AMGK_PSEPK
ID AMGK_PSEPK Reviewed; 339 AA.
AC Q88QT3;
DT 30-AUG-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=N-acetylmuramate/N-acetylglucosamine kinase {ECO:0000305|PubMed:23831760};
DE Short=MurNAc/GlcNAc kinase {ECO:0000305|PubMed:23831760};
DE EC=2.7.1.221 {ECO:0000269|PubMed:23831760};
DE AltName: Full=Anomeric sugar kinase {ECO:0000303|PubMed:23831760};
GN Name=amgK {ECO:0000303|PubMed:23831760};
GN OrderedLocusNames=PP_0405 {ECO:0000312|EMBL:AAN66035.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBSTRATE
RP SPECIFICITY, DISRUPTION PHENOTYPE, AND PATHWAY.
RX PubMed=23831760; DOI=10.1038/nchembio.1289;
RA Gisin J., Schneider A., Naegele B., Borisova M., Mayer C.;
RT "A cell wall recycling shortcut that bypasses peptidoglycan de novo
RT biosynthesis.";
RL Nat. Chem. Biol. 9:491-493(2013).
CC -!- FUNCTION: Sugar kinase that catalyzes the ATP-dependent phosphorylation
CC of N-acetylmuramate (MurNAc) and N-acetylglucosamine (GlcNAc) at its C1
CC hydroxyl group, leading to MurNAc alpha-1P and GlcNAc alpha-1P,
CC respectively. Is involved in peptidoglycan recycling as part of a cell
CC wall recycling pathway that bypasses de novo biosynthesis of the
CC peptidoglycan precursor UDP-MurNAc. Plays a role in intrinsic
CC resistance to fosfomycin, which targets the de novo synthesis of UDP-
CC MurNAc. Is also able to use N-acetylgalactosamine (GalNAc) as a
CC substrate, but not N-acetylmannosamine, N-deacetylated sugars or
CC glucose. {ECO:0000269|PubMed:23831760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-muramate = ADP + H(+) + N-acetyl-alpha-D-
CC muramate 1-phosphate; Xref=Rhea:RHEA:53720, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28881, ChEBI:CHEBI:30616, ChEBI:CHEBI:137594,
CC ChEBI:CHEBI:456216; EC=2.7.1.221;
CC Evidence={ECO:0000269|PubMed:23831760};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-alpha-D-
CC glucosamine 1-phosphate; Xref=Rhea:RHEA:53724, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57776, ChEBI:CHEBI:456216,
CC ChEBI:CHEBI:506227; Evidence={ECO:0000269|PubMed:23831760};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=80.5 uM for MurNAc (at pH 7.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23831760};
CC KM=176.6 uM for GlcNAc(at pH 7.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23831760};
CC KM=50.8 uM for ATP(at pH 7.6 and 25 degrees Celsius)
CC {ECO:0000269|PubMed:23831760};
CC Note=kcat is 5.15 sec(-1) for MurNAc phosphorylation. kcat is 6.64
CC sec(-1) for GlcNAc phosphorylation (at pH 7.6 and 25 degrees
CC Celsius). {ECO:0000269|PubMed:23831760};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000269|PubMed:23831760}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate GlcNAc and
CC MurNAc. Deletion of this gene increases fosfomycin sensitivity.
CC {ECO:0000269|PubMed:23831760}.
CC -!- SIMILARITY: Belongs to the kinase AmgK family. {ECO:0000305}.
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DR EMBL; AE015451; AAN66035.1; -; Genomic_DNA.
DR RefSeq; NP_742571.1; NC_002947.4.
DR RefSeq; WP_010951744.1; NC_002947.4.
DR AlphaFoldDB; Q88QT3; -.
DR SMR; Q88QT3; -.
DR STRING; 160488.PP_0405; -.
DR DNASU; 1044120; -.
DR EnsemblBacteria; AAN66035; AAN66035; PP_0405.
DR KEGG; ppu:PP_0405; -.
DR PATRIC; fig|160488.4.peg.437; -.
DR eggNOG; COG3178; Bacteria.
DR HOGENOM; CLU_021467_1_0_6; -.
DR OMA; HSRNLMV; -.
DR PhylomeDB; Q88QT3; -.
DR BioCyc; MetaCyc:G1G01-442-MON; -.
DR BioCyc; PPUT160488:G1G01-442-MON; -.
DR BRENDA; 2.7.1.221; 5092.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0019200; F:carbohydrate kinase activity; IDA:UniProtKB.
DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR GO; GO:0097172; P:N-acetylmuramic acid metabolic process; IDA:UniProtKB.
DR GO; GO:0009252; P:peptidoglycan biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IMP:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Antibiotic resistance; ATP-binding; Carbohydrate metabolism; Cell shape;
KW Cell wall biogenesis/degradation; Kinase; Nucleotide-binding;
KW Peptidoglycan synthesis; Reference proteome; Transferase.
FT CHAIN 1..339
FT /note="N-acetylmuramate/N-acetylglucosamine kinase"
FT /id="PRO_0000441265"
SQ SEQUENCE 339 AA; 38238 MW; 155738D17E4548FD CRC64;
MPEHDVRLQQ LTVWLDEQLN DLFRDNAWGE VPAGSLTAAS SDASFRRYFR WQGAGHSFVI
MDAPPPQENC RPFVAIDHLL ASADVHVPLI HAQDLERGFL LLGDLGTQTY LDIINADNAD
GLFADAIDAL LKFQRLPMDA PLPSYDDALL RREVELFPEW YVGRELGLTF TDAQKATWQR
VSQLLIDSAL AQPKVLVHRD YMPRNLMQST PNPGVLDFQD AVYGPVTYDI TCLFKDAFVS
WPQARVEGWL GDYWQQAQAA GIPVHAEFEA FHRASDLMGV QRHLKVIGIF ARICHRDGKP
RYLGDVPRFF AYINEVIGRR PELAELGELI AELQAGARA
