ID A0A132PT41_9MYCO Unreviewed; 400 AA.
AC A0A132PT41;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE RecName: Full=Glucosamine kinase {ECO:0000256|HAMAP-Rule:MF_02218};
DE Short=GlcN kinase {ECO:0000256|HAMAP-Rule:MF_02218};
DE Short=GlcNK {ECO:0000256|HAMAP-Rule:MF_02218};
DE EC=2.7.1.8 {ECO:0000256|HAMAP-Rule:MF_02218};
GN ORFNames=AFM11_04505 {ECO:0000313|EMBL:KWX25509.1};
OS Mycolicibacterium wolinskyi.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=59750 {ECO:0000313|EMBL:KWX25509.1, ECO:0000313|Proteomes:UP000070612};
RN [1] {ECO:0000313|EMBL:KWX25509.1, ECO:0000313|Proteomes:UP000070612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC_01 {ECO:0000313|EMBL:KWX25509.1,
RC ECO:0000313|Proteomes:UP000070612};
RA de Man T.J., Perry K.A., Coulliette A.D., Jensen B., Toney N.C.,
RA Limbago B.M., Noble-Wang J.;
RT "A draft genome sequence of Mycobacterium wolinskyi.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-
CC Rule:MF_02218}.
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:0000256|HAMAP-Rule:MF_02218};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_02218};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_02218};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_02218}.
CC -!- SIMILARITY: Belongs to the actinobacterial glucosamine kinase family.
CC {ECO:0000256|HAMAP-Rule:MF_02218}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_02218}.
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:KWX25509.1}.
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DR EMBL; LGTW01000002; KWX25509.1; -; Genomic_DNA.
DR RefSeq; WP_067844525.1; NZ_LGTW01000002.1.
DR AlphaFoldDB; A0A132PT41; -.
DR STRING; 59750.AWC31_20640; -.
DR PATRIC; fig|59750.3.peg.2779; -.
DR Proteomes; UP000070612; 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 Gene3D; 3.90.1200.10; -; 1.
DR HAMAP; MF_02218; GlcN_kinase; 1.
DR InterPro; IPR043674; GlcN_kinase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR NCBIfam; NF041273; GlcN_kinase; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_02218};
KW Carbohydrate metabolism {ECO:0000256|HAMAP-Rule:MF_02218};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_02218};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_02218};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_02218};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02218};
KW Reference proteome {ECO:0000313|Proteomes:UP000070612};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02218, ECO:0000313|EMBL:KWX25509.1}.
FT MOTIF 367..382
FT /note="Substrate specificity determinant motif"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 100
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 158
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 263
FT /ligand="D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:58723"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 268
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 280
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 282
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
FT BINDING 371
FT /ligand="D-glucosamine"
FT /ligand_id="ChEBI:CHEBI:58723"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02218"
SQ SEQUENCE 400 AA; 42477 MW; CA432DD2AE13AAD6 CRC64;
MIELDHLDLG PGRRLVVTTS PEGLAAVPAV RDPDGDWRRA RPGDGAAEAM LDMLCSVNGS
AKSGAFTVIS WTGRSAAGER PITVDQTNES VIVGDAAVVK WATHLQSGPH PAPHRISALR
AAGFRGMPAP WGLVTWQPAD GAETLVATID EYLPGAVDGW TWAVDLVTDA ARAGRPERIR
DAAADVGALI AELHAALAGT ASVADQTEVA RWRDAAFETL ETAVSLSASV CRAVLRDRRA
EIEQILDGLG DLGGTPVIEG HGDLHVGQVL LADGRFVITD FDGNPVLAAE ERMKPIPAAL
DVAGMVQSFA HVAIVARKYT ELDGATLAEV NTLTRSTLLD SYTTRLTELG HAESYDPAAL
RALRLQQVLR EIIYAARHLP RWMYVPDAAL PALLDEGSAP
//