ID G5Q3Y4_SALMO Unreviewed; 303 AA.
AC G5Q3Y4;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 24-JAN-2024, entry version 47.
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=LTSEMON_2733 {ECO:0000313|EMBL:EHC78368.1};
OS Salmonella enterica subsp. enterica serovar Montevideo str. S5-403.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913242 {ECO:0000313|EMBL:EHC78368.1, ECO:0000313|Proteomes:UP000003221};
RN [1] {ECO:0000313|EMBL:EHC78368.1, ECO:0000313|Proteomes:UP000003221}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S5-403 {ECO:0000313|EMBL:EHC78368.1,
RC ECO:0000313|Proteomes:UP000003221};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
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:EHC78368.1}.
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DR EMBL; AFCS01000636; EHC78368.1; -; Genomic_DNA.
DR AlphaFoldDB; G5Q3Y4; -.
DR PATRIC; fig|913242.3.peg.2379; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000003221; 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|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_01271};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_01271};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_01271};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_01271};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01271};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01271};
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; 33024 MW; DAC377A7A225EF9C CRC64;
MYYGFDIGGT KIALGVFDST RRLQWEKRVP TPHTSYSAFL DAVCELVAEA DQRFGVKGSV
GIGIPGMPET EDGTLYAANV PAASGKPLRA DLSARLDRDV RLDNDANCFA LSEAWDDEFT
QYPLVMGLIL GTGVGGGLVL NGKPITGQSY ITGEFGHMRL PVDALTLMGF DFPLRRCGCG
QMGCIENYLS GRGFAWLYQH YYHQSLQAPE IIALWEQGDE QAHAHVERYL DLLAVCLGNI
LTIVDPDLLV IGGGLSNFTA ITTQLAERLP RHLLPVARAP RIERARHGDA GGMRGAAFLH
LTD
//
