ID A0A0J5M1M9_PLUGE Unreviewed; 303 AA.
AC A0A0J5M1M9;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000256|ARBA:ARBA00014974, ECO:0000256|HAMAP-Rule:MF_01271};
DE EC=2.7.1.59 {ECO:0000256|ARBA:ARBA00012122, ECO:0000256|HAMAP-Rule:MF_01271};
DE AltName: Full=GlcNAc kinase {ECO:0000256|ARBA:ARBA00031123, ECO:0000256|HAMAP-Rule:MF_01271};
GN Name=nagK {ECO:0000256|HAMAP-Rule:MF_01271};
GN ORFNames=ABW06_03985 {ECO:0000313|EMBL:KMK15777.1};
OS Pluralibacter gergoviae (Enterobacter gergoviae).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Pluralibacter.
OX NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK15777.1, ECO:0000313|Proteomes:UP000036196};
RN [1] {ECO:0000313|EMBL:KMK15777.1, ECO:0000313|Proteomes:UP000036196}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS81F13 {ECO:0000313|EMBL:KMK15777.1,
RC ECO:0000313|Proteomes:UP000036196};
RA Greninger A.L., Miller S.;
RT "Genome sequences of Pluralibacter gergoviae.";
RL Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine
CC (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
CC {ECO:0000256|HAMAP-Rule:MF_01271}.
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 Evidence={ECO:0000256|ARBA:ARBA00001690, ECO:0000256|HAMAP-
CC Rule:MF_01271};
CC -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC {ECO:0000256|ARBA:ARBA00037880, ECO:0000256|HAMAP-Rule:MF_01271}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily.
CC {ECO:0000256|ARBA:ARBA00038116, ECO:0000256|HAMAP-Rule:MF_01271}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KMK15777.1}.
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DR EMBL; LDZF01000003; KMK15777.1; -; Genomic_DNA.
DR RefSeq; WP_048278245.1; NZ_VWRP01000008.1.
DR AlphaFoldDB; A0A0J5M1M9; -.
DR STRING; 61647.LG71_18800; -.
DR PATRIC; fig|61647.15.peg.3128; -.
DR eggNOG; COG1940; Bacteria.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000036196; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IEA:UniProtKB-UniRule.
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; IEA:UniProtKB-UniRule.
DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1.
DR Gene3D; 3.30.420.40; -; 2.
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:SF162; N-ACETYL-D-GLUCOSAMINE KINASE; 1.
DR PANTHER; PTHR18964; ROK (REPRESSOR, ORF, KINASE) FAMILY; 1.
DR Pfam; PF00480; ROK; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR PROSITE; PS01125; ROK; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_01271};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_01271, ECO:0000313|EMBL:KMK15777.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Reference proteome {ECO:0000313|Proteomes:UP000036196};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01271, ECO:0000313|EMBL:KMK15777.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01271}.
FT BINDING 4..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 133..140
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 157
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 177
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 179
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 184
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
SQ SEQUENCE 303 AA; 32653 MW; 08E0395B957C32DF CRC64;
MYYGFDIGGS KIALGVFDGQ RRQQWETRIP TPHSGYDAFL DAVCGLVAQA DSRFGVKGSV
GIGIPGMPET ADGTLYAANV PAASGRPLRA DLSARLGRDV RLDNDANCFA LSEAWDDEFT
AYPLVMGLIL GTGVGGGLVL NGKSITGHSY ITGEFGHIRL PVDALEVVGR DFPLTRCGCG
QLGCIENYLS GRGFAWLYQH YYQQPLSGPE IVERWQQGDK RAREHVERYL DLLAVCLGNI
LTIVDPDLLV IGGGLSNFSA IADGLATRLP RHLLPVARVP RIEQARHGDA GGMRGAAFLH
LTE
//