PROB_BURTA
ID PROB_BURTA Reviewed; 372 AA.
AC Q2SZF9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 24-JAN-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Glutamate 5-kinase {ECO:0000255|HAMAP-Rule:MF_00456};
DE EC=2.7.2.11 {ECO:0000255|HAMAP-Rule:MF_00456};
DE AltName: Full=Gamma-glutamyl kinase {ECO:0000255|HAMAP-Rule:MF_00456};
DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00456};
GN Name=proB {ECO:0000255|HAMAP-Rule:MF_00456}; OrderedLocusNames=BTH_I1143;
OS Burkholderia thailandensis (strain ATCC 700388 / DSM 13276 / CIP 106301 /
OS E264).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=271848;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700388 / DSM 13276 / CIP 106301 / E264;
RX PubMed=16336651; DOI=10.1186/1471-2164-6-174;
RA Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C.,
RA DeShazer D.;
RT "Bacterial genome adaptation to niches: divergence of the potential
RT virulence genes in three Burkholderia species of different survival
RT strategies.";
RL BMC Genomics 6:174-174(2005).
CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate to
CC form L-glutamate 5-phosphate. {ECO:0000255|HAMAP-Rule:MF_00456}.
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:0000255|HAMAP-Rule:MF_00456};
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate
CC 5-semialdehyde from L-glutamate: step 1/2. {ECO:0000255|HAMAP-
CC Rule:MF_00456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00456}.
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_00456}.
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DR EMBL; CP000086; ABC38938.1; -; Genomic_DNA.
DR RefSeq; WP_009888926.1; NZ_CP008785.1.
DR PDB; 4Q1T; X-ray; 2.15 A; A/B/C/D=1-372.
DR PDBsum; 4Q1T; -.
DR AlphaFoldDB; Q2SZF9; -.
DR SMR; Q2SZF9; -.
DR PRIDE; Q2SZF9; -.
DR EnsemblBacteria; ABC38938; ABC38938; BTH_I1143.
DR GeneID; 66548400; -.
DR KEGG; bte:BTH_I1143; -.
DR HOGENOM; CLU_025400_2_0_4; -.
DR OMA; TVIHRDN; -.
DR OrthoDB; 1480250at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000001930; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004349; F:glutamate 5-kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd04242; AAK_G5K_ProB; 1.
DR Gene3D; 2.30.130.10; -; 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 InterPro; IPR002478; PUA.
DR InterPro; IPR015947; PUA-like_sf.
DR InterPro; IPR036974; PUA_sf.
DR Pfam; PF00696; AA_kinase; 1.
DR Pfam; PF01472; PUA; 1.
DR PIRSF; PIRSF000729; GK; 1.
DR PRINTS; PR00474; GLU5KINASE.
DR SMART; SM00359; PUA; 1.
DR SUPFAM; SSF53633; SSF53633; 1.
DR SUPFAM; SSF88697; SSF88697; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS50890; PUA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Proline biosynthesis; Transferase.
FT CHAIN 1..372
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000252973"
FT DOMAIN 280..358
FT /note="PUA"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 54
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 141
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 173..174
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT HELIX 4..7
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 9..15
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 17..20
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 29..44
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 56..64
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:4Q1T"
FT TURN 97..99
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 102..107
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 109..113
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 115..130
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 134..139
FT /evidence="ECO:0007829|PDB:4Q1T"
FT TURN 141..143
FT /evidence="ECO:0007829|PDB:4Q1T"
FT TURN 146..148
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 167..175
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 219..229
FT /evidence="ECO:0007829|PDB:4Q1T"
FT TURN 230..232
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 256..260
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 265..276
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 277..285
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 287..294
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 305..310
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 317..321
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 327..332
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 337..343
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 351..355
FT /evidence="ECO:0007829|PDB:4Q1T"
FT HELIX 366..368
FT /evidence="ECO:0007829|PDB:4Q1T"
FT STRAND 369..371
FT /evidence="ECO:0007829|PDB:4Q1T"
SQ SEQUENCE 372 AA; 39330 MW; 777EE3DFCF77C4A6 CRC64;
MRSIIADSKR LVVKVGSSLV TNDGRGLDHD AIGRWAAQIA ALRNEGKEVV LVSSGAIAEG
MQRLGWSRRP REIDELQAAA AVGQMGLAQV YESRFAEHGI RTAQILLTHA DLADRERYLN
ARSTLLTLLR LGVVPIINEN DTVVTDEIKF GDNDTLGALV ANLIEGDALI ILTDQQGLFT
ADPRKDPGAT LVAEASAGAP ELEAMAGGAG SSIGRGGMLT KILAAKRAAH SGANTVIASG
RERDVLLRLA SGEAIGTQLI ARTARMAARK QWMADHLQVR GHVVIDAGAV DKLTAGGKSL
LPIGVVAVQG VFARGEVIAC VNDAGREVAR GITNYSSAEA KLIQRKPSGE IEAVLGYMLE
PELIHRDNLV LV
