ID A2W1R0_9BURK Unreviewed; 487 AA.
AC A2W1R0;
DT 20-MAR-2007, integrated into UniProtKB/TrEMBL.
DT 20-MAR-2007, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=BCPG_04279 {ECO:0000313|EMBL:EAY65906.1};
OS Burkholderia cenocepacia PC184.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=350702 {ECO:0000313|EMBL:EAY65906.1, ECO:0000313|Proteomes:UP000053735};
RN [1] {ECO:0000313|EMBL:EAY65906.1, ECO:0000313|Proteomes:UP000053735}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PC184 {ECO:0000313|EMBL:EAY65906.1,
RC ECO:0000313|Proteomes:UP000053735};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L.,
RA Jaffe D., Butler J., Alvarez P., Gnerre S., Grabherr M., Kleber M.,
RA Mauceli E., Brockman W., Young S., LaButti K., DeCaprio D., Crawford M.,
RA Koehrsen M., Engels R., Montgomery P., Pearson M., Howarth C., White J.,
RA Larson L., Alvarado L., Kodira C., Zeng Q., Yandava C., Oleary S.,
RA LiPuma J., Lory S.;
RT "The Genome Sequence of Burkholderia cenocepacia (strain PC184).";
RL Submitted (DEC-2005) 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:RU364073}.
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DR EMBL; CH482378; EAY65906.1; -; Genomic_DNA.
DR AlphaFoldDB; A2W1R0; -.
DR HOGENOM; CLU_559822_0_0_4; -.
DR Proteomes; UP000053735; 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; IPR018484; FGGY_N.
DR InterPro; IPR006000; Xylulokinase.
DR NCBIfam; TIGR01312; XylB; 1.
DR PANTHER; PTHR43095; SUGAR KINASE; 1.
DR PANTHER; PTHR43095:SF6; XYLULOSE KINASE; 1.
DR Pfam; PF00370; FGGY_N; 1.
DR SUPFAM; SSF53067; Actin-like ATPase domain; 2.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU364073};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU364073};
KW Kinase {ECO:0000256|RuleBase:RU364073, ECO:0000313|EMBL:EAY65906.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364073};
KW Transferase {ECO:0000256|RuleBase:RU364073};
KW Xylose metabolism {ECO:0000256|RuleBase:RU364073}.
FT DOMAIN 156..397
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT REGION 113..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 487 AA; 52694 MW; 4C91353273E4EE27 CRC64;
MPRAARARGA RLPQRRAALH VVDHQPGAVV PPAEPARHAA RNRRRRVRRH ERQHLHAVFP
ASHRLVVRAL PEPAAHQRGV RAADVFRPDG DRHLLPGWLQ QPVELQPSVS RDEAGAAVEV
PRAAPAQRTA RPRRRTARAT RAAAAHPRQD ASHVTFLGID LGTSEVKVLL TDSRSVPLAT
GAATLSISRP HPHWSEQSPQ AWWHAMLDAI ASVRAAQPAG FAALRGIALS GQMHGATLID
RADQVLRPAI LWNDTRAGTE CVELEALVPE SRAITGNMAM PGFTAPKLLW LAKYEPAVFR
AVHKVLLPKD YLIWRLSGEF VSDMSDASGT LWLDCARRDW SDRMLAATEL SRAQMPRLVE
GNAAAAQLRD ALRREWGIDG PVTIAGGAGD NAASAIGMGV RGAGSGFLSL GTSGVLFAGN
DRFAPNPDAA VHAFCHCVEG RWHQMSVILS AAASLDWLAR AHGTTPAVLA ARAEHADPRP
LVAVRRR
//
