GLSK_MOUSE
ID GLSK_MOUSE Reviewed; 674 AA.
AC D3Z7P3; E9PUF0; Q69ZX9;
DT 13-JUN-2012, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glutaminase kidney isoform, mitochondrial;
DE Short=GLS;
DE EC=3.5.1.2 {ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:23935106, ECO:0000269|PubMed:27542409};
DE Contains:
DE RecName: Full=Glutaminase kidney isoform, mitochondrial 68 kDa chain {ECO:0000250|UniProtKB:P13264};
DE Contains:
DE RecName: Full=Glutaminase kidney isoform, mitochondrial 65 kDa chain {ECO:0000250|UniProtKB:P13264};
DE Flags: Precursor;
GN Name=Gls; Synonyms=Gls1, Kiaa0838;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP INTERACTION WITH ATCAY.
RX PubMed=16899818; DOI=10.1242/jcs.03061;
RA Buschdorf J.P., Li Chew L., Zhang B., Cao Q., Liang F.Y., Liou Y.C.,
RA Zhou Y.T., Low B.C.;
RT "Brain-specific BNIP-2-homology protein Caytaxin relocalises glutaminase to
RT neurite terminals and reduces glutamate levels.";
RL J. Cell Sci. 119:3337-3350(2006).
RN [4]
RP DISRUPTION PHENOTYPE, FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=16641247; DOI=10.1523/jneurosci.4241-05.2006;
RA Masson J., Darmon M., Conjard A., Chuhma N., Ropert N., Thoby-Brisson M.,
RA Foutz A.S., Parrot S., Miller G.M., Jorisch R., Polan J., Hamon M., Hen R.,
RA Rayport S.;
RT "Mice lacking brain/kidney phosphate-activated glutaminase have impaired
RT glutamatergic synaptic transmission, altered breathing, disorganized goal-
RT directed behavior and die shortly after birth.";
RL J. Neurosci. 26:4660-4671(2006).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [6]
RP FUNCTION.
RX PubMed=22373647; DOI=10.1038/jcbfm.2012.22;
RA El Hage M., Masson J., Conjard-Duplany A., Ferrier B., Baverel G.,
RA Martin G.;
RT "Brain slices from glutaminase-deficient mice metabolize less glutamine: a
RT cellular metabolomic study with carbon 13 NMR.";
RL J. Cereb. Blood Flow Metab. 32:816-824(2012).
RN [7]
RP SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-135 AND LYS-169, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [8] {ECO:0007744|PDB:3SS3, ECO:0007744|PDB:3SS4, ECO:0007744|PDB:3SS5}
RP X-RAY CRYSTALLOGRAPHY (2.42 ANGSTROMS) OF 128-555 (ISOFORM 2) IN COMPLEX
RP WITH GLUTAMATE AND PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, ALTERNATIVE SPLICING, MUTAGENESIS OF PHE-394, AND SUBUNIT.
RX PubMed=22228304; DOI=10.1073/pnas.1112495109;
RA Cassago A., Ferreira A.P., Ferreira I.M., Fornezari C., Gomes E.R.,
RA Greene K.S., Pereira H.M., Garratt R.C., Dias S.M., Ambrosio A.L.;
RT "Mitochondrial localization and structure-based phosphate activation
RT mechanism of glutaminase C with implications for cancer metabolism.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:1092-1097(2012).
RN [9] {ECO:0007744|PDB:4JKT}
RP X-RAY CRYSTALLOGRAPHY (2.77 ANGSTROMS) OF 128-555, SUBUNIT, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND MUTAGENESIS OF LYS-202; LYS-207 AND
RP LYS-325.
RX PubMed=23935106; DOI=10.1074/jbc.m113.501346;
RA Ferreira A.P., Cassago A., Goncalves Kde A., Dias M.M., Adamoski D.,
RA Ascencao C.F., Honorato R.V., de Oliveira J.F., Ferreira I.M.,
RA Fornezari C., Bettini J., Oliveira P.S., Paes Leme A.F., Portugal R.V.,
RA Ambrosio A.L., Dias S.M.;
RT "Active glutaminase C self-assembles into a supratetrameric oligomer that
RT can be disrupted by an allosteric inhibitor.";
RL J. Biol. Chem. 288:28009-28020(2013).
