ID A0A1Z9D5F1_9ACTO Unreviewed; 477 AA.
AC A0A1Z9D5F1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
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=CBC75_04475 {ECO:0000313|EMBL:OUV52419.1};
OS Actinomycetales bacterium TMED115.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales.
OX NCBI_TaxID=1986615 {ECO:0000313|EMBL:OUV52419.1, ECO:0000313|Proteomes:UP000196314};
RN [1] {ECO:0000313|EMBL:OUV52419.1, ECO:0000313|Proteomes:UP000196314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TMED115 {ECO:0000313|EMBL:OUV52419.1};
RA Tully B.J., Sachdeva R., Graham E.D., Heidelberg J.F.;
RT "290 Metagenome-assembled Genomes from the Mediterranean Sea: a resource
RT for marine microbiology.";
RL Submitted (MAY-2017) 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:OUV52419.1}.
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DR EMBL; NHFQ01000011; OUV52419.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z9D5F1; -.
DR Proteomes; UP000196314; 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; 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 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 8..244
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 254..435
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
FT REGION 446..466
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 238
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT BINDING 73..74
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 477 AA; 49194 MW; 0D5962B5CCD9FF90 CRC64;
MTDQSLVAGV DTSTQSVKVV VREADTGAWV REGRASHPDG TEVAPEEWWT AFGAACSGGL
LDGVSAISIA GQQHGMVALD ESGDVVRPAL LWNDTRSAPD ASDLVTELGG PAMWAEAVGS
VPVAAFTVSK VRWMARNEPD NAERTSTIML PHDYLTWMLA DQPHAATTDR GDASGTGYWS
PIEGEYRRDL MQLALGKDVQ LPRVAGPDET VGEVGGRARS FLGINGSSPI AIGPGTGDNM
GAAFALEIAP GDVVVSLGTS GTAFAGSSQP TKDPTGLVAG FADASGVFLP LVCTLNAARI
LTSTAELLGV DMDSFAALAL AAEPGASGLV MLPYFDGERT PNLPGARGSL HGISRENLTP
QNLARAAIEG MLGGLADAVD ALVDVGVQPS RVLVVGGAAS NPAVADIAAT LVGVPVQIPP
AGEYVADGAA RQAAWILRGG EQPAWSDVRP GETVSRDPQP AAQVREQYRQ AREALYA
//
