ID PROB_MYCS2 Reviewed; 370 AA.
AC A0R148; I7GDU5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 1.
DT 29-MAY-2013, entry version 57.
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=MSMEG_4621, MSMEI_4505;
OS Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155).
OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC Corynebacterineae; Mycobacteriaceae; Mycobacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RA Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C.,
RA Fraser C.M.;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS], AND CLEAVAGE OF INITIATOR
RP METHIONINE.
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through
RT orthology and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
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; CP000480; ABK71775.1; -; Genomic_DNA.
DR EMBL; CP001663; AFP40959.1; -; Genomic_DNA.
DR RefSeq; YP_006569254.1; NC_018289.1.
DR RefSeq; YP_888886.1; NC_008596.1.
DR ProteinModelPortal; A0R148; -.
DR STRING; 246196.MSMEG_4621; -.
DR EnsemblBacteria; ABK71775; ABK71775; MSMEG_4621.
DR GeneID; 13429725; -.
DR GeneID; 4531097; -.
DR KEGG; msg:MSMEI_4505; -.
DR KEGG; msm:MSMEG_4621; -.
DR PATRIC; 18081557; VBIMycSme59918_4517.
DR eggNOG; COG0263; -.
DR HOGENOM; HOG000246368; -.
DR KO; K00931; -.
DR OMA; DHLQLRG; -.
DR ProtClustDB; PRK05429; -.
DR BioCyc; MSME246196:GJ4Y-4621-MONOMER; -.
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; 2.30.130.10; -; 1.
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 1: Evidence at protein level;
KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm;
KW Kinase; Nucleotide-binding; Proline biosynthesis; Reference proteome;
KW Transferase.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 370 Glutamate 5-kinase.
FT /FTId=PRO_1000081076.
FT DOMAIN 282 360 PUA.
FT NP_BIND 176 177 ATP (By similarity).
FT NP_BIND 220 226 ATP (By similarity).
FT BINDING 17 17 ATP (By similarity).
FT BINDING 57 57 Substrate (By similarity).
FT BINDING 144 144 Substrate (By similarity).
FT BINDING 156 156 Substrate; via amide nitrogen (By
FT similarity).
SQ SEQUENCE 370 AA; 38607 MW; 878693E7975F7CFB CRC64;
MSEHREAVRT ARSVVVKIGT TALTTPSGVF DANRLASLVE AIEGRMKAGS DVVIVSSGAI
AAGIEPLGLS KRPTDLATKQ AAASVGQVAL VNAWSAAFAV YNRTVGQVLL TAHDISMRVQ
HNNAQRTLDR LRALHAVAIV NENDTVATNE IRFGDNDRLS ALVAHLVGAD ALILLSDIDG
LYDGDPRKAT PDKPARFIPE VAAQGDLDGV VAGRGSSLGT GGMASKLSSA LLAADAGVPV
LLAAAADAGR ALDDASVGTV FAPRPERMSA RKFWMRYAAE SAGALTLDDG AVRAVIKQRR
SLLPAGITSV TGRFHGGDVV DLRALDGHTV ARGVVAYDQA ELASIIGRST HELPVEMRRP
AVHADDLVRT
//
