PHNN_LARHH
ID PHNN_LARHH Reviewed; 410 AA.
AC C1D7Y5;
DT 21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
DE RecName: Full=Ribose 1,5-bisphosphate phosphokinase PhnN;
DE EC=2.7.4.23;
DE AltName: Full=Ribose 1,5-bisphosphokinase;
GN Name=phnN; OrderedLocusNames=LHK_01589;
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales;
OC Chromobacteriaceae; Laribacter.
OX NCBI_TaxID=557598;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9;
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C.Y., Lau S.K.P., Tse H., Teng J.L.L., Curreem S.O., Tsang A.K.L.,
RA Fan R.Y.Y., Wong G.K.M., Huang Y., Loman N.J., Snyder L.A.S., Cai J.J.,
RA Huang J.-D., Mak W., Pallen M.J., Lok S., Yuen K.-Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
CC -!- FUNCTION: Catalyzes the phosphorylation of ribose 1,5-bisphosphate to
CC 5-phospho-D-ribosyl alpha-1-diphosphate (PRPP). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha-D-ribose 1,5-bisphosphate + ATP = 5-phospho-alpha-D-
CC ribose 1-diphosphate + ADP; Xref=Rhea:RHEA:20109, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:58017, ChEBI:CHEBI:68688, ChEBI:CHEBI:456216;
CC EC=2.7.4.23;
CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose
CC 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from
CC D-ribose 5-phosphate (route II): step 3/3.
CC -!- SIMILARITY: In the C-terminal section; belongs to the ribose 1,5-
CC bisphosphokinase family. {ECO:0000305}.
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DR EMBL; CP001154; ACO74575.1; -; Genomic_DNA.
DR AlphaFoldDB; C1D7Y5; -.
DR SMR; C1D7Y5; -.
DR STRING; 557598.LHK_01589; -.
DR PRIDE; C1D7Y5; -.
DR EnsemblBacteria; ACO74575; ACO74575; LHK_01589.
DR KEGG; lhk:LHK_01589; -.
DR eggNOG; COG3709; Bacteria.
DR HOGENOM; CLU_603790_0_0_4; -.
DR OMA; RATQANE; -.
DR UniPathway; UPA00087; UER00175.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0033863; F:ribose 1,5-bisphosphate phosphokinase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0019634; P:organic phosphonate metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00836; PhnN; 1.
DR InterPro; IPR009389; DUF1045.
DR InterPro; IPR008145; GK/Ca_channel_bsu.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR012699; PhnN.
DR Pfam; PF06299; DUF1045; 1.
DR SMART; SM00072; GuKc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02322; phosphon_PhnN; 1.
PE 3: Inferred from homology;
KW ATP-binding; Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..410
FT /note="Ribose 1,5-bisphosphate phosphokinase PhnN"
FT /id="PRO_0000412789"
FT REGION 1..220
FT /note="unknown"
FT REGION 221..410
FT /note="Ribose 1,5-bisphosphokinase"
FT BINDING 233..240
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 410 AA; 43805 MW; BA3CC5A8BEDF28A3 CRC64;
MRYAVYLAPP PASRFWQLGS AWLGRDAWLN RPVALPSGWS AADADRVAAA ARYGWHATLR
APFALAEGAS EAAVHATLRT LARRFATFGL TLAPATLNGF AALRPVSGQS QVAELATAAL
LALDALAAPA PLRTGLSARE AELCRRWGYP YVFECYRCHF TLTSQLDEVD IPSWLARAAA
HFDGALYQPV EGLALFVEPE AGAAFRLCRL VWLLMAGSTS MRTETGQLIY VMGPSGAGKD
SLLGYARERL AGQPLVFAHR YITRPATAGS ENHVALSEAE FALREAHGCF ALSWRRNGLA
YGLGCEVTDW LAAGLVVVVN GSRAALPQAR QCFPGLKPLW ITASPAVLAA RLAARGRESA
DDIAARLAAS AGFRPPADCR VLCNDGELAV AGDELVAWLS SHCHQPITAL
