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Database: UniProt
Entry: A0A075LG91_9BACI
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ID   A0A075LG91_9BACI        Unreviewed;       563 AA.
AC   A0A075LG91;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-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=GZ22_02570 {ECO:0000313|EMBL:AIF65640.1};
OS   Terribacillus goriensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX   NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF65640.1, ECO:0000313|Proteomes:UP000027980};
RN   [1] {ECO:0000313|EMBL:AIF65640.1, ECO:0000313|Proteomes:UP000027980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP602 {ECO:0000313|EMBL:AIF65640.1,
RC   ECO:0000313|Proteomes:UP000027980};
RA   Wang Y., Lu P., Zhang L.;
RT   "Complete genome sequence of a moderately halophilic bacterium
RT   Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT   Tianmu mountain in China.";
RL   Submitted (JUL-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}.
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DR   EMBL; CP008876; AIF65640.1; -; Genomic_DNA.
DR   RefSeq; WP_038558360.1; NZ_CP008876.1.
DR   AlphaFoldDB; A0A075LG91; -.
DR   KEGG; tap:GZ22_02570; -.
DR   HOGENOM; CLU_009281_9_1_9; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000027980; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000027980};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW   ECO:0000256|RuleBase:RU003455}.
FT   DOMAIN          8..278
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;  61742 MW;  B7D57E7EA4454B0E CRC64;
     MGTDKFSIGI DYGTQSGRAV LVRLQDGMEM AEHVTEYRHG VMDVKLPHLE KALGYEWALQ
     HPMDYLDVLR QSVPAVMQAA GVDPADVIGL GIDFTACTIL PVDVNLEPLC FDPAFRDNPH
     SWVKLWKHHA AQEEANKLNE IAGERGEGFL ARYGGKISSE WMIPKIWQIA DEAPEIYEAA
     DQFIEATDWV ISQLTGELKR NSCTAGYKAI WHKRDGYPTA DFFESLHPAM RDLADTKLRG
     EVYPLGTKAG ELQDSFAASM NLSPGIAIAV GNVDAHAAVP AMGVVTPGKL VMAMGTSICH
     MLLGTEEQTV EGMCGVVEDG IIEGYYGYEA GQSAVGDIFG WFVDEQVPAY VYRQAEAAGQ
     NVHQWLEERA STYRPGETGL LALDWMNGNR SVLVDTELSG MVLGLTLATK PEEVYRALLE
     ATAFGTRKIV DAFHQSGVSV EELYACGGLP QKNKLLMQIF ADVTNRPIYI ADSVQTPAVG
     AAMFGAVAAG AEAGGYDSVL DAADKMARVK EEVIQPIPEN VEIYELIYQE YNTLHDYFGR
     GANDVMKRLK SIRSQSERKL TVQ
//
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