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Database: UniProt
Entry: A0A0Q4N0E7_9GAMM
LinkDB: A0A0Q4N0E7_9GAMM
Original site: A0A0Q4N0E7_9GAMM 
ID   A0A0Q4N0E7_9GAMM        Unreviewed;       494 AA.
AC   A0A0Q4N0E7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=Xylulose kinase {ECO:0000313|EMBL:KQN57825.1};
GN   ORFNames=ASF13_03245 {ECO:0000313|EMBL:KQN57825.1};
OS   Erwinia sp. Leaf53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN57825.1, ECO:0000313|Proteomes:UP000050856};
RN   [1] {ECO:0000313|EMBL:KQN57825.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57825.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN57825.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN57825.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:KQN57825.1}.
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DR   EMBL; LMLK01000012; KQN57825.1; -; Genomic_DNA.
DR   RefSeq; WP_056235225.1; NZ_LMLK01000012.1.
DR   AlphaFoldDB; A0A0Q4N0E7; -.
DR   STRING; 1736225.ASF13_03245; -.
DR   Proteomes; UP000050856; 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; 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:SF3; L-XYLULOSE/3-KETO-L-GULONATE KINASE; 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, ECO:0000313|EMBL:KQN57825.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050856};
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          259..439
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   494 AA;  53610 MW;  CD1485658A15CD67 CRC64;
     MSYWLGLDCG GTFIKAGLYN AQGRELAVAR QSLPVLVPEP GRAERDLHQL WQQAATVIRQ
     VLENSGLDAA QVAGVGISAQ GKGLFLLDKQ GEPLGNGILS SDRRALALVQ QWQRDGVPAA
     LYPVTRQTLW TGHPVSLLRW VKLHEPQRYA AIGSVLMAHD YLRYRLTGEL ACEETNISES
     NLYDMQQGDF SPALAQRLGI AEILPALPAI IGSAAVAGTV TAGAAALCGL KPGTPVVGGL
     FDVVSTALCA GLDDDTRINA VMGTWSVTSG ITDRLSDEVD YPFVYGRYAI DGQYIIHEAS
     PTSAANLEWF CQQWGLNDYP RLNQWVAELP PAASSLLFVP FLYGNNAGGN LHASFYGLQA
     AHQRGHLLQA IYEGVVFAHL THLNRIRQRF PRVTALRLSG GPTRSACWMQ MFADISGLPV
     EIPQIEESGC LGAALVAMTG TGAYPSLLAA QQTLAPEVVC YQPDAERHRL YQQKYQRYQR
     LVAALTAVEQ ETTP
//
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