RN [10] {ECO:0007744|PDB:5W2J}
RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 141-551 OF MUTANT LYS-391,
RP SUBUNIT, CATALYTIC ACTIVITY, ACTIVITY REGULATION, SUBCELLULAR LOCATION,
RP DOMAIN, AND MUTAGENESIS OF LYS-316; GLY-320; LYS-325 AND ASP-391.
RX PubMed=27542409; DOI=10.1074/jbc.m116.720268;
RA Li Y., Erickson J.W., Stalnecker C.A., Katt W.P., Huang Q., Cerione R.A.,
RA Ramachandran S.;
RT "Mechanistic basis of glutaminase activation: a key enzyme that promotes
RT glutamine metabolism in cancer cells.";
RL J. Biol. Chem. 291:20900-20910(2016).
CC -!- FUNCTION: Catalyzes the first reaction in the primary pathway for the
CC renal catabolism of glutamine. Plays a role in maintaining acid-base
CC homeostasis. Regulates the levels of the neurotransmitter glutamate,
CC the main excitatory neurotransmitter in the brain.
CC {ECO:0000269|PubMed:16641247, ECO:0000269|PubMed:22228304,
CC ECO:0000269|PubMed:22373647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-glutamine = L-glutamate + NH4(+);
CC Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2;
CC Evidence={ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:23935106,
CC ECO:0000269|PubMed:27542409};
CC -!- ACTIVITY REGULATION: Isoform 1 and isoform 2 are activated by
CC phosphate, due to increased affinity for glutamine (PubMed:22228304,
CC PubMed:23935106, PubMed:27542409). At phosphate concentrations above 10
CC mM, isoform 2 is more efficient than isoform 1.
CC {ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:23935106,
CC ECO:0000269|PubMed:27542409}.
CC -!- SUBUNIT: Homotetramer, dimer of dimers (PubMed:22228304,
CC PubMed:27542409). The tetramers can assemble into rod-like oligomers
CC (in vitro), but the physiological significance of this is not clear
CC (PubMed:23935106). Interacts with RAF1 and MAP2K2 (By similarity).
CC Interacts with ATCAY; the interaction is direct and may control GLS
CC localization, negatively regulating its activity (PubMed:16899818).
CC {ECO:0000250|UniProtKB:O94925, ECO:0000269|PubMed:16899818,
CC ECO:0000269|PubMed:22228304, ECO:0000269|PubMed:23935106,
CC ECO:0000269|PubMed:27542409}.
CC -!- INTERACTION:
CC D3Z7P3-2; D3Z7P3-2: Gls; NbExp=3; IntAct=EBI-15962029, EBI-15962029;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion
CC {ECO:0000250|UniProtKB:P13264}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:P13264}. Note=The 74-kDa cytosolic precursor is
CC translocated into the mitochondria and processed via a 72-kDa
CC intermediate to yield the mature 68- and 65-kDa subunits.
CC {ECO:0000250|UniProtKB:P13264}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion
CC {ECO:0000269|PubMed:16641247, ECO:0000269|PubMed:27542409}.
CC -!- SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 68 kDa
CC chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}.
CC Note=Produced by the proteolytic processing of the 74-kDa cytosolic
CC precursor. {ECO:0000250|UniProtKB:P13264}.
CC -!- SUBCELLULAR LOCATION: [Glutaminase kidney isoform, mitochondrial 65 kDa
CC chain]: Mitochondrion matrix {ECO:0000250|UniProtKB:P13264}.
CC Note=Produced by the proteolytic processing of the 74-kDa cytosolic
CC precursor. {ECO:0000250|UniProtKB:P13264}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=KGA {ECO:0000303|PubMed:22228304};
CC IsoId=D3Z7P3-1; Sequence=Displayed;
CC Name=2; Synonyms=Glutaminase C {ECO:0000303|PubMed:23935106}, GAC
CC {ECO:0000303|PubMed:22228304, ECO:0000303|PubMed:23935106};
CC IsoId=D3Z7P3-2; Sequence=VSP_043804;
CC -!- DOMAIN: A highly mobile activation loop at the dimer-dimer interface is
CC important for enzyme activity. {ECO:0000269|PubMed:27542409}.
CC -!- DOMAIN: The C-terminal ANK repeats prevent the assembly of the supra-
CC tetrameric filaments. {ECO:0000250|UniProtKB:O94925}.
