ID Q1D7G8_MYXXD Unreviewed; 753 AA.
AC Q1D7G8;
DT 11-JUL-2006, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2006, sequence version 1.
DT 27-MAR-2024, entry version 116.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:ABF91365.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:ABF91365.1};
GN Name=relA {ECO:0000313|EMBL:ABF91365.1};
GN OrderedLocusNames=MXAN_3204 {ECO:0000313|EMBL:ABF91365.1};
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197 {ECO:0000313|EMBL:ABF91365.1, ECO:0000313|Proteomes:UP000002402};
RN [1] {ECO:0000313|EMBL:ABF91365.1, ECO:0000313|Proteomes:UP000002402}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622 {ECO:0000313|Proteomes:UP000002402};
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S.,
RA Eisen J.A., Ronning C.M., Barbazuk W.B., Blanchard M., Field C.,
RA Halling C., Hinkle G., Iartchuk O., Kim H.S., Mackenzie C., Madupu R.,
RA Miller N., Shvartsbeyn A., Sullivan S.A., Vaudin M., Wiegand R.,
RA Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- FUNCTION: In eubacteria ppGpp (guanosine 3'-diphosphate 5'-diphosphate)
CC is a mediator of the stringent response that coordinates a variety of
CC cellular activities in response to changes in nutritional abundance.
CC {ECO:0000256|RuleBase:RU003847}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; CP000113; ABF91365.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1D7G8; -.
DR STRING; 246197.MXAN_3204; -.
DR EnsemblBacteria; ABF91365; ABF91365; MXAN_3204.
DR KEGG; mxa:MXAN_3204; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_7; -.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR CDD; cd04876; ACT_RelA-SpoT; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 1.
DR CDD; cd01668; TGS_RSH; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR004811; RelA/Spo_fam.
DR InterPro; IPR045600; RelA/SpoT_AH_RIS.
DR InterPro; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR033655; TGS_RelA/SpoT.
DR NCBIfam; TIGR00691; spoT_relA; 1.
DR PANTHER; PTHR21262:SF31; BIFUNCTIONAL (P)PPGPP SYNTHASE_HYDROLASE SPOT; 1.
DR PANTHER; PTHR21262; GUANOSINE-3',5'-BIS DIPHOSPHATE 3'-PYROPHOSPHOHYDROLASE; 1.
DR Pfam; PF13291; ACT_4; 1.
DR Pfam; PF13328; HD_4; 1.
DR Pfam; PF19296; RelA_AH_RIS; 1.
DR Pfam; PF04607; RelA_SpoT; 1.
DR Pfam; PF02824; TGS; 1.
DR SMART; SM00471; HDc; 1.
DR SMART; SM00954; RelA_SpoT; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR PROSITE; PS51671; ACT; 1.
DR PROSITE; PS51831; HD; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000002402};
KW Transferase {ECO:0000313|EMBL:ABF91365.1}.
FT DOMAIN 59..161
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 402..463
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 681..753
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 567..588
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 84737 MW; C9F891E7D6B0144C CRC64;
MPLRWCKVTI APHSMIRLND ILQRVSQYHP DPDLDIIKKA YVYSAKVHQG QLRKSGEPYL
VHPLEVAGIL GELKLDEASI VTGLLHDTIE DTLATEEELT ELFGSEVAHL VDGVTKLSKF
SASASLSQEE KQAENFRKMI IAMAQDIRVI LVKLADRTHN MRTLDHMSEE KQARIAQETL
DIYAPLANRL GISWIKTELE DLSFRYVKPQ EFFALQAKLN KRKKEREKYI EDTCDLIRSK
LAERGLKGEV SGRFKHVYSI YKKIKSQGID FDQIHDIIAF RIIAPTAPSC YEALGLVHEM
WKPVPGRFKD FIAIPKPNMY QSLHTTIIGP LSERVEVQIR TSEMHKIAEE GIAAHWKYKE
GKAVISKDDE KFAWLRQLME WQQDLKDPKE FLETVKVDLF TDEVFVFTPK GDVRSLPRGA
TPVDFAYAIH SDVGNRCVGA KVNGKIVPLR YKMKNGDTVE VLTSPQQHPS KDWLTFVKTS
RAQQRIRGFI KQQQREKSLQ LGRELADREL KRFQLNFNRL LKSGEMKKAA VDLGFRVEDD
MLVAIGYGKV TPQQLSHRLV PQEKLNAAEA GGRADANPAA TTSGGAGNSV LPGLSRVTDL
AKRLVGRSNR SGVQIGGVDD VLVRFGRCCN PVPGDPIAGF ITRGRGVTVH TVGCEKALAT
DPERRVDVSW DVRGDFKRPV TLRVLTADRP GLLADITNTF SKKGVNISQA NCRATGDDRA
VNTFEVIISD LKQLTDLMRT IERLQGVYSV ERI
//
