UniProt: A0A0S7BJ46

Database: UniProt
Entry: A0A0S7BJ46_9CHLR

LinkDB:  A0A0S7BJ46_9CHLR 
Original site:  A0A0S7BJ46_9CHLR

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   PROSITE (1)   
All databases (16)   

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ID   A0A0S7BJ46_9CHLR        Unreviewed;       492 AA.
AC   A0A0S7BJ46;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   27-MAR-2024, entry version 35.
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=LARV_01648 {ECO:0000313|EMBL:GAP13889.1};
OS   Longilinea arvoryzae.
OC   Bacteria; Chloroflexota; Anaerolineae; Anaerolineales; Anaerolineaceae;
OC   Longilinea.
OX   NCBI_TaxID=360412 {ECO:0000313|EMBL:GAP13889.1};
RN   [1] {ECO:0000313|EMBL:GAP13889.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KOME-1 {ECO:0000313|EMBL:GAP13889.1};
RA   Sekiguchi Y., Ohashi A., Matsuura N., Tourlousse M.D.;
RT   "Draft Genome Sequences of Anaerolinea thermolimosa IMO-1, Bellilinea
RT   caldifistulae GOMI-1, Leptolinea tardivitalis YMTK-2, Levilinea
RT   saccharolytica KIBI-1,Longilinea arvoryzae KOME-1, Previously Described as
RT   Members of the Anaerolineaceae (Chloroflexi).";
RL   Submitted (JUL-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}.
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DR   EMBL; DF967972; GAP13889.1; -; Genomic_DNA.
DR   RefSeq; WP_075073192.1; NZ_DF967972.1.
DR   AlphaFoldDB; A0A0S7BJ46; -.
DR   STRING; 360412.LARV_01648; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000055060; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000055060};
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..248
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          260..442
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        241
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         82..83
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            9
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   492 AA;  52172 MW;  F1B8E60E675867C1 CRC64;
     MNRYLLGLDL GTSGLKAAVL DGSGRMLASA GREYAIDSPR PGWAEQDPQV WYTAACAAVS
     QVLAESGVRG DEVQGVGLAG QMHSLVCVDE NGAAVRPAIL WADQRSAPQV KRLNEQIGRE
     KLAASAGNPV AAGFAISSWL WLRENEPETV RRTRFLLQPK DMLRFMLTGV IGGEPSDASA
     TLLFDPHTWT WSPVLLEAAG LSPDRLPPLH PSAEVCAGLT SAAARDLNLK AGTPVVYGGS
     DQAVQALGQG IIDVGQVSGT IGTGGQWFAP LAQPVHDPQL RLHLFCHVLP ARWHLEAAIL
     TAGLALRWLR DQVLTGGGYT ELADAAAGVA AATDGLFFLP YLAGERTPHM DPLATAAFTG
     LTLRHGRAHL TRAVMEGVVF AMREGLDLLE GLGVHPEAVL ACGGSNRHPL WLKLQANIYN
     RPIQPAASPE ATARGAALLA GVGIGQFDSF SAAVQAVPAP HPAVLPDPAE VEKYDRAYPR
     FKQIYPALKK AE
//

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