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Database: UniProt
Entry: A0A1M7YDN5_9FIRM
LinkDB: A0A1M7YDN5_9FIRM
Original site: A0A1M7YDN5_9FIRM 
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
//
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