ID A0A1Q9HF59_9VIBR Unreviewed; 302 AA.
AC A0A1Q9HF59;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
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 ECO:0000313|EMBL:KAB1455503.1};
GN ORFNames=BIY22_09425 {ECO:0000313|EMBL:OLQ88372.1}, F7O85_15910
GN {ECO:0000313|EMBL:KAB1455503.1};
OS Vibrio panuliri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ88372.1, ECO:0000313|Proteomes:UP000186313};
RN [1] {ECO:0000313|EMBL:OLQ88372.1, ECO:0000313|Proteomes:UP000186313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ88372.1,
RC ECO:0000313|Proteomes:UP000186313};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAB1455503.1, ECO:0000313|Proteomes:UP000446972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBS 2 {ECO:0000313|EMBL:KAB1455503.1,
RC ECO:0000313|Proteomes:UP000446972};
RA Das S.S.;
RT "Whole genome sequence of Vibrio panuliri LBS 2.";
RL Submitted (SEP-2019) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OLQ88372.1}.
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DR EMBL; WAHU01000009; KAB1455503.1; -; Genomic_DNA.
DR EMBL; MJMJ01000023; OLQ88372.1; -; Genomic_DNA.
DR RefSeq; WP_075709544.1; NZ_WAHU01000009.1.
DR AlphaFoldDB; A0A1Q9HF59; -.
DR STRING; 1381081.BIY22_09425; -.
DR OrthoDB; 9810372at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000186313; Unassembled WGS sequence.
DR Proteomes; UP000446972; 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, ECO:0000313|EMBL:OLQ88372.1};
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 ECO:0000313|EMBL:KAB1455503.1};
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; 32896 MW; 980AAF4B44EE0030 CRC64;
MYYGFDVGGT KIEFGAFNEQ LERVATERVP TPTSDYQELL SAIAGLVSKY DQEFNCEGKI
GLGLPGMEDA DNGTILTVNI PAAKGMPLRK DLEAKIGRSV RIENDANCFA LSEAWDEELK
DSPSVMGLIL GTGFGGGLIY DGKPFSGRNN VAGEMGHMRL PIDAWFHLGE NAPLLDCGCD
KKGCIDNYLS GRGFELLYAH YYGEEKKAID IIKAQAEGEP KAVEHVERFM ELLAICFANL
FTANDPHVVV LGGGLSNYDL IYEEMPKRIP KHLLSVAKCP KIVKAKHGDS GGVRGAAFLN
IK
//
