ID A1QZX6_BORT9 Unreviewed; 406 AA.
AC A1QZX6;
DT 14-APR-2009, integrated into UniProtKB/TrEMBL.
DT 14-APR-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN OrderedLocusNames=BT0544 {ECO:0000313|EMBL:AAX17868.1};
OS Borrelia turicatae (strain 91E135).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Borreliaceae;
OC Borrelia.
OX NCBI_TaxID=314724 {ECO:0000313|EMBL:AAX17868.1, ECO:0000313|Proteomes:UP000001205};
RN [1] {ECO:0000313|Proteomes:UP000001205}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=91E135 {ECO:0000313|Proteomes:UP000001205};
RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T.,
RA Schwan T.G.;
RT "The genome sequence of Borrelia hermsii and Borrelia turicatae:
RT comparative analysis of two agents of endemic N. America relapsing fever.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|RuleBase:RU004324}.
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DR EMBL; CP000049; AAX17868.1; -; Genomic_DNA.
DR RefSeq; WP_011772486.1; NZ_CP073176.1.
DR AlphaFoldDB; A1QZX6; -.
DR KEGG; btu:BT0544; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_8_0_12; -.
DR Proteomes; UP000001205; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR NCBIfam; TIGR01251; ribP_PPkin; 1.
DR PANTHER; PTHR10210:SF32; RIBOSE-PHOSPHATE DIPHOSPHOKINASE; 1.
DR PANTHER; PTHR10210; RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER; 1.
DR Pfam; PF00156; Pribosyltran; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SMART; SM01400; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; PRTase-like; 2.
PE 3: Inferred from homology;
KW Nucleotide biosynthesis {ECO:0000256|ARBA:ARBA00022727,
KW ECO:0000256|RuleBase:RU004324}; Transferase {ECO:0000313|EMBL:AAX17868.1}.
FT DOMAIN 82..183
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT DOMAIN 211..326
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 406 AA; 45924 MW; 7A5CAB4C7EBA0F67 CRC64;
MGLLIKKSIG IIACPGGRVF ADKIMEELKK IFLDSESEVI EKISQTSSCF KEDVLKLEEI
LSPFLEGLEF SNLRFDESVE IPVNFVKFAN GEFKAEILKT IRNKDIFIVQ DVSNTYPVNV
NNNEKVVMTI NDHLMNLMTT IDACMQAKAN SVSVIIPSYP YSRQDKKHSR EGLTASLFGR
FLEELRVKHI LTLDIHSKAI ENVFRKTYFE NLNASYEIFD ALAELIDIRD SSLVVVSPDT
GAVNRNKFFA SNLKRPLALL YKERDYSKVT HNVNDSNISV TKLLGDVEGK NVFMSDDILA
TGGTLIKAVK LLKSMGAKKI ICAISLPFFN GDAIRYFDKA YEEGYFYKII GTNAVYHDDR
LISKPWYYEA NVAHLFAGAI FAIHNRVSLQ KILDRSHDIQ NLISKS
//
