ANMK_ZYMMO
ID ANMK_ZYMMO Reviewed; 365 AA.
AC Q5NLZ4; Q9EZA1;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 19-SEP-2006, sequence version 2.
DT 03-AUG-2022, entry version 86.
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=ZMO1642;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Shin I.S., Kang H.S.;
RT "Zymomonas mobilis ZM4 fosmid clone 43E12 complete sequence.";
RL Submitted (AUG-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG42405.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF300471; AAG42405.1; ALT_FRAME; Genomic_DNA.
DR EMBL; AE008692; AAV90266.2; -; Genomic_DNA.
DR RefSeq; WP_011241392.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NLZ4; -.
DR SMR; Q5NLZ4; -.
DR STRING; 264203.ZMO1642; -.
DR EnsemblBacteria; AAV90266; AAV90266; ZMO1642.
DR GeneID; 58027357; -.
DR KEGG; zmo:ZMO1642; -.
DR eggNOG; COG2377; Bacteria.
DR HOGENOM; CLU_038782_3_0_5; -.
DR OMA; GQTIRHE; -.
DR OrthoDB; 736294at2; -.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001173; 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..365
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250093"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
SQ SEQUENCE 365 AA; 39563 MW; E88DA1D34C8EED02 CRC64;
MLAIGLMSGT SLDGVDVALI ETNGEKQVKP LNFASYPYSD TDKACLREAC RRALTMAAPC
FIPEDEVIYQ AEHIVTLRHI QAVKDFLKKN ALGNQAIKVI GFHGQTIAHR PDLGWTWQIG
DGAALAQATK ISVVDDFRSH DVQAGGEGAP LLPIYHWALF SEASHPLAVL NLGGIANITW
IGADENDLIA CDTGPANGMI DDWVKAKTGL DYDESGLIAS KGVVHHDLVD AMMSQKFFSQ
LPPKSLDRSD FSIEAVANLS IEDGAATLTA FTAESVARSL SFFPERPSKI IVAGGGRHNV
TMMKMLHDSL KMPVQPIEDF HLNGDATEAE GFAYLAVRRV FNKPISFPKT TGVPHPMTGG
RIHYI