CC -!- PTM: Synthesized as a 74-kDa cytosolic precursor which is
CC proteolytically processed by the mitochondrial-processing peptidase
CC (MPP) via a 72-kDa intermediate to yield the mature mitochondrial
CC 68- and 65-kDa subunits. {ECO:0000250|UniProtKB:P13264}.
CC -!- DISRUPTION PHENOTYPE: Death during the first days after birth. Pups
CC appear normal and display normal levels of activity, but their activity
CC is disorganized. Pups do not orient to the dam, do not succeed in
CC grasping a nipple and do not feed properly. In addition, they display
CC altered respiration. {ECO:0000269|PubMed:16641247}.
CC -!- SIMILARITY: Belongs to the glutaminase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD32317.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173039; BAD32317.1; ALT_INIT; mRNA.
DR EMBL; AC123752; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS35561.1; -. [D3Z7P3-1]
DR CCDS; CCDS48256.1; -. [D3Z7P3-2]
DR RefSeq; NP_001074550.1; NM_001081081.2. [D3Z7P3-1]
DR RefSeq; NP_001106854.1; NM_001113383.1. [D3Z7P3-2]
DR PDB; 3SS3; X-ray; 2.42 A; A/B/C/D=128-602.
DR PDB; 3SS4; X-ray; 2.85 A; A/B/C/D=128-602.
DR PDB; 3SS5; X-ray; 2.80 A; A/B/C/D=128-602.
DR PDB; 4JKT; X-ray; 2.77 A; A/B/C/D=128-555.
DR PDB; 5W2J; X-ray; 2.50 A; A/B=141-551.
DR PDBsum; 3SS3; -.
DR PDBsum; 3SS4; -.
DR PDBsum; 3SS5; -.
DR PDBsum; 4JKT; -.
DR PDBsum; 5W2J; -.
DR AlphaFoldDB; D3Z7P3; -.
DR SMR; D3Z7P3; -.
DR BioGRID; 199955; 13.
DR DIP; DIP-60006N; -.
DR IntAct; D3Z7P3; 2.
DR MINT; D3Z7P3; -.
DR STRING; 10090.ENSMUSP00000110158; -.
DR BindingDB; D3Z7P3; -.
DR ChEMBL; CHEMBL4523110; -.
DR iPTMnet; D3Z7P3; -.
DR PhosphoSitePlus; D3Z7P3; -.
DR SwissPalm; D3Z7P3; -.
DR EPD; D3Z7P3; -.
DR jPOST; D3Z7P3; -.
DR MaxQB; D3Z7P3; -.
DR PaxDb; D3Z7P3; -.
DR PeptideAtlas; D3Z7P3; -.
DR PRIDE; D3Z7P3; -.
DR ProteomicsDB; 271395; -. [D3Z7P3-1]
DR ProteomicsDB; 271396; -. [D3Z7P3-2]
DR Antibodypedia; 34041; 460 antibodies from 33 providers.
DR Ensembl; ENSMUST00000114510; ENSMUSP00000110155; ENSMUSG00000026103. [D3Z7P3-2]
DR Ensembl; ENSMUST00000114513; ENSMUSP00000110158; ENSMUSG00000026103. [D3Z7P3-1]
DR GeneID; 14660; -.
DR KEGG; mmu:14660; -.
DR UCSC; uc007aye.2; mouse. [D3Z7P3-1]
DR UCSC; uc011wko.1; mouse. [D3Z7P3-2]
DR CTD; 2744; -.
DR MGI; MGI:95752; Gls.
DR VEuPathDB; HostDB:ENSMUSG00000026103; -.
DR eggNOG; KOG0506; Eukaryota.
DR GeneTree; ENSGT00390000010463; -.
DR HOGENOM; CLU_016439_1_1_1; -.
DR InParanoid; D3Z7P3; -.
DR OMA; QCCSMEA; -.
DR OrthoDB; 349094at2759; -.
DR PhylomeDB; D3Z7P3; -.
DR TreeFam; TF313359; -.
DR Reactome; R-MMU-210500; Glutamate Neurotransmitter Release Cycle.
DR Reactome; R-MMU-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-MMU-8964539; Glutamate and glutamine metabolism.
DR BioGRID-ORCS; 14660; 13 hits in 73 CRISPR screens.
DR ChiTaRS; Gls; mouse.
DR PRO; PR:D3Z7P3; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; D3Z7P3; protein.
