ANMK_PSEAE
ID ANMK_PSEAE Reviewed; 363 AA.
AC Q9I5Q5;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
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, ECO:0000303|PubMed:24819062};
GN Name=anmK {ECO:0000255|HAMAP-Rule:MF_01270, ECO:0000303|PubMed:24819062};
GN OrderedLocusNames=PA0666;
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=24819062; DOI=10.1089/mdr.2014.0036;
RA Borisova M., Gisin J., Mayer C.;
RT "Blocking peptidoglycan recycling in Pseudomonas aeruginosa attenuates
RT intrinsic resistance to fosfomycin.";
RL Microb. Drug Resist. 20:231-237(2014).
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 (By similarity). Is required
CC for the utilization of anhMurNAc either imported from the medium or
CC derived from its own cell wall murein, and thus plays a role in cell
CC wall recycling. Contributes to intrinsic fosfomycin resistance in
CC P.aeruginosa (PubMed:24819062). {ECO:0000255|HAMAP-Rule:MF_01270,
CC ECO:0000269|PubMed:24819062}.
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 ECO:0000269|PubMed:24819062}.
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000255|HAMAP-Rule:MF_01270, ECO:0000269|PubMed:24819062}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene accumulate anhMurNAc.
CC Deletion of this gene increases fosfomycin sensitivity. Growth rate is
CC not affected. {ECO:0000269|PubMed:24819062}.
CC -!- SIMILARITY: Belongs to the anhydro-N-acetylmuramic acid kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_01270}.
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DR EMBL; AE004091; AAG04055.1; -; Genomic_DNA.
DR PIR; A83563; A83563.
DR RefSeq; NP_249357.1; NC_002516.2.
DR RefSeq; WP_003113168.1; NZ_QZGE01000010.1.
DR PDB; 3QBW; X-ray; 2.23 A; A/B=1-363.
DR PDB; 3QBX; X-ray; 2.10 A; A/B=1-363.
DR PDB; 4MO4; X-ray; 1.67 A; A/B/C/D=1-363.
DR PDB; 4MO5; X-ray; 1.75 A; A/B/C/D=1-363.
DR PDBsum; 3QBW; -.
DR PDBsum; 3QBX; -.
DR PDBsum; 4MO4; -.
DR PDBsum; 4MO5; -.
DR AlphaFoldDB; Q9I5Q5; -.
DR SMR; Q9I5Q5; -.
DR STRING; 287.DR97_3619; -.
DR PaxDb; Q9I5Q5; -.
DR DNASU; 882072; -.
DR EnsemblBacteria; AAG04055; AAG04055; PA0666.
DR GeneID; 882072; -.
DR KEGG; pae:PA0666; -.
DR PATRIC; fig|208964.12.peg.697; -.
DR PseudoCAP; PA0666; -.
DR HOGENOM; CLU_038782_0_0_6; -.
DR InParanoid; Q9I5Q5; -.
DR OMA; GQTIRHE; -.
DR PhylomeDB; Q9I5Q5; -.
DR BioCyc; MetaCyc:MON-20215; -.
DR BioCyc; PAER208964:G1FZ6-671-MON; -.
DR BRENDA; 2.7.1.170; 5087.
DR UniPathway; UPA00343; -.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; Q9I5Q5; -.
DR Proteomes; UP000002438; 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 GO; GO:0046677; P:response to antibiotic; 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 1: Evidence at protein level;
KW 3D-structure; Antibiotic resistance; ATP-binding; Carbohydrate metabolism;
KW Kinase; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..363
FT /note="Anhydro-N-acetylmuramic acid kinase"
FT /id="PRO_0000250028"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01270"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 14..36
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 39..46
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 55..80
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 85..87
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 90..93
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 106..110
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 113..120
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 124..126
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 130..134
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 143..151
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 158..172
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 179..185
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 188..198
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 216..223
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 226..229
FT /evidence="ECO:0007829|PDB:3QBX"
FT TURN 238..240
FT /evidence="ECO:0007829|PDB:3QBX"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 258..280
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 286..291
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 292..295
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 297..306
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 310..314
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 325..338
FT /evidence="ECO:0007829|PDB:4MO4"
FT HELIX 346..349
FT /evidence="ECO:0007829|PDB:4MO4"
FT STRAND 359..361
FT /evidence="ECO:0007829|PDB:4MO4"
SQ SEQUENCE 363 AA; 39120 MW; 4BAC3CF820071F8A CRC64;
MPRYLGLMSG TSLDGMDIVL IEQGDRTTLL ASHYLPMPAG LREDILALCV PGPDEIARAA
EVEQRWVALA AQGVRELLLQ QQMSPDEVRA IGSHGQTIRH EPARHFTVQI GNPALLAELT
GIDVVADFRR RDVAAGGQGA PLVPAFHQAL FGDDDTSRAV LNIGGFSNVS LLSPGKPVRG
FDCGPGNVLM DAWIHHQRGE HFDRDGAWAA SGQVNHALLA SLLADEFFAA RGPKSTGRER
FNLPWLQEHL ARHPALPAAD IQATLLELSA RSISESLLDA QPDCEEVLVC GGGAFNTALM
KRLAMLMPEA RVASTDEYGI PPAWMEGMAF AWLAHRFLER LPGNCPDVTG ALGPRTLGAL
YPA
