NAGK_VIBVU
ID NAGK_VIBVU Reviewed; 303 AA.
AC Q8D9M7;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 99.
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=VV1_2570;
OS Vibrio vulnificus (strain CMCP6).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=216895;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CMCP6;
RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., Choy H.E.;
RT "Complete genome sequence of Vibrio vulnificus CMCP6.";
RL Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP SEQUENCE REVISION TO 297.
RC STRAIN=CMCP6;
RX PubMed=21245845; DOI=10.1038/msb.2010.115;
RA Kim H.U., Kim S.Y., Jeong H., Kim T.Y., Kim J.J., Choy H.E., Yi K.Y.,
RA Rhee J.H., Lee S.Y.;
RT "Integrative genome-scale metabolic analysis of Vibrio vulnificus for drug
RT targeting and discovery.";
RL Mol. Syst. Biol. 7:460-460(2011).
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; AE016795; AAO10921.2; -; Genomic_DNA.
DR RefSeq; WP_011080420.1; NC_004459.3.
DR PDB; 4DB3; X-ray; 1.95 A; A=1-303.
DR PDBsum; 4DB3; -.
DR AlphaFoldDB; Q8D9M7; -.
DR SMR; Q8D9M7; -.
DR EnsemblBacteria; AAO10921; AAO10921; VV1_2570.
DR KEGG; vvu:VV1_2570; -.
DR HOGENOM; CLU_036604_0_3_6; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000002275; 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Metal-binding;
KW Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..303
FT /note="N-acetyl-D-glucosamine kinase"
FT /id="PRO_0000270122"
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"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 9..17
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 23..30
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 36..54
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 59..68
FT /evidence="ECO:0007829|PDB:4DB3"
FT TURN 70..72
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 88..96
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 101..104
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 105..114
FT /evidence="ECO:0007829|PDB:4DB3"
FT TURN 117..121
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 123..140
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 155..157
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 182..184
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 185..187
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 191..202
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 208..217
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 220..244
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 247..253
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 254..257
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 260..268
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 269..272
FT /evidence="ECO:0007829|PDB:4DB3"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 288..290
FT /evidence="ECO:0007829|PDB:4DB3"
FT HELIX 291..298
FT /evidence="ECO:0007829|PDB:4DB3"
SQ SEQUENCE 303 AA; 32570 MW; F1804F008B123B61 CRC64;
MYYGFDVGGT KIEFGAFNEK LERVATERVP TPTDDYPLLL ETIAGLVAKY DQEFACEGKI
GLGLPGMEDA DDATVLTVNV PAAKGKPLRA DLEAKIGRSV KIENDANCFA LSEAWDEELQ
DAPSVMGLIL GTGFGGGLIY EGKVFSGRNN VAGELGHMRL PLDAWFHLGD NAPLLGCGCG
KKGCLDSYLS GRGFELLYAH YYGEEKKAID IIKANAAGDE KAAEHVERFM ELLAICFGNI
FTANDPHVVA LGGGLSNFEL IYEEMPKRVP KYLLSVAKCP KIIKAKHGDS GGVRGAAFLN
IKG
