ID A0A1M7YDN5_9FIRM Unreviewed; 767 AA.
AC A0A1M7YDN5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE RecName: Full=GTP diphosphokinase {ECO:0000256|ARBA:ARBA00013251};
DE EC=2.7.6.5 {ECO:0000256|ARBA:ARBA00013251};
GN ORFNames=SAMN02745217_02853 {ECO:0000313|EMBL:SHO50696.1};
OS Anaerocolumna xylanovorans DSM 12503.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Anaerocolumna.
OX NCBI_TaxID=1121345 {ECO:0000313|EMBL:SHO50696.1, ECO:0000313|Proteomes:UP000184612};
RN [1] {ECO:0000313|EMBL:SHO50696.1, ECO:0000313|Proteomes:UP000184612}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 12503 {ECO:0000313|EMBL:SHO50696.1,
RC ECO:0000313|Proteomes:UP000184612};
RA Song W.-J., Kurnit D.M.;
RL Submitted (DEC-2016) 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}.
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DR EMBL; FRFD01000008; SHO50696.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1M7YDN5; -.
DR STRING; 1121345.SAMN02745217_02853; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00884.
DR Proteomes; UP000184612; Unassembled WGS sequence.
DR GO; GO:0008728; F:GTP diphosphokinase activity; IEA:UniProtKB-EC.
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 Kinase {ECO:0000313|EMBL:SHO50696.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000184612};
KW Transferase {ECO:0000313|EMBL:SHO50696.1}.
FT DOMAIN 76..176
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 422..483
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 693..767
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 767 AA; 87332 MW; 1DD3DDA07E58EB8C CRC64;
MEDDANNKVM DDNLYRKKNT ELIVPADFTT PDELYGQLIK IVESYHPSAD ISIIEKAYHF
AAKAHQDQMR KSGEPYIIHP LCVAIILAEL ELDKETIVAG LLHDVVEDTV CTVEELAKEF
NEEIALLVDG VTKLTQLSYS KDKVEIQAEN LRKMFLAMAK DIRVILIKLA DRLHNMRTMQ
YQTPVKQKEK ARETMDIYAP IAQRLGISKI KIELDDLSLK YLEPEVYNDL TEKINSKKGE
REEIINQIVE EVRFHIQQAE IEAKIDGRVK HFFSIYKKMV NQHKTLDQIF DLFAVRIVVE
SVKDCYAALG VIHEMYKPIP GRFKDYIAMP KPNMYQSLHT TLIGPGGQPF EIQIRTYEMH
RTAEYGIAAH WKYKEGHDGK NSQDTEEAKL TWLRQILEWQ RDMSDNKEFL SLLKSDLDLF
SESVYCFTPT GDVKNLPNGS TPIDFAYSIH SAVGNKMVGA RVNGKLVNID YVIQNGDRIE
IITSQNSKGP SRDWLSLVKS TQAKNKINQW FKTELKEDNI VKGKEMIISY CKTKGIVLSD
LMKPEYMNKV MSKYGFRDWD SIYAAVGHGG LKEGQVINKL KDEYDKKHKK EITDEKVLDS
ITEIKDSKPN VKKSKSGIVV EGIHDVAVRF SKCCSPVPGD EIIGFVTRGR GVSIHRTDCV
NLMNLSEEDR ARLIEAEWNV PQDKAQGELY AAEIKIYANN RSGVLVDVSK ILTENKIDVT
SMTVRTSKQG TATISVGFEI NGVEQLRYIV GKLRSIESVL DIERTTG
//