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Database: UniProt
Entry: A0A074LNW1_9BACL
LinkDB: A0A074LNW1_9BACL
Original site: A0A074LNW1_9BACL 
ID   A0A074LNW1_9BACL        Unreviewed;       495 AA.
AC   A0A074LNW1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Carbohydrate kinase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=EL26_13655 {ECO:0000313|EMBL:KEO82789.1};
OS   Tumebacillus flagellatus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC   Tumebacillus.
OX   NCBI_TaxID=1157490 {ECO:0000313|EMBL:KEO82789.1, ECO:0000313|Proteomes:UP000027931};
RN   [1] {ECO:0000313|EMBL:KEO82789.1, ECO:0000313|Proteomes:UP000027931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GST4 {ECO:0000313|EMBL:KEO82789.1,
RC   ECO:0000313|Proteomes:UP000027931};
RX   PubMed=23435245; DOI=10.1099/ijs.0.045351-0;
RA   Wang Q., Xie N., Qin Y., Shen N., Zhu J., Mi H., Huang R.;
RT   "Tumebacillus flagellatus sp. nov., an alpha-amylase/pullulanase-producing
RT   bacterium isolated from cassava wastewater.";
RL   Int. J. Syst. Evol. Microbiol. 63:3138-3142(2013).
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
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:KEO82789.1}.
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DR   EMBL; JMIR01000018; KEO82789.1; -; Genomic_DNA.
DR   RefSeq; WP_052036329.1; NZ_JMIR01000018.1.
DR   AlphaFoldDB; A0A074LNW1; -.
DR   STRING; 1157490.EL26_13655; -.
DR   eggNOG; COG1070; Bacteria.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000027931; 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   CDD; cd07770; FGGY_GntK; 1.
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; PTHR43095:SF2; GLUCONOKINASE; 1.
DR   PANTHER; PTHR43095; 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; PS00445; FGGY_KINASES_2; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000256|RuleBase:RU003733};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027931};
KW   Transferase {ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          8..250
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          260..449
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   495 AA;  53481 MW;  2BB9029D670E1D8E CRC64;
     MERNVCSLGL DIGTTSVKVI ALDENGSLLT QRGQRLDLLQ PEEGAAEQDV TAVMAALMGV
     MEEVLEELRA GNWEVRRVGF SAAMHSVLAV DAAGNPLSNA ITWMDTRAKH AATDLWESVL
     GKNIYAVTGT PVHPMSPITK LRRWSLERPD WVKSVHKFVS IKEWIWHQWF GEWVVDASMA
     GATGLYNFAH GGWEPEALAF AGVSEEQLSA VVPTTTCKVA GASAALRGLG FEESVLFNVG
     STDGVLANLG VGAVKPDTLV LTVGTSCAVR VTSHHPQTDV ETRSFCYALD GERFVLGGPS
     NSGGISVETL YAQILAGIGV QWQPEELSAK LLEAGNVETD GLICLPYVAG ERAPLWAPEA
     KAAWIGVDRG HTGLHLLRAV VEGVLLNAYW IATSLFQMTG QPKQVMASGK LLEVAWVRQL
     VADIFGLPVY ESQNGDASAV GAVLLAEIAA GVKSFEDAVP QSESEQNVTY PRVEMQAYYR
     EKLEVFKRYA LFLNE
//
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