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Database: UniProt
Entry: A0A1Q4GS39_9PROT
LinkDB: A0A1Q4GS39_9PROT
Original site: A0A1Q4GS39_9PROT 
ID   A0A1Q4GS39_9PROT        Unreviewed;       295 AA.
AC   A0A1Q4GS39;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=phosphoribulokinase {ECO:0000256|ARBA:ARBA00012042};
DE            EC=2.7.1.19 {ECO:0000256|ARBA:ARBA00012042};
GN   ORFNames=BGP21_01075 {ECO:0000313|EMBL:OJZ18061.1};
OS   Thiobacillus sp. 65-29.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=1895862 {ECO:0000313|EMBL:OJZ18061.1, ECO:0000313|Proteomes:UP000186483};
RN   [1] {ECO:0000313|EMBL:OJZ18061.1, ECO:0000313|Proteomes:UP000186483}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=65-29 {ECO:0000313|EMBL:OJZ18061.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + D-ribulose 5-phosphate = ADP + D-ribulose 1,5-
CC         bisphosphate + H(+); Xref=Rhea:RHEA:19365, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57870, ChEBI:CHEBI:58121,
CC         ChEBI:CHEBI:456216; EC=2.7.1.19;
CC         Evidence={ECO:0000256|ARBA:ARBA00001430};
CC   -!- SIMILARITY: Belongs to the phosphoribulokinase family.
CC       {ECO:0000256|ARBA:ARBA00009719}.
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:OJZ18061.1}.
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DR   EMBL; MKWN01000033; OJZ18061.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q4GS39; -.
DR   STRING; 1895862.BGP21_01075; -.
DR   Proteomes; UP000186483; Unassembled WGS sequence.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0008974; F:phosphoribulokinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR006082; PRK.
DR   InterPro; IPR006083; PRK/URK.
DR   Pfam; PF00485; PRK; 1.
DR   PRINTS; PR00478; PHRIBLKINASE.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE   3: Inferred from homology;
KW   Kinase {ECO:0000313|EMBL:OJZ18061.1};
KW   Transferase {ECO:0000313|EMBL:OJZ18061.1}.
FT   DOMAIN          7..221
FT                   /note="Phosphoribulokinase/uridine kinase"
FT                   /evidence="ECO:0000259|Pfam:PF00485"
SQ   SEQUENCE   295 AA;  33184 MW;  0423E345541395A3 CRC64;
     MSKKHPVIAV TGSSGAGTTT VKRAFEHIFL REKINAAVIE GDSFHSLSRV EFKEAVKKAE
     GEGNKHFSHF GPQSNHFDKL ADLFRTYGET GGGKRRYYIH SDEEADQHNK RLNTSLNPGE
     FTPWEDLPAG SDVLFYEGLH GLVKTDTVDV SKHVDLGIGV VPIVNLEWIQ KIHRDGAERG
     YSADVIVDTI LRRMPDYVNY VTPQFSRTDI NFQRVSTVDT SNPFITRDIP TPDESFIVIR
     FRDPKGVDFP YLLNMIPNSF MSRRNTLVVP GGKMGFAMEL ILAPIIQDMI ASRSR
//
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