ID F8IDY1_ALIAT Unreviewed; 563 AA.
AC F8IDY1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 61.
DE RecName: Full=Ribulokinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
DE EC=2.7.1.16 {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
GN Name=araB {ECO:0000256|HAMAP-Rule:MF_00520,
GN ECO:0000313|EMBL:AEJ42635.1};
GN OrderedLocusNames=TC41_0677 {ECO:0000313|EMBL:AEJ42635.1};
OS Alicyclobacillus acidocaldarius (strain Tc-4-1) (Bacillus acidocaldarius).
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=1048834 {ECO:0000313|EMBL:AEJ42635.1, ECO:0000313|Proteomes:UP000000292};
RN [1] {ECO:0000313|EMBL:AEJ42635.1, ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|EMBL:AEJ42635.1,
RC ECO:0000313|Proteomes:UP000000292};
RX PubMed=21914900; DOI=10.1128/JB.05709-11;
RA Chen Y., He Y., Zhang B., Yang J., Li W., Dong Z., Hu S.;
RT "Complete Genome Sequence of Alicyclobacillus acidocaldarius Strain Tc-
RT 4-1.";
RL J. Bacteriol. 193:5602-5603(2011).
RN [2] {ECO:0000313|Proteomes:UP000000292}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tc-4-1 {ECO:0000313|Proteomes:UP000000292};
RA Chen Y., He Y., Dong Z., Hu S.;
RT "The complete genome sequence of Alicyclobacillus acidocaldarius sp. Tc-4-
RT 1.";
RL Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + D-ribulose = ADP + D-ribulose 5-phosphate + H(+);
CC Xref=Rhea:RHEA:17601, ChEBI:CHEBI:15378, ChEBI:CHEBI:17173,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58121, ChEBI:CHEBI:456216;
CC EC=2.7.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00520};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-ribulose = ADP + H(+) + L-ribulose 5-phosphate;
CC Xref=Rhea:RHEA:22072, ChEBI:CHEBI:15378, ChEBI:CHEBI:16880,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:58226, ChEBI:CHEBI:456216;
CC EC=2.7.1.16; Evidence={ECO:0000256|HAMAP-Rule:MF_00520,
CC ECO:0000256|RuleBase:RU003455};
CC -!- PATHWAY: Carbohydrate degradation; L-arabinose degradation via L-
CC ribulose; D-xylulose 5-phosphate from L-arabinose (bacterial route):
CC step 2/3. {ECO:0000256|HAMAP-Rule:MF_00520,
CC ECO:0000256|RuleBase:RU003455}.
CC -!- SIMILARITY: Belongs to the ribulokinase family. {ECO:0000256|HAMAP-
CC Rule:MF_00520, ECO:0000256|RuleBase:RU003455}.
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DR EMBL; CP002902; AEJ42635.1; -; Genomic_DNA.
DR AlphaFoldDB; F8IDY1; -.
DR STRING; 1048834.TC41_0677; -.
DR KEGG; aad:TC41_0677; -.
DR PATRIC; fig|1048834.4.peg.638; -.
DR eggNOG; COG1069; Bacteria.
DR HOGENOM; CLU_009281_9_1_9; -.
DR OrthoDB; 9805576at2; -.
DR UniPathway; UPA00145; UER00566.
DR Proteomes; UP000000292; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0019150; F:D-ribulokinase activity; IEA:RHEA.
DR GO; GO:0008741; F:ribulokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019569; P:L-arabinose catabolic process to xylulose 5-phosphate; IEA:UniProtKB-UniRule.
DR CDD; cd07781; FGGY_RBK; 1.
DR Gene3D; 3.30.420.40; -; 2.
DR HAMAP; MF_00520; Ribulokinase; 1.
DR InterPro; IPR043129; ATPase_NBD.
DR InterPro; IPR000577; Carb_kinase_FGGY.
DR InterPro; IPR018485; FGGY_C.
DR InterPro; IPR018484; FGGY_N.
DR InterPro; IPR005929; Ribulokinase.
DR NCBIfam; TIGR01234; L-ribulokinase; 1.
DR PANTHER; PTHR43435:SF4; FGGY CARBOHYDRATE KINASE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43435; RIBULOKINASE; 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 Arabinose catabolism {ECO:0000256|ARBA:ARBA00022935, ECO:0000256|HAMAP-
KW Rule:MF_00520}; ATP-binding {ECO:0000256|HAMAP-Rule:MF_00520};
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277, ECO:0000256|HAMAP-
KW Rule:MF_00520};
KW Kinase {ECO:0000256|HAMAP-Rule:MF_00520, ECO:0000256|RuleBase:RU003455};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00520};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW ECO:0000256|RuleBase:RU003455}.
FT DOMAIN 6..277
FT /note="Carbohydrate kinase FGGY N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00370"
FT DOMAIN 291..489
FT /note="Carbohydrate kinase FGGY C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02782"
SQ SEQUENCE 563 AA; 62176 MW; EAFD0E22611141AF CRC64;
MEMSEYSIGV DYGTQSGRAV LVEIGTGREI TKAVKNYTHG VMDEYLPDGV TRLGPDWALQ
HPRDYVEVLE ETIPRLLRES GVRPEDVIGI GIDFTSCTML PIRADGTPLC LEPRFERHPH
AYVKLWKHHA AQDEANKLNE IARERGEAFL ARYGGKISSE WMIPKIWQIL DEAPEIYDAA
DAMVEATDWI VMQLTGKLVR SSCPAGYKSI WHKRTGYPSR DFFKALHPRL EHVVEEKLWG
PILPIGSRAG ELTEAMARRI GLVPGTPVAV GNVDAHVSMP AVGITEPGKM LMIIGTSTCH
VLLGTEERAV PGMCGVVEDG IIPGYMGYEA GQSCVGDHFE WWIENGVPPA YWDEARREGI
GIHDLLTRKA AKLRPGETGL LALDWWNGNR STLVDADLTG LLIGATLATK PEDIYRALIE
ATAYGTRMIV ETFRASGVPV DEMYACGGIA QKNALMMQIY ADVLNMPIYI GASTQAPTLG
AAMFGAVAAG KARGGYDSIE EAAREMGSVR EKPYVPNPSA VKVYDELYRE YTRLYDYFGR
GENNVMKVLK RIKSAVAQEE VKI
//
