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Database: UniProt
Entry: E0XQ93_9GAMM
LinkDB: E0XQ93_9GAMM
Original site: E0XQ93_9GAMM 
ID   E0XQ93_9GAMM            Unreviewed;       376 AA.
AC   E0XQ93;
DT   02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2010, sequence version 1.
DT   03-MAY-2023, entry version 40.
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};
OS   uncultured gamma proteobacterium HF0010_01E20.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; environmental samples.
OX   NCBI_TaxID=710977 {ECO:0000313|EMBL:ADI16584.1};
RN   [1] {ECO:0000313|EMBL:ADI16584.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA   Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT   "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT   a 'genome proxy' microarray.";
RL   Environ. Microbiol. 13:116-134(2011).
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; GU474841; ADI16584.1; -; Genomic_DNA.
DR   AlphaFoldDB; E0XQ93; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase 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   GO; GO:0006508; P:proteolysis; 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   Hydrolase {ECO:0000313|EMBL:ADI16584.1};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Metalloprotease {ECO:0000313|EMBL:ADI16584.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Protease {ECO:0000313|EMBL:ADI16584.1};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT   BINDING         3..10
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   376 AA;  40215 MW;  FDA79EEC0D58DF18 CRC64;
     MTGTSVDGLD LALIEVSPLN RATGEKETIV VLNALTLPIP KALHDMLLAC GQPEDSSVDL
     LGECDTQLGR FIGTSIADWL KSLGIRASTI KAIGSHGQTV RHRPPGTLGT AFTLQIGDPN
     HIAEITGIDT VADFRRRDMA AGGEGAPLAP AFHKFLFGDT SENTCVVNIG GISNISPLDE
     RGGGFDTGPG NCLLDSWFCQ HHPNPSENYD AAGAWAASGS VNDGLLQRML EDPYFSKRPP
     KTTGREYFNM SWLRSHLQAL QDYPPAVDVQ ATLSQLTASS LAAAIIDTMP DVRDVPICGG
     GRLNDHLMRD IRESLNPREK LDLRVMPCET WGFDGDAIEA AAFAWLAFRR VAALTGNLPA
     VTGAKGERVL GALYPG
//
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