GLK_AERPE
ID GLK_AERPE Reviewed; 320 AA.
AC Q9YA47;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 2.
DT 25-MAY-2022, entry version 88.
DE RecName: Full=Glucokinase {ECO:0000303|PubMed:12374829};
DE EC=2.7.1.2 {ECO:0000269|PubMed:12374829};
DE AltName: Full=ATP-dependent glucokinase {ECO:0000303|PubMed:12374829};
DE Short=ATP-GLK {ECO:0000303|PubMed:12374829};
DE AltName: Full=Glucose kinase {ECO:0000305};
GN Name=glk {ECO:0000303|PubMed:12374829};
GN OrderedLocusNames=APE_2091.1 {ECO:0000312|EMBL:BAA81102.2};
OS Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 /
OS K1).
OC Archaea; Crenarchaeota; Thermoprotei; Desulfurococcales;
OC Desulfurococcaceae; Aeropyrum.
OX NCBI_TaxID=272557;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=10382966; DOI=10.1093/dnares/6.2.83;
RA Kawarabayasi Y., Hino Y., Horikawa H., Yamazaki S., Haikawa Y., Jin-no K.,
RA Takahashi M., Sekine M., Baba S., Ankai A., Kosugi H., Hosoyama A.,
RA Fukui S., Nagai Y., Nishijima K., Nakazawa H., Takamiya M., Masuda S.,
RA Funahashi T., Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A.,
RA Aoki K., Kubota K., Nakamura Y., Nomura N., Sako Y., Kikuchi H.;
RT "Complete genome sequence of an aerobic hyper-thermophilic crenarchaeon,
RT Aeropyrum pernix K1.";
RL DNA Res. 6:83-101(1999).
RN [2]
RP PROTEIN SEQUENCE OF 1-11, FUNCTION, CATALYTIC ACTIVITY, COFACTOR,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1;
RX PubMed=12374829; DOI=10.1128/jb.184.21.5955-5965.2002;
RA Hansen T., Reichstein B., Schmid R., Schoenheit P.;
RT "The first archaeal ATP-dependent glucokinase, from the hyperthermophilic
RT crenarchaeon Aeropyrum pernix, represents a monomeric, extremely
RT thermophilic ROK glucokinase with broad hexose specificity.";
RL J. Bacteriol. 184:5955-5965(2002).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBUNIT.
RX PubMed=12761185; DOI=10.1093/jb/mvg027;
RA Sakuraba H., Mitani Y., Goda S., Kawarabayasi Y., Ohshima T.;
RT "Cloning, expression, and characterization of the first archaeal ATP-
RT dependent glucokinase from aerobic hyperthermophilic archaeon Aeropyrum
RT pernix.";
RL J. Biochem. 133:219-224(2003).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6-
CC phosphate using ATP as the phosphate donor (PubMed:12374829,
CC PubMed:12761185). ITP can also serve as an effective phosphoryl donor
CC (PubMed:12374829, PubMed:12761185). According to Hansen et al., the
CC enzyme has a broad hexose specificity, and in addition to glucose,
CC which shows the highest catalytic efficiency, it can also phosphorylate
CC fructose, mannose, glucosamine, N-acetylglucosamine, N-
CC acetylmannosamine and 2-deoxyglucose (PubMed:12374829). However,
CC according to Sakuraba et al., the enzyme shows strict specificity for
CC D-glucose (PubMed:12761185). {ECO:0000269|PubMed:12374829,
CC ECO:0000269|PubMed:12761185}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC Evidence={ECO:0000269|PubMed:12374829, ECO:0000269|PubMed:12761185};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:12374829, ECO:0000269|PubMed:12761185};
CC Note=Mg(2+) is the most effective ion. It can be partially replaced
CC with Co(2+), Mn(2+), Ni(2+), Cu(2+) or Ca(2+).
CC {ECO:0000269|PubMed:12374829, ECO:0000269|PubMed:12761185};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=44 uM for glucose {ECO:0000269|PubMed:12374829};
CC KM=54 uM for D-glucose {ECO:0000269|PubMed:12761185};
CC KM=330 uM for 2-deoxyglucose {ECO:0000269|PubMed:12374829};
CC KM=60 uM for glucosamine {ECO:0000269|PubMed:12374829};
CC KM=150 uM for fructose {ECO:0000269|PubMed:12374829};
CC KM=110 uM for mannose {ECO:0000269|PubMed:12374829};
CC KM=420 uM for ATP {ECO:0000269|PubMed:12374829};
CC KM=500 uM for ATP {ECO:0000269|PubMed:12761185};
CC Note=kcat is 23 sec(-1) with glucose as substrate. kcat is 30 sec(-1)
CC with 2-deoxyglucose as substrate. kcat is 18 sec(-1) with glucosamine
CC as substrate. kcat is 10 sec(-1) with fructose as substrate. kcat is
CC 13 sec(-1) with mannose as substrate. {ECO:0000269|PubMed:12374829};
CC pH dependence:
CC Optimum pH is 6.2. {ECO:0000269|PubMed:12374829};
CC Temperature dependence:
CC Activity increases exponentially up to 100 degrees Celsius, the
CC highest temperature tested. {ECO:0000269|PubMed:12374829};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12374829,
CC ECO:0000269|PubMed:12761185}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; BA000002; BAA81102.2; -; Genomic_DNA.
DR PIR; F72514; F72514.
DR AlphaFoldDB; Q9YA47; -.
DR SMR; Q9YA47; -.
DR STRING; 272557.APE_2091.1; -.
DR EnsemblBacteria; BAA81102; BAA81102; APE_2091.1.
DR KEGG; ape:APE_2091.1; -.
DR PATRIC; fig|272557.25.peg.1395; -.
DR eggNOG; arCOG04280; Archaea.
DR OMA; DHLVMIT; -.
DR SABIO-RK; Q9YA47; -.
DR Proteomes; UP000002518; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Carbohydrate metabolism; Direct protein sequencing;
KW Glucose metabolism; Kinase; Magnesium; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..320
FT /note="Glucokinase"
FT /id="PRO_0000448973"
SQ SEQUENCE 320 AA; 33876 MW; 449F1CEA13213E1F CRC64;
MAEVVAVDVG ATWVRMAIVR GGVIEAIKRE RNPGTEEGLE RVLQGLAEGL GIDRGRVEKV
GAASIGPLDL RRGYIVGSPN IKSHIVRLST ILKRLFPKSK VAIANDAVAA AWGEYLLGRL
AGTPDLGYIT MSTGVGGGFV VGGRLLLGSR GNAHEVGHIV VDMGWEGGRC GCGGTGHWEA
IAGGRWIPRT SSVLARGWRG PETSLYRAAL EGRVGSAREV FEAAAVGDDF ALHVIDYIAR
ASAAGIASVK AAYDVDAVII GGSVYLNNRR MLRPLIERHL AAYAPFSSRI EVVDASFGDN
EGVMGAYAIA YRNPEDLPIF
