GenomeNet

Database: UniProt
Entry: D0IEX4_9VIBR
LinkDB: D0IEX4_9VIBR
Original site: D0IEX4_9VIBR 
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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
//
DBGET integrated database retrieval system