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N-acetylmuramic acid/N-acetylglucosamine kinase (MurNAc/GlcNAc kinase) (EC 2.7.1.-) (EC 2.7.1.59) (Murein sugar kinase)

 MURK_CLOAB              Reviewed;         306 AA.
Q97ML3;
06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 1.
05-DEC-2018, entry version 75.
RecName: Full=N-acetylmuramic acid/N-acetylglucosamine kinase {ECO:0000303|PubMed:21784936};
Short=MurNAc/GlcNAc kinase {ECO:0000303|PubMed:21784936};
EC=2.7.1.- {ECO:0000269|PubMed:21784936};
EC=2.7.1.59 {ECO:0000269|PubMed:21784936};
AltName: Full=Murein sugar kinase {ECO:0000303|PubMed:21784936};
Name=murK {ECO:0000303|PubMed:21784936};
OrderedLocusNames=CA_C0183 {ECO:0000312|EMBL:AAK78165.1};
Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG
5710 / VKM B-1787).
Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
Clostridium.
NCBI_TaxID=272562;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=11466286; DOI=10.1128/JB.183.16.4823-4838.2001;
Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q.,
Gibson R., Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I.,
Tatusov R.L., Sabathe F., Doucette-Stamm L.A., Soucaille P.,
Daly M.J., Bennett G.N., Koonin E.V., Smith D.R.;
"Genome sequence and comparative analysis of the solvent-producing
bacterium Clostridium acetobutylicum.";
J. Bacteriol. 183:4823-4838(2001).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND PATHWAY.
STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
PubMed=21784936; DOI=10.1128/JB.05514-11;
Reith J., Berking A., Mayer C.;
"Characterization of an N-acetylmuramic acid/N-acetylglucosamine
kinase of Clostridium acetobutylicum.";
J. Bacteriol. 193:5386-5392(2011).
-!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of both cell
wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc)
and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. Neither
the non-N-acetylated forms of the cell wall sugars, i.e.,
glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-
anhydro-MurNAc are substrates for the enzyme. May have a role in
the rescue of the murein sugars GlcNAc and MurNAc released from
muropeptides during cell wall turnover in C.acetobutylicum.
{ECO:0000269|PubMed:21784936}.
-!- CATALYTIC ACTIVITY:
Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-
glucosamine 6-phosphate; Xref=Rhea:RHEA:17417,
ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57513,
ChEBI:CHEBI:456216, ChEBI:CHEBI:506227; EC=2.7.1.59;
Evidence={ECO:0000269|PubMed:21784936};
-!- CATALYTIC ACTIVITY:
Reaction=ATP + N-acetyl-D-muramate = ADP + H(+) + N-acetyl-D-
muramate 6-phosphate; Xref=Rhea:RHEA:51500, ChEBI:CHEBI:15378,
ChEBI:CHEBI:28881, ChEBI:CHEBI:30616, ChEBI:CHEBI:58722,
ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:21784936};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:21784936};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=190.2 uM for N-acetylmuramate {ECO:0000269|PubMed:21784936};
KM=127.4 uM for N-acetyl-D-glucosamine
{ECO:0000269|PubMed:21784936};
KM=241.8 uM for ATP {ECO:0000269|PubMed:21784936};
Vmax=113.6 umol/min/mg enzyme with GlcNAc as substrate
{ECO:0000269|PubMed:21784936};
Vmax=74.8 umol/min/mg enzyme with MurNAc as substrate
{ECO:0000269|PubMed:21784936};
Note=kcat is 65.0 sec(-1) with GlcNAc as substrate. kcat is 42.8
sec(-1) with MurNAc as substrate. {ECO:0000269|PubMed:21784936};
pH dependence:
Optimum pH is 7.5 to 9.0. Retains half maximal activity at about
pH 6.5 and 10.5 and is inactive at pH 5 and below.
{ECO:0000269|PubMed:21784936};
-!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
{ECO:0000305|PubMed:21784936}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21784936}.
-!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine
kinase family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AE001437; AAK78165.1; -; Genomic_DNA.
PIR; B96922; B96922.
RefSeq; NP_346825.1; NC_003030.1.
RefSeq; WP_010963507.1; NC_003030.1.
ProteinModelPortal; Q97ML3; -.
SMR; Q97ML3; -.
STRING; 272562.CA_C0183; -.
EnsemblBacteria; AAK78165; AAK78165; CA_C0183.
GeneID; 1116366; -.
KEGG; cac:CA_C0183; -.
PATRIC; fig|272562.8.peg.369; -.
eggNOG; ENOG4105RD7; Bacteria.
eggNOG; COG2971; LUCA.
HOGENOM; HOG000248371; -.
OMA; PISDQGG; -.
UniPathway; UPA00544; -.
Proteomes; UP000000814; Chromosome.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0019200; F:carbohydrate kinase activity; IDA:UniProtKB.
GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:UniProtKB.
GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
GO; GO:0097172; P:N-acetylmuramic acid metabolic process; IDA:UniProtKB.
GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
InterPro; IPR002731; ATPase_BadF.
Pfam; PF01869; BcrAD_BadFG; 1.
1: Evidence at protein level;
ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding;
Reference proteome; Transferase.
CHAIN 1 306 N-acetylmuramic acid/N-acetylglucosamine
kinase.
/FTId=PRO_0000436514.
REGION 142 144 Substrate binding.
{ECO:0000250|UniProtKB:Q9UJ70}.
BINDING 12 12 ATP; via amide nitrogen.
{ECO:0000250|UniProtKB:Q9UJ70}.
BINDING 35 35 Substrate.
{ECO:0000250|UniProtKB:Q9UJ70}.
BINDING 124 124 ATP. {ECO:0000250|UniProtKB:Q9UJ70}.
BINDING 149 149 Substrate.
{ECO:0000250|UniProtKB:Q9UJ70}.
BINDING 208 208 ATP; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q9UJ70}.
SEQUENCE 306 AA; 33425 MW; 33EE5234E0F84778 CRC64;
MKYVIGIDGG GSKTHMKIST LDYKVLLEVF KGPSNINSST KEEVKRVLQE LIMEGLGKLG
QSLEECSAIC IGTAGADRTE DKSIIEDMIR SLGYMGKIIV VNDAEIALAG GIEKREGIIV
ISGTGSICYG RNKEGRSARS GGWGHIIGDE GSGYDIGIKA IKAALKSFDK RGEKTILEGD
ILDFLKLKSH EDLINYIYRS GVTKKEIASL TRVVNSAYIK GDLVSKRILK EAARELFLSV
KAVVEVLSMQ NKKVVLTTAG GVINNINYLY DEFRKFLNLN YPKVKIISMK NDSAFGAVII
ARSECD


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