ID D0IEX4_9VIBR Unreviewed; 302 AA.
AC D0IEX4;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000256|HAMAP-Rule:MF_01271};
DE EC=2.7.1.59 {ECO:0000256|HAMAP-Rule:MF_01271};
DE AltName: Full=GlcNAc kinase {ECO:0000256|HAMAP-Rule:MF_01271};
GN Name=nagK {ECO:0000256|HAMAP-Rule:MF_01271};
GN ORFNames=VOA_000175 {ECO:0000313|EMBL:EEZ00127.1};
OS Vibrio sp. RC586.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675815 {ECO:0000313|EMBL:EEZ00127.1, ECO:0000313|Proteomes:UP000006226};
RN [1] {ECO:0000313|EMBL:EEZ00127.1, ECO:0000313|Proteomes:UP000006226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RC586 {ECO:0000313|EMBL:EEZ00127.1,
RC ECO:0000313|Proteomes:UP000006226};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Chertkov O., Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C.,
RA Bruce D., Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A.,
RA Bartels D., Vonstein V.;
RL Submitted (NOV-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: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|HAMAP-Rule:MF_01271}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_01271}.
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DR EMBL; ADBD01000007; EEZ00127.1; -; Genomic_DNA.
DR RefSeq; WP_000291346.1; NZ_ADBD01000007.1.
DR AlphaFoldDB; D0IEX4; -.
DR eggNOG; COG1940; Bacteria.
DR OrthoDB; 9810372at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000006226; 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};
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 302 AA; 32702 MW; 4878E27CBBAC4941 CRC64;
MYYGFDVGGT KIEFGAFNEH LERVATERVP TPTDDYAKLI DTIAGLVQKY DAQFGVEGTV
GLGIPGMEDA DDGCVLTVNV PAAKGKPLRA DLEVKLGRTV KVENDANCFA LSEAWDDELK
EATSVMGLIL GTGFGGGLVY EGKVFSGRNH VAGEIGHMRL PIDAWFHLGE KAPLLSCGCG
NKGCMDNYLS GRGFELLYEH YYGEKKKAIE IITAQKEGEA KAVEHVERFM ELLAICFGNI
FTANDPHVVV LGGGLSNYDL IYEEMPKRVP KHLLSVAKCP KIVKAKHGDS GGVRGAAFLN
IK
//