ID A0A099JL93_9MICO Unreviewed; 467 AA.
AC A0A099JL93;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 37.
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 {ECO:0000256|HAMAP-Rule:MF_02220,
GN ECO:0000256|RuleBase:RU364073};
GN ORFNames=BJ997_003835 {ECO:0000313|EMBL:MBB5643287.1}, GY21_06090
GN {ECO:0000313|EMBL:KGJ79099.1};
OS Cryobacterium roopkundense.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Cryobacterium.
OX NCBI_TaxID=1001240 {ECO:0000313|EMBL:KGJ79099.1, ECO:0000313|Proteomes:UP000029864};
RN [1] {ECO:0000313|EMBL:KGJ79099.1, ECO:0000313|Proteomes:UP000029864}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RuG17 {ECO:0000313|EMBL:KGJ79099.1,
RC ECO:0000313|Proteomes:UP000029864};
RA Sisinthy S.;
RL Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:MBB5643287.1, ECO:0000313|Proteomes:UP000561726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21065 {ECO:0000313|EMBL:MBB5643287.1,
RC ECO:0000313|Proteomes:UP000561726};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (AUG-2020) 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:RU364073}.
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:KGJ79099.1}.
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DR EMBL; JPXF01000018; KGJ79099.1; -; Genomic_DNA.
DR EMBL; JACHBQ010000001; MBB5643287.1; -; Genomic_DNA.
DR RefSeq; WP_035835823.1; NZ_JPXF01000018.1.
DR AlphaFoldDB; A0A099JL93; -.
DR STRING; 1001240.GY21_06090; -.
DR eggNOG; COG1070; Bacteria.
DR OrthoDB; 9805576at2; -.
DR Proteomes; UP000029864; Unassembled WGS sequence.
DR Proteomes; UP000561726; 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 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: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; PS00933; FGGY_KINASES_1; 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:RU364073};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
KW Reference proteome {ECO:0000313|Proteomes:UP000029864};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073};
KW Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW Rule:MF_02220}.
FT DOMAIN 7..231
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 240..422
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT ACT_SITE 224
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 72..73
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT SITE 11
FT /note="Important for activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ SEQUENCE 467 AA; 48197 MW; 32E57960CD156CB2 CRC64;
MRARRVVAGV DSSTQSCKIV TVDANSGELL HLRSAPHPDG TSIDPERWWD AFVAAGGDEL
DGVAALGVSA QQHGMVALDE AGQPVHEALL WNDVRSAPQA AALTDQYGAA TWAEEVGVVP
VASFTITKLA WLAQNRPELA ARVEQVLLPH DWLTWNLLGR PAEATTDRSD ASGTGYFSVH
SNEYRPDLLE AALGRSARLP RVLGPAERAG VTTSGVIVSA GAGDNASAAL GLGIGEGDVV
VSIGTSGTVF ASTQARIADA SGSVAGFADA AGGQLPLLAT INGARTLVAT AQMLGVDIER
FGALAGQSPI DADGLLMLPY LDGERTPNLP DATGSLTGMR RANMTPAHLA QASVLGVVCS
LADALDSLRG QGVAVRQVIL IGGASQSPAI QKIAADVFGV PVVLPAPGEY VALGAARQAA
WALDGGTDFP DWPRGITARE FEPAADRSWA QAVRSNYAAQ RLALYGV
//
