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Database: UniProt
Entry: A0A1X1C0E4_9GAMM
LinkDB: A0A1X1C0E4_9GAMM
Original site: A0A1X1C0E4_9GAMM 
ID   A0A1X1C0E4_9GAMM        Unreviewed;       489 AA.
AC   A0A1X1C0E4;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=HA41_04150 {ECO:0000313|EMBL:ORM54860.1};
OS   Pantoea conspicua.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=472705 {ECO:0000313|EMBL:ORM54860.1, ECO:0000313|Proteomes:UP000193933};
RN   [1] {ECO:0000313|EMBL:ORM54860.1, ECO:0000313|Proteomes:UP000193933}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24534 {ECO:0000313|EMBL:ORM54860.1,
RC   ECO:0000313|Proteomes:UP000193933};
RX   PubMed=28255640;
RA   Palmer M., Steenkamp E.T., Coetzee M.P., Chan W.Y., van Zyl E.,
RA   De Maayer P., Coutinho T.A., Blom J., Smits T.H., Duffy B., Venter S.N.;
RT   "Phylogenomic resolution of the bacterial genus Pantoea and its
RT   relationship with Erwinia and Tatumella.";
RL   Antonie Van Leeuwenhoek 0:0-0(2017).
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}.
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:ORM54860.1}.
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DR   EMBL; MLFN01000006; ORM54860.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X1C0E4; -.
DR   OrthoDB; 9805576at2; -.
DR   Proteomes; UP000193933; 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: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.
DR   PROSITE; PS00933; FGGY_KINASES_1; 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:RU364073};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_02220,
KW   ECO:0000256|RuleBase:RU364073};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_02220};
KW   Xylose metabolism {ECO:0000256|ARBA:ARBA00022629, ECO:0000256|HAMAP-
KW   Rule:MF_02220}.
FT   DOMAIN          1..243
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          253..437
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        236
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
FT   BINDING         79..80
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   489 AA;  53394 MW;  0529570951335545 CRC64;
     MYLGIDIGTS ELKALIINTH GEIVASQHAT LSVQRPHPHW AEQDPECWWQ ACSEVLAGLR
     HQFPLAWAAI RAIGLSGQMH GAVLLDAGGK VLRPCILWND TRSAPQCERL RERYPRIMEI
     SGNMIMPGFT LPKLHWVAEN EPEIFSRVDK VLLPKDYLRW RLTGRFVSEP SDAAGTLWLD
     VSRRDWSDEL LTITGLTRAH MPELVEGSAI SGRLQPTLAS EWGLSTAVTV AGGGGDNAAS
     AVGVGAVNPG DAFISLGTSG VIFVVNDRLQ ADPQLGVHAF CHALPGRWHQ MSVMLSAASC
     LRWLCNLLSI SESQLMEEML QLSDEQMHSA PVFLPYLSGE RTPHNDPDAS GSFFNLRHET
     PRAVLGYAVL EGVAFGLADG LKVLGDARHL IQQCSLTGGG ARSALWAQLI ADVLQLPIVT
     HPASASGALG AARLAWLADG GSEHEVCLKP AVQARYQPDE RRGVVLQQRL RLFRELYIQQ
     QQVRSLLPA
//
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