ID K0YUA9_9CORY Unreviewed; 748 AA.
AC K0YUA9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:EJZ83054.1};
GN ORFNames=HMPREF9719_00003 {ECO:0000313|EMBL:EJZ83054.1};
OS Corynebacterium otitidis ATCC 51513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=883169 {ECO:0000313|EMBL:EJZ83054.1, ECO:0000313|Proteomes:UP000006078};
RN [1] {ECO:0000313|EMBL:EJZ83054.1, ECO:0000313|Proteomes:UP000006078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51513 {ECO:0000313|EMBL:EJZ83054.1,
RC ECO:0000313|Proteomes:UP000006078};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Turicella otitidis ATCC 51513.";
RL Submitted (AUG-2012) 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:EJZ83054.1}.
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; AHAE01000001; EJZ83054.1; -; Genomic_DNA.
DR AlphaFoldDB; K0YUA9; -.
DR STRING; 29321.AAV33_05685; -.
DR PATRIC; fig|883169.3.peg.3; -.
DR eggNOG; COG0317; Bacteria.
DR HOGENOM; CLU_012300_3_0_11; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000006078; 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:EJZ83054.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000006078};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EJZ83054.1}.
FT DOMAIN 66..163
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 405..468
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 674..748
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 748 AA; 83366 MW; C11B5A8A60A48F7F CRC64;
MSVRGIPARL ARSLAGSKHR ENPVLSPLLA IHRQYHPKAD AQLIDRAYTR AYKLHDGVYR
KSGDPYITHP LAVATIAAEI GMDTTTIVAA LLHDTVEDTD YTLKQLTDEF GQETARLVDG
VTKLDKVALG AAAEAETVRK MVVAMAQDPR VLVIKVADRL HNMRTMRFLP PEKQEKKARQ
TLEVIAPLAH RLGMASIKWE LEDLSFAILY PKKYDEIVRL VADRAPQRDK MIKEISSQLE
ASLKDNNISA EVQGRPKHYW SIYQKMKVRG HEFDEIFDLI GIRVLVDTVA DCYAVIGVVH
LLYNPMPGRF KDYISAPRFG VYQSLHTTVM TESGRPLEVQ VRTHEMHFNA EFGIAAHWRY
KETKGTHKGD QAEVDQMAWM RQLLDWQKEA ADPNEFLDSL RFDLSAKQIF VFTPRGEVIN
LPVGSTPVDF AYAVHTEVGH SCIGAKVNGK LVALETKLNS GDRVEIFTSK DENAGPSRDW
QDFVVSPRAK TKIRQWFSKE LREEHLEAGR DALAAEVQRG GLPLHRLFTA ESMKAVATEL
HYRDVNALYT AIGSGAVSAQ HVAQRLLAIV GDEDAAEEEL VSRTPFTHLI EERPDSTKGT
AGILVENSPG VMAKLARCCQ PVPGDEIFGF VTRGSGVSVH RTDCTNAPQL KKEPSRLVDV
AWANERGGSV FTAALQVEAL DRDGLLVEIT KTLSDQRVKV QSLKSSVSDE HIATIQISFT
VSDTKQLGSL IARLRNAEGV FDVYRIMG
//
