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Database: UniProt
Entry: A0A0Q4MHU0_9GAMM
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ID   A0A0Q4MHU0_9GAMM        Unreviewed;       505 AA.
AC   A0A0Q4MHU0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 31.
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=ASF13_10205 {ECO:0000313|EMBL:KQN54813.1};
OS   Erwinia sp. Leaf53.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=1736225 {ECO:0000313|EMBL:KQN54813.1, ECO:0000313|Proteomes:UP000050856};
RN   [1] {ECO:0000313|EMBL:KQN54813.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN54813.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQN54813.1, ECO:0000313|Proteomes:UP000050856}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf53 {ECO:0000313|EMBL:KQN54813.1,
RC   ECO:0000313|Proteomes:UP000050856};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-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: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:KQN54813.1}.
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DR   EMBL; LMLK01000023; KQN54813.1; -; Genomic_DNA.
DR   RefSeq; WP_056238647.1; NZ_LMLK01000023.1.
DR   AlphaFoldDB; A0A0Q4MHU0; -.
DR   STRING; 1736225.ASF13_10205; -.
DR   Proteomes; UP000050856; 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; cd07809; FGGY_D-XK_1; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000050856};
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          4..252
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          263..444
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
FT   ACT_SITE        245
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            8
FT                   /note="Important for activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_02220"
SQ   SEQUENCE   505 AA;  53666 MW;  DBEBB9E30E4B4F3E CRC64;
     MALYAGIDCG TQGTKVVIVD GDTGTLLGEG SAAHQLIADA SGRREQQADW WIEALISAFH
     QAVAAAGVAA ADIVALGVSG QQHGFVPLDE QGKVLHNVKL WCDTETDAEN QQLIAALGGV
     PAALAQLGLL PATGYTASKI LWFRQHHPEK WAQLHSVLLP HDYLNFWLTG ERVAEYGDAS
     GTGLLDVRSR QWDRRTVELI DDSGRLWNAL PPLLSAGQCI GTLRPEAAAA LGLSPATRVA
     TGGGDNMMSA IGSGTIAPGV VTLSLGTSGT LFAWSPEPLA SPSAEVAGFC SSDNGWLPLI
     CTMNVTSATS TVQTLLQEDI AGFNRLLEQA APGAGGVEML PFFNGERVPP LPHARASLHN
     LGSDNFTRAN LVRAVVESAT YGLRYGIELF RQQGITVSEI RLTGGGSRSA AWRQIVADVM
     GCPVICLQVG EAAALGGAIQ AMWMTALADE HTPPFSPLLA RLCQRFVALD PATRTEPDAA
     RQAEYDTLYQ RYLQRLQQSY PEVQP
//
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