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Database: UniProt
Entry: A0A071LXR8_9ENTR
LinkDB: A0A071LXR8_9ENTR
Original site: A0A071LXR8_9ENTR 
ID   A0A071LXR8_9ENTR        Unreviewed;       570 AA.
AC   A0A071LXR8;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 40.
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   ORFNames=DT73_07585 {ECO:0000313|EMBL:KEA53217.1};
OS   Mangrovibacter sp. MFB070.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Mangrovibacter.
OX   NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA53217.1, ECO:0000313|Proteomes:UP000027726};
RN   [1] {ECO:0000313|EMBL:KEA53217.1, ECO:0000313|Proteomes:UP000027726}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MFB070 {ECO:0000313|EMBL:KEA53217.1,
RC   ECO:0000313|Proteomes:UP000027726};
RA   Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT   "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT   Bacterium Isolated from an Aquaculture Farm.";
RL   Submitted (APR-2014) 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}.
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:KEA53217.1}.
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DR   EMBL; JJMI01000019; KEA53217.1; -; Genomic_DNA.
DR   RefSeq; WP_036106259.1; NZ_JJMI01000019.1.
DR   AlphaFoldDB; A0A071LXR8; -.
DR   eggNOG; COG1069; Bacteria.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000027726; Unassembled WGS sequence.
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; 1.20.58.2240; -; 1.
DR   Gene3D; 3.30.420.40; -; 1.
DR   HAMAP; MF_00520; Ribulokinase; 1.
DR   InterPro; IPR043129; ATPase_NBD.
DR   InterPro; IPR018485; FGGY_C.
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   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   Reference proteome {ECO:0000313|Proteomes:UP000027726};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00520}.
FT   DOMAIN          291..501
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   570 AA;  61388 MW;  61718E1703A8CF89 CRC64;
     MAIALGLDFG SDSVRALAVD TITGSELATS VEWYPRWQEG RYCNAPKNQF RHHPLDYIES
     MEKALKTVLA DLSAEQRDAV VGIGVDSTGS TPAPIDKDGN VLALTPEFAE NPNAMFVLWK
     DHTAVEEAEA ITRLCHAPGH KDYSRYIGGI YSSEWFWAKI LHVTRADQSV AKAAASWIEL
     CDWIPALLSD TTRPEAIRRG RCSAGHKSLW HESWGGLPPA SFFDELDPII NKHLPHPLFT
     DTWTADIPVG TLSAQWAERL GLPQTVVISG GAFDCHMGAV GAGAQANTLV KVIGTSTCDI
     LIADKPTVGD RAVKGICGQV DGSVVPHFIG LEAGQSAFGD IYAWFGRVLG WPLDQLAAQQ
     PELKETLQAS KKQLLPALTE AWAKDPALDH LPVVLDWFNG RRTPNANQRL KGVITDLNLG
     TDAPALFGGL IAATAFGARA IMECFTEQGI PVNGVMALGG IARKNPVIMQ VCCDVLNRPL
     QIVASDQCCA LGAAIFAAVA AGVHSDIPAA QQAMASNVEK TLQPKPVSAE RFEQLYQRYL
     AWASSAEQHY LPSVTASSSA KKTDETALTH
//
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