ID   GSPK_VIBCH              Reviewed;         294 AA.
AC   Q9KUA9;
DT   05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2012, sequence version 2.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Glucosamine kinase GspK;
DE            EC=2.7.1.8;
DE   AltName: Full=GlcN kinase;
GN   Name=gspK; OrderedLocusNames=VC_0614;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, SUBCELLULAR LOCATION, AND GENE NAME.
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=11850417; DOI=10.1074/jbc.m107953200;
RA   Park J.K., Wang L.X., Roseman S.;
RT   "Isolation of a glucosamine-specific kinase, a unique enzyme of Vibrio
RT   cholerae.";
RL   J. Biol. Chem. 277:15573-15578(2002).
CC   -!- FUNCTION: ATP-dependent kinase, which is specific for glucosamine. Does
CC       not show kinase activity with any other sugar.
CC       {ECO:0000269|PubMed:11850417}.
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:11850417};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.48 mM for glucosamine {ECO:0000269|PubMed:11850417};
CC         KM=1.96 mM for ATP {ECO:0000269|PubMed:11850417};
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:11850417};
CC       Temperature dependence:
CC         Optimum temperature is 40-42 degrees Celsius.
CC         {ECO:0000269|PubMed:11850417};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11850417}.
CC   -!- SIMILARITY: Belongs to the eukaryotic-type N-acetylglucosamine kinase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAF93780.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE003852; AAF93780.1; ALT_INIT; Genomic_DNA.
DR   PIR; B82301; B82301.
DR   RefSeq; NP_230263.1; NC_002505.1.
DR   RefSeq; WP_001110418.1; NZ_LT906614.1.
DR   AlphaFoldDB; Q9KUA9; -.
DR   SMR; Q9KUA9; -.
DR   STRING; 243277.VC_0614; -.
DR   DNASU; 2615402; -.
DR   EnsemblBacteria; AAF93780; AAF93780; VC_0614.
DR   GeneID; 57739331; -.
DR   KEGG; vch:VC_0614; -.
DR   PATRIC; fig|243277.26.peg.585; -.
DR   eggNOG; COG2971; Bacteria.
DR   HOGENOM; CLU_016274_2_0_6; -.
DR   BioCyc; MetaCyc:MON-16888; -.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0047931; F:glucosamine kinase activity; IDA:UniProtKB.
DR   GO; GO:0016310; P:phosphorylation; IDA:UniProtKB.
DR   InterPro; IPR002731; ATPase_BadF.
DR   InterPro; IPR043129; ATPase_NBD.
DR   Pfam; PF01869; BcrAD_BadFG; 1.
DR   SUPFAM; SSF53067; SSF53067; 2.
PE   1: Evidence at protein level;
KW   ATP-binding; Cytoplasm; Direct protein sequencing; Kinase;
KW   Nucleotide-binding; Reference proteome; Transferase.
FT   CHAIN           1..294
FT                   /note="Glucosamine kinase GspK"
FT                   /id="PRO_0000418396"
FT   BINDING         12
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         122
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         139..141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         146
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
FT   BINDING         202
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250|UniProtKB:Q9UJ70"
SQ   SEQUENCE   294 AA;  31565 MW;  384D07667E25C90F CRC64;
     MNYYVGIDGG GTSCRARIRN QQGEWVGEAK SGSANIMLGV EVALRSVVDA ITQAAEQGGL
     SPDDFPSMHV GLALAGAEQK EAWHAFMQQA HPFASITLNT DAYGACLGAH LGEEGAIMIA
     GTGSCGILLK GGKQYVVGGR EFPISDQGSG AVMGLRLIQQ VLLAQDGIRP HTPLCDVVMN
     HFNHDIDSIV AWSKTALPRD YGQFSPQIFS HAYCGDPLAI ELLKQTAADI EMFLIALHHK
     GAERICLMGS IAERIQDWLS PPVQQWIVKP QSDAIEGALM FAGKPEHNLY KDGL