ID   ANMK_SULDN              Reviewed;         368 AA.
AC   Q30NT6;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   06-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=Suden_2071;
OS   Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS   denitrificans (strain ATCC 33889 / DSM 1251)).
OC   Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC   Thiovulaceae; Sulfurimonas.
OX   NCBI_TaxID=326298;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33889 / DSM 1251;
RX   PubMed=18065616; DOI=10.1128/aem.01844-07;
RA   Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA   Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA   Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA   Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA   Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA   Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT   "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT   denitrificans.";
RL   Appl. Environ. Microbiol. 74:1145-1156(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; CP000153; ABB45345.1; -; Genomic_DNA.
DR   RefSeq; WP_011373685.1; NC_007575.1.
DR   AlphaFoldDB; Q30NT6; -.
DR   SMR; Q30NT6; -.
DR   STRING; 326298.Suden_2071; -.
DR   PRIDE; Q30NT6; -.
DR   EnsemblBacteria; ABB45345; ABB45345; Suden_2071.
DR   KEGG; tdn:Suden_2071; -.
DR   eggNOG; COG2377; Bacteria.
DR   HOGENOM; CLU_038782_0_0_7; -.
DR   OMA; GQTIRHE; -.
DR   OrthoDB; 736294at2; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000002714; 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..368
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_0000250077"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   368 AA;  40961 MW;  F47D47571A77A705 CRC64;
     MSEFYIGVMS GTSLDGIDLA LCEIEDDAFE LLLCASYPFD AELKSDILNA INAQTTLKNI
     GEIDIRLGKM YADALEKFIE ENSLKRVKIR AIGLHGQTLW HEPESQNPFS MQLGNANILT
     ARLGICVVSD FRQKDIALGG QGAPFTPAFH EFLFSKLSGN VAVLNIGGMA NITLLREMLS
     GYDTGCGNVL MDYWISKYNG SPYDKDGEWA KSGTPNRELL REFLKEPYFL KSPPKSTGRE
     LFGEKWLKKQ LSEFAKKNQN CSYLKARDIQ ATLLELSVQS IANEIKKSDT TLLIVCGGGI
     NNRYLMERLQ EELGDIKIAS SDEYGVSSEF MEAMAFAWLA HERIHKKCVK ISSVSGALRD
     SILGAIYE