ID A0A254N2N4_9BURK Unreviewed; 632 AA.
AC A0A254N2N4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 31.
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=CDO81_19775 {ECO:0000313|EMBL:OWR02429.1};
OS Roseateles puraquae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Roseateles.
OX NCBI_TaxID=431059 {ECO:0000313|EMBL:OWR02429.1, ECO:0000313|Proteomes:UP000197446};
RN [1] {ECO:0000313|EMBL:OWR02429.1, ECO:0000313|Proteomes:UP000197446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 52769 {ECO:0000313|EMBL:OWR02429.1,
RC ECO:0000313|Proteomes:UP000197446};
RX PubMed=17978231; DOI=10.1099/ijs.0.65149-0;
RA Gomila M., Bowien B., Falsen E., Moore E.R., Lalucat J.;
RT "Description of Pelomonas aquatica sp. nov. and Pelomonas puraquae sp.
RT nov., isolated from industrial and haemodialysis water.";
RL Int. J. Syst. Evol. Microbiol. 57:2629-2635(2007).
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: 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:OWR02429.1}.
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DR EMBL; NISI01000009; OWR02429.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A254N2N4; -.
DR OrthoDB; 257751at2; -.
DR Proteomes; UP000197446; 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 Reference proteome {ECO:0000313|Proteomes:UP000197446};
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 333..409
FT /note="HTH rpiR-type"
FT /evidence="ECO:0000259|PROSITE:PS51071"
FT DOMAIN 453..592
FT /note="SIS"
FT /evidence="ECO:0000259|PROSITE:PS51464"
FT REGION 597..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00524"
SQ SEQUENCE 632 AA; 67528 MW; DDD5E2B61D81B6F5 CRC64;
MPRFDSPRLL ADIGGTYARF ALETGPGEFT QMASLRCADH ADFHAAVRAY LESLNWPEGA
QQIAHAAVAI ANPVEGDRVR MTNYHWQFSI DEMRQRLGFD TLVVVNDFTA LAMALPRLAE
VDVRQVGGGQ ARRPSVIGLL GAGTGLGVSG LIPAGEGWIA LGTEGGHVNF GPRDEREMDI
LKFAWQTLDH VSYERLISGP GLELIHRALA ARHGVDAPTL QAPAITQRAL DEGDALCLET
LEVFCGLLGT AAANLAVTLG SLGGIYIGGG IVPRLGEYFD RSPFRARFED KGRFRDYVSA
IPTFVITAEN ATFKGASAIL ENQLRNLQAS PGSAILGQIR RARSELSPAE LRVADLVLAQ
PRSVLNDPIA EIARAAGVSQ PTVIRFCRSL GCEGLSDFKL RLASGLTGTV PVTHTQVNTN
DSMLELGAKV LGNTASAILQ VRSHLNRDTI DRAIDLLLSA HRIEFFALGH YSVVAQDAQF
KFLRFGMPCG AYTDPRLQLL AADVLREGDV AVVISSGGRL PELLSVVEKA QERGAKVVAI
TASQSPLAKK ADVTLIVDHI EDIATHLPMV SRILHLLVID ILAVGVAMRR SPDSIAALGD
GPDEEVAKSG RSGAAPGVST ASPLARLTSH SR
//
