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Database: UniProt
Entry: T0IMR1_9SPHN
LinkDB: T0IMR1_9SPHN
Original site: T0IMR1_9SPHN 
ID   T0IMR1_9SPHN            Unreviewed;       365 AA.
AC   T0IMR1;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=RLDS_26095 {ECO:0000313|EMBL:EQB10909.1};
OS   Sphingobium lactosutens DS20.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1331060 {ECO:0000313|EMBL:EQB10909.1, ECO:0000313|Proteomes:UP000015531};
RN   [1] {ECO:0000313|EMBL:EQB10909.1, ECO:0000313|Proteomes:UP000015531}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS20 {ECO:0000313|EMBL:EQB10909.1,
RC   ECO:0000313|Proteomes:UP000015531};
RX   PubMed=24051323;
RA   Kumar R., Dwivedi V., Negi V., Khurana J.P., Lal R.;
RT   "Draft Genome Sequence of Sphingobium lactosutens Strain DS20T, Isolated
RT   from a Hexachlorocyclohexane Dumpsite.";
RL   Genome Announc. 1:e00753-13(2013).
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:EQB10909.1}.
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DR   EMBL; ATDP01000109; EQB10909.1; -; Genomic_DNA.
DR   RefSeq; WP_021228653.1; NZ_ATDP01000109.1.
DR   AlphaFoldDB; T0IMR1; -.
DR   PATRIC; fig|1331060.3.peg.5070; -.
DR   eggNOG; COG2377; Bacteria.
DR   OrthoDB; 9763949at2; -.
DR   UniPathway; UPA00343; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000015531; 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:EQB10909.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01270};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01270}.
FT   BINDING         13..20
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01270"
SQ   SEQUENCE   365 AA;  37835 MW;  E680F7B728E47082 CRC64;
     MPPSTLAIGL MSGTSRDGID AALIETDGEG AVAALEFHAM AYDEGFRLRL AEACQRAMAM
     ERPGFEPLIA SVEAELTERH VQAVADLLGR SGHIAQDIGV IGFHGHTLAH RPERGWTWQI
     GDGAGLAGAF GIPVVADLRQ ADVVAGGQGA PLLPVYHRAL ADALAKPAAI LNLGGVANIT
     FIGSDGALIA FDTGMASGLI DNWMQTQGNA PYDEGGACAG RGQVDAAILS TMLADPWFDL
     PPPKSIDREA FSIEAVRGLS LEDGAATLTA FTAAAVARAI DHLPQRPAEI HVAGGGRHNA
     TLMAMIAERT GASVRSVDHL GWDGDALEAQ GFAYMAVRHL KGLPISFPGT TGAPAPMTGG
     VLFRS
//
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