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Database: UniProt
Entry: A0A0B4XEP7_9GAMM
LinkDB: A0A0B4XEP7_9GAMM
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ID   A0A0B4XEP7_9GAMM        Unreviewed;       705 AA.
AC   A0A0B4XEP7;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE            EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
GN   ORFNames=S7S_00275 {ECO:0000313|EMBL:AJD46479.1};
OS   Isoalcanivorax pacificus W11-5.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Isoalcanivorax.
OX   NCBI_TaxID=391936 {ECO:0000313|EMBL:AJD46479.1, ECO:0000313|Proteomes:UP000006764};
RN   [1] {ECO:0000313|EMBL:AJD46479.1, ECO:0000313|Proteomes:UP000006764}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W11-5 {ECO:0000313|EMBL:AJD46479.1,
RC   ECO:0000313|Proteomes:UP000006764};
RX   PubMed=23209202; DOI=10.1128/JB.01845-12;
RA   Lai Q., Shao Z.;
RT   "Genome sequence of an alkane-degrading bacterium, Alcanivorax pacificus
RT   type strain W11-5, isolated from deep sea sediment.";
RL   J. Bacteriol. 194:6936-6936(2012).
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=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC         H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC         Evidence={ECO:0000256|ARBA:ARBA00024273};
CC   -!- PATHWAY: Purine metabolism; ppGpp biosynthesis; ppGpp from GDP: step
CC       1/1. {ECO:0000256|ARBA:ARBA00024329}.
CC   -!- SIMILARITY: Belongs to the relA/spoT family.
CC       {ECO:0000256|RuleBase:RU003847}.
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DR   EMBL; CP004387; AJD46479.1; -; Genomic_DNA.
DR   RefSeq; WP_008734291.1; NZ_CP004387.1.
DR   AlphaFoldDB; A0A0B4XEP7; -.
DR   STRING; 391936.S7S_00275; -.
DR   KEGG; apac:S7S_00275; -.
DR   HOGENOM; CLU_012300_3_0_6; -.
DR   OrthoDB; 9805041at2; -.
DR   UniPathway; UPA00908; UER00886.
DR   Proteomes; UP000006764; Chromosome.
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:SF36; 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   Kinase {ECO:0000313|EMBL:AJD46479.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006764};
KW   Transferase {ECO:0000313|EMBL:AJD46479.1}.
FT   DOMAIN          45..144
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          387..448
FT                   /note="TGS"
FT                   /evidence="ECO:0000259|PROSITE:PS51880"
FT   DOMAIN          631..705
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
SQ   SEQUENCE   705 AA;  79052 MW;  270FD53CB5E6F317 CRC64;
     MPTVNNLVKR LKSYLSDDQI AQVVRAYEFA ERAHEGQYRR TGDPYITHPL AVANILTDMH
     MDHQSLMAAM LHDVIEDTGV TKEQLAELFS PDVAELVDGV SKIAQIKFES KAEQQAENLR
     KMMLAMTRDI RVILVKLADR LHNMRTLHSM PSEKRKRIAT ETLEIYAPIA NRLGMYNMRV
     EYEDLGFNAI YPMRANLISK AVKAARGHRK EILSTLKASI EHCLEEEGIP ARILGREKHL
     YSIYMKMKEQ HKPLNEIMDV YGFRIIVDKV DTCYRVLGAV HNYFTPIPGR FKDYIAIPKA
     NGYQSLHTTL KARSGIPLEI QIRTEEMEAM ANNGIAAHWL YKAEEAGSNT PTHTRAQAWM
     GRLLEMQQKA GNSMEFIENV KVDLFPDEAY VFTPKGEIKE LPVGATPVDF AYAVHTKVGN
     TCVAARIDGK LAALSTPLES GQTVRIITAP NATPNPSWLN FVVTGKARSN IRHFLKHQRR
     DDSIHLGERL LEKALAGYGI TMNELPIERV VAELAANGYA SLDDLLEDIG LGNRLAPLVA
     RKLAGGREEE RQDADDRKPL AIRGTEGLMV SYAKCCHPLP GDAVVGHLSA GRGIVVHRDT
     CNNLLSEMRS NPEKCIALYW DRDVEQEFSV AIRVELVNKK GVLATLATTF SELGSNIDTI
     TMAEKDATVT VINATVTVRD RIHLARLIKR LRKLENVIRI SRLNA
//
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