ID A0A0Q0CEP1_PSESX Unreviewed; 346 AA.
AC A0A0Q0CEP1;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Xylulose kinase {ECO:0000256|RuleBase:RU364073};
DE Short=Xylulokinase {ECO:0000256|RuleBase:RU364073};
DE EC=2.7.1.17 {ECO:0000256|RuleBase:RU364073};
GN Name=xylB {ECO:0000256|RuleBase:RU364073};
GN ORFNames=ALO94_200001 {ECO:0000313|EMBL:KPZ06888.1};
OS Pseudomonas syringae pv. spinaceae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=264459 {ECO:0000313|EMBL:KPZ06888.1, ECO:0000313|Proteomes:UP000050384};
RN [1] {ECO:0000313|EMBL:KPZ06888.1, ECO:0000313|Proteomes:UP000050384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP16929 {ECO:0000313|EMBL:KPZ06888.1,
RC ECO:0000313|Proteomes:UP000050384};
RA Thakur S., Wang P.W., Gong Y., Weir B.S., Guttman D.S.;
RT "Genome announcement of multiple Pseudomonas syringae strains.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-xylulose = ADP + D-xylulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:10964, ChEBI:CHEBI:15378, ChEBI:CHEBI:17140,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:57737, ChEBI:CHEBI:456216;
CC EC=2.7.1.17; Evidence={ECO:0000256|RuleBase:RU364073};
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:KPZ06888.1}.
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DR EMBL; LJRI01000308; KPZ06888.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0Q0CEP1; -.
DR PATRIC; fig|264459.3.peg.2226; -.
DR Proteomes; UP000050384; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0005997; P:xylulose metabolic process; IEA:InterPro.
DR Gene3D; 3.30.420.40; -; 2.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR018483; Carb_kinase_FGGY_CS.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR006000; Xylulokinase.
DR NCBIfam; TIGR01312; XylB; 1.
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 SUPFAM; SSF53067; Actin-like ATPase domain; 2.
DR PROSITE; PS00445; FGGY_KINASES_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364073};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU364073};
KW Kinase {ECO:0000256|RuleBase:RU003733};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364073};
KW Transferase {ECO:0000256|RuleBase:RU003733};
KW Xylose metabolism {ECO:0000256|RuleBase:RU364073}.
FT DOMAIN 2..103
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 177..294
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 346 AA; 36999 MW; CC110F252DFC33CA CRC64;
MFERIDKVLL PHDYLNYWLT GRCCTEFGDA SGTGYFNVRG REWDLPLLAH IDPSGRLGKA
LPQLLEADAP VGTLLPDIAR LLGLNPDALV SSGGGDNMMG AIGTGNIQPG LITMSLGSSG
TVYAYGDEVR VSEHESVATF CSSSGGWLPL ICTMNLTNAT TAIRELFALD IKDFNQAIAQ
APIGAEGVLM LPFFNGERVP ALPDATASIV GLDSTNLTQV NLCRAVVEGT TFGLRYGLDL
LRDSGIKSEK IRLIGGGSKS AVWRQIVADI MNTPVICTVQ PEAAALGAAI QAAWCRSKAD
GTPEALLQLC ERCIGLDPDS ETHPVAQNVA AYQQVYQRYQ AQLRKV
//
