ID J7SJZ4_MORMO Unreviewed; 503 AA.
AC J7SJZ4;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 52.
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=MU9_3131 {ECO:0000313|EMBL:AGG32175.1};
OS Morganella morganii subsp. morganii KT.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Morganella.
OX NCBI_TaxID=1124991 {ECO:0000313|EMBL:AGG32175.1, ECO:0000313|Proteomes:UP000011834};
RN [1] {ECO:0000313|EMBL:AGG32175.1, ECO:0000313|Proteomes:UP000011834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT {ECO:0000313|EMBL:AGG32175.1,
RC ECO:0000313|Proteomes:UP000011834};
RX PubMed=23282187;
RA Chen Y.T., Peng H.L., Shia W.C., Hsu F.R., Ken C.F., Tsao Y.M., Chen C.H.,
RA Liu C.E., Hsieh M.F., Chen H.C., Tang C.Y., Ku T.H.;
RT "Whole-genome sequencing and identification of Morganella morganii KT
RT pathogenicity-related genes.";
RL BMC Genomics 13:S4-S4(2012).
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; CP004345; AGG32175.1; -; Genomic_DNA.
DR RefSeq; WP_004237726.1; NC_020418.1.
DR AlphaFoldDB; J7SJZ4; -.
DR GeneID; 69677834; -.
DR KEGG; mmk:MU9_3131; -.
DR eggNOG; COG1070; Bacteria.
DR HOGENOM; CLU_009281_3_0_6; -.
DR Proteomes; UP000011834; 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 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; 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:UP000011834};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_02220};
KW Xylose metabolism {ECO:0000256|HAMAP-Rule:MF_02220,
KW ECO:0000256|RuleBase:RU364073}.
FT DOMAIN 4..252
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 263..443
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 503 AA; 53852 MW; FBFFC34956CA3251 CRC64;
MTLYAGIDCG TQSTKVIIAD NRTARILGEG SASHPMISES DGSREQEAVW WTDALQTAFA
QAIKNAGIDG RDIRALAVSG QQHGFVPVSH DGTVLAPAKL WCDTSTSAEN QWFIDALGGE
QAALDRLGVL PQTGYTVSKI IRFKQQHPEL WKQLRYVLLP HDYLNFWLTG QACAEYGDAS
GTGLLNIRSR EWDQAAADLI DPEGRLWQAL PPLVRAEQII GTVRPEIAEK LGISPETRVA
SGGGDNMMAA IGTGNIRPGI TTMSLGTSGT LFTFAEQPVV ADSAMIAGFC SSSNGWLPLI
CTMNVTSATT TVQSLLGMDI QAFNDALNSS KPGAGGLIML PFFNGERVPQ LPEARASLHN
MDGSNLTPQN LSLAVVESAT YGLRFGIDLF RQQGITTSEI RLTGGGARSV KWRQIVADIM
AAPVVCVTNQ EAAALGAAVQ AIWCDTLSAD SAPEAQLAAL CDRFVQLDDS SRTQPDPANV
AVYESLYQNY LALLTSEYPE VTV
//
