ID E1RBH2_SEDSS Unreviewed; 412 AA.
AC E1RBH2;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=ribose-phosphate diphosphokinase {ECO:0000256|ARBA:ARBA00013247};
DE EC=2.7.6.1 {ECO:0000256|ARBA:ARBA00013247};
GN OrderedLocusNames=Spirs_0557 {ECO:0000313|EMBL:ADK79702.1};
OS Sediminispirochaeta smaragdinae (strain DSM 11293 / JCM 15392 / SEBR 4228)
OS (Spirochaeta smaragdinae).
OC Bacteria; Spirochaetota; Spirochaetia; Spirochaetales; Spirochaetaceae;
OC Sediminispirochaeta.
OX NCBI_TaxID=573413 {ECO:0000313|EMBL:ADK79702.1, ECO:0000313|Proteomes:UP000002318};
RN [1] {ECO:0000313|EMBL:ADK79702.1, ECO:0000313|Proteomes:UP000002318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11293 / JCM 15392 / SEBR 4228
RC {ECO:0000313|Proteomes:UP000002318};
RX PubMed=21304743; DOI=10.4056/sigs.1143106;
RA Mavromatis K., Yasawong M., Chertkov O., Lapidus A., Lucas S., Nolan M.,
RA Del Rio T.G., Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N.,
RA Tapia R., Han C., Bruce D., Goodwin L., Pati A., Chen A., Palaniappan K.,
RA Land M., Hauser L., Chang Y.J., Jeffries C.D., Detter J.C., Rohde M.,
RA Brambilla E., Spring S., Goker M., Sikorski J., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT "Complete genome sequence of Spirochaeta smaragdinae type strain (SEBR
RT 4228).";
RL Stand. Genomic Sci. 3:136-144(2010).
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000256|RuleBase:RU004324}.
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DR EMBL; CP002116; ADK79702.1; -; Genomic_DNA.
DR RefSeq; WP_013253166.1; NC_014364.1.
DR AlphaFoldDB; E1RBH2; -.
DR STRING; 573413.Spirs_0557; -.
DR KEGG; ssm:Spirs_0557; -.
DR eggNOG; COG0462; Bacteria.
DR HOGENOM; CLU_033546_8_0_12; -.
DR OrthoDB; 9777067at2; -.
DR Proteomes; UP000002318; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000002318};
KW Transferase {ECO:0000313|EMBL:ADK79702.1}.
FT DOMAIN 87..192
FT /note="Ribose-phosphate pyrophosphokinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF13793"
FT DOMAIN 223..331
FT /note="Phosphoribosyltransferase"
FT /evidence="ECO:0000259|Pfam:PF00156"
SQ SEQUENCE 412 AA; 47130 MW; 55DBE16D0AACA574 CRC64;
MSIIKPASLG IIACPGAEQF TSDVIRHLKR QYVKKYHKLA DDLSAKYNMT TEEVWKRMNF
IEDLHRLEDD PRKRPVDRFR PPKFRLPVRF TRFANGEFKS ELLSSVKGMS VFIIQDVENH
YPLAFYNLEE NVCLSVNDHV MMLFTTIDAA LEAGAESVTL VLPTYPYSRQ HKKRGREALT
ARWFGQMCEH SGASRIITVD IHSKEIENTF NKLILENLHG SYQIIRALKD LVDLNDPDLV
VVSPDTGAVD RNKFYAGNLK KPLALLYKER DYSRVSRDAS SSNITNIRLL GDVKGKIVFM
ADDMLGTGGT LMKAMRELKR LGARQIIAAA SLPFFTGDAI EHFEQAYKEG IFYRIIGTNA
VYHDATLLER EWYVSADITD LHARIISRLH HGRSLSPLLE NSRIIQKLLR KE
//