AGAK_SHESA
ID AGAK_SHESA Reviewed; 308 AA.
AC A0KYQ6;
DT 27-MAY-2015, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=N-acetylgalactosamine kinase AgaK {ECO:0000303|PubMed:22711537};
DE Short=GalNAc kinase {ECO:0000303|PubMed:22711537};
DE EC=2.7.1.- {ECO:0000269|PubMed:22711537};
DE AltName: Full=N-acetylglucosamine kinase {ECO:0000303|PubMed:22711537};
DE Short=GlcNAc kinase {ECO:0000305|PubMed:22711537};
DE EC=2.7.1.59 {ECO:0000269|PubMed:22711537};
GN Name=agaK {ECO:0000303|PubMed:22711537}; OrderedLocusNames=Shewana3_2698;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBSTRATE
RP SPECIFICITY.
RC STRAIN=ANA-3;
RX PubMed=22711537; DOI=10.1074/jbc.m112.382333;
RA Leyn S.A., Gao F., Yang C., Rodionov D.A.;
RT "N-acetylgalactosamine utilization pathway and regulon in proteobacteria:
RT genomic reconstruction and experimental characterization in Shewanella.";
RL J. Biol. Chem. 287:28047-28056(2012).
CC -!- FUNCTION: Involved in the pathway of N-acetyl-D-galactosamine
CC degradation. Catalyzes the phosphorylation of N-acetyl-D-galactosamine
CC (GalNAc) to yield D-galactosamine 6-phosphate (GalN-6-P). It can also
CC phosphorylate N-acetylglucosamine (GlcNAc).
CC {ECO:0000269|PubMed:22711537}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + N-acetyl-D-galactosamine = ADP + H(+) + N-acetyl-D-
CC galactosamine 6-phosphate; Xref=Rhea:RHEA:47676, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:28037, ChEBI:CHEBI:30616, ChEBI:CHEBI:71673,
CC ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:22711537};
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:0000269|PubMed:22711537};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.98 mM for GalNAc {ECO:0000269|PubMed:22711537};
CC KM=37.2 mM for GlcNAc {ECO:0000269|PubMed:22711537};
CC Note=kcat is 40.3 sec(-1) for kinase activity with GalNAc as
CC substrate. kcat is 7.1 sec(-1) for kinase activity with GlcNAc as
CC substrate. {ECO:0000269|PubMed:22711537};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:22711537}.
CC -!- MISCELLANEOUS: In Shewanella sp., the active phosphotransferase system
CC (PTS) specific for the transport of GalNAc and GalN is replaced by a
CC set of GalNAc- and GalN-specific permeases and kinases (AgaP and AgaK,
CC respectively). {ECO:0000305|PubMed:22711537}.
CC -!- SIMILARITY: Belongs to the ROK (NagC/XylR) family. {ECO:0000305}.
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DR EMBL; CP000469; ABK48925.1; -; Genomic_DNA.
DR RefSeq; WP_011717582.1; NC_008577.1.
DR AlphaFoldDB; A0KYQ6; -.
DR SMR; A0KYQ6; -.
DR STRING; 94122.Shewana3_2698; -.
DR EnsemblBacteria; ABK48925; ABK48925; Shewana3_2698.
DR KEGG; shn:Shewana3_2698; -.
DR eggNOG; COG1940; Bacteria.
DR HOGENOM; CLU_036604_0_3_6; -.
DR OMA; GEWGHNV; -.
DR OrthoDB; 1130699at2; -.
DR BioCyc; MetaCyc:MON-17510; -.
DR SABIO-RK; A0KYQ6; -.
DR Proteomes; UP000002589; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0045127; F:N-acetylglucosamine kinase activity; IDA:UniProtKB.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR InterPro; IPR043129; ATPase_NBD.
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 ATP-binding; Carbohydrate metabolism; Cytoplasm; Kinase; Metal-binding;
KW Nucleotide-binding; Transferase; Zinc.
FT CHAIN 1..308
FT /note="N-acetylgalactosamine kinase AgaK"
FT /id="PRO_5000165395"
FT BINDING 4..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 132..139
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 156
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPZ9"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPZ9"
FT BINDING 176
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPZ9"
FT BINDING 181
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q8ZPZ9"
SQ SEQUENCE 308 AA; 32282 MW; 297D1A85B672DCA8 CRC64;
MYYGLDIGGT KIELAIFDTQ LALQDKWRLS TPGQDYSAFM ATLAEQIEKA DQQCGERGTV
GIALPGVVKA DGTVISSNVP CLNQRRVAHD LAQLLNRTVA IGNDCRCFAL SEAVLGVGRG
YSRVLGMILG TGTGGGLCID GKLYLGANRL AGEFGHQGVS ANVACRHQLP LYVCGCGLEG
CAETYVSGTG LGRLYQDIAG QTADTFAWLN ALRCNDPLAI KTFDTYMDIL GSLMASLVLA
MDPDIIVLGG GLSEVEEILA ALPQATKAHL FDGVTLPQFK LADFGSASGV RGAALLGHGL
DAGISYEA
