ID A0A1H0Y3X7_9ACTN Unreviewed; 770 AA.
AC A0A1H0Y3X7;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SDQ09864.1};
GN ORFNames=SAMN04489718_0208 {ECO:0000313|EMBL:SDQ09864.1};
OS Actinopolyspora saharensis.
OC Bacteria; Actinomycetota; Actinomycetes; Actinopolysporales;
OC Actinopolysporaceae; Actinopolyspora.
OX NCBI_TaxID=995062 {ECO:0000313|EMBL:SDQ09864.1, ECO:0000313|Proteomes:UP000199301};
RN [1] {ECO:0000313|EMBL:SDQ09864.1, ECO:0000313|Proteomes:UP000199301}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45459 {ECO:0000313|EMBL:SDQ09864.1,
RC ECO:0000313|Proteomes:UP000199301};
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; FNKO01000001; SDQ09864.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0Y3X7; -.
DR STRING; 995062.SAMN04489718_0208; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000199301; 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:SDQ09864.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDQ09864.1}.
FT DOMAIN 85..182
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 427..488
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 694..768
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 601..624
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 604..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 770 AA; 85821 MW; 5D69580E3437E180 CRC64;
MSQEAESPAT ESSAQRPASA PRRVRARLAR RITAQRPTQV KQVLEPLASV HRELHPQADL
GLLQRAYDVA EEQHSTQQRK SGDPYITHPL AVATILAELG MDTTTLVAAL LHDTVEDTDY
PLDQLRADFG EEVSHLVDGV TKLDKVKLGN AAEAETIRKM VIAMARDPRV VVIKLADRLH
NMRTMRFLPP EKQVRKARET LEVLAPLAHR LGMATIKWEL EDLAFAILQP KKYDEIVRLV
ANRAPSRDIY LRQVVDEISG NLDAARLSAK VEGRPKHYYS IHQKMIVRGR DFDDIHDLVG
VRILVDQVRD CYAAMGVVHA LWQPMPGRFK DYIAQPKFGV YQSLHTTVIG PEGKPLEIQI
RTEEMHRTAE YGIAAHWRYK ESKGRGRGGA GVEIDEMAWM RQLLDWQREA ADPGEFLESL
RYDLNTREIF VFTPKGDVIT LPAGATPVDF AYAVHTEVGH RCIGSRVNGR LVALERKLEN
GEVVEIFTSK AEGSGPSRDW LSFVASPRAK TKIKQWFAKE RREEAIESGK QAIAKELRRL
GLPVQRLVSA DSIGSVAKEL HYTDVTALYA AVGERQVSAH HVVQRLVASL GGVEQAEDEI
AERATPSTVQ QQQRRSSGDS GVRVEGAGAG EVWAKLARCC TPVPGDEILG FVTRDGGVSV
HRTDCNNAED LRNKPERLVD VYWAPSNSSV FLVAIQVEAL DRHRLLSDVT KVLADEKVNI
LSASVTTSKD RVAVSRFSFE MGDPKHLGHV LKAVRNIEGV YDVYRMTSAS
//
