GLKIN_CAMJE
ID GLKIN_CAMJE Reviewed; 779 AA.
AC Q0P8J6;
DT 10-OCT-2018, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=L-glutamine kinase {ECO:0000303|PubMed:28650156, ECO:0000303|PubMed:30142271};
DE EC=2.7.3.13 {ECO:0000269|PubMed:28650156, ECO:0000269|PubMed:30142271};
GN OrderedLocusNames=Cj1418c {ECO:0000312|EMBL:CAL35527.1};
OS Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC
OS 11168).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Campylobacteraceae; Campylobacter.
OX NCBI_TaxID=192222;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=10688204; DOI=10.1038/35001088;
RA Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M.,
RA Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S.,
RA Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A.,
RA Rajandream M.A., Rutherford K.M., van Vliet A.H.M., Whitehead S.,
RA Barrell B.G.;
RT "The genome sequence of the food-borne pathogen Campylobacter jejuni
RT reveals hypervariable sequences.";
RL Nature 403:665-668(2000).
RN [2]
RP FUNCTION IN CAPSULE BIOSYNTHESIS, PATHWAY, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 700819 / NCTC 11168;
RX PubMed=17675288; DOI=10.1074/jbc.m704413200;
RA McNally D.J., Lamoureux M.P., Karlyshev A.V., Fiori L.M., Li J.,
RA Thacker G., Coleman R.A., Khieu N.H., Wren B.W., Brisson J.R.,
RA Jarrell H.C., Szymanski C.M.;
RT "Commonality and biosynthesis of the O-methyl phosphoramidate capsule
RT modification in Campylobacter jejuni.";
RL J. Biol. Chem. 282:28566-28576(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=28650156; DOI=10.1021/jacs.7b04824;
RA Taylor Z.W., Brown H.A., Narindoshvili T., Wenzel C.Q., Szymanski C.M.,
RA Holden H.M., Raushel F.M.;
RT "Discovery of a glutamine kinase required for the biosynthesis of the O-
RT methyl phosphoramidate modifications found in the capsular polysaccharides
RT of Campylobacter jejuni.";
RL J. Am. Chem. Soc. 139:9463-9466(2017).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, DOMAIN, REACTION MECHANISM, ACTIVE SITE, AND MUTAGENESIS OF
RP HIS-737.
RC STRAIN=ATCC 700819 / NCTC 11168 {ECO:0000303|PubMed:30142271};
RX PubMed=30142271; DOI=10.1021/acs.biochem.8b00811;
RA Taylor Z.W., Chamberlain A.R., Raushel F.M.;
RT "Substrate Specificity and Chemical Mechanism for the Reaction Catalyzed by
RT Glutamine Kinase.";
RL Biochemistry 57:5447-5455(2018).
CC -!- FUNCTION: Involved in the biosynthesis of the O-methyl phosphoramidate
CC (MeOPN) group found on the capsular polysaccharide (CPS) of C.jejuni
CC (PubMed:17675288). Catalyzes the ATP-dependent phosphorylation of the
CC amide nitrogen of L-glutamine to form L-glutamine phosphate, the first
CC committed step in MeOPN biosynthesis (PubMed:28650156,
CC PubMed:30142271). Catalyzes also the phosphorylation of D-glutamine,
CC gamma-L-glutamyl hydroxamate, gamma-L-glutamyl-hydrazide and beta-L-
CC aspartyl hydroxamate (PubMed:30142271). Does not phosphorylate L-
CC glutamate or L-asparagine (PubMed:28650156, PubMed:30142271). Does not
CC act on L-glutamine derivatives with removed alpha-amino or alpha-
CC carboxy groups (PubMed:30142271). {ECO:0000269|PubMed:17675288,
CC ECO:0000269|PubMed:28650156, ECO:0000269|PubMed:30142271}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O + L-glutamine = AMP + 2 H(+) + N(5)-phospho-L-
CC glutamine + phosphate; Xref=Rhea:RHEA:55580, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58359, ChEBI:CHEBI:139073, ChEBI:CHEBI:456215;
CC EC=2.7.3.13; Evidence={ECO:0000269|PubMed:28650156,
CC ECO:0000269|PubMed:30142271};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=640 uM for L-glutamine (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:28650156, ECO:0000269|PubMed:30142271};
CC KM=340 uM for ATP {ECO:0000269|PubMed:28650156};
CC KM=10.5 mM for D-glutamine (at pH 8.0 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:30142271};
CC KM=1.5 mM for gamma-L-glutamyl hydroxamate (at pH 8.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:30142271};
CC KM=17.2 mM for gamma-L-glutamyl-hydrazide (at pH 8.0 and 25 degrees
CC Celsius) {ECO:0000269|PubMed:30142271};
CC Note=kcat is 2.5 sec(-1) with L-glutamine as substrate
CC (PubMed:28650156, PubMed:30142271). kcat is 1.5 sec(-1) with D-
CC glutamine as substrate. kcat is 2.1 sec(-1) with gamma-L-glutamyl
CC hydroxamate as substrate. kcat is 0.41 sec(-1) with gamma-L-glutamyl-
CC hydrazide as substrate (PubMed:30142271).
CC {ECO:0000269|PubMed:28650156, ECO:0000269|PubMed:30142271};
CC -!- PATHWAY: Capsule biogenesis; capsule polysaccharide biosynthesis.
CC {ECO:0000269|PubMed:17675288}.
