ID A0A085UA55_YERRU Unreviewed; 331 AA.
AC A0A085UA55;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE RecName: Full=N-acetyl-D-glucosamine kinase {ECO:0000256|ARBA:ARBA00014974, ECO:0000256|HAMAP-Rule:MF_01271};
DE EC=2.7.1.59 {ECO:0000256|ARBA:ARBA00012122, ECO:0000256|HAMAP-Rule:MF_01271};
DE AltName: Full=GlcNAc kinase {ECO:0000256|ARBA:ARBA00031123, ECO:0000256|HAMAP-Rule:MF_01271};
GN Name=nagK {ECO:0000256|HAMAP-Rule:MF_01271,
GN ECO:0000313|EMBL:SUP99408.1};
GN ORFNames=CSF007_7465 {ECO:0000313|EMBL:CEK27249.1}, NCTC10476_00638
GN {ECO:0000313|EMBL:SUP99408.1};
OS Yersinia ruckeri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=29486 {ECO:0000313|EMBL:CEK27249.1};
RN [1] {ECO:0000313|EMBL:CEK27249.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CSF007-82 {ECO:0000313|EMBL:CEK27249.1};
RA Nelson M.C., LaPatra S.E., Welch T.J., Graf J.;
RT "Complete Genome Sequence of Yersinia ruckeri Strain CSF007-82, Etiologic
RT Agent of Red Mouth Disease in Salmonid Fish.";
RL Genome Announc. 3:1-2(2015).
RN [2] {ECO:0000313|EMBL:SUP99408.1, ECO:0000313|Proteomes:UP000255169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC10476 {ECO:0000313|EMBL:SUP99408.1,
RC ECO:0000313|Proteomes:UP000255169};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) 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|ARBA:ARBA00037880, ECO:0000256|HAMAP-Rule:MF_01271}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. NagK subfamily.
CC {ECO:0000256|ARBA:ARBA00038116, ECO:0000256|HAMAP-Rule:MF_01271}.
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DR EMBL; LN681231; CEK27249.1; -; Genomic_DNA.
DR EMBL; UHJG01000001; SUP99408.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A085UA55; -.
DR STRING; 29486.UGYR_00380; -.
DR PATRIC; fig|29486.44.peg.783; -.
DR eggNOG; COG1940; Bacteria.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000255169; 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:CEK27249.1};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_01271};
KW Reference proteome {ECO:0000313|Proteomes:UP000255169};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_01271, ECO:0000313|EMBL:CEK27249.1};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|HAMAP-Rule:MF_01271}.
FT BINDING 29..36
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 157..164
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 201
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 203
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
FT BINDING 208
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01271"
SQ SEQUENCE 331 AA; 36506 MW; DB8ABEBD38414998 CRC64;
MAYQYEYFSE RRMVLINPLL NKGGHMYYGF DMGGTKIELG IFDADLQRIW HKRVATPKQD
YSQLLQVFTE LTHEADVFCG TQGSVGIGIP GLPNDDGTLF TANVPAAMGK PLQADLCRIL
EREVRIDNDA NCFALSEAWD PEFQAYPSVL GIILGTGVGG GIILNGQVVT GRNHIAGEFG
HFRLPLDTLD VLGADIPRVT CGCGQRGCIE NYISGRGFEW MYAHFYGHAL PAAQIIEYYY
AGNVQAIEHV ERFMAVLAIC LGNLLTILDP HLVVIGGGLS NFEHLYQELE QRLPAHLLPV
ARLPRIEKAR YGDAGGVRGA AFLHLSDRNP L
//
