ID A0A263DWE7_9PSEU Unreviewed; 743 AA.
AC A0A263DWE7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:OZM81695.1};
GN ORFNames=CFP66_16000 {ECO:0000313|EMBL:OZM81695.1};
OS Pseudonocardia sp. MH-G8.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Pseudonocardia.
OX NCBI_TaxID=1854588 {ECO:0000313|EMBL:OZM81695.1, ECO:0000313|Proteomes:UP000216936};
RN [1] {ECO:0000313|EMBL:OZM81695.1, ECO:0000313|Proteomes:UP000216936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MH-G8 {ECO:0000313|EMBL:OZM81695.1,
RC ECO:0000313|Proteomes:UP000216936};
RA Wang J., Leiva S., Huang J., Huang Y.;
RT "Non-contiguous finished genome sequence and description of Pseudonocardia
RT marinum sp. nov., an obligate marine actinomycete from a macroalgal
RT phycosphere.";
RL Submitted (JUL-2017) 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:OZM81695.1}.
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DR EMBL; NKYF01000005; OZM81695.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A263DWE7; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000216936; 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:OZM81695.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000216936};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OZM81695.1}.
FT DOMAIN 54..151
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 398..461
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 667..741
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 743 AA; 82233 MW; 28A451BCB289EE17 CRC64;
MTPQRVAVVA PVLEPLASVH RTLHPKADLG LLQRAYDVAE AKHEGQKRKS GDPYITHPLA
VSTILAELGM DTTTLVAALL HDTVEDTDYS LERLREDFGE EVAHLVDGVT KLDKVELGSA
AEAETIRKMV VAMARDPRVL VIKLSDRLHN MRTMRFLPPE KQAKKARETL EVLAPLAHRL
GMATVKWELE DLSFAILHPK KYSEIVRLVA TRAPSRDTYL KQVIDEVMQQ LESARISATV
EGRPKHYYSI YRKMIVKGRD FDDIHDLVGA RVLVDEVRDC YAAMGMVHAL WQPMPGRFKD
YIAQPRFGVY QSLHTTVIGP DGKPLEVQIR TRDMHHTAEY GIAAHWRYKE TRGSQGAGAS
RGQAVEVDEM AWMRQLLDWQ REAADPGDFL ESLRFDLGSQ QIFVFTPKGD VVTLPAGSTP
VDLAYAVHTE VGNRCIGSRV NGKLVALERK LESGDVVEIF TSKAEGAGPS RDWLQFVASP
RAKTKVKQWF AKERREEAIE AGKEAITREA RRTSFPLHRL VSADAMAALS RELHFPDLSG
LYAAVGEGHA SARHVVQRLV ALLGGEEQAE EDLAERATPS TVRLRRTGGD AGVVARGEAG
DLADLYTKLA RCCTPVPGDD ILGFVTRGGG ISVHRTDCTN AGDLQARSER LVDVAWSVSP
GSVFLVAIQV EALDRHRLLS DVTKVLADER VNILSASVTT SRDRVAVSRF TFEMGDPKHL
GHVLRAVRNV EGVYDVYRVT SAS
//
