GCK_THEMA
ID GCK_THEMA Reviewed; 417 AA.
AC Q9X1S1; G4FFX3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 117.
DE RecName: Full=D-glycerate 2-kinase;
DE Short=GCK;
DE EC=2.7.1.165;
GN OrderedLocusNames=TM_1585; ORFNames=THEMA_06355, Tmari_1593;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=23637642; DOI=10.1371/journal.pgen.1003485;
RA Latif H., Lerman J.A., Portnoy V.A., Tarasova Y., Nagarajan H.,
RA Schrimpe-Rutledge A.C., Smith R.D., Adkins J.N., Lee D.H., Qiu Y.,
RA Zengler K.;
RT "The genome organization of Thermotoga maritima reflects its lifestyle.";
RL PLoS Genet. 9:E1003485-E1003485(2013).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RG DOE Joint Genome Institute;
RA Noll K.M., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, MUTAGENESIS OF LYS-47 AND ARG-325,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RX PubMed=18156253; DOI=10.1128/jb.01469-07;
RA Yang C., Rodionov D.A., Rodionova I.A., Li X., Osterman A.L.;
RT "Glycerate 2-kinase of Thermotoga maritima and genomic reconstruction of
RT related metabolic pathways.";
RL J. Bacteriol. 190:1773-1782(2008).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.53 ANGSTROMS), AND SUBUNIT.
RX PubMed=16865707; DOI=10.1002/prot.21058;
RA Schwarzenbacher R., McMullan D., Krishna S.S., Xu Q., Miller M.D.,
RA Canaves J.M., Elsliger M.A., Floyd R., Grzechnik S.K., Jaroszewski L.,
RA Klock H.E., Koesema E., Kovarik J.S., Kreusch A., Kuhn P., McPhillips T.M.,
RA Morse A.T., Quijano K., Spraggon G., Stevens R.C., van den Bedem H.,
RA Wolf G., Hodgson K.O., Wooley J., Deacon A.M., Godzik A., Lesley S.A.,
RA Wilson I.A.;
RT "Crystal structure of a glycerate kinase (TM1585) from Thermotoga maritima
RT at 2.70 A resolution reveals a new fold.";
RL Proteins 65:243-248(2006).
CC -!- FUNCTION: Involved in the degradation of serine via 3-hydroxypyruvate.
CC Catalyzes the ATP-dependent phosphorylation of D-glycerate to 2-
CC phosphoglycerate. {ECO:0000269|PubMed:18156253}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-glycerate + ATP = (2R)-2-phosphoglycerate + ADP + H(+);
CC Xref=Rhea:RHEA:27377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16659,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58289, ChEBI:CHEBI:456216;
CC EC=2.7.1.165; Evidence={ECO:0000269|PubMed:18156253};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:18156253};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.095 mM for ATP {ECO:0000269|PubMed:18156253};
CC KM=0.15 mM for D-glycerate {ECO:0000269|PubMed:18156253};
CC Note=kcat is 14.4 sec(-1) for phosphorylation of D-glycerate.;
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16865707,
CC ECO:0000269|PubMed:18156253}.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
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DR EMBL; AE000512; AAD36652.1; -; Genomic_DNA.
DR EMBL; CP004077; AGL50517.1; -; Genomic_DNA.
DR EMBL; CP007013; AHD18518.1; -; Genomic_DNA.
DR PIR; A72236; A72236.
DR RefSeq; NP_229385.1; NC_000853.1.
DR RefSeq; WP_004082016.1; NZ_CP011107.1.
DR PDB; 2B8N; X-ray; 2.53 A; A/B=1-417.
DR PDBsum; 2B8N; -.
DR AlphaFoldDB; Q9X1S1; -.
DR SMR; Q9X1S1; -.
DR STRING; 243274.THEMA_06355; -.
DR EnsemblBacteria; AAD36652; AAD36652; TM_1585.
DR EnsemblBacteria; AGL50517; AGL50517; Tmari_1593.
DR KEGG; tma:TM1585; -.
