ID A0A1H8PAR1_9ACTN Unreviewed; 821 AA.
AC A0A1H8PAR1;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SEO38857.1};
GN ORFNames=SAMN05216267_10257 {ECO:0000313|EMBL:SEO38857.1};
OS Actinacidiphila rubida.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Actinacidiphila.
OX NCBI_TaxID=310780 {ECO:0000313|EMBL:SEO38857.1, ECO:0000313|Proteomes:UP000181951};
RN [1] {ECO:0000313|EMBL:SEO38857.1, ECO:0000313|Proteomes:UP000181951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.2026 {ECO:0000313|EMBL:SEO38857.1,
RC ECO:0000313|Proteomes:UP000181951};
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; FODD01000025; SEO38857.1; -; Genomic_DNA.
DR RefSeq; WP_075017522.1; NZ_FODD01000025.1.
DR AlphaFoldDB; A0A1H8PAR1; -.
DR STRING; 310780.SAMN05216267_10257; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000181951; 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:SEO38857.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000181951};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SEO38857.1}.
FT DOMAIN 127..224
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 479..540
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 743..817
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 821 AA; 90974 MW; 36371DA3500D05ED CRC64;
MPDQAQPLGA AGGPEPATDG SGSPASGSAV EHTDSPAPAP PAVRPVRTPG SVAPTRPGAS
SSRVRARLAR LGVQRSSPYN PVLEPLLRVV RGNDPKGDSA QLRQIERAYQ VAERWHRGQK
RKSGDPYITH PLAVTTILAE LGMDPATLMA GLLHDTVEDT EYGLEQLRRD FGDQVALLVD
GVTKLDKVKF GEAAQAETVR KMVVAMAKDP RVLVIKLADR LHNMRTMRYL KREKQEKKAR
ETLEIYAPLA HRLGMNTIKW ELEDLAFAIL YPKMYDEIVR LVAERAPKRD EYLAVVTDQV
QQDLRAARIK ATVTGRPKHY YSVYQKMIVR GRDFAEIYDL VGIRVLVDTV RDCYAALGTI
HARWNPVPGR FKDYIAMPKF NMYQSLHTTV IGPSGKPVEL QIRTFDMHRR AEYGIAAHWK
YKQEAVAGAS KVRTDSPRSD KKDDAVNDMA WLRQLLDWQK ETEDPGEFLE SLRFDLSQNE
VFVFTPKGDV IALPAGATPV DFAYAVHTEV GHRTIGARVN GRLVPLESTL DNGDTVEVFT
SKAAGAGPSR DWLGFVKSPR ARNKIRAWFS KERREEAVEQ GKEAIARAMR KQNLPIQRVL
TGDSLVTLAH EMRYPDISAL YAAIGEGHIT AQSVVQKLVD ALGGEEGATE DIAEITTPTQ
GRTKRRANAD PGVIVKGTSD VWVKLSRCCT PVPGDPIIGF VTRGNGVSVH RADCVNVESL
SQQPERIIDV EWAPTQSSVF LVAIQVEALD RSRLLSDVTR VLSDQHVNIL SAAVQTSRDR
VATSRFTFEM GDPKHLGHVL KAVRGVEGVY DVYRVTSGRQ R
//
