ID A0A6A7Y4P2_9RHIZ Unreviewed; 495 AA. AC A0A6A7Y4P2; DT 17-JUN-2020, integrated into UniProtKB/TrEMBL. DT 17-JUN-2020, sequence version 1. DT 07-OCT-2020, entry version 3. 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:MQT13178.1}; GN ORFNames=F0357_11100 {ECO:0000313|EMBL:MQT13178.1}; OS Rhizobiales bacterium Sp-1. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales. OX NCBI_TaxID=2608987 {ECO:0000313|EMBL:MQT13178.1, ECO:0000313|Proteomes:UP000332515}; RN [1] {ECO:0000313|EMBL:MQT13178.1, ECO:0000313|Proteomes:UP000332515} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Sp-1 {ECO:0000313|EMBL:MQT13178.1, RC ECO:0000313|Proteomes:UP000332515}; RA Akter S., Shazib S.U.A., Shin M.K.; RT "Segnochrobactrum spirostomi gen. nov., sp. nov., isolated from the ciliate RT Spirostomum cf. yagiui and description of a novel family, RT Segnochrobactraceae fam. nov. within the order Rhizobiales of the class RT Alphaproteobacteria."; RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases. 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 -!- 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|ARBA:ARBA00001373, CC ECO:0000256|HAMAP-Rule:MF_00186}; CC -!- ACTIVITY REGULATION: Inhibited by fructose 1,6-bisphosphate (FBP). CC {ECO:0000256|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:0000256|HAMAP-Rule:MF_00186}. CC -!- SIMILARITY: Belongs to the FGGY kinase family. CC {ECO:0000256|ARBA:ARBA00009156, ECO:0000256|HAMAP-Rule:MF_00186, CC ECO:0000256|RuleBase:RU003733}. 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:MQT13178.1}. 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; VWNA01000001; MQT13178.1; -; Genomic_DNA. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000332515; Unassembled WGS sequence. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004370; F:glycerol kinase activity; IEA:UniProtKB-UniRule. 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; 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; PS00933; FGGY_KINASES_1; 1. DR PROSITE; PS00445; FGGY_KINASES_2; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00186}; KW Glycerol metabolism {ECO:0000256|ARBA:ARBA00022798, ECO:0000256|HAMAP- KW Rule:MF_00186}; KW Kinase {ECO:0000256|HAMAP-Rule:MF_00186, ECO:0000256|RuleBase:RU003733, KW ECO:0000313|EMBL:MQT13178.1}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00186}; Reference proteome {ECO:0000313|Proteomes:UP000332515}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186, KW ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:MQT13178.1}. FT DOMAIN 4..249 FT /note="FGGY_N" FT /evidence="ECO:0000259|Pfam:PF00370" FT DOMAIN 259..449 FT /note="FGGY_C" FT /evidence="ECO:0000259|Pfam:PF02782" FT NP_BIND 11..13 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT NP_BIND 410..414 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT REGION 81..82 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT REGION 242..243 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 11 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 15 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 133 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 264 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 307 FT /note="ATP; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 311 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" FT BINDING 326 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00186" SQ SEQUENCE 495 AA; 53598 MW; 442EC35584C87030 CRC64; MTHILAIDQG TTSSRAILFD AAMRLKAVAQ QEFPQHFPAS GWVEHDPADL WSSVAGTARA AIEQAGLTGA DIAAIGITNQ RETVVIWDRA TGEPIHRAIV WQDRRTADLC ARLKADGLEP EISAKTGLLI DPYFSATKIK WLLDHVEGAR ERARRGELAF GTVDCFLIWK LTDGAVHATD ATNAARTMLY DIREGRWDEA LCAAFGVPMA MLPEVRDCAA PYGTTRPDLF GRAIPILGVA GDQQAATVGQ ACFRPGMLKS TYGTGCFALL NTGDDLVASK NRLLGTIAYR LKGRTTYALE GSIFIAGAVV QWLRDGLKII RHAAETHPLA EKADPAQDLV LVPAFTGLGA PYWRPDCRGA VFGLTRNSGP AEFARAALES VGYQTRDLLE AMHADWKDAT AEGVLRVDGG MTASDWTMQF LADILGAPVD RPVVRETTAL GAAYLAGLEA GLYPDPDAFA ATWALERRFL PALDETTRTA KYARWRRAVE ATMAA //