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Database: UniProt
Entry: A0A494XTW2_9BACL
LinkDB: A0A494XTW2_9BACL
Original site: A0A494XTW2_9BACL 
ID   A0A494XTW2_9BACL        Unreviewed;       557 AA.
AC   A0A494XTW2;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 16.
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=D7Z26_15325 {ECO:0000313|EMBL:RKP53101.1};
OS   Cohnella endophytica.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Cohnella.
OX   NCBI_TaxID=2419778 {ECO:0000313|EMBL:RKP53101.1, ECO:0000313|Proteomes:UP000282076};
RN   [1] {ECO:0000313|EMBL:RKP53101.1, ECO:0000313|Proteomes:UP000282076}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M2MS4P-1 {ECO:0000313|EMBL:RKP53101.1,
RC   ECO:0000313|Proteomes:UP000282076};
RA   Tuo L.;
RT   "Cohnella sp. M2MS4P-1, whole genome shotgun sequence.";
RL   Submitted (OCT-2018) 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:RKP53101.1}.
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DR   EMBL; RBZM01000006; RKP53101.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A494XTW2; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000282076; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000282076};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW   ECO:0000256|RuleBase:RU003455}.
FT   DOMAIN          5..277
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   557 AA;  60683 MW;  BD8B9D5702455CCD CRC64;
     MSHKYAIGVD YGTQSGRAVL VDLTNGHEVA DHVTPYPHGV IDETLPTSGK QLEHDWALQH
     PGDYIEVLRR SIPAVLAQSG VSPADVIGLG IDFTACTMLP VDERGTPLCF KPEWSDNPHG
     WVKLWKHHAA QDEADRLNAM AAQRGEKFLP RYGGKISSEW MIAKVWQIAN EAPDVYDASD
     LFTEATDWVI SQLTGNFVRN SCTAGYKSIW HKREGYPSSD FFKALDPRLE NLTETKLRGD
     IVPLGTKAGE LTEEMAKLTG LNAGTAIAVG NVDAHAAVPA VGVVTPGKLV MAMGTSICHM
     LLGTEEVEVE GMCGVVEDGI IPGYLGYEAG QSAVGDIFEW FVEEAVPAYV KEAAGKEGVG
     VHQWLTERAS AYRPGETGLL ALDWWNGNRS VLVDTNLTGV IVGFSLLTKP EEVYRTLLES
     TAFGTRKIID AFHHNGVPVD EVYACGGLPQ RNRLLMQIYA DVTNREIKIA DSKQTPAVGA
     AMFGAVAAGS AKGGYDSVVD AAKAMARVRE ETFKPIPENV AIYDKLYREY GELHDYFGRG
     ANDVMKRLKA LKDETSR
//
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