ID   ANMK_CLOD6              Reviewed;         383 AA.
AC   Q184N9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   03-AUG-2022, entry version 86.
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};
GN   Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; OrderedLocusNames=CD630_30510;
OS   Clostridioides difficile (strain 630) (Peptoclostridium difficile).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Clostridioides.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K., Unwin L.,
RA   Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a highly
RT   mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(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:0000255|HAMAP-Rule:MF_01270}.
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   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_01270}.
CC   -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01270}.
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DR   EMBL; AM180355; CAJ69944.2; -; Genomic_DNA.
DR   RefSeq; YP_001089566.2; NC_009089.1.
DR   AlphaFoldDB; Q184N9; -.
DR   SMR; Q184N9; -.
DR   STRING; 272563.CD630_30510; -.
DR   EnsemblBacteria; CAJ69944; CAJ69944; CD630_30510.
DR   KEGG; cdf:CD630_30510; -.
DR   KEGG; pdc:CDIF630_03335; -.
DR   PATRIC; fig|272563.120.peg.3217; -.
DR   eggNOG; COG2377; Bacteria.
DR   OMA; GQTIRHE; -.
DR   PhylomeDB; Q184N9; -.
DR   BioCyc; PDIF272563:G12WB-3213-MON; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001978; 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   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   ATP-binding; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW   Reference proteome; Transferase.
FT   CHAIN           1..383
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_1000067343"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   383 AA;  42192 MW;  32C8EC5378726A01 CRC64;
     MYSVGLMSGT SLDGIDAVLA EISGNGRNTK VKQIEFITLE ISKDIKDEIR KCCIEEESSV
     DLICSLNFKL GYLFSKAVKS VCHKANFHIA NLDFIASHGQ TIFHIPRSYN NFVSSTLQIG
     EPAVIAYETN TKVISNFRVM DIAAGGEGAP LVPYSEFLLY SDKNKNLALQ NIGGIGNITI
     IPKSCNIDDV FAFDTGPGNM IIDGVCQRLF NRKYDKNGYF ASKGKINEEM LKDLMSHKYL
     SQAPPKSTGR EVFGQVYLDN MLNKYKHVDK YDLIATVTMF TAKAIYYNYK NFILPKVNVD
     TLLIGGGGAH NLTLIGYIKE LLLEVEVLTQ DEYGYSSDAK EALAFVILGN ETLNNSFSNV
     ISATGAKNKV ILGNITPKPF GGK