UniProt: C7DDV2

Database: UniProt
Entry: C7DDV2_9RHOB

LinkDB:  C7DDV2_9RHOB 
Original site:  C7DDV2_9RHOB

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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 (7)   
   InterPro (5)   
   Pfam (2)   
All databases (14)   

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ID   C7DDV2_9RHOB            Unreviewed;       478 AA.
AC   C7DDV2;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   24-JAN-2024, entry version 44.
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, ECO:0000313|EMBL:EET49739.1};
GN   ORFNames=TR2A62_0320 {ECO:0000313|EMBL:EET49739.1};
OS   Thalassobium sp. R2A62.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Thalassobium.
OX   NCBI_TaxID=633131 {ECO:0000313|EMBL:EET49739.1, ECO:0000313|Proteomes:UP000004701};
RN   [1] {ECO:0000313|EMBL:EET49739.1, ECO:0000313|Proteomes:UP000004701}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R2A62 {ECO:0000313|EMBL:EET49739.1,
RC   ECO:0000313|Proteomes:UP000004701};
RA   Suzuki M., Ferriera S., Johnson J., Kravitz S., Beeson K., Sutton G.,
RA   Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (MAY-2009) 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; GG697169; EET49739.1; -; Genomic_DNA.
DR   RefSeq; WP_009160789.1; NZ_GG697169.2.
DR   AlphaFoldDB; C7DDV2; -.
DR   STRING; 633131.TR2A62_0320; -.
DR   eggNOG; COG1070; Bacteria.
DR   HOGENOM; CLU_009281_3_0_5; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000004701; 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; 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:SF6; 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:UP000004701};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Xylose metabolism {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073}.
FT   DOMAIN          1..239
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          249..433
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        232
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         77..78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   SITE            6
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   478 AA;  49906 MW;  346C96E151CC3116 CRC64;
     MYIGLDLGTS SLKAVLMNDD QQIVAEHVVS LSVARPHDGW SEQDPQSWGV ATDEAMRALG
     KSHDLSGVTG IGLSGHMHGA TLIGADDAVL RPCMLWNDTR SAVQAAAMDA DPQFRATSGN
     IVFPGFTAPK VDWVRANEPE VFDKIAKVLL PKDYLRLCLT GEHVSEMSDA AGTSWLDTGA
     RDWSDDLLAA CHLDRSHMPR LVEGSQVSGA LRADLAAVWG IRSAVVAGGG GDNAAAAIGA
     GVVQDGTAFL SLGTSGVLFA ANVGYRPDPA TAVHTFCHAA PDTWHQMGVI LAATDALNWL
     SGITGQSAAE LTADLGDLRA PSKTLFLPYL GGERTPHNDA AIRGQFLHLD HSSDTAAMTR
     AVLEGVAYAF ADCRDALAAT GTTLTRALAI GGGAKSDQWL RILASTLNIP LDVPKDGDFG
     AALGAARLGM MAATGAGAEI ATQPPLSHEV APDTTLTDAF REAHQNYKAA YAAIKALK
//

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