ID A0A0M8MH69_9MICO Unreviewed; 749 AA.
AC A0A0M8MH69;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=GTP pyrophosphokinase {ECO:0000313|EMBL:KOS11418.1};
GN ORFNames=XI38_06085 {ECO:0000313|EMBL:KOS11418.1};
OS Microbacterium chocolatum.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=84292 {ECO:0000313|EMBL:KOS11418.1, ECO:0000313|Proteomes:UP000037737};
RN [1] {ECO:0000313|EMBL:KOS11418.1, ECO:0000313|Proteomes:UP000037737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SIT 101 {ECO:0000313|EMBL:KOS11418.1,
RC ECO:0000313|Proteomes:UP000037737};
RA Li X., Xu Y.;
RT "Complete genome sequence of Microbacterium chocolatum SIT 101, a bacterium
RT enantioselectively hydrolyzing mesomeric diesters.";
RL Submitted (APR-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:KOS11418.1}.
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DR EMBL; LAVO01000005; KOS11418.1; -; Genomic_DNA.
DR RefSeq; WP_053547418.1; NZ_KQ440286.1.
DR AlphaFoldDB; A0A0M8MH69; -.
DR KEGG; mcw:A8L33_09975; -.
DR PATRIC; fig|84292.3.peg.1242; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000037737; 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:KOS11418.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Reference proteome {ECO:0000313|Proteomes:UP000037737};
KW Transferase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KOS11418.1}.
FT DOMAIN 71..168
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 413..474
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 674..748
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 749 AA; 83155 MW; EEDAF1208293FE11 CRC64;
MAETVPPAST SSLRRLVPRI FSRSARRDDV EQLLRTVRTH HPKGDLVILE RAYAVADKAH
SGQTRQSGEP YITHPLAVAQ ILADLGLGPR AIAAALLHDT VEDTSYGLDD LSAEFGDEVA
MLVDGVTKLD KVKYGESAQA ETVRKMIVAM SRDIRVLLIK LADRLHNART WGFVPPEKAR
KKATETLEIY APLAHRLGIQ AIKSELEDLS FAVLHPKLYA EIESLVLQRT PQREQYVRNV
IESVDADLRE LRIRGRVMGR PKQLYSVYQK MIVRGREFDD IYDLIGIRVL VGSVRDCYAV
LGAIHARWTP LPGRFKDYIA TPKFNLYQSL HTTVIGPNGR TVEIQIRTNE MHQQAEFGVA
AHWKYKEQMA GAKPDAKAVD TDMAWLAHIS DWQAETADPG EFLDSLRFEI GAKEVYVFTP
KGRVIGLPAG ATPVDFAYAV HTEVGHRTMG SKVNGRLVPL ESELKSGDVV EVFTSKNPDA
GPSQDWLSFV KSTRARSKIR GWFTKERREE AIEQGKESIA RAMRRQNLPL QRLMSQDSFG
EVAQQLKYED VSALYAAVGE GHVSTQSVIE KVTALVSAQD TSTGPIDIPV VGRARQPRSG
DSGVLVRGAP DILVKLAKCC TPVPGDEIVG FVTRGSGVSV HREDCTNVAS LKQDPQRLID
VEWAPTTKSL FLVQIQVEAL DRSGLLSDVT RVLSEHHVNI LSATVSTNND RLAISRFVFE
MGDTVHLDRV LNAVRRIDAV YDVYRVTSS
//
