ID A0A0N1B3V3_9PROT Unreviewed; 619 AA.
AC A0A0N1B3V3;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=Glucokinase {ECO:0000256|HAMAP-Rule:MF_00524};
DE EC=2.7.1.2 {ECO:0000256|HAMAP-Rule:MF_00524};
DE AltName: Full=Glucose kinase {ECO:0000256|HAMAP-Rule:MF_00524};
GN Name=glk {ECO:0000256|HAMAP-Rule:MF_00524};
GN ORFNames=IP84_15915 {ECO:0000313|EMBL:KPF66480.1};
OS beta proteobacterium AAP99.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1523428 {ECO:0000313|EMBL:KPF66480.1, ECO:0000313|Proteomes:UP000037960};
RN [1] {ECO:0000313|EMBL:KPF66480.1, ECO:0000313|Proteomes:UP000037960}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP99 {ECO:0000313|EMBL:KPF66480.1,
RC ECO:0000313|Proteomes:UP000037960};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-glucose = ADP + D-glucose 6-phosphate + H(+);
CC Xref=Rhea:RHEA:17825, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61548, ChEBI:CHEBI:456216; EC=2.7.1.2;
CC Evidence={ECO:0000256|ARBA:ARBA00001632, ECO:0000256|HAMAP-
CC Rule:MF_00524};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524}.
CC -!- SIMILARITY: Belongs to the bacterial glucokinase family.
CC {ECO:0000256|HAMAP-Rule:MF_00524}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the bacterial
CC glucokinase family. {ECO:0000256|ARBA:ARBA00007693}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00524}.
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:KPF66480.1}.
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DR EMBL; LJIA01000021; KPF66480.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0N1B3V3; -.
DR STRING; 1523428.IP84_15915; -.
DR PATRIC; fig|1523428.3.peg.2067; -.
DR OrthoDB; 257751at2; -.
DR Proteomes; UP000037960; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0004340; F:glucokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005536; F:glucose binding; IEA:InterPro.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR CDD; cd05013; SIS_RpiR; 1.
DR Gene3D; 3.30.420.40; -; 1.
DR Gene3D; 3.40.367.20; -; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR HAMAP; MF_00524; Glucokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR003836; Glucokinase.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR000281; HTH_RpiR.
DR InterPro; IPR035472; RpiR-like_SIS.
DR InterPro; IPR001347; SIS_dom.
DR InterPro; IPR046348; SIS_dom_sf.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR NCBIfam; TIGR00749; glk; 1.
DR PANTHER; PTHR47690; GLUCOKINASE; 1.
DR PANTHER; PTHR47690:SF1; GLUCOKINASE; 1.
DR Pfam; PF02685; Glucokinase; 1.
DR Pfam; PF01418; HTH_6; 1.
DR Pfam; PF01380; SIS; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 1.
DR SUPFAM; SSF53697; SIS domain; 1.
DR PROSITE; PS00356; HTH_LACI_1; 1.
DR PROSITE; PS51071; HTH_RPIR; 1.
DR PROSITE; PS51464; SIS; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00524};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Glycolysis {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_00524}; Kinase {ECO:0000256|HAMAP-Rule:MF_00524};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
KW Reference proteome {ECO:0000313|Proteomes:UP000037960};
KW Transcription {ECO:0000256|ARBA:ARBA00023163};
KW Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00524}.
FT DOMAIN 327..403
FT /note="HTH rpiR-type"
FT /evidence="ECO:0000259|PROSITE:PS51071"
FT DOMAIN 447..586
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 598..619
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..619
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 619 AA; 66642 MW; 61C0BCB51EACBD2E CRC64;
MAFSDGARLL ADIGSTFARF AVERERGRFE RLETLRCADY PDFGSALKAY LAMVEDMDVR
HGAVAISNPV EGDLVRMTNY HWQFSIEQTR LDCGLDTLLV VNDFTALAVG VPHLREDQRR
QIGGGQARAR SVIGLLGAGT GLGVSGLIPA DDGWISLGSE GGHVSFSPTD EREAAILEFA
WTQYSHVSAE RLLSGSGLEL IYKALCHLAG KPAEVLSALD ITSRGLSKQC ALCEQTLEVF
CGMLGAVAAN LAVTLGAFGG IYIGGAIVPR LGEYFDQSAF RRRFESKGRF SGFVASIPTY
VITADQATFI GVAAILDAQL RKRSGGASIL DRIRQLHREL SPAERRVADV VLSRPRSILN
DPIMEIARAA DVSQPTVIRF CRTLGCEGLS DFKLRLASSL TGTIPVTHTQ VTVEDTALEL
GAKVLGNTAS AILQIRDQLN RKAIDQAIEL LLKAKRIDFY AVGNYGIVAE DAQYKFLRFG
LPTAAHTEPR LQLMAANVLT PDDVLVVISS TGRIPELNAA VDAALERGAQ VVAITANQSP
LSKKATITIA LDHSEDVATQ VPMISRVLYL LVIDILAVGV AMRAGLTDEL GTSELAEAMD
PSEAGSEHRL ARMVSHSQR
//
