ID A0A0Q5D1U1_9BURK Unreviewed; 623 AA.
AC A0A0Q5D1U1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 50.
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=ASF61_10885 {ECO:0000313|EMBL:KQQ33571.1};
OS Duganella sp. Leaf126.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Duganella.
OX NCBI_TaxID=1736266 {ECO:0000313|EMBL:KQQ33571.1, ECO:0000313|Proteomes:UP000051032};
RN [1] {ECO:0000313|EMBL:KQQ33571.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33571.1};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ33571.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf126 {ECO:0000313|EMBL:KQQ33571.1};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQQ33571.1}.
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DR EMBL; LMNW01000031; KQQ33571.1; -; Genomic_DNA.
DR RefSeq; WP_056157323.1; NZ_LMNW01000031.1.
DR AlphaFoldDB; A0A0Q5D1U1; -.
DR STRING; 1736266.ASF61_10885; -.
DR OrthoDB; 257751at2; -.
DR Proteomes; UP000051032; 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};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000256|HAMAP-Rule:MF_00524};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00524};
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 339..415
FT /note="HTH rpiR-type"
FT /evidence="ECO:0000259|PROSITE:PS51071"
FT DOMAIN 459..598
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
SQ SEQUENCE 623 AA; 67271 MW; 3542EB37D7B7ACD8 CRC64;
MKQAEVDQKL NRTAFADGPR LLADIGATHA RFALQTAPGD FRAVRVLKCD DYADIVAMLR
SYLADHADLT LHHGALAVAN PVSGDYIRMT NRDWEFSTDE VRRALGLHTL LVVNDFTALA
MSLPGLKPAD LMQVGGGKPA SNSVIGVLGP GTGLGVSGVI PTVDGFVTLG SEGGHTNFAP
ADEREYAILQ YAWQTWSHVS TERLISGPGM EIIYRAIAKR NGRQVRDLTS QEIMAGALTD
RDPLCLEVLE CFCAMLGGAS ANLAVTLGAF GGMFIGGGIV PRMGEWFAQS PFRSRFEAKG
RFTSYLSEIP TYVITTPNPA FYGVATILSE HLRGRSGANT LMERVRHLQH ELTPAEQRVA
QLVLEQPRLV LNEPIADIAR LAEVSQPTVI RFCRSLGFLG LADFKLKFAS SLTGAIPVRH
SQVRVSDSTH DLSAKVIDNT VSAILKFRDQ LDVRSIDKAI ALVAKAKRVE FYAMGNSRVV
ALDGQHKFFR FRIPTSAYGD SHLLNLAAEL LKPGDVVIAI SNSGKLNDLL EAVDVARAAG
ADVIAITASN SPLAKKASVC LAVDHSEDST TFLSMISRIL QLLLIDILSV GISLDAQNGK
LVIEHKAKGE ADGRRLMISH LDG
//
