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Database: UniProt
Entry: A0A1H3CY09_9PSEU
LinkDB: A0A1H3CY09_9PSEU
Original site: A0A1H3CY09_9PSEU 
ID   A0A1H3CY09_9PSEU        Unreviewed;       461 AA.
AC   A0A1H3CY09;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=SAMN05216215_1012189 {ECO:0000313|EMBL:SDX58920.1};
OS   Saccharopolyspora shandongensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharopolyspora.
OX   NCBI_TaxID=418495 {ECO:0000313|EMBL:SDX58920.1, ECO:0000313|Proteomes:UP000199529};
RN   [1] {ECO:0000313|EMBL:SDX58920.1, ECO:0000313|Proteomes:UP000199529}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.3530 {ECO:0000313|EMBL:SDX58920.1,
RC   ECO:0000313|Proteomes:UP000199529};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNOK01000012; SDX58920.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H3CY09; -.
DR   STRING; 418495.SAMN05216215_1012189; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000199529; 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.
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|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
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          4..211
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          236..418
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        220
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         69..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            8
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   461 AA;  47828 MW;  42D2B958B8176945 CRC64;
     MNLVAGIDSS TQSTKVVVCD ADTGTVLREG RAPHPDGTVA DPEDWRQALT TASDGLLDDV
     AAIGIAAQQH GMVALDEHGV PVRPALLWND NRSAQAAIDL TEELGGPQAC AEAIGSVLVA
     SFTASKLRWL AEHEPDLADR VTDVLLPHDW LTWRLTGEFV TDRGDASGTG YWSPREGRYR
     EDVLATAFGG RKPRTPRVLG PAEAAGHTPD GKLVSAGTGD NMGAALGLDV RPGDVVVSLG
     TSGTVFARAE RPSADPSGQI AGFADATGGF LPLVCTLNAA RVLTATAAML GVGMAEFDEL
     ARRAEPGAGG LALLPYLDGE RTPLLPDAAG TLTGLRRDNM TPENLARAAV EGMLCGLAAG
     VDALRAEDIE VGRVLLIGGA AQSRAVQVVA PLIFGVPVTV PAPAEYVARG AARQAAWALA
     GTPDPPEWQL PGATELDVTD PAAGARIRDQ HTDAFTQVHR T
//
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