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Database: UniProt
Entry: X6KR55_9RHOB
LinkDB: X6KR55_9RHOB
Original site: X6KR55_9RHOB 
ID   X6KR55_9RHOB            Unreviewed;       366 AA.
AC   X6KR55;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 2.
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   ORFNames=P279_25930 {ECO:0000313|EMBL:ETA49207.2};
OS   Rhodobacteraceae bacterium PD-2.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae.
OX   NCBI_TaxID=1169855 {ECO:0000313|EMBL:ETA49207.2, ECO:0000313|Proteomes:UP000023196};
RN   [1] {ECO:0000313|EMBL:ETA49207.2, ECO:0000313|Proteomes:UP000023196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PD-2 {ECO:0000313|EMBL:ETA49207.2,
RC   ECO:0000313|Proteomes:UP000023196};
RX   PubMed=25700405;
RA   Zheng L., Cui Z., Xu L., Sun C., Powell R.J., Hill R.T.;
RT   "Draft Genome Sequence of Rhodobacteraceae Strain PD-2, an Algicidal
RT   Bacterium with a Quorum-Sensing System, Isolated from the Marine Microalga
RT   Prorocentrum donghaiense.";
RL   Genome Announc. Announc.3:e01549-14(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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:ETA49207.2}.
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DR   EMBL; AWRV02000005; ETA49207.2; -; Genomic_DNA.
DR   AlphaFoldDB; X6KR55; -.
DR   HOGENOM; CLU_038782_3_0_5; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000023196; Unassembled WGS sequence.
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:ETA49207.2};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Reference proteome {ECO:0000313|Proteomes:UP000023196};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT   BINDING         18..25
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   366 AA;  38272 MW;  66FC58AD849BD71F CRC64;
     MKGKIAAGPV RALGAMSGTS LDGVDAAEIV TDGLRILEFG ESGYRAYSDA ERATLRAVLG
     RWPGEGLEAA TRVVHEAHTE LMAGFPEAEM LGFHGQTLAH DPKGRGTHQL GDGAVLAEAL
     ARPVIWDFRS ADVALGGEGA PLAPFFHFAC AKWIGAEAPL ALLNLGGVGN LTWVDPRHAT
     PEAEGALLAF DTGPANAPIN DLVALRLGLD CDRDGALARQ GRVEDGALEL FLDEQYFRRM
     PPKSLDRDDF SLMLDLVREL SDADAAATMT AMAAAAVMQG MEHCPVAPDR LLVTGGGRHN
     PVMMEMLAVG LDCPVLPVEA VGLDGDMLEA QAFAYLAVRV AHGLPTSCPG TTGVAAPVGG
     GQISRP
//
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