltName: Full=Probable sugar kinase {ECO:0000303|PubMed:27223615};
DE Short=SePSK {ECO:0000303|PubMed:27223615};
GN Name=PSK {ECO:0000303|PubMed:27223615};
GN OrderedLocusNames=Synpcc7942_2462 {ECO:0000312|EMBL:ABB58492.1};
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH ADP; ATP ANALOG AND
RP SUBSTRATE, FUNCTION, AND MUTAGENESIS OF ASP-8; THR-11 AND ASP-221.
RC STRAIN=PCC 7942 / FACHB-805;
RX PubMed=27223615; DOI=10.1371/journal.pone.0156067;
RA Xie Y., Li M., Chang W.;
RT "Crystal structures of putative sugar kinases from Synechococcus elongatus
RT PCC 7942 and Arabidopsis thaliana.";
RL PLoS ONE 11:E0156067-E0156067(2016).
CC -!- FUNCTION: Exhibits ATP hydrolysis without substrate. Phosphorylates D-
CC ribulose. {ECO:0000269|PubMed:27223615}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.47; Evidence={ECO:0000269|PubMed:27223615};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:P11553};
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000305}.
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DR EMBL; CP000100; ABB58492.1; -; Genomic_DNA.
DR RefSeq; WP_011378475.1; NC_007604.1.
DR PDB; 5HTJ; X-ray; 2.00 A; A=1-426.
DR PDB; 5HTN; X-ray; 2.30 A; A=1-426.
DR PDB; 5HTP; X-ray; 2.30 A; A=1-426.
DR PDB; 5HTY; X-ray; 2.81 A; A=1-426.
DR PDB; 5HU2; X-ray; 2.60 A; A=1-426.
DR PDB; 5HUX; X-ray; 1.96 A; A=1-426.
DR PDB; 5HV7; X-ray; 2.35 A; A=1-426.
DR PDBsum; 5HTJ; -.
DR PDBsum; 5HTN; -.
DR PDBsum; 5HTP; -.
DR PDBsum; 5HTY; -.
DR PDBsum; 5HU2; -.
DR PDBsum; 5HUX; -.
DR PDBsum; 5HV7; -.
DR AlphaFoldDB; Q31KC7; -.
DR SMR; Q31KC7; -.
DR STRING; 1140.Synpcc7942_2462; -.
DR PRIDE; Q31KC7; -.
DR EnsemblBacteria; ABB58492; ABB58492; Synpcc7942_2462.
DR KEGG; syf:Synpcc7942_2462; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_0_0_3; -.
DR OMA; FLHQADW; -.
DR OrthoDB; 1619686at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2462-MON; -.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019150; F:D-ribulokinase activity; IDA:UniProtKB.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR Pfam; PF02782; FGGY_C; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Transferase.
FT CHAIN 1..426
FT /note="D-ribulose kinase"
FT /id="PRO_0000443301"
FT BINDING 8
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HV7"
FT BINDING 12..15
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HV7"
FT BINDING 72
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HV7"
FT BINDING 221
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HV7"
FT BINDING 243
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HTP, ECO:0007744|PDB:5HUX"
FT BINDING 281
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HTP, ECO:0007744|PDB:5HUX"
FT BINDING 376..380
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000269|PubMed:27223615,
FT ECO:0007744|PDB:5HTP, ECO:0007744|PDB:5HUX"
FT MUTAGEN 8
FT /note="D->A: Reduced ATP hydrolysis in the presence of D-
FT ribulose."
FT /evidence="ECO:0000269|PubMed:27223615"
FT MUTAGEN 11
FT /note="T->A: Reduced ATP hydrolysis in the presence of D-
FT ribulose."
FT /evidence="ECO:0000269|PubMed:27223615"
FT MUTAGEN 221
FT /note="D->A: Reduced ATP hydrolysis in the presence of D-
FT ribulose."
FT /evidence="ECO:0000269|PubMed:27223615"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 11..20
FT /evidence="ECO:0007829|PDB:5HUX"
FT TURN 21..24
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 25..32
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 40..54
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 57..60
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 65..70
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 75..78
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 99..102
FT /evidence="ECO:0007829|PDB:5HUX"
FT TURN 103..105
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 118..129
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 137..140
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 141..150
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:5HUX"
FT TURN 158..161
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 162..164
FT /evidence="ECO:0007829|PDB:5HUX"
FT TURN 168..171
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 175..178
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 180..182
FT /evidence="ECO:0007829|PDB:5HV7"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 188..190
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 194..198
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 201..207
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 214..216
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 221..229
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 236..253
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 258..260
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 264..267
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 270..276
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 281..287
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 290..297
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 320..322
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 338..362
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 370..375
FT /evidence="ECO:0007829|PDB:5HUX"
FT TURN 376..379
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 381..391
FT /evidence="ECO:0007829|PDB:5HUX"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 403..413
FT /evidence="ECO:0007829|PDB:5HUX"
FT TURN 414..417
FT /evidence="ECO:0007829|PDB:5HUX"
FT HELIX 420..422
FT /evidence="ECO:0007829|PDB:5HUX"
SQ SEQUENCE 426 AA; 46010 MW; C34202152B738E48 CRC64;
MVVALGLDFG TSGARAIACD FDSDRSVSVS VTFPKTSQNW PQVWREALWQ LLTQIPADWR
SRIERIAIDG TSGTVLLCDR EGQPQTEPLL YNQACPIDLA DLADWVPADH AALSSTSSLA
KLWFWQQQFG ALPPDWQILA QADWLSLQLH GCSQQSDYHN ALKLGYSPDR ERFSKNLLDS
ELGALLPVVH EPGVAIGPIL PAIAQEFGLS PDCQICAGTT DSIAAFLASG AHQPGEAVTS
LGSTIVLKLL SQVAVSDRLT GVYSHKLGGY WLTGGASNCG GATLRQFFPD TELESLSCQI
DPTKKSGLDY YPLPSRGERF PIADPDRLPQ LEPRPENPVQ FLQGLLEGLT QVETLGYQRL
QDLGATPLKR IWTAGGGAKN AVWQQLRQQA IGVPIAIAPN TEAAFGTARL AAFGLAAFHS
AGLKRT
