ID D9W9V9_9ACTN Unreviewed; 748 AA.
AC D9W9V9;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 24-JAN-2024, entry version 66.
DE SubName: Full=GTP diphosphokinase {ECO:0000313|EMBL:EFL22773.1};
GN ORFNames=SSOG_02487 {ECO:0000313|EMBL:EFL22773.1};
OS Streptomyces himastatinicus ATCC 53653.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces violaceusniger group.
OX NCBI_TaxID=457427 {ECO:0000313|EMBL:EFL22773.1, ECO:0000313|Proteomes:UP000003963};
RN [1] {ECO:0000313|EMBL:EFL22773.1, ECO:0000313|Proteomes:UP000003963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53653 {ECO:0000313|EMBL:EFL22773.1,
RC ECO:0000313|Proteomes:UP000003963};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces hygroscopicus strain ATCC 53653.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the RelA/SpoT family.
CC {ECO:0000256|ARBA:ARBA00007476}.
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DR EMBL; GG657754; EFL22773.1; -; Genomic_DNA.
DR RefSeq; WP_009714594.1; NZ_GG657754.1.
DR AlphaFoldDB; D9W9V9; -.
DR STRING; 457427.SSOG_02487; -.
DR HOGENOM; CLU_012300_4_1_11; -.
DR OrthoDB; 9805041at2; -.
DR Proteomes; UP000003963; 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:0015969; P:guanosine tetraphosphate metabolic process; IEA:InterPro.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05399; NT_Rel-Spo_like; 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; IPR007685; RelA_SpoT.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
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; 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:EFL22773.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EFL22773.1}.
FT DOMAIN 87..184
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 429..490
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..741
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 549..581
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 551..579
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 748 AA; 80785 MW; AC66DC5F54F47F5B CRC64;
MSAEAPDQAA LGRRRGLPRI DLRNIRRFGR AALQGPASRD RLPDAIEHVA KVHRAYHPGA
DLDVLRKAYV LAESSHRGQM RKSGEPYITH PLAVTLILAE LGAETTTLTA SLLHDTVEDT
EVTLDQVGEE FGEEVRYLVD GVTKLEKVDY GAAAEPETFR KMLVATGNDV RVMSIKLADR
LHNMRTLGVM RPEKQARIAK VTRDVLIPLA ERLGVQALKT ELEDLVFAIL HPEEYARTRE
LLQSHADRPD PLARAAGDVR AVLQEAGITA EVLVRPRHFV SVHRVGIKRG ELTGSDLGRL
LVLVADDADC YAVLGELHTC FTPVISEFKD FIAVPKFNLY QSLHTAVAGR SGEVAEVLIR
THQMHRVAEA GVIALGNPYA PTEAAAAPEG ERADPTRPGW LSRLLEWQSA TPDPDIFWTA
LRDDLAQDRE ITVFRSDGGT LGLPAGASCV DAAYAQYGED AHSCIGARVN GRIATLSTVL
CDGDTLQLLM TGDAASSGPS PEWLDHARTP AARIAINRWL AAHPADPAHE PPQGEAPGAE
HLHAPVEPEE AELEGIDPDG IDPDGADLEE AEEDAGEDAG DVLPVAPAGR PEAGIVVDLP
GVIVRLARCC TPVPPDAITG FAVRGGAVTV HRERCPAVAR MTAAGRTRVG VRWSEEDDGD
GGDYRVTLFA EAFSRPHLLA DLTEAIAAEG AEVVAAAVEP PREQRVRHTY TLQLSDAGRL
PTLMRAMRDV PGVYDVTREG RRVATARS
//