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Database: UniProt
Entry: A0A0N1CJR0_9ENTE
LinkDB: A0A0N1CJR0_9ENTE
Original site: A0A0N1CJR0_9ENTE 
ID   A0A0N1CJR0_9ENTE        Unreviewed;       482 AA.
AC   A0A0N1CJR0;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=ATP:glycerol 3-phosphotransferase {ECO:0000256|ARBA:ARBA00043149};
GN   ORFNames=AEQ18_13850 {ECO:0000313|EMBL:KPG68787.1};
OS   Enterococcus sp. RIT-PI-f.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1690244 {ECO:0000313|EMBL:KPG68787.1, ECO:0000313|Proteomes:UP000037898};
RN   [1] {ECO:0000313|EMBL:KPG68787.1, ECO:0000313|Proteomes:UP000037898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RIT-PI-f {ECO:0000313|EMBL:KPG68787.1,
RC   ECO:0000313|Proteomes:UP000037898};
RA   Tan N.E.H., Lee Y.P., Gan H.M., Savka M.A.;
RT   "Whole genome sequencing of endophytes isolated from poison ivy
RT   (Toxicodendron radicans).";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|ARBA:ARBA00009156, 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:KPG68787.1}.
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DR   EMBL; LHOX01000021; KPG68787.1; -; Genomic_DNA.
DR   RefSeq; WP_054116936.1; NZ_LHOX01000021.1.
DR   AlphaFoldDB; A0A0N1CJR0; -.
DR   STRING; 1690244.AEQ18_13850; -.
DR   PATRIC; fig|1690244.3.peg.2681; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000037898; Unassembled WGS sequence.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.420.40; -; 2.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR000577; Carb_kinase_FGGY.
DR   InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR   InterPro; IPR018485; FGGY_C.
DR   InterPro; IPR018484; FGGY_N.
DR   PANTHER; PTHR10196:SF69; GLYCEROL KINASE; 1.
DR   PANTHER; PTHR10196; SUGAR KINASE; 1.
DR   Pfam; PF02782; FGGY_C; 1.
DR   Pfam; PF00370; FGGY_N; 1.
DR   PIRSF; PIRSF000538; GlpK; 1.
DR   SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR   PROSITE; PS00933; FGGY_KINASES_1; 1.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:KPG68787.1};
KW   Transferase {ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          5..244
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          254..439
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   482 AA;  54058 MW;  74FED6F172DEE553 CRC64;
     MEKPYQIVLD QSTSGTKLLL FENGRIGYRK DKKHQQIYPK VGWVEHDPLE IWHNVQTLLS
     DVFTEKEITP AEVASISITN QRETIVAWDR STGKPLYNAI VWQCNRSAGI CAEMIAKGLE
     PMINQKTGLR IDPYFSGTKI NWLVKEITAI KEKSGSGDLA IGTMDSWLLW NLTEGATFAT
     EASNACRTLL YNISTMDWDP VLIELFGIDV IDLPKLTPAD TIFGYYQTIP IIGVLADSQA
     ALFGEGCKEV GDVKITMGTG CSIMMQVQQQ NQLRDQRILT TTAWQTEKGC VFALEGIIRS
     CGDAINWFSE QIAPLPNVAA ICDQVLVRDT DEAIYFVPAL QGMGAPFWHN QLTASFLGMK
     RTTTQQDLLR AVLESILFQI KAVIDVMEEV SGRMINHVMI DGGMSKNHPL MTMLATLLHK
     EVIVSEVEEF SAIGTMTLAR PQQMAHPWRQ ERIQPEADQA TIRLKYEKWK RLIDLSVALE
     GE
//
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