GLCNK_STRJI
ID GLCNK_STRJI Reviewed; 438 AA.
AC A0A1H7TQR5;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2017, sequence version 1.
DT 03-AUG-2022, entry version 17.
DE RecName: Full=Glucosamine kinase {ECO:0000303|PubMed:31088917};
DE Short=GlcN kinase {ECO:0000303|PubMed:31088917};
DE Short=GlcNK {ECO:0000303|PubMed:31088917};
DE EC=2.7.1.8 {ECO:0000269|PubMed:31088917};
GN ORFNames=SAMN05414137_114149 {ECO:0000312|EMBL:SEL87111.1};
OS Streptacidiphilus jiangxiensis.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptacidiphilus.
OX NCBI_TaxID=235985;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277 /
RC KCTC 19219 / NBRC 100920 / 33214;
RA Varghese N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.98 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP ADP; PHOSPHATE; GLUCOSAMINE AND MAGNESIUM, FUNCTION, CATALYTIC ACTIVITY,
RP SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBUNIT,
RP AND MUTAGENESIS OF GLN-405.
RC STRAIN=DSM 45096 / BCRC 16803 / CGMCC 4.1857 / CIP 109030 / JCM 12277 /
RC KCTC 19219 / NBRC 100920 / 33214;
RX PubMed=31088917; DOI=10.1128/mbio.00239-19;
RA Manso J.A., Nunes-Costa D., Macedo-Ribeiro S., Empadinhas N.,
RA Pereira P.J.B.;
RT "Molecular Fingerprints for a Novel Enzyme Family in Actinobacteria with
RT Glucosamine Kinase Activity.";
RL MBio 10:0-0(2019).
CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of D-glucosamine
CC (GlcN) to D-glucosamine 6-phosphate. May be involved in the
CC phosphorylation of acquired extracellular GlcN derived from the
CC hydrolysis of chitosan, i.e., in the incorporation of exogenous GlcN
CC into the bacterial GlcNAc metabolism. To a lesser extent, is also
CC active on glucose, but is unable to phosphorylate maltose, 18 other
CC sugars and several aminoglycoside antibiotics.
CC {ECO:0000269|PubMed:31088917}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucosamine = ADP + D-glucosamine 6-phosphate + H(+);
CC Xref=Rhea:RHEA:10948, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58723, ChEBI:CHEBI:58725, ChEBI:CHEBI:456216; EC=2.7.1.8;
CC Evidence={ECO:0000269|PubMed:31088917};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:31088917};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:31088917};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 mM for D-glucosamine {ECO:0000269|PubMed:31088917};
CC KM=100 mM for D-glucose {ECO:0000269|PubMed:31088917};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:31088917}.
CC -!- SIMILARITY: Belongs to the actinobacterial glucosamine kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_02218, ECO:0000305|PubMed:31088917}.
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; FOAZ01000014; SEL87111.1; -; Genomic_DNA.
DR PDB; 6HWJ; X-ray; 1.98 A; A/B=1-438.
DR PDB; 6HWK; X-ray; 2.69 A; A/B/C/D=1-438.
DR PDB; 6HWL; X-ray; 2.15 A; A/B=1-438.
DR PDBsum; 6HWJ; -.
DR PDBsum; 6HWK; -.
DR PDBsum; 6HWL; -.
DR AlphaFoldDB; A0A1H7TQR5; -.
DR SASBDB; A0A1H7TQR5; -.
DR SMR; A0A1H7TQR5; -.
DR STRING; 235985.BBPN01000035_gene745; -.
DR EnsemblBacteria; SEL87111; SEL87111; SAMN05414137_114149.
DR eggNOG; COG3281; Bacteria.
DR BRENDA; 2.7.1.8; 17853.
DR Proteomes; UP000183015; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0047931; F:glucosamine kinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_02218; GlcN_kinase; 1.
DR InterPro; IPR043674; GlcN_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Carbohydrate metabolism; Kinase; Magnesium;
KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..438
FT /note="Glucosamine kinase"
FT /id="PRO_0000447645"
FT MOTIF 405..420
FT /note="Substrate specificity determinant motif"
FT /evidence="ECO:0000305|PubMed:31088917"
FT BINDING 133
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:31088917"
FT BINDING 186..188
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:31088917"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000305|PubMed:31088917"
FT BINDING 300
FT /ligand="D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:58723"
FT /evidence="ECO:0000269|PubMed:31088917"
FT BINDING 305
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31088917"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:31088917"
FT BINDING 317
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31088917"
FT BINDING 319
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:31088917"
FT BINDING 409
FT /ligand="D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:58723"
FT /evidence="ECO:0000269|PubMed:31088917"
FT MUTAGEN 405
FT /note="Q->A: Marked decrease of the GlcN-phosphorylating
FT activity of the enzyme, while no effect is observed for
FT glucose."
FT /evidence="ECO:0000269|PubMed:31088917"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 14..17
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 25..27
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 57..65
FT /evidence="ECO:0007829|PDB:6HWJ"
FT TURN 66..68
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 79..88
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 98..102
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 112..115
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 123..126
FT /evidence="ECO:0007829|PDB:6HWJ"
FT TURN 127..129
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 148..157
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 166..172
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 179..186
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 194..206
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 212..234
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 243..263
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 266..284
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 285..289
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:6HWJ"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 326..328
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 335..356
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 362..386
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 390..392
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 395..397
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 398..416
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 418..421
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 422..431
FT /evidence="ECO:0007829|PDB:6HWJ"
FT HELIX 434..438
FT /evidence="ECO:0007829|PDB:6HWL"
SQ SEQUENCE 438 AA; 46730 MW; 217B20AD9A777FA6 CRC64;
MTPNWSELVA AADPALVLPS GERRAEVAVP GPLRLDALLD LGEGHAVGVV RSADAARWTV
PLVRDGAGGV RRSRPGDGTA EHLVAALARR GATPDAAFVL EAFTGAAPVT GERGIIVDQT
NESVIVGECA VVKWAVRLPA EGEPGSPAAQ RIAALARGGF TEMPRPWGLL TLAEGAQPVL
LASVVAYLPG ALDGWDWAVD DVRRLARGEL TMDQALLPAA QLGTLTARMH AALAARGRTP
ATAADVAAWG VRMREELDEA VASVPGAEGE RLKAWAPRIA DVYAELDALA GTPLIDVHGD
FHVGQILRAD GRYAVVDFDG NPVLPADQRA ARQPAALDVV GMTASLDHVG RVVVFRTPDV
DPAPVRAWIA AAQRSFLDAY RTTLARLDAD DLFDDRLLTP LRYAQEVREY LYAVRHLPHW
VYVPDLSLTD LLPERLKD
