(data stored in SCRATCH zone)

SWISSPROT: D3VH16_XENNA

ID   D3VH16_XENNA            Unreviewed;       507 AA.
AC   D3VH16;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   08-MAY-2019, entry version 58.
DE   RecName: Full=Glycerol kinase {ECO:0000256|HAMAP-Rule:MF_00186};
DE            EC=2.7.1.30 {ECO:0000256|HAMAP-Rule:MF_00186};
DE   AltName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|HAMAP-Rule:MF_00186};
DE   AltName: Full=Glycerokinase {ECO:0000256|HAMAP-Rule:MF_00186};
DE            Short=GK {ECO:0000256|HAMAP-Rule:MF_00186};
GN   Name=glpK {ECO:0000256|HAMAP-Rule:MF_00186,
GN   ECO:0000313|EMBL:CBJ88301.1};
GN   OrderedLocusNames=XNC1_0213 {ECO:0000313|EMBL:CBJ88301.1};
OS   Xenorhabdus nematophila (strain ATCC 19061 / DSM 3370 / LMG 1036 /
OS   NCIB 9965 / AN6).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=406817 {ECO:0000313|EMBL:CBJ88301.1, ECO:0000313|Proteomes:UP000008075};
RN   [1] {ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RA   Goodrich-Blair H., Barbazuk B., Bode H.B., Darby C., Du Z., Forst S.,
RA   Gaudriault S., Goldman B.S., Goodner B., Henkhaus J., Latreille P.,
RA   Medigue C., Miller N., Norton S., Ogier J.C., Rouy Z., Slater S.,
RA   Suen G.;
RT   "Complete genome sequence of Xenorhabdus nematophila (strain ATCC
RT   19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6).";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBJ88301.1, ECO:0000313|Proteomes:UP000008075}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19061 / DSM 3370 / LMG 1036 / NCIB 9965 / AN6
RC   {ECO:0000313|Proteomes:UP000008075};
RX   PubMed=22125637; DOI=10.1371/journal.pone.0027909;
RA   Chaston J.M., Suen G., Tucker S.L., Andersen A.W., Bhasin A., Bode E.,
RA   Bode H.B., Brachmann A.O., Cowles C.E., Cowles K.N., Darby C.,
RA   de Leon L., Drace K., Du Z., Givaudan A., Herbert Tran E.E.,
RA   Jewell K.A., Knack J.J., Krasomil-Osterfeld K.C., Kukor R., Lanois A.,
RA   Latreille P., Leimgruber N.K., Lipke C.M., Liu R., Lu X.,
RA   Martens E.C., Marri P.R., Medigue C., Menard M.L., Miller N.M.,
RA   Morales-Soto N., Norton S., Ogier J.C., Orchard S.S., Park D.,
RA   Park Y., Qurollo B.A., Sugar D.R., Richards G.R., Rouy Z.,
RA   Slominski B., Slominski K., Snyder H., Tjaden B.C., van der Hoeven R.,
RA   Welch R.D., Wheeler C., Xiang B., Barbazuk B., Gaudriault S.,
RA   Goodner B., Slater S.C., Forst S., Goldman B.S., Goodrich-Blair H.;
RT   "The entomopathogenic bacterial endosymbionts xenorhabdus and
RT   photorhabdus: convergent lifestyles from divergent genomes.";
RL   PLoS ONE 6:e27909-e27909(2011).
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:0000256|HAMAP-Rule:MF_00186,
CC       ECO:0000256|SAAS:SAAS01185168}.
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:0000256|HAMAP-Rule:MF_00186,
CC         ECO:0000256|SAAS:SAAS01119553};
CC   -!- ACTIVITY REGULATION: Activity of this regulatory enzyme is
CC       affected by several metabolites. Allosterically and non-
CC       competitively inhibited by fructose 1,6-bisphosphate (FBP) and
CC       unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an
CC       integral component of the bacterial phosphotransferase (PTS)
CC       system. {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- PATHWAY: Polyol metabolism; glycerol degradation via glycerol
CC       kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1.
CC       {ECO:0000256|HAMAP-Rule:MF_00186, ECO:0000256|SAAS:SAAS00029305}.
CC   -!- SUBUNIT: Homotetramer and homodimer (in equilibrium). Heterodimer
CC       with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc
CC       dimer. The zinc ion is important for dimerization.
CC       {ECO:0000256|HAMAP-Rule:MF_00186}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00186, ECO:0000256|RuleBase:RU003733,
CC       ECO:0000256|SAAS:SAAS00546148}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; FN667742; CBJ88301.1; -; Genomic_DNA.
DR   RefSeq; WP_013183162.1; NC_014228.1.
DR   STRING; 406817.XNC1_0213; -.
DR   EnsemblBacteria; CBJ88301; CBJ88301; XNC1_0213.
DR   KEGG; xne:XNC1_0213; -.
DR   eggNOG; ENOG4108JQ0; Bacteria.
DR   eggNOG; COG0554; LUCA.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; WQDTRTQ; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000008075; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00186; Glycerol_kin; 1.
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   TIGRFAMs; TIGR01311; glycerol_kin; 1.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D3VH16.
DR   SWISS-2DPAGE; D3VH16.
KW   Allosteric enzyme {ECO:0000256|HAMAP-Rule:MF_00186};
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00029449};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008075};
KW   Glycerol metabolism {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00430474};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00183374,
KW   ECO:0000313|EMBL:CBJ88301.1};
KW   Metal-binding {ECO:0000256|HAMAP-Rule:MF_00186};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00430403};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008075};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00183399,
KW   ECO:0000313|EMBL:CBJ88301.1}; Zinc {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   DOMAIN       11    259       FGGY_N. {ECO:0000259|Pfam:PF00370}.
FT   DOMAIN      268    457       FGGY_C. {ECO:0000259|Pfam:PF02782}.
FT   NP_BIND      19     21       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   NP_BIND     418    422       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   REGION       89     90       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      240    242       Allosteric FBP inhibitor binding.
FT                                {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   REGION      252    253       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00186}.
FT   METAL       485    485       Zinc; shared with EIIA-Glc.
FT                                {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING      19     19       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00186}.
FT   BINDING      23     23       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     142    142       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00186}.
FT   BINDING     274    274       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     317    317       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     321    321       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     336    336       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   507 AA;  55891 MW;  6613351B7616B350 CRC64;
     MTIENITEKK YIVALDQGTT SSRAVVLDHD ANIVCISQRE FPQIYPKPGW VEHDPMEIWA
     SQSSTLVEVL AKADISSDQI AGIGITNQRE TTIVWEKETG KPVYNAIVWQ CRRTADICTK
     LKQKEGLEEY IHHNTGLVID PYFSGTKIKW ILDNVAGVRE RAEKGELLFG TVDTWLVWKM
     TQGRVHVTDS TNASRTMLFN IHNLDWDQKI LNELGIPRII LPKVAASSEI YGQTNIGGKG
     GTRIPIAGIA GDQQAALYGQ LCVHPGMAKN TYGTGCFLLM NTGKDAVRSN HGLLTTIACG
     PRGEINYALE GAVFVGGASI QWLRDELKLI ADAADSEYFA SKVKDSNGVY VVPAFTGLGA
     PYWDPYARGA IFGLTRGTNS NHIIRATLES IAYQTRDVLD AMQADAGTRL QALRVDGGAV
     ANNFLMQFQA DILGTRVERP EVRESTALGA AFLAGLAVGF WQDLDEVKSK ATIEKEFRPG
     IETTERNHKY NGWKKAVARA QEWEDRA
//

If you have problems or comments...

PBIL Back to PBIL home page