ANMK_GLOVI
ID ANMK_GLOVI Reviewed; 379 AA.
AC Q7NEY1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Anhydro-N-acetylmuramic acid kinase {ECO:0000255|HAMAP-Rule:MF_01270};
DE EC=2.7.1.170 {ECO:0000255|HAMAP-Rule:MF_01270};
DE AltName: Full=AnhMurNAc kinase {ECO:0000255|HAMAP-Rule:MF_01270};
GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270}; OrderedLocusNames=glr3746;
OS Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC Bacteria; Cyanobacteria; Gloeobacteria; Gloeobacterales; Gloeobacteraceae;
OC Gloeobacter.
OX NCBI_TaxID=251221;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29082 / PCC 7421;
RX PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT cyanobacterium that lacks thylakoids.";
RL DNA Res. 10:137-145(2003).
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}.
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DR EMBL; BA000045; BAC91687.1; -; Genomic_DNA.
DR RefSeq; NP_926692.1; NC_005125.1.
DR RefSeq; WP_011143735.1; NC_005125.1.
DR AlphaFoldDB; Q7NEY1; -.
DR SMR; Q7NEY1; -.
DR STRING; 251221.35214319; -.
DR EnsemblBacteria; BAC91687; BAC91687; BAC91687.
DR KEGG; gvi:glr3746; -.
DR PATRIC; fig|251221.4.peg.3780; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_1_0_3; -.
DR InParanoid; Q7NEY1; -.
DR OMA; GQTIRHE; -.
DR OrthoDB; 736294at2; -.
DR PhylomeDB; Q7NEY1; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000557; 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..379
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250002"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ SEQUENCE 379 AA; 39927 MW; EA9DE7DB1B95F029 CRC64;
MDPTLAVGLI SGTSLDGMDG ALVEIAGSAQ QPAVTTLATL ALPYPAGLRG RLLHLAEGKP
VPVAEVSALH RDVALAFADC ALQLIEQAGF RCGQIACIGS HGQTVHHQPP ADNAAGHTLQ
LGDGAWIAER TGVTTVGNFR TRDMAAGGQG APLVPILDYL LLRDARRDRC IQNLGGIANV
TYLRAGGGPE EVIAFDTGPA NLLIDGTVQI ALGEPFDRGG SLALQGTVDR DCLERWLADP
YFRRPPPKST GREYFGYARA RRLAEESAHL PVADRVATVS ELTVRSIERA YRDFLPRLPD
EVFLCGGGAR NGYIRARLGR LLAPARVAVS DEAGIDPDFK EAMAFALLAW LRCTGAPGNL
PAVTGAGRAV PLGDVHPAG