ID   ANMK_PRB01              Reviewed;         364 AA.
AC   Q9F7Q9;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 47.
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};
OS   Gamma-proteobacterium EBAC31A08.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; environmental samples.
OX   NCBI_TaxID=133804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10988064; DOI=10.1126/science.289.5486.1902;
RA   Beja O., Aravind L., Koonin E.V., Suzuki M.T., Hadd A., Nguyen L.P.,
RA   Jovanovich S.B., Gates C.M., Feldman R.A., Spudich J.L., Spudich E.N.,
RA   DeLong E.F.;
RT   "Bacterial rhodopsin: evidence for a new type of phototrophy in the sea.";
RL   Science 289:1902-1906(2000).
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; AF279106; AAG10460.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F7Q9; -.
DR   SMR; Q9F7Q9; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
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   Transferase.
FT   CHAIN           1..364
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_0000250001"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   364 AA;  40285 MW;  595570382133B87E CRC64;
     MSKKIYIGAM TGTSHDAIDI SFLSIGTKIH LEYFHSIKFP KSLRLKVKKL IENNESSLSD
     LGTINKEIGF LFSKSINEAI GFSKIKKSSI ECVAISGQTI RHEINKRFPF SMQIGDPNIV
     AKETGLLVVS DFRNMHIALG GEGAPLVPEF HNQLFYKARN PRIILNIGGI SNYSFVKNRN
     DIWGTDVGPG NAILDAYCSD FLQIPFDKNG AIAAKGKVDH IELGRLLQNN FFKRKCPKST
     GKELFNIKIL SKKFLKKKAE DILCTLVEFS AKSIINSIHK NGHNNCDIVI CGGGAHNKYL
     VKRISEMASN DIVLSSDLGH DVFAIESMAF AWMGYKRVSN EALIVQTSSK NVKGLLGSIT
     KSKL