ID   NAGK_ALISL              Reviewed;         302 AA.
AC   B6EKQ4;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 61.
DE   RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000255|HAMAP-Rule:MF_01271};
DE            EC=2.7.1.59 {ECO:0000255|HAMAP-Rule:MF_01271};
DE   AltName: Full=GlcNAc kinase {ECO:0000255|HAMAP-Rule:MF_01271};
GN   Name=nagK {ECO:0000255|HAMAP-Rule:MF_01271};
GN   OrderedLocusNames=VSAL_I1392;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- FUNCTION: Catalyzes the phosphorylation of N-acetyl-D-glucosamine
CC       (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P.
CC       {ECO:0000255|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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01271};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000255|HAMAP-Rule:MF_01271}.
CC   -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01271}.
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DR   EMBL; FM178379; CAQ79077.1; -; Genomic_DNA.
DR   RefSeq; WP_012550085.1; NC_011312.1.
DR   AlphaFoldDB; B6EKQ4; -.
DR   SMR; B6EKQ4; -.
DR   KEGG; vsa:VSAL_I1392; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_0_3_6; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000001730; Chromosome 1.
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; Carbohydrate metabolism; Kinase; Metal-binding;
KW   Nucleotide-binding; Transferase; Zinc.
FT   CHAIN           1..302
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_1000140179"
FT   BINDING         4..11
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         133..140
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         157
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         177
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         179
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
FT   BINDING         184
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01271"
SQ   SEQUENCE   302 AA;  32608 MW;  F88548B03D7493EE CRC64;
     MYYGFDVGGT KIEFGAFNEK LERVATERIP TQTEDYSLLV NDIASLIAKY DAEFGVEGKV
     GLGIPGMEDA ETGALLTSNV PAAKGQFLRK DLEAKIGRSV KIDNDANCFA LSEAWDEELK
     DSPSVLGLIL GTGFGGGLVF DGKVFSGYSH VAGELGHSRL PIDAWFHLGE KAPLLECGCG
     NKGCIDNYLS GRGFELLYAH YYGQEKKAID IIKANEAGDA DAVEHVDRFM ELLAICFANL
     FTCFDPHVVA LGGGLSNFAL IYDELPKRLP KHLLSVARVP RIIKAKHGDS GGVRGAAFLN
     IK
//