ANMK_PSEPK
ID ANMK_PSEPK Reviewed; 363 AA.
AC Q88QQ4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270};
DE EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270};
DE AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270, ECO:0000303|PubMed:23831760};
GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270, ECO:0000303|PubMed:23831760};
GN OrderedLocusNames=PP_0434;
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, 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: Catalyzes the specific phosphorylation of 1,6-anhydro-N-
CC acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the
CC 1,6-anhydro ring, generating MurNAc-6-P (By similarity). Is required
CC for the utilization of anhMurNAc either imported from the medium or
CC derived from its own cell wall murein, and thus plays a role in cell
CC wall recycling. Contributes to intrinsic fosfomycin resistance in
CC P.putida (PubMed:23831760). {ECO:0000255|HAMAP-Rule:MF_01270,
CC ECO:0000269|PubMed:23831760}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = ADP + H(+) +
CC N-acetyl-D-muramate 6-phosphate; Xref=Rhea:RHEA:24952,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58690, ChEBI:CHEBI:58722, ChEBI:CHEBI:456216;
CC EC=2.7.1.170; Evidence={ECO:0000255|HAMAP-Rule:MF_01270};
CC -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC degradation. {ECO:0000255|HAMAP-Rule:MF_01270,
CC ECO:0000269|PubMed:23831760}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_01270, ECO:0000269|PubMed:23831760}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate anhMurNAc and
CC are fosfomycin sensitive, in contrast to wild-type P.putida, which is
CC resistant to fosfomycin. {ECO:0000269|PubMed:23831760}.
CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01270}.
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; AE015451; AAN66064.1; -; Genomic_DNA.
DR RefSeq; NP_742600.1; NC_002947.4.
DR RefSeq; WP_010951767.1; NC_002947.4.
DR AlphaFoldDB; Q88QQ4; -.
DR SMR; Q88QQ4; -.
DR STRING; 160488.PP_0434; -.
DR PRIDE; Q88QQ4; -.
DR EnsemblBacteria; AAN66064; AAN66064; PP_0434.
DR KEGG; ppu:PP_0434; -.
DR PATRIC; fig|160488.4.peg.465; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_0_0_6; -.
DR OMA; GQTIRHE; -.
DR PhylomeDB; Q88QQ4; -.
DR BioCyc; PPUT160488:G1G01-470-MON; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:UniProtKB-UniRule.
DR GO; GO:0097175; P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006040; P:amino sugar metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0046677; P:response to antibiotic; IEA:UniProtKB-KW.
DR HAMAP; MF_01270; AnhMurNAc_kinase; 1.
DR InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR30605; PTHR30605; 1.
DR Pfam; PF03702; AnmK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
PE 3: Inferred from homology;
KW Antibiotic resistance; ATP-binding; Carbohydrate metabolism; Kinase;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..363
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250031"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ SEQUENCE 363 AA; 38236 MW; 50DD8C264FB7BC29 CRC64;
MALYLGVMSG TSLDGLDIAL VEQGEQLELL ATHYLPMPPD LRQDLLALCS SGPDEIARAA
LAENRWASLA GEGIRQLLAR QGLKPEAVRA IGSHGQTIRH EPARGFTVQI GNPALLAELT
GISVVADFRR RDVAAGGQGA PLVPAFHETL FSQLGRRLAI LNVGGFSNLS LIEQDKPVHG
FDCGPGNVLL DAWIEREHGH PYDADGAWAA SGVAQPGLLS ALMADPFFAG SGPKSTGREV
FNLPWLDRHL ANLPAYRAQD VQATLLELTA RSIIDSLGKA QQGTEALLVC GGGARNGALM
ARLGQLLPAA RVASTGAYGV DPDWVEAMAF AWLAHCCLEG IAANRPSVTA AKGLRVLGAI
YPA
