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Database: UniProt
Entry: A0A1A7NUV0_9PAST
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ID   A0A1A7NUV0_9PAST        Unreviewed;       559 AA.
AC   A0A1A7NUV0;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=QS62_07475 {ECO:0000313|EMBL:OBW93355.1};
OS   Gallibacterium salpingitidis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Gallibacterium.
OX   NCBI_TaxID=505341 {ECO:0000313|EMBL:OBW93355.1, ECO:0000313|Proteomes:UP000092649};
RN   [1] {ECO:0000313|EMBL:OBW93355.1, ECO:0000313|Proteomes:UP000092649}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F150 {ECO:0000313|EMBL:OBW93355.1,
RC   ECO:0000313|Proteomes:UP000092649};
RA   Kudirkiene E., Bojesen A.M.;
RT   "Pan-genome of Gallibacterium spp.";
RL   Submitted (NOV-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:OBW93355.1}.
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DR   EMBL; JTJL01000039; OBW93355.1; -; Genomic_DNA.
DR   RefSeq; WP_066108197.1; NZ_JTJL01000039.1.
DR   AlphaFoldDB; A0A1A7NUV0; -.
DR   PATRIC; fig|505341.3.peg.1503; -.
DR   OrthoDB; 9805576at2; -.
DR   UniPathway; UPA00145; UER00566.
DR   Proteomes; UP000092649; 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; 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:UP000092649};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00520,
KW   ECO:0000256|RuleBase:RU003455}.
FT   DOMAIN          6..283
FT                   /note="Carbohydrate kinase FGGY N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00370"
FT   DOMAIN          293..501
FT                   /note="Carbohydrate kinase FGGY C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02782"
SQ   SEQUENCE   559 AA;  61400 MW;  B692917981A168C5 CRC64;
     MEENKYVIGL DFGSDSIRAL IVDVLNGNEL GSGVCHYPRW MEGKYSDAKI SQFRHHPQDY
     IDAMTSAVQQ ALSSVNKDIV NNIIGIGVDT TGSTPAPVDE NGVVLALKPE FAENPNAMFI
     LWKDHTAIDE AEKINLLAHS GEFPDYTQYV GGVYSSEWYW AKIAHINEQD SAVAKAAYTW
     VELADWVPAL LTGNIAPNQI RRGVCAAGHK ALWHADWDGL PSEEFLTAIS PTLKSLRAHY
     SKQVYTSDQE AGKLNQQWAE KLGLPIGISV AVGAFDCHMG AVGAGAREND LVKVIGTSTC
     DILMVKREDV TGKLIEGICG QVEGSALPDF VALEAGQSAF GDVYAWYQRL LAWPLQLGAE
     KYPELKEKLQ DISSSLLPTL SQLIEHHSDS HVLALDWFNG RRTPFANQHL KGAIVNMNLG
     TNAVDIFRCL VESTAFGAKA INDCFLDQGM TIKRIIAIGG ISKKSASIMQ LCSDVMETEI
     AVVKSDQCCA LGAAIFAALA AGVYTDSISA QKAMSSKFIK VYQPDRERSR YYRERYEQYL
     MFGNYMEEII MATAAQTEK
//
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