ID   ANMK_CAUVC              Reviewed;         371 AA.
AC   Q9A757;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 88.
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=CC_1869;
OS   Caulobacter vibrioides (strain ATCC 19089 / CB15) (Caulobacter crescentus).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Caulobacter.
OX   NCBI_TaxID=190650;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19089 / CB15;
RX   PubMed=11259647; DOI=10.1073/pnas.061029298;
RA   Nierman W.C., Feldblyum T.V., Laub M.T., Paulsen I.T., Nelson K.E.,
RA   Eisen J.A., Heidelberg J.F., Alley M.R.K., Ohta N., Maddock J.R.,
RA   Potocka I., Nelson W.C., Newton A., Stephens C., Phadke N.D., Ely B.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Gwinn M.L., Haft D.H., Kolonay J.F.,
RA   Smit J., Craven M.B., Khouri H.M., Shetty J., Berry K.J., Utterback T.R.,
RA   Tran K., Wolf A.M., Vamathevan J.J., Ermolaeva M.D., White O.,
RA   Salzberg S.L., Venter J.C., Shapiro L., Fraser C.M.;
RT   "Complete genome sequence of Caulobacter crescentus.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:4136-4141(2001).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK23844.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE005673; AAK23844.1; ALT_INIT; Genomic_DNA.
DR   PIR; H87480; H87480.
DR   RefSeq; NP_420676.1; NC_002696.2.
DR   AlphaFoldDB; Q9A757; -.
DR   SMR; Q9A757; -.
DR   STRING; 190650.CC_1869; -.
DR   EnsemblBacteria; AAK23844; AAK23844; CC_1869.
DR   KEGG; ccr:CC_1869; -.
DR   PATRIC; fig|190650.5.peg.1886; -.
DR   eggNOG; COG2377; Bacteria.
DR   HOGENOM; CLU_038782_3_0_5; -.
DR   OMA; GQTIRHE; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001816; 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..371
FT                   /note="Anhydro-N-acetylmuramic acid kinase"
FT                   /id="PRO_0000249991"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   371 AA;  38853 MW;  6B8DB2D8F4673CCE CRC64;
     MKILGFMTGT SLDAVDMAVL ETDGVEISAF GPAGERKLRE ATRDLLLKTT DIARAWPRGE
     PEPVIFEEAR RAVADEHFQA AESFLDEHGL SWSDFDLLGV HGQTVLHERP TAQRVGRTVQ
     LLDADRLARL CGRPVAFDFR TADVAVGGEG APLAPIYHAA RARASGLAAP VAALNVGGVA
     NITLIGANGD LLAFDTGPGN GMIDLMLQAR GLGRFDEDGR LALAGRVDEA VLAALLDSPY
     FDAPAPKSLD RYDFSLTPVD HLSAEDAAAT LVAFTAEAVF KAFAQSGEAP SALIVCGGGR
     HNPAIMQTLA ARAPVPVKSA EAYGWRGDSI EAEAFAYLAA RTAKGLPISF PGTTGVPAPM
     TGGRIVGLIS A