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Database: UniProt
Entry: A0A0M8XJ67_9ACTN
LinkDB: A0A0M8XJ67_9ACTN
Original site: A0A0M8XJ67_9ACTN 
ID   A0A0M8XJ67_9ACTN        Unreviewed;       725 AA.
AC   A0A0M8XJ67;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 32.
DE   SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KOX07302.1};
GN   ORFNames=ADL05_29095 {ECO:0000313|EMBL:KOX07302.1};
OS   Nocardiopsis sp. NRRL B-16309.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Nocardiopsis.
OX   NCBI_TaxID=1519494 {ECO:0000313|EMBL:KOX07302.1, ECO:0000313|Proteomes:UP000037694};
RN   [1] {ECO:0000313|Proteomes:UP000037694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL B-16309 {ECO:0000313|Proteomes:UP000037694};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL   Submitted (JUL-2015) 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   -!- 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:KOX07302.1}.
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DR   EMBL; LGEC01000148; KOX07302.1; -; Genomic_DNA.
DR   RefSeq; WP_053620200.1; NZ_LGEC01000148.1.
DR   AlphaFoldDB; A0A0M8XJ67; -.
DR   STRING; 1519494.ADL05_29095; -.
DR   PATRIC; fig|1519494.3.peg.6354; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00884.
DR   Proteomes; UP000037694; 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; GTP PYROPHOSPHOKINASE; 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:KOX07302.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037694};
KW   Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOX07302.1}.
FT   DOMAIN          46..143
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          387..450
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          651..725
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   725 AA;  81657 MW;  5C59A430637F3164 CRC64;
     MNPVLEPLIK TVRATHPKVD VRLIERAYEV AAHHHRDQKR KSGDPYITHP LAVATILAEL
     GMQEATLAAA LLHDTVEDTE YSLDELRADF GDEIAELVDG VTKLDKVKYG EATQAETVRK
     MVVAMARDIR VLVIKLCDRL HNMRTLRYLP SKAKREKKAR ETLEIFAPLA HRLGMNTIKW
     ELEDLAFATL YPKRFDEIAR LVSERAPRRD VYLQEVIEAV SADLRESKLK ATVRGRPKHY
     YSIYQKMIAR NCGFDEIYDL IAVRVLVDSV RDCYAALGTI HARWNPVPGR FKDYIAMPKF
     NMYQSLHTTV IGPSGNPVEL QIRTRAMHRR AEYGIAAHWK YKEDRGGGSE PKAKGTTDMQ
     WLRQLIDWQQ ETKDPGEFLE SLRFDLSVQE VFVFTPQGDV ISLPQGATAV DFAYAVHTEV
     GHRTVGARIN GRLVPLENEL HNGEAVEILT SKDPDAGPSR DWLNFVKSAR ARNKIRHWFT
     KERREAAIEQ GKDEIAKVMR KQELPVKRMF SGEALIALAS DLRYPDVDSL YAAVGEHQVS
     AQNVVSKLVD SMGGLESHTE DIAESALPGR TAVRRTKTGN PGVVVEGDSD VWVRLSKCCT
     PVPGDDIVGF VTRGNGVSVH RADCVNAKTL DTERMVAVQW RPTEDSMFLV ALQVEALDRS
     RLLSDITRVL SDQHVNILSA TVQTSRDRVA QSRFTFEMAD PAHLGSVLRA VRGVDGVYDV
     YRVRN
//
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