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Database: UniProt
Entry: G4HGU5_9BACL
LinkDB: G4HGU5_9BACL
Original site: G4HGU5_9BACL 
ID   G4HGU5_9BACL            Unreviewed;       559 AA.
AC   G4HGU5;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   27-MAR-2024, entry version 58.
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=PaelaDRAFT_3082 {ECO:0000313|EMBL:EHB63968.1};
OS   Paenibacillus lactis 154.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX   NCBI_TaxID=743719 {ECO:0000313|EMBL:EHB63968.1, ECO:0000313|Proteomes:UP000003891};
RN   [1] {ECO:0000313|EMBL:EHB63968.1, ECO:0000313|Proteomes:UP000003891}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=154 {ECO:0000313|EMBL:EHB63968.1,
RC   ECO:0000313|Proteomes:UP000003891};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Land M.L., Hauser L., Siebers A., Thelen M., Hugenholtz P.,
RA   Allgaier M., Woyke T.J.;
RT   "The draft genome of Paenibacillus lactis 154.";
RL   Submitted (SEP-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; AGIP01000006; EHB63968.1; -; Genomic_DNA.
DR   RefSeq; WP_007130250.1; NZ_AGIP01000006.1.
DR   AlphaFoldDB; G4HGU5; -.
DR   STRING; 743719.PaelaDRAFT_3082; -.
DR   PATRIC; fig|743719.3.peg.3112; -.
DR   eggNOG; COG1069; Bacteria.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000003891; 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; 3.30.420.40; -; 2.
DR   HAMAP; MF_00520; Ribulokinase; 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; 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.
DR   PROSITE; PS00445; FGGY_KINASES_2; 1.
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          5..275
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          290..488
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   559 AA;  60903 MW;  D54E2C78A6BCC0F8 CRC64;
     MKQLYTIGVD FGTESGRALL VDITTGQEVA THVTPYKHGV MDEVLVHSGL KLEQDWALQH
     PGDYLEVLRQ SIPHVLSEAD VSPDQVIGIG IDFTACTMMP LDAGGTPLCM LDEWRDNPHS
     WVKLWKHHAA QDEANLINET AKRRGEKFLS RYGGKLSSEW MLAKSLQILH EAPELYEQAV
     LFMEAADWVV MQLTGQLARS SCTAGYKANW HKREGYPSKE FLQSLDPRFG DLVETKLRGP
     IKPLGSKAGG LTESMAALTG LLPGTAVAVA NIDAHAMVPA VSVVTPGKLV LAMGTSTCHL
     ILSDKEMTGE GICGVVEDGI IPGYYGYEAG QSAVGDIFAW YVDEAVPEYV RRKAAEERLG
     IHEWLEREAA QYAPGQTGLL AIDWWNGSRS VLMDADLSGV ILGLTLQTKP AEIYRALLEA
     TAFGTRAIIE AFTESGVEVQ ELYACGGLPQ RNRLLMQIYA DVTGKEIKVA DTVQTAAFGA
     AMFGAVAAGK EQGGFGSIVE AAEAIARVRE ETFKPIEANV RVYDQLYKEY KRLHDYLGRG
     ENGVLKRLKS LKSGAGSEG
//
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