GLPK_RHIME
ID GLPK_RHIME Reviewed; 497 AA.
AC O86033;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 18-OCT-2001, sequence version 2.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Glycerol kinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE EC=2.7.1.30 {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000255|HAMAP-Rule:MF_00186};
DE AltName: Full=Glycerokinase {ECO:0000255|HAMAP-Rule:MF_00186};
DE Short=GK {ECO:0000255|HAMAP-Rule:MF_00186};
GN Name=glpK {ECO:0000255|HAMAP-Rule:MF_00186}; OrderedLocusNames=RB1135;
GN ORFNames=SMb21009;
OS Rhizobium meliloti (strain 1021) (Ensifer meliloti) (Sinorhizobium
OS meliloti).
OG Plasmid pSymB (megaplasmid 2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=266834;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11481431; DOI=10.1073/pnas.161294698;
RA Finan T.M., Weidner S., Wong K., Buhrmester J., Chain P., Vorhoelter F.J.,
RA Hernandez-Lucas I., Becker A., Cowie A., Gouzy J., Golding B., Puehler A.;
RT "The complete sequence of the 1,683-kb pSymB megaplasmid from the N2-fixing
RT endosymbiont Sinorhizobium meliloti.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9889-9894(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1021;
RX PubMed=11474104; DOI=10.1126/science.1060966;
RA Galibert F., Finan T.M., Long S.R., Puehler A., Abola P., Ampe F.,
RA Barloy-Hubler F., Barnett M.J., Becker A., Boistard P., Bothe G.,
RA Boutry M., Bowser L., Buhrmester J., Cadieu E., Capela D., Chain P.,
RA Cowie A., Davis R.W., Dreano S., Federspiel N.A., Fisher R.F., Gloux S.,
RA Godrie T., Goffeau A., Golding B., Gouzy J., Gurjal M., Hernandez-Lucas I.,
RA Hong A., Huizar L., Hyman R.W., Jones T., Kahn D., Kahn M.L., Kalman S.,
RA Keating D.H., Kiss E., Komp C., Lelaure V., Masuy D., Palm C., Peck M.C.,
RA Pohl T.M., Portetelle D., Purnelle B., Ramsperger U., Surzycki R.,
RA Thebault P., Vandenbol M., Vorhoelter F.J., Weidner S., Wells D.H.,
RA Wong K., Yeh K.-C., Batut J.;
RT "The composite genome of the legume symbiont Sinorhizobium meliloti.";
RL Science 293:668-672(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-59.
RC STRAIN=SU47 / 1021;
RX PubMed=9922248; DOI=10.1128/jb.181.3.849-857.1999;
RA Aneja P., Charles T.C.;
RT "Poly-3-hydroxybutyrate degradation in Rhizobium (Sinorhizobium) meliloti:
RT isolation and characterization of a gene encoding 3-hydroxybutyrate
RT dehydrogenase.";
RL J. Bacteriol. 181:849-857(1999).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.33 ANGSTROMS) IN COMPLEX WITH GLYCEROL.
RG New York structural genomics research consortium (NYSGRC);
RT "Crystal structure of glycerol kinase in complex with glycerol from
RT Sinorhizobium meliloti 1021.";
RL Submitted (MAR-2012) to the PDB data bank.
CC -!- FUNCTION: Key enzyme in the regulation of glycerol uptake and
CC metabolism. Catalyzes the phosphorylation of glycerol to yield sn-
CC glycerol 3-phosphate. {ECO:0000255|HAMAP-Rule:MF_00186}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycerol = ADP + H(+) + sn-glycerol 3-phosphate;
CC Xref=Rhea:RHEA:21644, ChEBI:CHEBI:15378, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57597, ChEBI:CHEBI:456216;
CC EC=2.7.1.30; Evidence={ECO:0000255|HAMAP-Rule:MF_00186};
CC -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC {ECO:0000255|HAMAP-Rule:MF_00186}.
CC -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase
CC pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC {ECO:0000255|HAMAP-Rule:MF_00186}.
CC -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000255|HAMAP-
CC Rule:MF_00186}.
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DR EMBL; AL591985; CAC49535.1; -; Genomic_DNA.
DR EMBL; AF080548; AAD12735.1; -; Genomic_DNA.
