G5K_LEIDO
ID G5K_LEIDO Reviewed; 263 AA.
AC A0A0R6Y3I5;
DT 13-NOV-2019, integrated into UniProtKB/Swiss-Prot.
DT 17-FEB-2016, sequence version 1.
DT 03-AUG-2022, entry version 18.
DE RecName: Full=Glutamate 5-kinase {ECO:0000303|PubMed:29777624};
DE Short=LdG5K {ECO:0000303|PubMed:29777624};
DE EC=2.7.2.11 {ECO:0000269|PubMed:29777624};
DE AltName: Full=Gamma-glutamyl kinase {ECO:0000305};
GN Name=G5K {ECO:0000303|PubMed:29777624};
OS Leishmania donovani.
OC Eukaryota; Discoba; Euglenozoa; Kinetoplastea; Metakinetoplastina;
OC Trypanosomatida; Trypanosomatidae; Leishmaniinae; Leishmania.
OX NCBI_TaxID=5661 {ECO:0000312|EMBL:AKK31242.1};
RN [1] {ECO:0000312|EMBL:AKK31242.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MHOM/ET/67/HU3 / LV9 {ECO:0000312|EMBL:AKK31242.1};
RX PubMed=26730948; DOI=10.1371/journal.pntd.0004326;
RA Vikeved E., Backlund A., Alsmark C.;
RT "The Dynamics of Lateral Gene Transfer in Genus Leishmania - A Route for
RT Adaptation and Species Diversification.";
RL PLoS Negl. Trop. Dis. 10:E0004326-E0004326(2016).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, PATHWAY, COFACTOR, SUBUNIT, AND DEVELOPMENTAL STAGE.
RC STRAIN=MHOM/SD/62/1S-CL2D {ECO:0000303|PubMed:29777624};
RX PubMed=29777624; DOI=10.1111/febs.14511;
RA Sienkiewicz N., Ong H.B., Fairlamb A.H.;
RT "Characterisation of a putative glutamate 5-kinase from Leishmania
RT donovani.";
RL FEBS J. 285:2662-2678(2018).
CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to
CC form L-glutamate 5-phosphate (PubMed:29777624). May be important for
CC growth and survival (PubMed:29777624). {ECO:0000269|PubMed:29777624}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-glutamate = ADP + L-glutamyl 5-phosphate;
CC Xref=Rhea:RHEA:14877, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58274, ChEBI:CHEBI:456216; EC=2.7.2.11;
CC Evidence={ECO:0000269|PubMed:29777624};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14878;
CC Evidence={ECO:0000269|PubMed:29777624};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:29777624};
CC -!- ACTIVITY REGULATION: Inhibited by L-proline as part of a negative
CC feedback loop. Also inhibited by L-proline analogs 3,4-dehydro-L-
CC proline, L-azetidine-2-carboxylic acid and L-4-thiazolidine carboxylic
CC acid. {ECO:0000269|PubMed:29777624}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 mM for L-glutamate {ECO:0000269|PubMed:29777624};
CC KM=0.6 mM for ATP {ECO:0000269|PubMed:29777624};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2.
CC {ECO:0000269|PubMed:29777624}.
CC -!- SUBUNIT: Homotetramer; oligomerization is not affected by L-proline
CC feedback inhibition. {ECO:0000269|PubMed:29777624}.
CC -!- DEVELOPMENTAL STAGE: Expressed in promastigotes.
CC {ECO:0000269|PubMed:29777624}.
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family. {ECO:0000305}.
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DR EMBL; KM411797; AKK31242.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R6Y3I5; -.
DR SMR; A0A0R6Y3I5; -.
DR VEuPathDB; TriTrypDB:LdBPK_262740.1; -.
DR VEuPathDB; TriTrypDB:LdCL_260033500; -.
DR VEuPathDB; TriTrypDB:LDHU3_26.3600; -.
DR BRENDA; 2.7.2.11; 2947.
DR UniPathway; UPA00098; UER00359.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0055129; P:L-proline biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04242; AAK_G5K_ProB; 1.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00456; ProB; 1.
DR InterPro; IPR036393; AceGlu_kinase-like_sf.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR InterPro; IPR041739; G5K_ProB.
DR InterPro; IPR001057; Glu/AcGlu_kinase.
DR InterPro; IPR011529; Glu_5kinase.
DR InterPro; IPR005715; Glu_5kinase/COase_Synthase.
DR InterPro; IPR019797; Glutamate_5-kinase_CS.
DR Pfam; PF00696; AA_kinase; 1.
DR PIRSF; PIRSF000729; GK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SUPFAM; SSF53633; SSF53633; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
PE 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Kinase; Magnesium;
KW Nucleotide-binding; Proline biosynthesis; Transferase.
FT CHAIN 1..263
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000448586"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 52
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 169..170
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
FT BINDING 211..217
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:P0A7B5"
SQ SEQUENCE 263 AA; 29046 MW; 3A3AA7DF6BF35FF7 CRC64;
MADILKSVKR IVVKVGSSIL VDNQEIAAHR IEALCQFIAD LQTKYEVILV TSGAVAAGYT
KKEMDKSYVP NKQALASMGQ PLLMHMYYTE LQKHGILCAQ MLLAAYDLDS RKRTINAHNT
IEVLISHKVI PIINENDATA LEELVFGDND RLSALVAHHF KANLLVILSD IDGYYTENPR
TSTNATIRSV VHELSPDDLV AEATPNNRFA TGGIVTKLQA AQFLLERGGK MYLSSGFHLE
KARQFLLGGS HEIGTLFYSR VSS
