ID A0A1H2KX25_9ACTN Unreviewed; 767 AA.
AC A0A1H2KX25;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:SDU72856.1};
GN ORFNames=SAMN04488563_4420 {ECO:0000313|EMBL:SDU72856.1};
OS Jiangella alkaliphila.
OC Bacteria; Actinomycetota; Actinomycetes; Jiangellales; Jiangellaceae;
OC Jiangella.
OX NCBI_TaxID=419479 {ECO:0000313|EMBL:SDU72856.1, ECO:0000313|Proteomes:UP000182977};
RN [1] {ECO:0000313|Proteomes:UP000182977}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45079 {ECO:0000313|Proteomes:UP000182977};
RA Varghese 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LT629791; SDU72856.1; -; Genomic_DNA.
DR RefSeq; WP_046770413.1; NZ_LT629791.1.
DR AlphaFoldDB; A0A1H2KX25; -.
DR STRING; 419479.SAMN04488563_4420; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000182977; Chromosome i.
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:SDU72856.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:SDU72856.1}.
FT DOMAIN 75..172
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 424..485
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 686..760
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 593..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 598..612
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 85472 MW; FD915ED691A3F383 CRC64;
MAEQTVPSGA LTPVRVRARL ARLTAQRQQS DPALEPLFRI IRANHPKADL EVIEKAYRTA
ARAHSGQKRK SGDPYITHPL AVTTILAELG MTPPTLAAAL LHDTVEDTDY GLDQLRGEFG
EEIAMLVDGV TKLDKVKYGQ AAQAETVRKM VIAMAKDIRV LVIKLADRLH NARTWRYVPK
ESARRKAHET LEIYAPLAHR LGMNTIKWEL EDLSFATLHP KVYDEIVRLV AERAPSRDDY
LASVIDQVQG DLRVSKIKAN VYGRPKHYYS IYQKMIVRGR DFADIYDLVG IRVLVESVRD
CYAVLGIVHA RWNPVPGRFK DFIAMPKFNM YQSLHTTVIG PGGKPVELQI RTHAMHRRAE
YGIAAHWKYK EDSNSSRETD KQINNNGDNA GNDMTWLRQL LDWQKETEDP GEFLESLRFE
MESNEVFVFT PKGDVVALPA AATPVDFAYA VHTDIGHRTI GARVNGRLVP LESNLDNGDV
VEVFTSKAQG AGPSRDWLTF VTSARARNKI KQWFSKERRE EAIEHGKDAI ARAMRKQDLP
LQRMMSQESL KAVADDLRYP DISALYAAVG EGNVSAQSIV QKLVQILGGE EGTTEDVAEA
ATPDRPRRRS GGDPGVVVKG VSDVWVKLAR CCTPVPGDTI VGFVTRGSGV SVHREDCVNV
DGLRRQHGRM VEVEWAPTAN SMFLVAIQVE ALDRARLLSD VTRVLSDQHV NILSATVSTN
TDRIATSRFT FEMADPKHLG HVLKAVRGVE GVFDAYRLTS GIPAPTH
//
