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Database: UniProt
Entry: C6D9Z2_PECCP
LinkDB: C6D9Z2_PECCP
Original site: C6D9Z2_PECCP 
ID   C6D9Z2_PECCP            Unreviewed;       515 AA.
AC   C6D9Z2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 78.
DE   SubName: Full=Carbohydrate kinase FGGY {ECO:0000313|EMBL:ACT13748.1};
GN   OrderedLocusNames=PC1_2718 {ECO:0000313|EMBL:ACT13748.1};
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230 {ECO:0000313|EMBL:ACT13748.1, ECO:0000313|Proteomes:UP000002736};
RN   [1] {ECO:0000313|EMBL:ACT13748.1, ECO:0000313|Proteomes:UP000002736}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1 {ECO:0000313|EMBL:ACT13748.1,
RC   ECO:0000313|Proteomes:UP000002736};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C.,
RA   Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FGGY kinase family.
CC       {ECO:0000256|RuleBase:RU003733}.
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DR   EMBL; CP001657; ACT13748.1; -; Genomic_DNA.
DR   RefSeq; WP_015840916.1; NC_012917.1.
DR   AlphaFoldDB; C6D9Z2; -.
DR   STRING; 561230.PC1_2718; -.
DR   KEGG; pct:PC1_2718; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_0_6; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000002736; Chromosome.
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; cd07802; FGGY_L-XK; 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; SUGAR KINASE; 1.
DR   PANTHER; PTHR43095:SF5; XYLULOSE 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, ECO:0000313|EMBL:ACT13748.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU003733}.
FT   DOMAIN          3..249
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          260..438
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   515 AA;  55565 MW;  2D4207E367736766 CRC64;
     MDYYIGIDIG TSKVKSVLFD ADFNELQIES ANTVTYSPQP GYAEQNMHHV WDGVLSTLKT
     LAASPLLHHG RVRAIGLTGQ GEGVWLSDRH GQPIRQAILW SDTRTAEQVH QLKQRPNLEA
     TLFPETGSPL LPCNSAQQLR WLAQHQPDVL NDADYFFFAK DWVRFRLTGQ ANLELTDAGT
     SLLDLHSETL SKTVLDKLDL HAIRPLFPPL LYPDDIAGTL SDAIAAQTGL PAGIPVCAGA
     LDVSAAALGI GAIHDGDIFT ILGTTCCTGI VCRGLTQVSL QTRFVAHAWP GHYLNLFAMQ
     SGTPNIDWAL STLTNDADFQ TINARIARVP PGSGGVFYQP YLNGERAPFY STSARAGFFG
     IEQSTTNAHL LRAVFEGLAY AITDALSGYP AHGDLYIAGG GAASAIWLQI IADCTGRRVI
     ASSVKELSAC GAARLAALSI GESANMVPSA NAQASTFLPD ADAHRQYQTL FPIFRQLRDQ
     LQPLWQARAR ALNALDNHNA ARSYTAPSSQ ESLAS
//
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