UniProt: A0A0A1CZM9

Database: UniProt
Entry: A0A0A1CZM9_9MICC

LinkDB:  A0A0A1CZM9_9MICC 
Original site:  A0A0A1CZM9_9MICC

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Ontology (4)   
   GO (4)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (7)   
   InterPro (5)   
   Pfam (2)   
All databases (14)   

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ID   A0A0A1CZM9_9MICC        Unreviewed;       473 AA.
AC   A0A0A1CZM9;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
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=ART_2839 {ECO:0000313|EMBL:AIY02438.1};
OS   Arthrobacter sp. PAMC 25486.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1494608 {ECO:0000313|EMBL:AIY02438.1, ECO:0000313|Proteomes:UP000030301};
RN   [1] {ECO:0000313|EMBL:AIY02438.1, ECO:0000313|Proteomes:UP000030301}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PAMC25486 {ECO:0000313|EMBL:AIY02438.1,
RC   ECO:0000313|Proteomes:UP000030301};
RA   Jung J.-H., Joe M.-H., Cho Y.-J., Lee S.G., Han S.J., Lim S., Choi J.-I.;
RT   "Complete genome sequence of Arthrobacter sp. PAMC25486 isolated from the
RT   Arctic.";
RL   Submitted (APR-2014) 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}.
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DR   EMBL; CP007595; AIY02438.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A1CZM9; -.
DR   STRING; 1494608.ART_2839; -.
DR   KEGG; arm:ART_2839; -.
DR   HOGENOM; CLU_009281_12_0_11; -.
DR   Proteomes; UP000030301; Chromosome.
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; 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.
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:RU364073};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030301};
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          11..242
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          251..434
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        235
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         81..82
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            15
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   473 AA;  48494 MW;  A2F27BC37343A900 CRC64;
     MPGSTAPGTL VVGVDSSTQS CKVVAVDIAT GAQVTAGSAT HPDGTSIDPR LWTAALAEAW
     DAAGIAGLGD RVVGVAVAAQ QHGMVGVDGA GVPVHDALLW NDVRSADDAA RMVAELGPEA
     WVGAVNILPV ASFTLTKLAW LARSQPDAAA RLDTVGLPHD WLNLQLSGSW STDRSDASGT
     AYFDPVANKY RTELLEQFFG AVPSLPQVLA PNESAGQLLP RWGSSAAVVG AGMGDNAGAA
     LGLELAPGEV AVSIGTSGTV FTVSETAVHD VSGQLAGFAD ATGRHLPLLA TINAARVMAA
     GAAMLNVDLA EFDRLALAAA PDADGLTLMP YLDGERTPNL PDATGTLVGM TRANMTPENL
     ARASVLAVVN SLADALAALT SFGVPVERVL LIGGGAKSRA LREAAATVFG VPVDVPEQRE
     YVALGAARQA AWAATGELPV WGRRIERSFM PDGGWGALVR ERYATARRTV YGV
//

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