GCK_PYRHO
ID GCK_PYRHO Reviewed; 440 AA.
AC O58231;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Glycerate 2-kinase;
DE Short=GCK;
DE EC=2.7.1.165 {ECO:0000269|PubMed:17563835};
DE AltName: Full=2-phosphoglycerate forming glycerate kinase;
GN Name=gck; OrderedLocusNames=PH0495;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2]
RP FUNCTION AS A GLYCERATE KINASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, SUBUNIT, AND NOMENCLATURE.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=17563835; DOI=10.1007/s00792-007-0079-9;
RA Liu B., Hong Y., Wu L., Li Z., Ni J., Sheng D., Shen Y.;
RT "A unique highly thermostable 2-phosphoglycerate forming glycerate kinase
RT from the hyperthermophilic archaeon Pyrococcus horikoshii: gene cloning,
RT expression and characterization.";
RL Extremophiles 11:733-739(2007).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS).
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RA Mizutani H., Kunishima N.;
RT "Crystal structure of the PH0495 protein from Pyrococccus horikoshii OT3.";
RL Submitted (MAY-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-glycerate to
CC 2-phosphoglycerate. It can also utilize GTP, CTP, UTP, ADP or
CC pyrophosphate as phosphate donor. {ECO:0000269|PubMed:17563835}.
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:17563835};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:17563835};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:17563835};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:17563835};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:17563835};
CC Note=Magnesium. It could be replaced to some extent by nickel,
CC manganese or cobalt. {ECO:0000269|PubMed:17563835};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for glycerate (at 45 degrees Celsius and at pH 7.0)
CC {ECO:0000269|PubMed:17563835};
CC KM=102 uM for ATP (at 45 degrees Celsius and at pH 7.0)
CC {ECO:0000269|PubMed:17563835};
CC Vmax=624 umol/min/mg enzyme with glycerate as substrate (at 45
CC degrees Celsius and at pH 7.0) {ECO:0000269|PubMed:17563835};
CC Vmax=639 umol/min/mg enzyme with ATP as substrate (at 45 degrees
CC Celsius and at pH 7.0) {ECO:0000269|PubMed:17563835};
CC pH dependence:
CC Optimum pH is 7.0 and half of the maximum activity remains at pH 6-
CC 10. {ECO:0000269|PubMed:17563835};
CC Temperature dependence:
CC Optimum temperature is 45 degrees Celsius. It has strong activity at
CC moderate temperature 30-50 degrees Celsius and about half of the
CC maximal activity is retained at 100 degrees Celsius.
CC {ECO:0000269|PubMed:17563835};
CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:17563835}.
CC -!- SIMILARITY: Belongs to the glycerate kinase type-1 family.
CC {ECO:0000305}.
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DR EMBL; BA000001; BAA29583.1; -; Genomic_DNA.
DR PIR; B71162; B71162.
DR PDB; 1X3L; X-ray; 2.10 A; A=1-440.
DR PDBsum; 1X3L; -.
DR AlphaFoldDB; O58231; -.
DR SMR; O58231; -.
DR STRING; 70601.3256900; -.
DR EnsemblBacteria; BAA29583; BAA29583; BAA29583.
DR KEGG; pho:PH0495; -.
DR eggNOG; arCOG04170; Archaea.
DR OMA; GKAAWRM; -.
DR BRENDA; 2.7.1.165; 5244.
DR EvolutionaryTrace; O58231; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0043798; F:glycerate 2-kinase activity; IDA:UniProtKB.
DR GO; GO:0008887; F:glycerate kinase activity; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; Transferase.
FT CHAIN 1..440
FT /note="Glycerate 2-kinase"
FT /id="PRO_0000415150"
FT BINDING 58
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT HELIX 6..20
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 23..30
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 35..40
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 51..57
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 60..70
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 74..81
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 89..96
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 98..100
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 103..118
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 123..129
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 133..136
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 146..158
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 163..171
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 174..176
FT /evidence="ECO:0007829|PDB:1X3L"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 180..183
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 186..194
FT /evidence="ECO:0007829|PDB:1X3L"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 205..207
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 217..226
FT /evidence="ECO:0007829|PDB:1X3L"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 235..245
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 260..266
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 268..281
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 285..293
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 297..314
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 320..328
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 335..337
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:1X3L"
FT TURN 352..357
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 358..366
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 372..375
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 378..382
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 385..391
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 396..401
FT /evidence="ECO:0007829|PDB:1X3L"
FT HELIX 405..411
FT /evidence="ECO:0007829|PDB:1X3L"
FT STRAND 427..435
FT /evidence="ECO:0007829|PDB:1X3L"
SQ SEQUENCE 440 AA; 47375 MW; C9C3E4FE4207F4B1 CRC64;
MIAMDIREIG LRLVGEAIKA ADPYRAVLNA VKVSDDKIIV QGKEFEIKGK VYVIALGKAA
CEMARAIEDI LDVEDGVAVT KYGYGKELKR IKVIEAGHPI PDEKSILGAK EALSILNRAR
ENDIVFILIS GGGSALFELP EEGISLEDLK LTTDLLLKSG AKIHEINTVR KHISKVKGGK
LAKMIKGTGI VLIISDVVGD NLEAIASGPT VKDPTTFEDA KRILELYDIW EKVPESVRLH
IERGLRGEVE ETLKEDLPNV HNFLIASNSI SCEAIAREAQ RLGFKAYIMT TTLEGEAKDA
GLFIGSIVQE IAERGRPFEP PVVLVFGGET TVTIEGKGGK GGPNQEIALS ATRKISDLEA
LIVAFDTDGT DGPTDAAGGI VDGTTYKKLR EKGIDVEKVL KEHNSYEALK KVGGLLFTGP
TGTNVNSIVI AIVTSKRGRT
