(data stored in SCRATCH zone)

SWISSPROT: Q3IK59_PSEHT

ID   Q3IK59_PSEHT            Unreviewed;       501 AA.
AC   Q3IK59;
DT   08-NOV-2005, integrated into UniProtKB/TrEMBL.
DT   08-NOV-2005, sequence version 1.
DT   07-JUN-2017, entry version 96.
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:CAI85293.1};
GN   OrderedLocusNames=PSHAa0190 {ECO:0000313|EMBL:CAI85293.1};
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442 {ECO:0000313|EMBL:CAI85293.1, ECO:0000313|Proteomes:UP000006843};
RN   [1] {ECO:0000313|EMBL:CAI85293.1, ECO:0000313|Proteomes:UP000006843}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125 {ECO:0000313|Proteomes:UP000006843};
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.,
RA   Cheung F., Cruveiller S., Damico S., Duilio A., Fang G., Feller G.,
RA   Mangenot S., Marino G., Nilsson J., Parilli E., Rocha E., Rouy Z.,
RA   Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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:SAAS00193194}.
CC   -!- CATALYTIC ACTIVITY: ATP + glycerol = ADP + sn-glycerol 3-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_00186,
CC       ECO:0000256|SAAS:SAAS00029899}.
CC   -!- ENZYME REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP).
CC       {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:SAAS00030105}.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_00186, ECO:0000256|SAAS:SAAS00546148}.
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DR   EMBL; CR954246; CAI85293.1; -; Genomic_DNA.
DR   RefSeq; WP_011326908.1; NC_007481.1.
DR   ProteinModelPortal; Q3IK59; -.
DR   STRING; 326442.PSHAa0190; -.
DR   EnsemblBacteria; CAI85293; CAI85293; PSHAa0190.
DR   KEGG; pha:PSHAa0190; -.
DR   PATRIC; fig|326442.8.peg.183; -.
DR   eggNOG; ENOG4108JQ0; Bacteria.
DR   eggNOG; COG0554; LUCA.
DR   HOGENOM; HOG000222134; -.
DR   KO; K00864; -.
DR   OMA; FMPETTA; -.
DR   OrthoDB; POG091H02FA; -.
DR   UniPathway; UPA00618; UER00672.
DR   Proteomes; UP000006843; Chromosome I.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0019563; P:glycerol catabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006072; P:glycerol-3-phosphate metabolic process; IEA:UniProtKB-HAMAP.
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.
PE   3: Inferred from homology;
DR   PRODOM; Q3IK59.
DR   SWISS-2DPAGE; Q3IK59.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00082951};
KW   Complete proteome {ECO:0000313|Proteomes:UP000006843};
KW   Glycerol metabolism {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00029437};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00430777, ECO:0000313|EMBL:CAI85293.1};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00029383};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006843};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00186,
KW   ECO:0000256|SAAS:SAAS00193248, ECO:0000313|EMBL:CAI85293.1}.
FT   DOMAIN        4    250       FGGY_N. {ECO:0000259|Pfam:PF00370}.
FT   DOMAIN      259    447       FGGY_C. {ECO:0000259|Pfam:PF02782}.
FT   NP_BIND      12     14       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   NP_BIND     408    412       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   REGION       82     83       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00186}.
FT   REGION      243    244       Substrate binding. {ECO:0000256|HAMAP-
FT                                Rule:MF_00186}.
FT   BINDING      12     12       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00186}.
FT   BINDING      16     16       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     134    134       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_00186}.
FT   BINDING     265    265       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     308    308       ATP; via carbonyl oxygen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     312    312       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00186}.
FT   BINDING     327    327       ATP. {ECO:0000256|HAMAP-Rule:MF_00186}.
SQ   SEQUENCE   501 AA;  55109 MW;  C805395FFCF41C14 CRC64;
     MSKYILSIDQ GTTSSRAILF TKDAKVVDTV QQTFPQHFPN NGWVEHDPND ILQTVLSTCK
     TVLANNQVTA EQVIAIGITN QRETTLVWNK KTGQPIYNAI VWQDRRTSEY CEQIRSDKLS
     KKISDKTGLL LDPYFSATKI RWILDNVTDA QQQALAGELA FGTVDSYLLW HLTAGKVHRT
     DATNASRTLL FNIHQQCWDE ELLTQFNIPH SMLPEVMDSA AEFGSTSSEI FGAPIKICAM
     AGDQQAALIG QACFKEGMAK STYGTGCFLM LNTGDKALTS NNRLLTTVAY RLNGRVTYAI
     EGSIFMAGAT MQWIVEGLKL LEHAGDSEAM VKDVPLDHGV FLVPSFTGLG APYWDANARG
     AILGLTRDSG ISTIVAAALQ SVGYQTKDLQ KAMEGDGLRP SILRVDGGMA KNNWAMQFLA
     NILGASVERP ALTETTSLGV AYLAGLQTGI YKSTEQLATM WQCDRRFEPT MSIDERNDLY
     AKWQHCIAQV TLSNNATKDD C
//

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