MURK_CLOAB
ID MURK_CLOAB Reviewed; 306 AA.
AC Q97ML3;
DT 06-JUL-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=N-acetylmuramic acid/N-acetylglucosamine kinase {ECO:0000303|PubMed:21784936};
DE Short=MurNAc/GlcNAc kinase {ECO:0000303|PubMed:21784936};
DE EC=2.7.1.- {ECO:0000269|PubMed:21784936};
DE EC=2.7.1.59 {ECO:0000269|PubMed:21784936};
DE AltName: Full=Murein sugar kinase {ECO:0000303|PubMed:21784936};
GN Name=murK {ECO:0000303|PubMed:21784936};
GN OrderedLocusNames=CA_C0183 {ECO:0000312|EMBL:AAK78165.1};
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND PATHWAY.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=21784936; DOI=10.1128/jb.05514-11;
RA Reith J., Berking A., Mayer C.;
RT "Characterization of an N-acetylmuramic acid/N-acetylglucosamine kinase of
RT Clostridium acetobutylicum.";
RL J. Bacteriol. 193:5386-5392(2011).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of both cell wall
CC (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-
CC acetylglucosamine (GlcNAc), at the 6-hydroxyl group. Neither the non-N-
CC acetylated forms of the cell wall sugars, i.e., glucosamine and/or
CC muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates
CC for the enzyme. May have a role in the rescue of the murein sugars
CC GlcNAc and MurNAc released from muropeptides during cell wall turnover
CC in C.acetobutylicum. {ECO:0000269|PubMed:21784936}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:17417, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57513, ChEBI:CHEBI:456216,
CC ChEBI:CHEBI:506227; EC=2.7.1.59;
CC Evidence={ECO:0000269|PubMed:21784936};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-muramate = ADP + H(+) + N-acetyl-D-muramate
CC 6-phosphate; Xref=Rhea:RHEA:51500, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28881, ChEBI:CHEBI:30616, ChEBI:CHEBI:58722,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:21784936};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:21784936};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=190.2 uM for N-acetylmuramate {ECO:0000269|PubMed:21784936};
CC KM=127.4 uM for N-acetyl-D-glucosamine {ECO:0000269|PubMed:21784936};
CC KM=241.8 uM for ATP {ECO:0000269|PubMed:21784936};
CC Vmax=113.6 umol/min/mg enzyme with GlcNAc as substrate
CC {ECO:0000269|PubMed:21784936};
CC Vmax=74.8 umol/min/mg enzyme with MurNAc as substrate
CC {ECO:0000269|PubMed:21784936};
CC Note=kcat is 65.0 sec(-1) with GlcNAc as substrate. kcat is 42.8
CC sec(-1) with MurNAc as substrate. {ECO:0000269|PubMed:21784936};
CC pH dependence:
CC Optimum pH is 7.5 to 9.0. Retains half maximal activity at about pH
CC 6.5 and 10.5 and is inactive at pH 5 and below.
CC {ECO:0000269|PubMed:21784936};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000305|PubMed:21784936}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:21784936}.
CC -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE001437; AAK78165.1; -; Genomic_DNA.
DR PIR; B96922; B96922.
DR RefSeq; NP_346825.1; NC_003030.1.
DR RefSeq; WP_010963507.1; NC_003030.1.
DR AlphaFoldDB; Q97ML3; -.
DR SMR; Q97ML3; -.
DR STRING; 272562.CA_C0183; -.
DR PRIDE; Q97ML3; -.
DR EnsemblBacteria; AAK78165; AAK78165; CA_C0183.
DR GeneID; 44996675; -.
DR KEGG; cac:CA_C0183; -.
DR PATRIC; fig|272562.8.peg.369; -.
DR eggNOG; COG2971; Bacteria.
DR HOGENOM; CLU_016274_1_1_9; -.
DR OMA; DTMGSMF; -.
DR OrthoDB; 1589192at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000814; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019200; F:carbohydrate kinase activity; IDA:UniProtKB.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:UniProtKB.
DR GO; GO:0046835; P:carbohydrate phosphorylation; IDA:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:0097172; P:N-acetylmuramic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR InterPro; IPR002731; ATPase_BadF.
DR InterPro; IPR043129; ATPase_NBD.
DR Pfam; PF01869; BcrAD_BadFG; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
PE 1: Evidence at protein level;
KW ATP-binding; Cytoplasm; Kinase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..306
FT /note="N-acetylmuramic acid/N-acetylglucosamine kinase"
FT /id="PRO_0000436514"
FT BINDING 12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 35
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 124
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 142..144
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 149
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT BINDING 208
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:Q9UJ70"
SQ 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