CC -!- DOMAIN: Contains an N-terminal ATP-grasp domain, a specialized central
CC substrate-binding domain for L-glutamine and a C-terminal phospho-
CC histidine domain. {ECO:0000305|PubMed:30142271}.
CC -!- DISRUPTION PHENOTYPE: Mutant does not express the MeOPN CPS
CC modification. {ECO:0000269|PubMed:17675288}.
CC -!- MISCELLANEOUS: The reaction mechanism comprises three steps. First, a
CC histidine residue of the enzyme attacks ATP at the beta-phosphoryl
CC group to form AMP and a pyrophosphorylated enzyme intermediate. Next,
CC the pyrophosphorylated enzyme intermediate is hydrolyzed to generate
CC inorganic phosphate and a phosphorylated enzyme intermediate. Finally,
CC the phosphorylated enzyme intermediate transfers the phosphate to the
CC amide nitrogen of the acceptor substrate L-glutamine. In this
CC mechanism, the gamma-phosphoryl group of ATP is converted to phosphate
CC and the beta-phosphoryl group is utilized in the phosphorylation of L-
CC glutamine. {ECO:0000269|PubMed:30142271}.
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DR EMBL; AL111168; CAL35527.1; -; Genomic_DNA.
DR PIR; B81287; B81287.
DR RefSeq; WP_010891934.1; NC_002163.1.
DR RefSeq; YP_002344801.1; NC_002163.1.
DR AlphaFoldDB; Q0P8J6; -.
DR SMR; Q0P8J6; -.
DR IntAct; Q0P8J6; 1.
DR STRING; 192222.Cj1418c; -.
DR PaxDb; Q0P8J6; -.
DR PRIDE; Q0P8J6; -.
DR EnsemblBacteria; CAL35527; CAL35527; Cj1418c.
DR GeneID; 905707; -.
DR KEGG; cje:Cj1418c; -.
DR PATRIC; fig|192222.6.peg.1399; -.
DR eggNOG; COG0574; Bacteria.
DR eggNOG; COG3848; Bacteria.
DR HOGENOM; CLU_011659_0_0_7; -.
DR OMA; HDKVEFE; -.
DR BRENDA; 2.7.3.13; 1087.
DR SABIO-RK; Q0P8J6; -.
DR UniPathway; UPA00934; -.
DR Proteomes; UP000000799; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016775; F:phosphotransferase activity, nitrogenous group as acceptor; IDA:UniProtKB.
DR GO; GO:0045227; P:capsule polysaccharide biosynthetic process; IDA:UniProtKB.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR008279; PEP-util_enz_mobile_dom.
DR InterPro; IPR036637; Phosphohistidine_dom_sf.
DR InterPro; IPR002192; PPDK_AMP/ATP-bd.
DR Pfam; PF00391; PEP-utilizers; 1.
DR Pfam; PF01326; PPDK_N; 1.
DR SUPFAM; SSF52009; SSF52009; 1.
PE 1: Evidence at protein level;
KW Capsule biogenesis/degradation; Kinase; Reference proteome; Transferase.
FT CHAIN 1..779
FT /note="L-glutamine kinase"
FT /id="PRO_0000445428"
FT ACT_SITE 737
FT /note="Nucleophile"
FT /evidence="ECO:0000269|PubMed:30142271"
FT MUTAGEN 737
FT /note="H->N: Loss of activity."
FT /evidence="ECO:0000269|PubMed:30142271"
SQ SEQUENCE 779 AA; 90325 MW; 8161396E368D1109 CRC64;
MAELKFKTKA QNLKNLQTKL KKAKVLPLVL TSLEELISNE DKVLQDIQTL KANRLIIRSS
SLSEDSMKNS NAGAFLSLAN IKADSKDELL KALYEVANSM PSKSDEILVQ PMLENITLCG
VGFSVDKDNF SPYFCLQYDE NGSNSSITDG SSKSAKTYYH YRNYLEFKDI RLQKIIELIK
ELEVLYDCHF LDVEFAFAIQ DDKEELFCLQ VRPLVMHEKN NLFHSLPKEA LYRFYKRFES
LKESRSRVLG DKAIFGVMPD WNPAEIIGLR PKRLAFSLYK EIITDNIWAY QRDNYGYRDL
RSHPLIHSFL GIPYVDVRLS FNSFIPKKLD ENIAQKLVNF YLDKLNKNHE LHDKIEFNIV
YSCYDFNSSK KLEELLNHGF NENEIKRLEF SLLELTNKII NPRSGFYLKD IQKAYKLKER
YDGIINSNFS LIDKIYWLIE ECKRYGTLPF AGVARAAFVA MQLLNSLVEI DFITKEEKDD
FLNSLNTVSK NLSKQTNHLN FHNKDQFLKD FGHLRAGTYN ILSPRYDEDF ELYFDADQKD
SKVYLQDKAF VFSKEKTRAL NALLKEHGLE INACEFFDFL KQAIEGRELV KFEFTRLLSK
AIVYIEELGK YYDIEKEDLA HLDIKSILNL YSSLYSINPK EQFIEEINRN KKEYELTQAI
KLPSLLCNAD EIFSFYNHSI IPNFITQKSI TAFTAKENDK DLEGKIVLIY AADPGYDYLF
TKNIAGLITC YGGANSHMAI RASELGMPAV IGVGEENFEK YLKAKKINIE CESEQIFCL
