ID A6T7H8_KLEP7 Unreviewed; 303 AA.
AC A6T7H8;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 88.
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=ycfX {ECO:0000313|EMBL:ABR76549.1};
GN Synonyms=nagK {ECO:0000256|HAMAP-Rule:MF_01271};
GN ORFNames=KPN_01116 {ECO:0000313|EMBL:ABR76549.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620 {ECO:0000313|EMBL:ABR76549.1, ECO:0000313|Proteomes:UP000000265};
RN [1] {ECO:0000313|EMBL:ABR76549.1, ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
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] {ECO:0000313|EMBL:ABR76549.1, ECO:0000313|Proteomes:UP000000265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000313|Proteomes:UP000000265};
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) 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}.
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DR EMBL; CP000647; ABR76549.1; -; Genomic_DNA.
DR RefSeq; WP_015958185.1; NC_009648.1.
DR AlphaFoldDB; A6T7H8; -.
DR STRING; 272620.KPN_01116; -.
DR PaxDb; 272620-KPN_01116; -.
DR EnsemblBacteria; ABR76549; ABR76549; KPN_01116.
DR KEGG; kpn:KPN_01116; -.
DR HOGENOM; CLU_036604_0_3_6; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000000265; Chromosome.
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};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Transferase {ECO:0000256|HAMAP-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; 33126 MW; FD64C283F8AC4BA9 CRC64;
MYYGFDIGGS KIALGVFNQE RRLQWEKRVA TPKSSYEDFL QAVEALVREA DERFDQQGSV
GIGIPGMPET ADGTLYAANV PAASGRPLRA DLSARLGREV RLDNDANCFA LSEAWDDEFT
QYPLVMGLIL GTGVGGGLVL NGKSITGHSY ITGEFGHIRL PVDALEVVGR DFPLLRCGCG
QLGCIENYLS GRGFAWLYEH FYQQPLSSPE IVAQWQQHDP RAQAHVERYL DLLAVCLGNI
LTIVDPDLLV LGGGLSNFTA ISEGLAQRLP RHLLPVARVP RIERARHGDA GGMRGAAFLH
LTH
//
