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Database: UniProt
Entry: A0A0J5M1M9_PLUGE
LinkDB: A0A0J5M1M9_PLUGE
Original site: A0A0J5M1M9_PLUGE 
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
//
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