DR Bgee; ENSMUSG00000026103; Expressed in pontine nuclear group and 231 other tissues.
DR ExpressionAtlas; D3Z7P3; baseline and differential.
DR Genevisible; D3Z7P3; MM.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR GO; GO:0005739; C:mitochondrion; ISO:MGI.
DR GO; GO:0045202; C:synapse; IEA:GOC.
DR GO; GO:0004359; F:glutaminase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007268; P:chemical synaptic transmission; IMP:MGI.
DR GO; GO:0006537; P:glutamate biosynthetic process; IDA:UniProtKB.
DR GO; GO:0090461; P:glutamate homeostasis; ISO:MGI.
DR GO; GO:0006543; P:glutamine catabolic process; IDA:UniProtKB.
DR GO; GO:0051289; P:protein homotetramerization; IDA:UniProtKB.
DR GO; GO:0002087; P:regulation of respiratory gaseous exchange by nervous system process; IMP:MGI.
DR GO; GO:0001967; P:suckling behavior; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 3.40.710.10; -; 1.
DR HAMAP; MF_00313; Glutaminase; 1.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR012338; Beta-lactam/transpept-like.
DR InterPro; IPR015868; Glutaminase.
DR InterPro; IPR041541; Glutaminase_EF-hand.
DR PANTHER; PTHR12544; PTHR12544; 1.
DR Pfam; PF12796; Ank_2; 1.
DR Pfam; PF17959; EF-hand_14; 1.
DR Pfam; PF04960; Glutaminase; 1.
DR SMART; SM00248; ANK; 2.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF56601; SSF56601; 1.
DR TIGRFAMs; TIGR03814; Gln_ase; 1.
DR PROSITE; PS50297; ANK_REP_REGION; 1.
DR PROSITE; PS50088; ANK_REPEAT; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; ANK repeat; Cytoplasm;
KW Hydrolase; Mitochondrion; Phosphoprotein; Reference proteome; Repeat;
KW Transit peptide.
FT TRANSIT 1..54
FT /note="Mitochondrion"
FT /evidence="ECO:0000255"
FT CHAIN 55..674
FT /note="Glutaminase kidney isoform, mitochondrial 68 kDa
FT chain"
FT /id="PRO_0000417583"
FT CHAIN 73..674
FT /note="Glutaminase kidney isoform, mitochondrial 65 kDa
FT chain"
FT /evidence="ECO:0000250|UniProtKB:P13264"
FT /id="PRO_0000447413"
FT REPEAT 590..619
FT /note="ANK 1"
FT REPEAT 624..653
FT /note="ANK 2"
FT REGION 56..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 320..327
FT /note="Highly mobile activation loop"
FT /evidence="ECO:0000269|PubMed:27542409"
FT REGION 652..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT BINDING 340
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT BINDING 386
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT BINDING 393
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT BINDING 419
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT BINDING 471
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT BINDING 489
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:22228304,
FT ECO:0007744|PDB:3SS5"
FT SITE 72..73
FT /note="Cleavage; by MPP"
FT /evidence="ECO:0000250|UniProtKB:P13264"
FT MOD_RES 135
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 169
FT /note="N6-succinyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 316
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O94925"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P13264"
FT VAR_SEQ 556..674
FT /note="VKSVINLLFAAYTGDVSALRRFALSAMDMEQRDYDSRTALHVAAAEGHVEVV
FT KFLLEACKVNPFPKDRWNNTPMDEALHFGHHDVFKILQEYQVQYTPQGDSDDGKGNQTV
FT HKNLDGLL -> HSFGPLDYESLQQELALKDTVWKKVSPESSDDTSTTVVYRMESLGER
FT S (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_043804"
FT MUTAGEN 202
FT /note="K->E: Increased stimulation of enzyme activity by
FT phosphate."
FT /evidence="ECO:0000269|PubMed:23935106"
FT MUTAGEN 207
FT /note="K->E: Increased stimulation of enzyme activity by
FT phosphate."
FT /evidence="ECO:0000269|PubMed:23935106"
FT MUTAGEN 254
FT /note="Y->F: Increased enzyme activity in the absence of
FT phosphate. No effect on stimulation of enzyme activity by
FT phosphate."
FT /evidence="ECO:0000269|PubMed:27542409"
FT MUTAGEN 316
FT /note="K->Q: Forms dimers with full, phosphate-independent
FT activity; when associated with A-325 and K-391."
