ID   ANMK_SHEPW              Reviewed;         369 AA.
AC   B8CQQ1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 67.
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=swp_3839;
OS   Shewanella piezotolerans (strain WP3 / JCM 13877).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=225849;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WP3 / JCM 13877;
RX   PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA   Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA   Bartlett D.H., Yu J., Hu S., Xiao X.;
RT   "Environmental adaptation: genomic analysis of the piezotolerant and
RT   psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT   WP3.";
RL   PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ30517.1; -; Genomic_DNA.
DR   RefSeq; WP_020913859.1; NC_011566.1.
DR   AlphaFoldDB; B8CQQ1; -.
DR   SMR; B8CQQ1; -.
DR   STRING; 225849.swp_3839; -.
DR   EnsemblBacteria; ACJ30517; ACJ30517; swp_3839.
DR   KEGG; swp:swp_3839; -.
DR   eggNOG; COG2377; Bacteria.
DR   HOGENOM; CLU_038782_0_0_6; -.
DR   OMA; GQTIRHE; -.
DR   OrthoDB; 736294at2; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000753; 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   Transferase.
FT   CHAIN           1..369
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_1000140175"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   369 AA;  39865 MW;  B6B3F83CFCB8A759 CRC64;
     MNKSYFIGLM SGTSMDGVDA VLVKFSGDTP SLIAHHSEEI PAALLRNLQK LCLPGNDEIN
     RLGHLDRAVG KLFAKAVNTL LDKAGVDKLA VIAIGSHGQT VRHMPNLEMG FTLQIGDPNT
     IAAETGIDVI ADFRRKDIAL GGQGAPLVPA FHQQVFATPE HKRIILNIGG IANITYLPGN
     TEAVTGFDTG PGNTLMDAWT QYHQDLPYDK DGAWAKTGTT DDKMLLHLLS HPYFSLAAPK
     STGRELFNQA WLEQQLAEFN HLSDADIQST LLDLTCFSIA NDTLALSTMG EMYVCGGGAY
     NTELMCRLKQ LLPHYKITTT AELGINPQWV EGIAFAWLAM RFHLGLPGNL PAVTGANRAA
     ILGGKFSAL