ID A0A1Q3SIJ1_9CHLR Unreviewed; 490 AA.
AC A0A1Q3SIJ1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=BGO39_04670 {ECO:0000313|EMBL:OJV88797.1};
OS Chloroflexi bacterium 54-19.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV88797.1, ECO:0000313|Proteomes:UP000186384};
RN [1] {ECO:0000313|EMBL:OJV88797.1, ECO:0000313|Proteomes:UP000186384}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54-19 {ECO:0000313|EMBL:OJV88797.1};
RA Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT "Genome-resolved meta-omics ties microbial dynamics to process performance
RT in biotechnology for thiocyanate degradation.";
RL Submitted (SEP-2016) 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:OJV88797.1}.
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DR EMBL; MKTJ01000080; OJV88797.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Q3SIJ1; -.
DR STRING; 1895928.BGO39_04670; -.
DR Proteomes; UP000186384; 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; IPR000577; Carb_kinase_FGGY.
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 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 ATP-binding {ECO:0000256|RuleBase:RU364073};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277,
KW ECO:0000256|RuleBase:RU364073};
KW Kinase {ECO:0000256|RuleBase:RU003733, ECO:0000313|EMBL:OJV88797.1};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU364073};
KW Transferase {ECO:0000256|RuleBase:RU003733};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629,
KW ECO:0000256|RuleBase:RU364073}.
FT DOMAIN 9..249
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 260..439
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 490 AA; 51877 MW; 1E26754599DDB2DD CRC64;
MKGSKAVAVL GIDLGTSSVK ALILDKAGRT LALDKAAYPV EAPQPGWAES DPARWWHATV
ETVRSVLAQL PASEKIEGIG LSGQMHGVVL ADETGQPLRP AILWADTRAT AELDTYCNLP
HATLLRLANP LVAGMAGPSL AWVKKHEPEV FRKIHVALQP KDWVRLRLTG EIATDPSDAS
ATLLYDLPAD GWAEDVFTAL GLNRELFPQI KPSAACGGEL SKTAAVTLGL PAGIPVAVGG
GDTPVAALGT GLLEPGLAQL TLGTGAQLIQ LYREPLADKT GRTHLYRTVV PGSWYGMAAV
QNCGLALDWV RQTLGATWDE FYTSAATVAP GAEGVTFLPY MVHERAHQPH SQQGGAFTGL
KTNHRREHLL HAALEGVAFG VRLALEALPK VDRAPYLRLS GGGSLHPAWR QMLADILGVE
LVAVDTANAS ARGAALLGGL VAGTWPDAQS TAELAPAKEN STYPDTTRQP LFEAAYSRFI
DLSKTLSPTN
//
