ID ANMK_MANSM Reviewed; 375 AA.
AC Q65R57;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=MS1946;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38553.1; -; Genomic_DNA.
DR RefSeq; WP_011201105.1; NC_006300.1.
DR AlphaFoldDB; Q65R57; -.
DR SMR; Q65R57; -.
DR STRING; 221988.MS1946; -.
DR KEGG; msu:MS1946; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_0_0_6; -.
DR OrthoDB; 9763949at2; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000607; 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 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; Carbohydrate metabolism; Kinase; Nucleotide-binding;
KW Transferase.
FT CHAIN 1..375
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250012"
FT BINDING 12..19
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ SEQUENCE 375 AA; 41405 MW; DD80754DB77E01F3 CRC64;
MMKQYYIGVM SGTSLDGVDL ALMDFTLNPP KLMATDFTPM PEKIREKLTA LLRSGETSLR
NLGEIDHQLG LLYAESINRF LQKVRLKSED ICAVGCHGQT VWHSPNCEFP FTMQIGDMNL
VAAKTGITTV GDFRRKDMAL GGQGAPLVPA FHQDLFFAAE RLTVVLNIGG ISNISVLEEN
CPTVGYDVSV GNALLDSWIE LHQGKRYDKD ALWAKNGKIS TALLTDLLAE PFFQQAPPKS
TGRELFNLAW LNKKLEKFTA LSQPMPSPQD VQRTLVEFTA LSIANELKKL QKSDRTNLLL
VCGGGARNPL IMQRLTALLA EWQVSTTSEF GLDIDYVEAA AFAWLAYRRI HNLPSNLPSV
TGAKSEVSLG VIFPK
//
