ID   NAGK_VIBA3              Reviewed;         302 AA.
AC   B7VNU4;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 57.
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}; OrderedLocusNames=VS_1507;
OS   Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=575788;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LGP32;
RA   Mazel D., Le Roux F.;
RT   "Vibrio splendidus str. LGP32 complete genome.";
RL   Submitted (FEB-2009) 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: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; FM954972; CAV18676.1; -; Genomic_DNA.
DR   RefSeq; WP_012603950.1; NC_011753.2.
DR   AlphaFoldDB; B7VNU4; -.
DR   SMR; B7VNU4; -.
DR   STRING; 575788.VS_1507; -.
DR   EnsemblBacteria; CAV18676; CAV18676; VS_1507.
DR   KEGG; vsp:VS_1507; -.
DR   eggNOG; COG1940; Bacteria.
DR   HOGENOM; CLU_036604_0_3_6; -.
DR   OMA; VNVPGWR; -.
DR   OrthoDB; 1130699at2; -.
DR   UniPathway; UPA00544; -.
DR   Proteomes; UP000009100; 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   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; PTHR18964; 1.
DR   Pfam; PF00480; ROK; 1.
DR   SUPFAM; SSF53067; SSF53067; 1.
DR   PROSITE; PS01125; ROK; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW   Nucleotide-binding; Reference proteome; Transferase; Zinc.
FT   CHAIN           1..302
FT                   /note="N-acetyl-D-glucosamine kinase"
FT                   /id="PRO_1000165176"
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;  32820 MW;  B7FA4E58A87C649F CRC64;
     MYYGFDVGGT KIEFGAFNEK LERVATERVP TPTEDYQLLL DTIAGLVKKY DNEFSCEGKI
     GLGLPGMEDA DDGTMLVVNV PASTGKPLRK DLEALIGRSV KIENDANCFA LSEAWDDELK
     DEPSVAGLIL GTGFGGGLVY EGKVFSGRNH VAGELGHMRL PLDAWFHLGD NAPLLGCGCG
     KKGCLDSYLS GRGFELIYEH YFGEKKKAIE IIQAYNEGES KAAEHVDRFM ELLAICFANL
     FTGLDPHVVA LGGGLSNFEL IYEEMPKRIP KYLLSVAKCP KIIKAKHGDS GGVRGAAFLN
     IK