ID A0A2M9R036_9GAMM Unreviewed; 499 AA. AC A0A2M9R036; DT 25-APR-2018, integrated into UniProtKB/TrEMBL. DT 25-APR-2018, sequence version 1. DT 16-JAN-2019, entry version 6. 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:PJO53693.1}; GN ORFNames=CR156_16690 {ECO:0000313|EMBL:PJO53693.1}; OS Stenotrophomonas lactitubi. OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Stenotrophomonas. OX NCBI_TaxID=2045214 {ECO:0000313|EMBL:PJO53693.1, ECO:0000313|Proteomes:UP000231985}; RN [1] {ECO:0000313|EMBL:PJO53693.1, ECO:0000313|Proteomes:UP000231985} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=M15 {ECO:0000313|EMBL:PJO53693.1, RC ECO:0000313|Proteomes:UP000231985}; RA Weber M., Schuenemann W., Fuss J., Kaempfer P., Lipski A.; RT "Stenotrophomonas lactitubi sp. nov., and Stenotrophomonas indicatrix RT sp. nov., isolated from food related matrices."; RL Submitted (NOV-2017) 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 ECO:0000256|SAAS:SAAS00193194}. 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: 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|RuleBase:RU003733, CC ECO:0000256|SAAS:SAAS00546148}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:PJO53693.1}. 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; PHQX01000001; PJO53693.1; -; Genomic_DNA. DR UniPathway; UPA00618; UER00672. DR Proteomes; UP000231985; 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; 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; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00186, KW ECO:0000256|SAAS:SAAS00082951}; KW Complete proteome {ECO:0000313|Proteomes:UP000231985}; 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|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00430777, KW ECO:0000313|EMBL:PJO53693.1}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00186, KW ECO:0000256|SAAS:SAAS00029383}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00186, KW ECO:0000256|RuleBase:RU003733, ECO:0000256|SAAS:SAAS00193248}. FT DOMAIN 5 252 FGGY_N. {ECO:0000259|Pfam:PF00370}. FT DOMAIN 262 450 FGGY_C. {ECO:0000259|Pfam:PF02782}. FT NP_BIND 13 15 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}. FT NP_BIND 411 415 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}. FT REGION 83 84 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00186}. FT REGION 245 246 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00186}. FT BINDING 13 13 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00186}. FT BINDING 17 17 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}. FT BINDING 135 135 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00186}. FT BINDING 267 267 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}. FT BINDING 310 310 ATP; via carbonyl oxygen. FT {ECO:0000256|HAMAP-Rule:MF_00186}. FT BINDING 314 314 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00186}. FT BINDING 329 329 ATP. {ECO:0000256|HAMAP-Rule:MF_00186}. SQ SEQUENCE 499 AA; 54914 MW; 7BACE7110AAC7995 CRC64; MTPRYVLAID QGTTSSRAIL FDRTGDTVGS AQREFAQLFP QPGWVEHDPR EILTSVYATI TELLSREQID PRHIAALGIT NQRETTVVWD RASGQPIHNA IVWQSRQSQA ICERLKSGGH EALIRERTGL LIDAYFSATK IRWILDHVEG AQQRAERGEL LFGTIDSWLV WNLSGGQAHV TDYSNAARTL LFNIHTLEWD DDLLALLDIP RAMLPQVRDS SSVYAHTRPQ FFFDHPIPIA GIAGDQQAAL FGQACFQPGM VKNTYGTGCF MLMHTGTQAV RSRNGLLTTI AWGLDGKVEY ALEGSIFVAG SVVQWLRDGL RMIDRAADSQ ALAAQVPDSA GVYLVPAFVG LGAPYWRSDV RGAMFGLTRG TRKAHFVRAA LEAMAYQTRD VLDAMQSDAG ISLSELRADG GAIGNDFLAG FQADILGVPL LRPRLTETTA LGAAYLAGLA VGFWESREQI AAQWGLDRRF EPQMAVARRE KLYAGWQQAV AATLAFHVD //