ID Q2LU33_SYNAS Unreviewed; 501 AA.
AC Q2LU33;
DT 21-FEB-2006, integrated into UniProtKB/TrEMBL.
DT 21-FEB-2006, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE SubName: Full=GTP pyrophosphokinase / guanosine-3',5'-bis(Diphosphate) 3'-pyrophosphohydrolase {ECO:0000313|EMBL:ABC77592.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ABC77592.1};
DE EC=3.1.7.2 {ECO:0000313|EMBL:ABC77592.1};
GN ORFNames=SYN_01901 {ECO:0000313|EMBL:ABC77592.1};
OS Syntrophus aciditrophicus (strain SB).
OC Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC Syntrophus.
OX NCBI_TaxID=56780 {ECO:0000313|EMBL:ABC77592.1, ECO:0000313|Proteomes:UP000001933};
RN [1] {ECO:0000313|EMBL:ABC77592.1, ECO:0000313|Proteomes:UP000001933}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB {ECO:0000313|EMBL:ABC77592.1,
RC ECO:0000313|Proteomes:UP000001933};
RX PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA Campbell J.W., Gunsalus R.P.;
RT "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT of microbial growth.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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DR EMBL; CP000252; ABC77592.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2LU33; -.
DR STRING; 56780.SYN_01901; -.
DR KEGG; sat:SYN_01901; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_0_2_7; -.
DR InParanoid; Q2LU33; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000001933; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR016155; Mopterin_synth/thiamin_S_b.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR007685; RelA_SpoT.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF54285; MoaD/ThiS; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000313|EMBL:ABC77592.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001933};
KW Transferase {ECO:0000313|EMBL:ABC77592.1}.
FT DOMAIN 233..346
FT /note="RelA/SpoT"
FT /evidence="ECO:0000259|SMART:SM00954"
SQ SEQUENCE 501 AA; 56391 MW; 59A6F6B951EF22C4 CRC64;
MGRDTQVLAC GSLFIEKIEN TYTAKDANLL KKAYAFSRQR ESDCDSSSFK AAELLIEQGA
DGETVACALV APHFWQGRVK PEEIREHVSQ DVADTLAYLK QPFSLRIDTE IHRRKDINAL
LVSMSETPRA AILLIVFRLI ELETTLESQG KNPCHMAQET LHFYVPIADR LSLGEMRRRL
EDVCFRILHP FQYEKLKQDV TPIQSEDEKC LEILIEGVKR LLDKNRIHAE VHGRAKSLYS
IHLKMTLKGT ALEDIMDRIG LRIIVSSVPE CYAVLGLLHT HFKPIPGTFD DYIGLPKDNG
YQSLHTCVYP MREVTHKPIE FQVRTELMHM EAEHGSAAHW LYKSAVAMGK DSLKNQWLKG
LVRRHDQAKS TDAFIELLRR QVCEDHMVVF GKGGRITRLP DKATVLEYLD AANFFASRSS
VVKVNGKLAS LDQTLRDGDS IEIVDCEDSA SPGTVVDDMG DIIGQHKASP MNTEGCKVWA
TAQGSILRHK EENSHASTEG P
//
