ID A0A1H6W6C1_9FIRM Unreviewed; 744 AA.
AC A0A1H6W6C1;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=SAMN05660742_103258 {ECO:0000313|EMBL:SEJ12581.1};
OS Propionispira arboris.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Propionispira.
OX NCBI_TaxID=84035 {ECO:0000313|EMBL:SEJ12581.1, ECO:0000313|Proteomes:UP000199662};
RN [1] {ECO:0000313|EMBL:SEJ12581.1, ECO:0000313|Proteomes:UP000199662}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2179 {ECO:0000313|EMBL:SEJ12581.1,
RC ECO:0000313|Proteomes:UP000199662};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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 -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + GTP = AMP + guanosine 3'-diphosphate 5'-triphosphate;
CC Xref=Rhea:RHEA:22088, ChEBI:CHEBI:30616, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:142410, ChEBI:CHEBI:456215; EC=2.7.6.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001157};
CC -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GTP: step
CC 1/2. {ECO:0000256|ARBA:ARBA00004976}.
CC -!- SIMILARITY: Belongs to the relA/spoT family.
CC {ECO:0000256|RuleBase:RU003847}.
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DR EMBL; FNZK01000003; SEJ12581.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H6W6C1; -.
DR STRING; 84035.SAMN05660742_103258; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000199662; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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 Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEJ12581.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000199662};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEJ12581.1}.
FT DOMAIN 57..156
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 400..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 664..739
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 744 AA; 84954 MW; 55D58714E0A3761E CRC64;
MGLNKMKEKE TIPITIDAII QDVLHYQPDA QVDLIRKAYD LAHAAHAGQT RVSGEEYIYH
PLSVAAILTE LQIDALTISA ALLHDVVEDT TYTIEEMKDL FGEEVAMLID GVTKLSRIEY
KSKEEQQLEN YRKMFLAMAK DIRVILIKLA DRLHNMRTLK FMREDKQKRI AKETIEIYAP
LANRLGISNI KWELEDLCLR YLEPETYYNL VEKVKQKRKE RQEFIDKSIQ KLRIYLEKAD
IETEIQGRAK HFYSIYKKMK RDNKDISEIY DLSAVRVLVS SVKDCYGVLG IIHTLWKPLP
GRFKDYIAMP KSNGYQSLHT TVIGTEGYPL EIQIRTFLMH KVSEYGVAAH WKYKESGKSV
GAGKEYDQKM SWLRQLVNLQ QELSDPREYV EALKVDVFSD EVFVFTPKGD VIDLPKGSIP
LDFAYRIHTD VGHHCVGAKV NGKIVPLEYK LKNGDILSII TNKQNNGPSR DWLNIVASTE
TRNKIRQWFK KAKREENIER GSDLIDKEAK RLGYEPKELL KNDRLKDVAK KLNILTEDDL
LATLGYGGIT INGILGKLIE LYKKELQQAT PPDISQMLEK LKPHGEKKKS SHGILVEGEG
GVLVRIARCC NPIPGDPITG YITRGRGVSV HRSDCPNVIN ENNDFARVIE VNWDIGLDKV
YTVTIDITCN DKAGVLTNLM SVPSESKINI SSINARTYKN NKTSTVTMGL EVKSSLQVEQ
IMTKFRRLKD VYSVSRTLVS NKEE
//
