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Entry: A0A132PT41_9MYCO
LinkDB: A0A132PT41_9MYCO
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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
//
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