ID Q3ZAI9_DEHM1 Unreviewed; 728 AA.
AC Q3ZAI9;
DT 27-SEP-2005, integrated into UniProtKB/TrEMBL.
DT 27-SEP-2005, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:AAW39180.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:AAW39180.1};
GN Name=relA {ECO:0000313|EMBL:AAW39180.1};
GN OrderedLocusNames=DET0005 {ECO:0000313|EMBL:AAW39180.1};
OS Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS (Dehalococcoides ethenogenes (strain 195)).
OC Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC Dehalococcoidaceae; Dehalococcoides.
OX NCBI_TaxID=243164 {ECO:0000313|EMBL:AAW39180.1, ECO:0000313|Proteomes:UP000008289};
RN [1] {ECO:0000313|EMBL:AAW39180.1, ECO:0000313|Proteomes:UP000008289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-2266 / KCTC 15142 / 195
RC {ECO:0000313|Proteomes:UP000008289};
RX PubMed=15637277; DOI=10.1126/science.1102226;
RA Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA Ward N.L., Nelson W.C., Deboy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA Zinder S.H., Heidelberg J.F.;
RT "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT ethenogenes.";
RL Science 307:105-108(2005).
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; CP000027; AAW39180.1; -; Genomic_DNA.
DR RefSeq; WP_010935815.1; NC_002936.3.
DR AlphaFoldDB; Q3ZAI9; -.
DR STRING; 243164.DET0005; -.
DR GeneID; 60794057; -.
DR KEGG; det:DET0005; -.
DR PATRIC; fig|243164.10.peg.5; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_0; -.
DR InParanoid; Q3ZAI9; -.
DR Proteomes; UP000008289; Chromosome.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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; 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; 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 Kinase {ECO:0000313|EMBL:AAW39180.1};
KW Transferase {ECO:0000313|EMBL:AAW39180.1}.
FT DOMAIN 44..154
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 398..459
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 648..722
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 728 AA; 82193 MW; 0E4D1D61F0AA43CE CRC64;
MEFADLKEKA SKYLPPEKLV FLEEAYNYAA AAHTGQMRKS GEPFIEHPLN VAITLADLQL
DSATLAAALL HDVPEDAHIS LEQIEKKFGA DVAKLVDGVT KLSKLALGPG IEDARRPGGN
ASLRQAENLR KMLVAMSEDL RVVFIKLADR FHNMRTLQAL SAEKRRSIAK ETMEIYAPLA
HRLGIWELKW QLEDLAFRYL DPRHYRQVAN LVDSKLAQRK NYIEHVSAIL QSEFEKNGLK
VELSGRPKHL YSIYQKMEKY ASQGKQFEDI YDVLALRVLV NDIPDCYHAI GIVHSLWHPI
PGAFDDYIAN PKPNGYQSLH TAVMSLGTTP LEVQVRTYQM HHIAEYGVAA HWRYKTAGKE
DVNFEDRIGW LRQLIEWHRD MRGAEEFLES VKTDIFNDQV FVFTPKGEIK DLAKGATPID
FAYRIHTELG NRCIGAKANG RLVPLDYQLK NGEVVEIVTT KKDRGPSRDW LNANMGYIKT
HHAREKILAW FKKQERTENL ERGRELLEKE LKHIGIKTVD REALAKAFKY ENADEFLAAI
GYGAVSVHQV SMKLLSQQEQ PRVITPTVQT AKPSSQSSVS VMGTGSLLTN IAKCCNPVPG
DDIIGYVTRN RGVTVHRQDC HNILHEEEKE RLVSVDWGIP KEELYPASIR MQAWDRVGLV
RDISTMVAEE KISILSMTVT ENDDKTTTLA MTAQIKSLSQ LTRLMAKLEG IRGIISISRV
GADGSRSG
//
