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Database: UniProt
Entry: W0VBE7_9BURK
LinkDB: W0VBE7_9BURK
Original site: W0VBE7_9BURK 
ID   W0VBE7_9BURK            Unreviewed;       365 AA.
AC   W0VBE7;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000256|HAMAP-Rule:MF_01270};
DE            EC=2.7.1.170 {ECO:0000256|HAMAP-Rule:MF_01270};
DE   AltName: Full=AnhMurNAc kinase {ECO:0000256|HAMAP-Rule:MF_01270};
GN   Name=anmK {ECO:0000256|HAMAP-Rule:MF_01270,
GN   ECO:0000313|EMBL:CDG85206.1};
GN   ORFNames=GJA_4599 {ECO:0000313|EMBL:CDG85206.1};
OS   Janthinobacterium agaricidamnosum NBRC 102515 = DSM 9628.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1349767 {ECO:0000313|EMBL:CDG85206.1, ECO:0000313|Proteomes:UP000027604};
RN   [1] {ECO:0000313|EMBL:CDG85206.1, ECO:0000313|Proteomes:UP000027604}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 102515 / DSM 9628 {ECO:0000313|Proteomes:UP000027604};
RX   PubMed=25883287; DOI=10.1128/genomeA.00277-15;
RA   Graupner K., Lackner G., Hertweck C.;
RT   "Genome Sequence of Mushroom Soft-Rot Pathogen Janthinobacterium
RT   agaricidamnosum.";
RL   Genome Announc. 3:e00277-e00277(2015).
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:0000256|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:0000256|HAMAP-Rule:MF_01270};
CC   -!- PATHWAY: Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate
CC       degradation. {ECO:0000256|HAMAP-Rule:MF_01270}.
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000256|HAMAP-Rule:MF_01270}.
CC   -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01270}.
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DR   EMBL; HG322949; CDG85206.1; -; Genomic_DNA.
DR   RefSeq; WP_038496309.1; NZ_HG322949.1.
DR   AlphaFoldDB; W0VBE7; -.
DR   STRING; 1349767.GJA_4599; -.
DR   KEGG; jag:GJA_4599; -.
DR   PATRIC; fig|1349767.4.peg.1233; -.
DR   eggNOG; COG2377; Bacteria.
DR   HOGENOM; CLU_038782_0_0_4; -.
DR   OrthoDB; 9763949at2; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000027604; 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   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_01270; AnhMurNAc_kinase; 1.
DR   InterPro; IPR005338; Anhydro_N_Ac-Mur_kinase.
DR   InterPro; IPR043129; ATPase_NBD.
DR   PANTHER; PTHR30605; ANHYDRO-N-ACETYLMURAMIC ACID KINASE; 1.
DR   PANTHER; PTHR30605:SF0; ANHYDRO-N-ACETYLMURAMIC ACID KINASE; 1.
DR   Pfam; PF03702; AnmK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01270, ECO:0000313|EMBL:CDG85206.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027604};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT   BINDING         10..17
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   365 AA;  38436 MW;  F36E4DDF906266E1 CRC64;
     MAYFIGLMSG TSLDGVDGEL VDFTDGAARG IGAAYVPFPA ALRSDLMALQ SAGHNEIERE
     ALAANQLVRH YADCVKQLLL DNAIGAGQIV AIGVHGQTIR HRPELGFTRQ TNNPSLLAEL
     SGIDVIADFR SRDVAAGGQG APLVPAFHQA RFGQSGRTRV VANIGGISNI SVLHGDGAVI
     GFDTGPGNAL MDGWIARHQG RSYDAAGAWA ATGKEIPALL QALLAEPYFT QAAPKSTGRD
     LFHMEWLAEK LLPFADARPE DVQYTLTQLT ALSLAQAIQQ YAPAADAVYV CGGGAYNGTL
     LSQLAVALDN KVTVESTAVL GVAPNRVEAL AFAWLAYRFT QRQAGNLAAV TGAQGERILG
     ALYPR
//
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