ID H0EAX3_9ACTN Unreviewed; 829 AA.
AC H0EAX3;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EHN09191.1};
DE EC=2.7.6.5 {ECO:0000313|EMBL:EHN09191.1};
GN ORFNames=PAI11_39980 {ECO:0000313|EMBL:EHN09191.1};
OS Patulibacter medicamentivorans.
OC Bacteria; Actinomycetota; Thermoleophilia; Solirubrobacterales;
OC Patulibacteraceae; Patulibacter.
OX NCBI_TaxID=1097667 {ECO:0000313|EMBL:EHN09191.1, ECO:0000313|Proteomes:UP000005143};
RN [1] {ECO:0000313|EMBL:EHN09191.1, ECO:0000313|Proteomes:UP000005143}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=I11 {ECO:0000313|EMBL:EHN09191.1,
RC ECO:0000313|Proteomes:UP000005143};
RX PubMed=23212173; DOI=10.1007/s10532-012-9610-5;
RA Almeida B., Kjeldal H., Lolas I., Knudsen A.D., Carvalho G., Nielsen K.L.,
RA Barreto Crespo M.T., Stensballe A., Nielsen J.L.;
RT "Quantitative proteomic analysis of ibuprofen-degrading Patulibacter sp.
RT strain I11.";
RL Biodegradation 24:615-630(2013).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHN09191.1}.
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DR EMBL; AGUD01000299; EHN09191.1; -; Genomic_DNA.
DR RefSeq; WP_007578537.1; NZ_AGUD01000299.1.
DR AlphaFoldDB; H0EAX3; -.
DR PATRIC; fig|1097667.3.peg.3962; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000005143; 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 ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EHN09191.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000005143};
KW Transferase {ECO:0000313|EMBL:EHN09191.1}.
FT DOMAIN 126..225
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 486..547
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 754..827
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 92017 MW; 3852AA41BCA58CD1 CRC64;
MAERHDDRPG AVTGTVSVAR DADDQRNGGG VPVTDERTRE RIGLSAADLA AGHHVPTPPE
PADDEAERGP EALTAEELSL RADLHAVIAE HAEPDRSPVD LERVDDAFRF ACLHHRDQRR
KSGEAFIAHP TEVAKICAGM RLDTDAIVAA LLHDTVEDTA AELEEIETRY GSNVRLLVDG
VTKLDGIQFT SRDEAQAENY RKMVVAMAAD VRVILIKLAD RLHNARTLEH HKRPKQLEIA
KETLEVYAPI AHRLGIHAIK WELEDLAFAT LHPRKYQEIK GLVNQQRGER ETYVAKAGEY
LGRELEAVGI DAEISGRAKH FYSIYLKMTR KGREFNEIYD LTAMRVVVDS VNDCYGAIGV
IHALWKPLPR RFKDFVAMPK ANMYQSLHTT VVGPEGRPLE IQIRTNDMQR TAEFGVAAHW
MYKESAPERG TATARPGELA AAAGNAKEAR SDGDKFSWLR AMLDTSRDND DPAEFMDDLK
VALFEDEVYV FTPKGDVKSL SRGATPVDFA YEVHTDVGHR CVGAKVNGKI VPLSYQLRSG
DIVEVLTANR ERGPSRDWLS LAQTSRARSK IKAWFKAAGR EDSEHQGREL LQEQLRKAGL
PAQRIVGSPL LADVIHEMGY KKADDFYIAV GGGKVSPKVV VNKVLKHLKE GEAADDEPAG
PVEQLLRPDV ARRQPTGTAS SYGVTVDGVG DVMLRMAKCC RPVPGDPIVG YVSLGRGITI
HRDDCQNAQQ LRKDPERFVP VDWAGQHQQS FKVEIQVDGY DRHRLLEDLT RVFAETGVNI
VSAVCTTTPP MVRNRFVVEV GDTKVLRSTI NRLRNIDAVF DAFRITPSA
//