DR PIR; G95983; G95983.
DR RefSeq; NP_437675.1; NC_003078.1.
DR RefSeq; WP_010975967.1; NC_003078.1.
DR PDB; 4E1J; X-ray; 2.33 A; A/B/C/D=1-497.
DR PDBsum; 4E1J; -.
DR AlphaFoldDB; O86033; -.
DR SMR; O86033; -.
DR STRING; 266834.SM_b21009; -.
DR EnsemblBacteria; CAC49535; CAC49535; SM_b21009.
DR GeneID; 61601086; -.
DR KEGG; sme:SM_b21009; -.
DR PATRIC; fig|266834.11.peg.6063; -.
DR eggNOG; COG0554; Bacteria.
DR HOGENOM; CLU_009281_2_3_5; -.
DR OMA; FMLMNIG; -.
DR UniPathway; UPA00618; UER00672.
DR Proteomes; UP000001976; Plasmid pSymB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004370; F:glycerol kinase activity; ISS:UniProtKB.
DR GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0006071; P:glycerol metabolic process; ISS:UniProtKB.
DR GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR HAMAP; MF_00186; Glycerol_kin; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; Carb_kinase_FGGY_C.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018484; Carb_kinase_FGGY_N.
DR InterPro; IPR005999; Glycerol_kin.
DR Pfam; PF02782; FGGY_C; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR PIRSF; PIRSF000538; GlpK; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Glycerol metabolism; Kinase; Nucleotide-binding;
KW Plasmid; Reference proteome; Transferase.
FT CHAIN 1..497
FT /note="Glycerol kinase"
FT /id="PRO_0000059483"
FT BINDING 12..14
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 12
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 82..83
FT /ligand="substrate"
FT BINDING 134
FT /ligand="substrate"
FT BINDING 243..244
FT /ligand="substrate"
FT BINDING 265
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 308
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 312
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT BINDING 411..415
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00186"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 12..20
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 48..64
FT /evidence="ECO:0007829|PDB:4E1J"
FT TURN 65..67
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 73..80
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 85..89
FT /evidence="ECO:0007829|PDB:4E1J"
FT TURN 90..92
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 108..116
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 120..127
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 136..146
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 150..155
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 159..163
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:4E1J"
FT TURN 173..175
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 179..181
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 182..185
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:4E1J"
FT TURN 193..196
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 200..206
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 210..212
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 228..231
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 236..240
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 243..250
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 259..272
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 281..283
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 285..292
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 295..305
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 308..316
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 328..332
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 341..343
FT /evidence="ECO:0007829|PDB:4E1J"
FT TURN 351..353
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 371..396
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 406..410
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 411..414
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 416..426
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 430..434
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 438..451
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 457..462
FT /evidence="ECO:0007829|PDB:4E1J"
FT STRAND 466..470
FT /evidence="ECO:0007829|PDB:4E1J"
FT HELIX 476..494
FT /evidence="ECO:0007829|PDB:4E1J"
SQ SEQUENCE 497 AA; 54419 MW; 42D3428335ACC2B7 CRC64;
MGGYILAIDQ GTTSTRAIVF DGNQKIAGVG QKEFKQHFPK SGWVEHDPEE IWQTVVSTVK
EAIEKSGITA NDIAAIGITN QRETVVVWDR ETGKPIHNAI VWQDRRTAAF CDKLKKKGLE
KTFVKKTGLL LDPYFSGTKL NWLLSNVKGA QVRAAKGELC FGTIDTFLIW RLTGGECFCT
DATNASRTLL YNIAENAWDD ELTEVLRVPK EMLPEVKDCA ADFGVTDPSL FGAAIPILGV
AGDQQAATIG QACFKPGMLK STYGTGCFAL LNTGKDMVRS KNRLLTTIAY RLDGETTYAL
EGSIFVAGAA VQWLRDGLKV IKAAPDTGSL AESADPSQEV YLVPAFTGLG APHWDPDARG
AIFGMTRNTG PAEFARAALE AVCYQTRDLL EAMHKDWRRN GNDTVLRVDG GMVASDWTMQ
RLSDLLDAPV DRPVILETTA LGVAWLAGSR AGVWPNQEAF AKSWARDRRF EPHMDEATRK
VKLKGWRSAV KRTLIAA
