GLCNK_MYCS2
ID GLCNK_MYCS2 Reviewed; 399 AA.
AC I7FJX8;
DT 31-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2012, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 OrderedLocusNames=MSMEI_5186 {ECO:0000312|EMBL:AFP41630.1};
OS Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium
OS smegmatis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=246196;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=17295914; DOI=10.1186/gb-2007-8-2-r20;
RA Deshayes C., Perrodou E., Gallien S., Euphrasie D., Schaeffer C.,
RA Van-Dorsselaer A., Poch O., Lecompte O., Reyrat J.-M.;
RT "Interrupted coding sequences in Mycobacterium smegmatis: authentic
RT mutations or sequencing errors?";
RL Genome Biol. 8:R20.1-R20.9(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700084 / mc(2)155;
RX PubMed=18955433; DOI=10.1101/gr.081901.108;
RA Gallien S., Perrodou E., Carapito C., Deshayes C., Reyrat J.-M.,
RA Van Dorsselaer A., Poch O., Schaeffer C., Lecompte O.;
RT "Ortho-proteogenomics: multiple proteomes investigation through orthology
RT and a new MS-based protocol.";
RL Genome Res. 19:128-135(2009).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL
RP PROPERTIES.
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. Is unable to phosphorylate
CC maltose. {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:0000250|UniProtKB:A0A1H7TQR5};
CC Note=Binds 2 Mg(2+) ions per subunit.
CC {ECO:0000250|UniProtKB:A0A1H7TQR5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=14 mM for D-glucosamine {ECO:0000269|PubMed:31088917};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:A0A1H7TQR5}.
CC -!- SIMILARITY: Belongs to the actinobacterial glucosamine kinase family.
CC {ECO:0000255|HAMAP-Rule:MF_02218, ECO:0000305|PubMed:31088917}.
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DR EMBL; CP001663; AFP41630.1; -; Genomic_DNA.
DR RefSeq; WP_003896729.1; NZ_SIJM01000014.1.
DR AlphaFoldDB; I7FJX8; -.
DR SMR; I7FJX8; -.
DR STRING; 246196.MSMEI_5186; -.
DR EnsemblBacteria; AFP41630; AFP41630; MSMEI_5186.
DR GeneID; 66736639; -.
DR KEGG; msg:MSMEI_5186; -.
DR PATRIC; fig|246196.56.peg.5306; -.
DR OrthoDB; 268166at2; -.
DR BRENDA; 2.7.1.8; 3512.
DR Proteomes; UP000006158; Chromosome.
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 ATP-binding; Carbohydrate metabolism; Kinase; Magnesium; Metal-binding;
KW Nucleotide-binding; Transferase.
FT CHAIN 1..399
FT /note="Glucosamine kinase"
FT /id="PRO_0000447644"
FT MOTIF 366..381
FT /note="Substrate specificity determinant motif"
FT /evidence="ECO:0000305|PubMed:31088917"
FT BINDING 98
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 149..151
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 156
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 262
FT /ligand="D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:58723"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 267
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 279
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 281
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
FT BINDING 370
FT /ligand="D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:58723"
FT /evidence="ECO:0000250|UniProtKB:A0A1H7TQR5"
SQ SEQUENCE 399 AA; 42337 MW; 8397526BC1B4CD91 CRC64;
MIELDRLDLG GGRRLVITSE PDAAVPQVRD ADGHWRRAGP GDGVAEAMLD ALNQNPGTTK
HGNFTLLSWA SQTARGERPI TVDQTNESVI VGDAAVVKWA THLQEGPHPA PARIKALRGN
GFRGMPMPWG LVTWQTADHP ETLVVTVDEY LPDAVDGWTW AVALVTDAAQ DRAAVPALVD
AVTAVGCVVA ELHAAQADTA RPATAADARS WREAALETVE TAATLGTSVS GELLRARRED
VEAVVGTLGD LAGIPVLAGH GDLHVGQVLR AGGRYVVTDF DGNPVLPAEA RVKPVPAALD
VAGMAQSLAH VAIVACKYTE LAPAALADVD RLARTTFVGA YTDRLETLGH RSVYDPAPLR
ALRLQQVLRE IIYAARHLPR WMYVPDAALP ALLDEGTST
