ID   ANMK1_JANSC             Reviewed;         375 AA.
AC   Q28RF2;
DT   19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2006, sequence version 2.
DT   03-AUG-2022, entry version 78.
DE   RecName: Full=Anhydro-N-acetylmuramic acid kinase 1 {ECO:0000255|HAMAP-Rule:MF_01270};
DE            EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270};
DE   AltName: Full=AnhMurNAc kinase 1 {ECO:0000255|HAMAP-Rule:MF_01270};
GN   Name=anmK1 {ECO:0000255|HAMAP-Rule:MF_01270}; OrderedLocusNames=Jann_1793;
OS   Jannaschia sp. (strain CCS1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Jannaschia; unclassified Jannaschia.
OX   NCBI_TaxID=290400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCS1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D.,
RA   Han C., Tapia R., Gilna P., Chertkov O., Saunders E., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Lykidis A., Moran M.A., Belas R., Ye W.,
RA   Buchan A., Gonzalez J.M., Schell M.A., Richardson P.;
RT   "Complete sequence of chromosome of Jannaschia sp. CCS1.";
RL   Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
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=ABD54710.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000264; ABD54710.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_044006588.1; NC_007802.1.
DR   AlphaFoldDB; Q28RF2; -.
DR   SMR; Q28RF2; -.
DR   STRING; 290400.Jann_1793; -.
DR   EnsemblBacteria; ABD54710; ABD54710; Jann_1793.
DR   KEGG; jan:Jann_1793; -.
DR   eggNOG; COG2377; Bacteria.
DR   HOGENOM; CLU_038782_3_0_5; -.
DR   OrthoDB; 736294at2; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000008326; 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..375
FT                   /note="Anhydro-N-acetylmuramic acid kinase 1"
FT                   /id="PRO_0000250006"
FT   REGION          351..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         20..27
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   375 AA;  38361 MW;  5D55BA3AD806B9B5 CRC64;
     MAGKEKAVWP PVWAAGAMSG TSFDGVDVAL LLTDGVRIEA FGDAREVAYS DADRAILREA
     MGAWPGEARA EVAAQVVEAA HITAMVDLPD VALLGFHGQT LAHDPEARRT HQVGDGAVLA
     NALGVEVIWD FRSADMGLGG QGAPLAPFYH WACARWIGAQ GPVAILNLGG VGNITWVDPS
     IEGPELPGAC LAFDTGPANA PIDDLMVRRG LGACDVGGAL AARGEIDLKI LEEALEAPWF
     DLAPPKSLDR DAFSGLADAV SGLSDADASA TLTAVSAGAV ARGLAHLSSR PRQVLVAGGG
     RKNATLMAMV QDALGCDVRA VEDVGLNGDA LEAQAFAYLA VRVARGLPTS APSTTGVAAP
     VGGGRRSKPG ARELS