ID A0A1T0ATD7_9PAST Unreviewed; 569 AA.
AC A0A1T0ATD7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=B0187_02780 {ECO:0000313|EMBL:OOR99750.1};
OS Haemophilus paracuniculus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=734 {ECO:0000313|EMBL:OOR99750.1, ECO:0000313|Proteomes:UP000190867};
RN [1] {ECO:0000313|EMBL:OOR99750.1, ECO:0000313|Proteomes:UP000190867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 43573 {ECO:0000313|EMBL:OOR99750.1,
RC ECO:0000313|Proteomes:UP000190867};
RA Engstrom-Jakobsson H., Salva-Serra F., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome sequence of Haemophilus paracuniculus CCUG 43573 type
RT strain.";
RL Submitted (FEB-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=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}.
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:OOR99750.1}.
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DR EMBL; MUYA01000004; OOR99750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T0ATD7; -.
DR STRING; 734.B0187_02780; -.
DR OrthoDB; 9805041at2; -.
DR UniPathway; UPA00908; UER00886.
DR Proteomes; UP000190867; Unassembled WGS sequence.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0015970; P:guanosine tetraphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
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; 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; 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 Hydrolase {ECO:0000313|EMBL:OOR99750.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000190867}.
FT DOMAIN 45..144
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 385..446
FT /note="TGS"
FT /evidence="ECO:0000259|PROSITE:PS51880"
FT DOMAIN 496..569
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
SQ SEQUENCE 569 AA; 64564 MW; 4C46A97F576FFAC6 CRC64;
MYLFQPLNQI IQGYLPADKI ELVERAFVVA RDAHEGQTRS SGEPYITHPV AVACIIAEMK
LDHEAVMAAL LHDVIEDTPY TQEQLAAEFG TSVAEIVQGV SKLDKLKFRT RQEAEVANFR
KMILAMTKDI RVVLIKLADR THNMRTLGSL RPDKRRRIAK ETLEIYSPLA HRLGIEHLKN
ELEDLCLEAI YPHRYRVLKL AIEMARNTRQ DLIAKITHEI EQRLHEVGIP CRVYGKEKHL
YALYQKMLQR DQHFHSILDI YAFRVVVENV DNCYRTLGQM HALYKPRPQG IKDYIAVPKT
NGYQSLHTSM IGHKGVPIDV QIRTEEMDQM ATLGVAAFWR YSEQLQATSV QQKAQRWLQS
IVELQQSAGN SQEFIESVKS DLFSDDIYVF TPKGRIVELP AHATAIDFAY AVHSDIGDQC
VGAVVDRNPY PLSQPLKSGQ TVEILIEQGH CPNPHWLKFV VSAKAKARIR HALKIQQEQA
VSSDEISTQV AEMETDIVLK IRHQAGILAS ITSTIATMNG NIVSIQSEPT NEENIFKLNL
KISVTDNAHY YLILRKLLNL TGVVKAEKA
//