FT /evidence="ECO:0000269|PubMed:27542409"
FT MUTAGEN 320
FT /note="G->P: Loss of enzyme activity."
FT /evidence="ECO:0000269|PubMed:27542409"
FT MUTAGEN 325
FT /note="K->A: Constitutive enzyme activity that is fully
FT active also in the absence phosphate. Forms oligomers with
FT full, phosphate-independent activity; when associated with
FT K-391. Forms dimers with full, phosphate-independent
FT activity; when associated with Q-316 and K-391."
FT /evidence="ECO:0000269|PubMed:23935106,
FT ECO:0000269|PubMed:27542409"
FT MUTAGEN 391
FT /note="D->K: Abolishes assembly of dimers into functional
FT tetramers. Loss of enzyme activity. Forms oligomers with
FT full, phosphate-independent activity; when associated with
FT A-325. Forms dimers with full, phosphate-independent
FT activity; when associated with Q-316 and A-325."
FT /evidence="ECO:0000269|PubMed:27542409"
FT MUTAGEN 394
FT /note="F->S: Impairs tetramerization and promotes formation
FT of homodimers. Impairs activation by phosphate."
FT /evidence="ECO:0000269|PubMed:22228304"
FT HELIX 145..151
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 157..160
FT /evidence="ECO:0007829|PDB:3SS5"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 178..180
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:5W2J"
FT HELIX 202..209
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:5W2J"
FT HELIX 213..220
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 229..243
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 249..251
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 256..259
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 267..272
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 277..282
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 290..293
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 294..313
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 321..328
FT /evidence="ECO:0007829|PDB:4JKT"
FT STRAND 332..335
FT /evidence="ECO:0007829|PDB:3SS5"
FT HELIX 340..349
FT /evidence="ECO:0007829|PDB:3SS3"
FT TURN 350..353
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 356..370
FT /evidence="ECO:0007829|PDB:3SS3"
FT TURN 371..373
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 376..378
FT /evidence="ECO:0007829|PDB:4JKT"
FT HELIX 380..388
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 391..402
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 412..423
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 425..427
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:3SS3"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:3SS3"
FT TURN 446..448
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 455..468
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:3SS3"
FT HELIX 474..480
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 485..487
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 491..497
FT /evidence="ECO:0007829|PDB:3SS3"
FT TURN 498..500
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 501..506
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 508..510
FT /evidence="ECO:0007829|PDB:3SS3"
FT STRAND 514..516
FT /evidence="ECO:0007829|PDB:3SS5"
FT HELIX 517..529
FT /evidence="ECO:0007829|PDB:3SS3"
SQ SEQUENCE 674 AA; 73964 MW; C46824C83E1D9639 CRC64;
MMRLRGSAML RELLLRPPAA VGAVLRRAQP LGTLCRRPRG GSRPTAGLVA AARLHPWWGG
GGRAKGPGAG GLSSSPSEIL QELGKGGTPP QQQQQQQQQP GASPPAAPGP KDSPGETDAF
GNSEGKEMVA AGDNKIKQGL LPSLEDLLFY TIAEGQEKIP VHKFITALKS TGLRTSDPRL
KECMDMLRLT LQTTSDGVML DKDLFKKCVQ SNIVLLTQAF RRKFVIPDFM SFTSHIDELY
ESAKKQSGGK VADYIPQLAK FSPDLWGVSV CTVDGQRHSI GDTKVPFCLQ SCVKPLKYAI
AVNDLGTEYV HRYVGKEPSG LRFNKLFLNE DDKPHNPMVN AGAIVVTSLI KQGVNNAEKF
DYVMQFLNKM AGNEYVGFSN ATFQSERESG DRNFAIGYYL KEKKCFPEGT DMVGILDFYF
QLCSIEVTCE SASVMAATLA NGGFCPITGE RVLSPEAVRN TLSLMHSCGM YDFSGQFAFH
VGLPAKSGVA GGILLVVPNV MGMMCWSPPL DKMGNSVKGI HFCHDLVSLC NFHNYDNLRH
FAKKLDPRRE GGDQRVKSVI NLLFAAYTGD VSALRRFALS AMDMEQRDYD SRTALHVAAA
EGHVEVVKFL LEACKVNPFP KDRWNNTPMD EALHFGHHDV FKILQEYQVQ YTPQGDSDDG
KGNQTVHKNL DGLL