DR KEGG; tmi:THEMA_06355; -.
DR KEGG; tmm:Tmari_1593; -.
DR KEGG; tmw:THMA_1620; -.
DR PATRIC; fig|243274.17.peg.1593; -.
DR eggNOG; COG2379; Bacteria.
DR InParanoid; Q9X1S1; -.
DR OMA; GKAAWRM; -.
DR OrthoDB; 1358712at2; -.
DR BRENDA; 2.7.1.165; 6331.
DR SABIO-RK; Q9X1S1; -.
DR EvolutionaryTrace; Q9X1S1; -.
DR Proteomes; UP000008183; Chromosome.
DR Proteomes; UP000013901; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043798; F:glycerate 2-kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008887; F:glycerate kinase activity; IBA:GO_Central.
DR GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IDA:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR Gene3D; 3.40.1480.10; -; 1.
DR Gene3D; 3.40.50.10180; -; 1.
DR InterPro; IPR037035; GK-like_C_sf.
DR InterPro; IPR038614; GK_N_sf.
DR InterPro; IPR007835; MOFRL.
DR InterPro; IPR025286; MOFRL_assoc_dom.
DR InterPro; IPR039760; MOFRL_protein.
DR PANTHER; PTHR12227; PTHR12227; 1.
DR Pfam; PF13660; DUF4147; 1.
DR Pfam; PF05161; MOFRL; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..417
FT /note="D-glycerate 2-kinase"
FT /id="PRO_0000428994"
FT MUTAGEN 47
FT /note="K->A: Very low residual kinase activity."
FT /evidence="ECO:0000269|PubMed:18156253"
FT MUTAGEN 47
FT /note="K->R: Significant decrease of the kinase activity
FT with a 180-fold decrease of catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:18156253"
FT MUTAGEN 325
FT /note="R->A,K: Significant decrease of the kinase activity
FT with a 17-fold decrease of catalytic efficiency."
FT /evidence="ECO:0000269|PubMed:18156253"
FT HELIX 5..20
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 24..29
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 32..35
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 39..46
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 61..63
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 64..72
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 90..92
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 116..121
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 125..128
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 155..163
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 166..168
FT /evidence="ECO:0007829|PDB:2B8N"
FT TURN 169..171
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 172..177
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 180..187
FT /evidence="ECO:0007829|PDB:2B8N"
FT TURN 195..197
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 198..200
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 210..219
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 226..232
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 241..249
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 251..264
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 268..276
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 280..297
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 303..311
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 325..336
FT /evidence="ECO:0007829|PDB:2B8N"
FT TURN 337..339
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 343..349
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 355..358
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 368..374
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 379..384
FT /evidence="ECO:0007829|PDB:2B8N"
FT HELIX 388..394
FT /evidence="ECO:0007829|PDB:2B8N"
FT STRAND 410..416
FT /evidence="ECO:0007829|PDB:2B8N"
SQ SEQUENCE 417 AA; 44722 MW; FEE01EC89CC8E445 CRC64;
MFDPESLKKL AIEIVKKSIE AVFPDRAVKE TLPKLNLDRV ILVAVGKAAW RMAKAAYEVL
GKKIRKGVVV TKYGHSEGPI DDFEIYEAGH PVPDENTIKT TRRVLELVDQ LNENDTVLFL
LSGGGSSLFE LPLEGVSLEE IQKLTSALLK SGASIEEINT VRKHLSQVKG GRFAERVFPA
KVVALVLSDV LGDRLDVIAS GPAWPDSSTS EDALKVLEKY GIETSESVKR AILQETPKHL
SNVEIHLIGN VQKVCDEAKS LAKEKGFNAE IITTSLDCEA REAGRFIASI MKEVKFKDRP
LKKPAALIFG GETVVHVKGN GIGGRNQELA LSAAIALEGI EGVILCSAGT DGTDGPTDAA
GGIVDGSTAK TLKAMGEDPY QYLKNNDSYN ALKKSGALLI TGPTGTNVND LIIGLIV
