ID PROB_BURMA Reviewed; 372 AA.
AC Q62GV5;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 60.
DE RecName: Full=Glutamate 5-kinase;
DE EC=2.7.2.11;
DE AltName: Full=Gamma-glutamyl kinase;
DE Short=GK;
GN Name=proB; OrderedLocusNames=BMA2520;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
CC -!- FUNCTION: Catalyzes the transfer of a phosphate group to glutamate
CC to form glutamate 5-phosphate which rapidly cyclizes to 5-
CC oxoproline (By similarity).
CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate = ADP + L-glutamate 5-
CC phosphate.
CC -!- PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-
CC glutamate 5-semialdehyde from L-glutamate: step 1/2.
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- SIMILARITY: Belongs to the glutamate 5-kinase family.
CC -!- SIMILARITY: Contains 1 PUA domain.
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DR EMBL; CP000010; AAU50094.1; -; Genomic_DNA.
DR RefSeq; YP_104066.1; NC_006348.1.
DR ProteinModelPortal; Q62GV5; -.
DR STRING; 243160.BMA2520; -.
DR EnsemblBacteria; AAU50094; AAU50094; BMA2520.
DR GeneID; 3089375; -.
DR KEGG; bma:BMA2520; -.
DR PATRIC; 19120191; VBIBurMal55007_2600.
DR eggNOG; COG0263; -.
DR HOGENOM; HOG000246368; -.
DR KO; K00931; -.
DR OMA; DHLQLRG; -.
DR ProtClustDB; PRK05429; -.
DR UniPathway; UPA00098; UER00359.
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:HAMAP.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0055129; P:L-proline biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.1160.10; -; 1.
DR HAMAP; MF_00456; ProB; 1; -.
DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
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_domain.
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; Aa_kinase; 1.
DR SUPFAM; SSF88697; PUA-like; 1.
DR TIGRFAMs; TIGR01027; proB; 1.
DR PROSITE; PS00902; GLUTAMATE_5_KINASE; 1.
DR PROSITE; PS50890; PUA; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW Kinase; Nucleotide-binding; Proline biosynthesis; Transferase.
FT CHAIN 1 372 Glutamate 5-kinase.
FT /FTId=PRO_0000109654.
FT DOMAIN 280 358 PUA.
FT NP_BIND 173 174 ATP (By similarity).
FT BINDING 14 14 ATP (By similarity).
FT BINDING 54 54 Substrate (By similarity).
FT BINDING 141 141 Substrate (By similarity).
FT BINDING 153 153 Substrate; via amide nitrogen (By
FT similarity).
SQ SEQUENCE 372 AA; 39233 MW; 614D38AC8CBA8C19 CRC64;
MRSIIADSKR LVVKVGSSLV TNDGRGLDHD AIGRWAAQIA ALRGAGKEVV LVSSGAIAEG
MQRLGWSKRP REIDELQAAA AVGQMGLAQV YESRFAEHGI RTAQILLTHA DLADRERYLN
ARSTLLTLLR LGVVPIINEN DTVVTDEIKF GDNDTLGALV ANLIEGDTLV ILTDQPGLFT
ADPRKDPGAT LVAEASAGAP ELEAMAGGAG SSIGRGGMLT KILAAKRAAH SGANTVIASG
RERDVLVRLA AGEAIGTQLI ARTARMAARK QWMADHLQVR GHVVIDAGAV DKLTAGGKSL
LPIGVVAVQG VFARGEVIAC VDDTGREVAR GITNYSSAET KLIQRKPSGE IETVLGYMLE
PELIHRDNLV LV
//
