ID A0A239MMH9_9ACTN Unreviewed; 823 AA.
AC A0A239MMH9;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SNT43282.1};
GN ORFNames=SAMN05216252_12557 {ECO:0000313|EMBL:SNT43282.1};
OS Actinacidiphila glaucinigra.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=235986 {ECO:0000313|EMBL:SNT43282.1, ECO:0000313|Proteomes:UP000198280};
RN [1] {ECO:0000313|EMBL:SNT43282.1, ECO:0000313|Proteomes:UP000198280}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.1858 {ECO:0000313|EMBL:SNT43282.1,
RC ECO:0000313|Proteomes:UP000198280};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOF01000025; SNT43282.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239MMH9; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000198280; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SNT43282.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000198280};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SNT43282.1}.
FT DOMAIN 129..226
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 481..542
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 745..819
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 91264 MW; 1C6857064D696C97 CRC64;
MTAEDGKKQA ASLSTAPPVA PAAPAAPAEG KAAKPAPAAP ATPAARPVRT PGSVAPNRPA
TSSNRVRARL ARLGVQRSSP YNPVLEPLLR IVRSNDPKGD PSQLRQIERA YQVAERWHRG
QKRKSGDPYI THPLAVTTIL AELGMDPATL MAGLLHDTVE DTEYGLDALR RDFGDSVALL
VDGVTKLDKV KFGEAAQAET VRKMVVAMAK DPRVLVIKLA DRLHNMRTMR YLKREKQEKK
ARETLEIYAP LAHRLGMNTI KWELEDLAFA ILYPKMYDEI VRLVAERAPK RDEYLAVVTD
QVQQDLRAAR IKATVTGRPK HYYSVYQKMI VRGRDFAEIY DLVGIRVLVD TVRDCYAALG
TIHARWNPVP GRFKDYIAMP KFNMYQSLHT TVIGPSGKPV EIQIRTFDMH RRAEYGIAAH
WKYKQEAVAG ASKVRTDSPK SAKKDDAVND MAWLRQLLDW QKETEDPGEF LESLRFDLSR
NEVFVFTPKG DVIALPAGAT PVDFAYAVHT EVGHRTIGAR VNGRLVPLES TLDNGDTVEV
FTSKAAGAGP SRDWLGFVKS PRARNKIRAW FSKERREEAV EQGKEAIARA MRKQNLPIQR
VLTGDSLVTL AHEMRYPDIS ALYAAIGEGH ITAQSVVHKL VEALGGEEGA TEDIAEITTP
SRSRTKRRSA ADPGVIVKGE KDVWVKLSRC CTPVPGDPII GFVTRGNGVS VHRADCVNVE
SLSQQPERII DVEWAPTQSS VFLVAIQVEA LDRSRLLSDV TRVLSDQHVN ILSAAVQTSR
DRVATSRFTF EMGDPKHLGH VLKAVRGVEG VYDVYRVTSA RQR
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