ID   ANMK_ECOLI              Reviewed;         369 AA.
AC   P77570;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 134.
DE   RecName: Full=Anhydro-N-acetylmuramic acid kinase;
DE            EC=2.7.1.170;
DE   AltName: Full=AnhMurNAc kinase;
GN   Name=anmK; Synonyms=ydhH; OrderedLocusNames=b1640, JW1632;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA   Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA   Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA   Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA   Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA   Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA   Wada C., Yamamoto Y., Horiuchi T.;
RT   "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT   the 28.0-40.1 min region on the linkage map.";
RL   DNA Res. 3:363-377(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, IDENTIFICATION BY MASS SPECTROMETRY, ACTIVITY
RP   REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=15901686; DOI=10.1128/jb.187.11.3643-3649.2005;
RA   Uehara T., Suefuji K., Valbuena N., Meehan B., Donegan M., Park J.T.;
RT   "Recycling of the anhydro-N-acetylmuramic acid derived from cell wall
RT   murein involves a two-step conversion to N-acetylglucosamine-phosphate.";
RL   J. Bacteriol. 187:3643-3649(2005).
RN   [5]
RP   FUNCTION.
RX   PubMed=16452451; DOI=10.1128/jb.188.4.1660-1662.2006;
RA   Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T.;
RT   "MurQ etherase is required by Escherichia coli in order to metabolize
RT   anhydro-N-acetylmuramic acid obtained either from the environment or from
RT   its own cell wall.";
RL   J. Bacteriol. 188:1660-1662(2006).
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. Is required for the
CC       utilization of anhMurNAc either imported from the medium or derived
CC       from its own cell wall murein, and thus plays a role in cell wall
CC       recycling. {ECO:0000269|PubMed:15901686, ECO:0000269|PubMed:16452451}.
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:0000269|PubMed:15901686};
CC   -!- ACTIVITY REGULATION: Strongly inhibited by ADP.
CC       {ECO:0000269|PubMed:15901686}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=1 mM for anhMurNAc {ECO:0000269|PubMed:15901686};
CC         KM=1 mM for ATP {ECO:0000269|PubMed:15901686};
CC         Vmax=180 umol/min/mg enzyme {ECO:0000269|PubMed:15901686};
CC       pH dependence:
CC         Optimum pH is 10-11. Inactive at pH 4.5.
CC         {ECO:0000269|PubMed:15901686};
CC   -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC       degradation.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC   -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC       {ECO:0000305}.
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DR   EMBL; U00096; AAC74712.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAA15401.1; -; Genomic_DNA.
DR   PIR; B64921; B64921.
DR   RefSeq; NP_416157.1; NC_000913.3.
DR   RefSeq; WP_000835039.1; NZ_LN832404.1.
DR   AlphaFoldDB; P77570; -.
DR   SMR; P77570; -.
DR   BioGRID; 4263491; 14.
DR   IntAct; P77570; 7.
DR   STRING; 511145.b1640; -.
DR   jPOST; P77570; -.
DR   PaxDb; P77570; -.
DR   PRIDE; P77570; -.
DR   EnsemblBacteria; AAC74712; AAC74712; b1640.
DR   EnsemblBacteria; BAA15401; BAA15401; BAA15401.
DR   GeneID; 946810; -.
DR   KEGG; ecj:JW1632; -.
DR   KEGG; eco:b1640; -.
DR   PATRIC; fig|1411691.4.peg.620; -.
DR   EchoBASE; EB3700; -.
DR   eggNOG; COG2377; Bacteria.
DR   HOGENOM; CLU_038782_0_0_6; -.
DR   InParanoid; P77570; -.
DR   OMA; GQTIRHE; -.
DR   PhylomeDB; P77570; -.
DR   BioCyc; EcoCyc:G6880-MON; -.
DR   BioCyc; MetaCyc:G6880-MON; -.
DR   BRENDA; 2.7.1.170; 2026.
DR   SABIO-RK; P77570; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   PRO; PR:P77570; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IDA:EcoCyc.
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   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   1: Evidence at protein level;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..369
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_0000214821"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   369 AA;  39496 MW;  E0B439314E60F51B CRC64;
     MKSGRFIGVM SGTSLDGVDV VLATIDEHRV AQLASLSWPI PVSLKQAVLD ICQGQQLTLS
     QFGQLDTQLG QLFADAVNAL LKEQNLQARD IVAIGCHGQT VWHEPTGVAP HTLQIGDNNQ
     IVARTGITVV GDFRRRDIAL GGQGAPLVPA FHHALLAHPT ERRMVLNIGG IANLSLLIPG
     QPVGGYDTGP GNMLMDAWIW RQAGKPYDKD AEWARAGKVI LPLLQNMLSD PYFSQPAPKS
     TGREYFNYGW LERHLRHFPG VDPRDVQATL AELTAVTISE QVLLSGGCER LMVCGGGSRN
     PLLMARLAAL LPGTEVTTTD AVGISGDDME ALAFAWLAWR TLAGLPGNLP SVTGASQETV
     LGAIFPANP