PROB_TREPA
ID PROB_TREPA Reviewed; 296 AA.
AC P74936;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=TP_0351;
OS Treponema pallidum (strain Nichols).
OC Bacteria; Spirochaetes; Spirochaetales; Treponemataceae; Treponema.
OX NCBI_TaxID=243276;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9522123; DOI=10.3109/10425179709020887;
RA Stamm L.V., Barnes N.Y.;
RT "Nucleotide sequences of the proA and proB genes of Treponema pallidum, the
RT syphilis agent.";
RL DNA Seq. 8:63-70(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Nichols;
RX PubMed=9665876; DOI=10.1126/science.281.5375.375;
RA Fraser C.M., Norris S.J., Weinstock G.M., White O., Sutton G.G.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Clayton R.A., Ketchum K.A.,
RA Sodergren E., Hardham J.M., McLeod M.P., Salzberg S.L., Peterson J.D.,
RA Khalak H.G., Richardson D.L., Howell J.K., Chidambaram M., Utterback T.R.,
RA McDonald L.A., Artiach P., Bowman C., Cotton M.D., Fujii C., Garland S.A.,
RA Hatch B., Horst K., Roberts K.M., Sandusky M., Weidman J.F., Smith H.O.,
RA Venter J.C.;
RT "Complete genome sequence of Treponema pallidum, the syphilis spirochete.";
RL Science 281:375-388(1998).
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; U61535; AAB39981.1; -; Genomic_DNA.
DR EMBL; AE000520; AAC65336.1; -; Genomic_DNA.
DR PIR; F71336; F71336.
DR RefSeq; WP_010881799.1; NC_021490.2.
DR AlphaFoldDB; P74936; -.
DR SMR; P74936; -.
DR IntAct; P74936; 5.
DR STRING; 243276.TPANIC_0351; -.
DR EnsemblBacteria; AAC65336; AAC65336; TP_0351.
DR KEGG; tpa:TP_0351; -.
DR eggNOG; COG0263; Bacteria.
DR HOGENOM; CLU_025400_0_2_12; -.
DR OMA; TVIHRDN; -.
DR OrthoDB; 1480250at2; -.
DR UniPathway; UPA00098; UER00359.
DR Proteomes; UP000000811; Chromosome.
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: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; 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 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Cytoplasm; Kinase;
KW Nucleotide-binding; Proline biosynthesis; Reference proteome; Transferase.
FT CHAIN 1..296
FT /note="Glutamate 5-kinase"
FT /id="PRO_0000109750"
FT BINDING 15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 55
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 159
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 206..207
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
FT BINDING 248..254
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00456"
SQ SEQUENCE 296 AA; 31315 MW; 4276927F287E4F14 CRC64;
MIRALFAAAK KIVIKIGSNT LAQADGTPDE EFLAECARAC AALMRDGKQI VVVSSGAQVA
GISALHCLSS PPQGAGLERH ESRGVIPGDG ASCKQALCAV GQAELISRWR SAFAAHQQCV
GQFLCTKEDF TDSDRAAQVR YTLSFLLERR VVPILNENDA LCCSDVPSVP ADRRVSLSPQ
KRIGDNDSLS AFVALLWQAD LLLLLSDIDG VYDKDPKAHT DAQHVPLVTD VSALVGKTSM
GSSNVFGTGG IATKLDAARL VTRAGIPLVL ANGRHLDPIL SLMRGDARGT LFVPVS
