ID   ANMK_BRUAB              Reviewed;         373 AA.
AC   Q57DI4;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=BruAb1_0936;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74300.1; -; Genomic_DNA.
DR   RefSeq; WP_002964051.1; NC_006932.1.
DR   AlphaFoldDB; Q57DI4; -.
DR   SMR; Q57DI4; -.
DR   EnsemblBacteria; AAX74300; AAX74300; BruAb1_0936.
DR   GeneID; 45051985; -.
DR   GeneID; 55590627; -.
DR   KEGG; bmb:BruAb1_0936; -.
DR   HOGENOM; CLU_038782_3_0_5; -.
DR   OMA; GQTIRHE; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000000540; Chromosome I.
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..373
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_0000249980"
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   373 AA;  39828 MW;  F12C16EFF7C8773F CRC64;
     MPDLKRAIGL MSGTSMDGID IALLATDGEN WIERRASASM DYSDGFRARL KAGLVDARAI
     KDRAERPGLL RQLEHDLTLL HAVAVHDFLH EQGLQPHEID VIGFHGQTVL HRPNESLTVQ
     IGDGALLARE TGIPVVYDMR AEDMRHGGQG APLIPAYHAA LAANLPLGLK GPVVFVNIGG
     ISNLTYVGED GALIAYDSGP GNMLIDQWME LHGHGRFDPG GATAMSGSVD RNTAHRYLEH
     EFFKGNHRRS LDRGDFAIPA KGELNLADGA RTLAFVSAAA ILKSASHLPA RPRTYVVSGG
     GRKNGALMDE LTALAEREGA HVIDADNAGF DGDAMEAEAW AYLAVRSLCG LPLTYPSTTG
     CDKPVSGGVP VRP