NANK_ECOLI
ID NANK_ECOLI Reviewed; 291 AA.
AC P45425; Q2M8Z1;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=N-acetylmannosamine kinase;
DE EC=2.7.1.60 {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299};
DE AltName: Full=ManNAc kinase;
DE AltName: Full=N-acetyl-D-mannosamine kinase;
GN Name=nanK; Synonyms=yhcI; OrderedLocusNames=b3222, JW5538;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [3]
RP PUTATIVE FUNCTION.
RX PubMed=9864311; DOI=10.1128/jb.181.1.47-54.1999;
RA Plumbridge J., Vimr E.;
RT "Convergent pathways for utilization of the amino sugars N-
RT acetylglucosamine, N-acetylmannosamine, and N-acetylneuraminic acid by
RT Escherichia coli.";
RL J. Bacteriol. 181:47-54(1999).
RN [4]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=15157072; DOI=10.1021/bi049424m;
RA Miller B.G., Raines R.T.;
RT "Identifying latent enzyme activities: substrate ambiguity within modern
RT bacterial sugar kinases.";
RL Biochemistry 43:6387-6392(2004).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF LEU-84 AND VAL-138.
RX PubMed=17979299; DOI=10.1021/bi700924d;
RA Larion M., Moore L.B., Thompson S.M., Miller B.G.;
RT "Divergent evolution of function in the ROK sugar kinase superfamily: role
RT of enzyme loops in substrate specificity.";
RL Biochemistry 46:13564-13572(2007).
RN [6]
RP INDUCTION.
RX PubMed=23935044; DOI=10.1128/jb.00692-13;
RA Kalivoda K.A., Steenbergen S.M., Vimr E.R.;
RT "Control of the Escherichia coli sialoregulon by transcriptional repressor
RT NanR.";
RL J. Bacteriol. 195:4689-4701(2013).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-289 IN COMPLEX WITH ZINC IONS,
RP AND SUBUNIT.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of Escherichia coli putative N-acetylmannosamine
RT kinase.";
RL Submitted (JUL-2005) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetylmannosamine (ManNAc)
CC to ManNAc-6-P. Has also low level glucokinase activity in vitro.
CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-mannosamine = ADP + H(+) + N-acetyl-D-
CC mannosamine 6-phosphate; Xref=Rhea:RHEA:25253, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:17122, ChEBI:CHEBI:30616, ChEBI:CHEBI:58557,
CC ChEBI:CHEBI:456216; EC=2.7.1.60;
CC Evidence={ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25254;
CC Evidence={ECO:0000269|PubMed:15157072};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.36 mM for N-acyl-D-mannosamine (at 25 degrees Celsius and pH
CC 7.6) {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299};
CC KM=0.26 mM for ATP (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299};
CC KM=20 mM for D-glucose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299};
CC KM=84 mM for D-mannose (at 25 degrees Celsius and pH 7.6)
CC {ECO:0000269|PubMed:15157072, ECO:0000269|PubMed:17979299};
CC Note=Catalytic efficiency with N-acyl-D-mannosamine as substrate is
CC 136-fold higher than that with D-glucose.;
CC -!- PATHWAY: Amino-sugar metabolism; N-acetylneuraminate degradation; D-
CC fructose 6-phosphate from N-acetylneuraminate: step 2/5.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|Ref.7}.
CC -!- INDUCTION: Negatively regulated by the transcriptional repressor NanR.
CC Induced by N-acetylneuraminate, via inactivation of NanR.
CC {ECO:0000269|PubMed:23935044}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NanK subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA58024.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA58024.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76254.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77265.1; -; Genomic_DNA.
DR PIR; H65113; H65113.
DR RefSeq; NP_417689.4; NC_000913.3.
DR RefSeq; WP_000209011.1; NZ_SSZK01000034.1.
DR PDB; 2AA4; X-ray; 2.20 A; A/B=1-289.
DR PDBsum; 2AA4; -.
DR AlphaFoldDB; P45425; -.
DR SMR; P45425; -.
DR BioGRID; 4261227; 316.
DR DIP; DIP-12282N; -.
DR IntAct; P45425; 1.
DR STRING; 511145.b3222; -.
DR jPOST; P45425; -.
DR PaxDb; P45425; -.
DR PRIDE; P45425; -.
DR EnsemblBacteria; AAC76254; AAC76254; b3222.
DR EnsemblBacteria; BAE77265; BAE77265; BAE77265.
DR GeneID; 947757; -.
DR KEGG; ecj:JW5538; -.
DR KEGG; eco:b3222; -.
DR PATRIC; fig|1411691.4.peg.3506; -.
DR EchoBASE; EB2666; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_4_6; -.
DR InParanoid; P45425; -.
DR OMA; APNIDWR; -.
DR PhylomeDB; P45425; -.
DR BioCyc; EcoCyc:NANK-MON; -.
DR BioCyc; MetaCyc:NANK-MON; -.
DR SABIO-RK; P45425; -.
DR UniPathway; UPA00629; UER00681.
DR EvolutionaryTrace; P45425; -.
DR PRO; PR:P45425; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009384; F:N-acylmannosamine kinase activity; IDA:EcoCyc.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0006051; P:N-acetylmannosamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019262; P:N-acetylneuraminate catabolic process; IDA:EcoCyc.
DR HAMAP; MF_01234; ManNAc_kinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR023945; ManNAc_kinase_bac.
DR InterPro; IPR000600; ROK.
DR PANTHER; PTHR18964; PTHR18964; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; SSF53067; 1.
DR PROSITE; PS01125; ROK; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT CHAIN 1..291
FT /note="N-acetylmannosamine kinase"
FT /id="PRO_0000095695"
FT BINDING 5..12
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 166
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 168
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT BINDING 173
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT MUTAGEN 84
FT /note="L->P: 12-fold increase in catalytic efficiency for
FT glucose phosphorylation. 2-fold decrease in catalytic
FT efficiency for N-acetylmannosamine phosphorylation."
FT /evidence="ECO:0000269|PubMed:17979299"
FT MUTAGEN 138
FT /note="V->M: 6-fold increase in catalytic efficiency for
FT glucose phosphorylation. No change in catalytic efficiency
FT for N-acetylmannosamine phosphorylation."
FT /evidence="ECO:0000269|PubMed:17979299"
FT STRAND 3..8
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 10..18
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 24..31
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 38..49
FT /evidence="ECO:0007829|PDB:2AA4"
FT TURN 50..52
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 57..68
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 77..83
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 105..115
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 124..139
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 171..173
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 174..178
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 180..185
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 189..191
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 196..204
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 208..232
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 235..240
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 241..244
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 249..257
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:2AA4"
FT STRAND 267..270
FT /evidence="ECO:0007829|PDB:2AA4"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:2AA4"
SQ SEQUENCE 291 AA; 29644 MW; E3109E2756B08612 CRC64;
MTTLAIDIGG TKLAAALIGA DGQIRDRREL PTPASQTPEA LRDALSALVS PLQAHAQRVA
IASTGIIRDG SLLALNPHNL GGLLHFPLVK TLEQLTNLPT IAINDAQAAA WAEFQALDGD
ITDMVFITVS TGVGGGVVSG CKLLTGPGGL AGHIGHTLAD PHGPVCGCGR TGCVEAIASG
RGIAAAAQGE LAGADAKTIF TRAGQGDEQA QQLIHRSART LARLIADIKA TTDCQCVVVG
GSVGLAEGYL ALVETYLAQE PAAFHVDLLA AHYRHDAGLL GAALLAQGEK L
