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Database: UniProt
Entry: A0A0M2WFA3_9BURK
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Original site: A0A0M2WFA3_9BURK 
ID   A0A0M2WFA3_9BURK        Unreviewed;       489 AA.
AC   A0A0M2WFA3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Xylulose kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE            Short=Xylulokinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
DE            EC=2.7.1.17 {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU364073};
GN   Name=xylB_3 {ECO:0000313|EMBL:KKO61484.1};
GN   Synonyms=xylB {ECO:0000256|HAMAP-Rule:MF_02220,
GN   ECO:0000256|RuleBase:RU364073};
GN   ORFNames=VM94_05257 {ECO:0000313|EMBL:KKO61484.1};
OS   Janthinobacterium sp. KBS0711.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1649647 {ECO:0000313|EMBL:KKO61484.1, ECO:0000313|Proteomes:UP000034315};
RN   [1] {ECO:0000313|EMBL:KKO61484.1, ECO:0000313|Proteomes:UP000034315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS0711 {ECO:0000313|EMBL:KKO61484.1,
RC   ECO:0000313|Proteomes:UP000034315};
RA   Shoemaker W.R., Muscarella M.E., Lennon J.T.;
RT   "Genome sequence of the soil bacterium Jantinobacterium sp. KBS0711.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the phosphorylation of D-xylulose to D-xylulose 5-
CC       phosphate. {ECO:0000256|HAMAP-Rule:MF_02220}.
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|HAMAP-Rule:MF_02220,
CC         ECO:0000256|RuleBase:RU364073};
CC   -!- SIMILARITY: Belongs to the FGGY kinase family. {ECO:0000256|HAMAP-
CC       Rule:MF_02220, 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:KKO61484.1}.
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DR   EMBL; LBCO01000035; KKO61484.1; -; Genomic_DNA.
DR   RefSeq; WP_046686043.1; NZ_VCCE02000001.1.
DR   AlphaFoldDB; A0A0M2WFA3; -.
DR   PATRIC; fig|1649647.5.peg.5407; -.
DR   Proteomes; UP000034315; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004856; F:xylulokinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0042732; P:D-xylose metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0005998; P:xylulose catabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd07808; FGGY_D-XK_EcXK-like; 1.
DR   Gene3D; 3.30.420.40; -; 2.
DR   HAMAP; MF_02220; XylB; 1.
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:SF6; 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|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW   Rule:MF_02220};
KW   Kinase {ECO:0000256|HAMAP-Rule:MF_02220, ECO:0000256|RuleBase:RU003733};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034315};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU003733};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_02220}.
FT   DOMAIN          3..244
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          255..438
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        237
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         80..81
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            7
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   489 AA;  51641 MW;  14D1032AF5B553F8 CRC64;
     MTYLGIDIGT SEVKAILTDD AQAILASAGV TLRVSSPHPG WTEQNPEDWW HATLDVIAAI
     RAAQPVAFSG LRGIALSGQM HGATLLDKQQ HVLRAAILWN DTRAFAECVE LEALVPESRA
     ITGNQAMPGF TAPKLLWLQK YEPSLFRATA KVLLPKDYVA LRLTGEYVSD MSDASGTLWL
     DVAKRDWSER MLAATGLTRE HMPRLVEGSA AAAQVRPSLC QEWGIAHPVL LAGGAGDNAA
     AAVGLGVVEP GAGLLSLGTS GVLFAGSDGF APNPGQGVHA FCHCLPERWH QMSVILSAAS
     SLSWVARLTQ SSDIGELVTL AESVEARTAP VFLPYLSGER TPHNDASARG VFFGLSTEHG
     RAELAYSVME GVAFAMADGN AALRSAGTHL EEASFVGGGS RSRFWAQLCA NASGLNVLRH
     DHGAAGGTMG AARLAQMAVT GLPPAQVCTR PPVQETVAPQ ASAVLDERLA RYRRLYPLLR
     EEFAGAAAA
//
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