NAGK_SALTY
ID NAGK_SALTY Reviewed; 303 AA.
AC Q8ZPZ9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=N-acetyl-D-glucosamine kinase;
DE EC=2.7.1.59;
DE AltName: Full=GlcNAc kinase;
GN Name=nagK; Synonyms=ycfX; OrderedLocusNames=STM1220;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH ZINC.
RG Midwest center for structural genomics (MCSG);
RT "Crystal structure of the putative regulatory protein.";
RL Submitted (SEP-2005) to the PDB data bank.
RN [3]
RP INDUCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=20889757; DOI=10.1128/jb.00874-10;
RA Tucker A.C., Escalante-Semerena J.C.;
RT "Biologically active isoforms of CobB sirtuin deacetylase in Salmonella
RT enterica and Erwinia amylovora.";
RL J. Bacteriol. 192:6200-6208(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine
CC (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-glucosamine = ADP + H(+) + N-acetyl-D-
CC glucosamine 6-phosphate; Xref=Rhea:RHEA:17417, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57513, ChEBI:CHEBI:456216,
CC ChEBI:CHEBI:506227; EC=2.7.1.59;
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC -!- INDUCTION: Expressed in mid-log phase, part of the nagK-cobB operon
CC (PubMed:20889757). {ECO:0000269|PubMed:20889757}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily.
CC {ECO:0000305}.
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DR EMBL; AE006468; AAL20149.1; -; Genomic_DNA.
DR RefSeq; NP_460190.1; NC_003197.2.
DR RefSeq; WP_000291338.1; NC_003197.2.
DR PDB; 2AP1; X-ray; 1.90 A; A=1-303.
DR PDBsum; 2AP1; -.
DR AlphaFoldDB; Q8ZPZ9; -.
DR SMR; Q8ZPZ9; -.
DR STRING; 99287.STM1220; -.
DR PaxDb; Q8ZPZ9; -.
DR DNASU; 1252738; -.
DR EnsemblBacteria; AAL20149; AAL20149; STM1220.
DR GeneID; 1252738; -.
DR KEGG; stm:STM1220; -.
DR PATRIC; fig|99287.12.peg.1289; -.
DR HOGENOM; CLU_036604_0_3_6; -.
DR OMA; VNVPGWR; -.
DR PhylomeDB; Q8ZPZ9; -.
DR BioCyc; SENT99287:STM1220-MON; -.
DR UniPathway; UPA00544; -.
DR EvolutionaryTrace; Q8ZPZ9; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009254; P:peptidoglycan turnover; IBA:GO_Central.
DR HAMAP; MF_01271; GlcNAc_kinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR023505; N-acetyl-D-glucosamine_kinase.
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..303
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000270114"
FT BINDING 4..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000269|Ref.2"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 9..18
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:2AP1"
FT TURN 81..85
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 100..104
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 123..140
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 143..145
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 162..168
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 186..189
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 208..216
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 220..244
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 266..268
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 270..272
FT /evidence="ECO:0007829|PDB:2AP1"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:2AP1"
FT TURN 288..290
FT /evidence="ECO:0007829|PDB:2AP1"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:2AP1"
SQ SEQUENCE 303 AA; 33060 MW; 3BF0B7587DDAA469 CRC64;
MYYGFDIGGT KIALGVFDST RRLQWEKRVP TPHTSYSAFL DAVCELVEEA DQRFGVKGSV
GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT
QYPLVMGLIL GTGVGGGLVL NGKPITGQSY ITGEFGHMRL PVDALTLMGF DFPLRRCGCG
QMGCIENYLS GRGFAWLYQH YYDQSLQAPE IIALWEQGDE QAHAHVERYL DLLAVCLGNI
LTIVDPDLLV IGGGLSNFTA ITTQLAERLP RHLLPVARAP RIERARHGDA GGMRGAAFLH
LTD
