ID A0A1V2ZVA9_9GAMM Unreviewed; 889 AA.
AC A0A1V2ZVA9;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=guanosine-3',5'-bis(diphosphate) 3'-diphosphatase {ECO:0000256|ARBA:ARBA00024387};
DE EC=3.1.7.2 {ECO:0000256|ARBA:ARBA00024387};
DE Flags: Fragment;
GN ORFNames=B1A74_13300 {ECO:0000313|EMBL:OOC08986.1};
OS Thioalkalivibrio halophilus.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=252474 {ECO:0000313|EMBL:OOC08986.1, ECO:0000313|Proteomes:UP000189177};
RN [1] {ECO:0000313|EMBL:OOC08986.1, ECO:0000313|Proteomes:UP000189177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL17 {ECO:0000313|EMBL:OOC08986.1,
RC ECO:0000313|Proteomes:UP000189177};
RA Ahn A.-C., Meier-Kolthoff J., Overmars L., Richter M., Woyke T.,
RA Sorokin D.Y., Muyzer G.;
RT "Genomic diversity within the haloalkaliphilic genus Thioalkalivibrio.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:OOC08986.1}.
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DR EMBL; MUZR01000070; OOC08986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V2ZVA9; -.
DR STRING; 252474.B1A74_13300; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000189177; Unassembled WGS sequence.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd04899; ACT_ACR-UUR-like_2; 1.
DR CDD; cd04900; ACT_UUR-like_1; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 1.10.3210.10; Hypothetical protein af1432; 1.
DR HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR InterPro; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR010043; UTase/UR.
DR NCBIfam; TIGR01693; UTase_glnD; 1.
DR PANTHER; PTHR47320; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR47320:SF1; BIFUNCTIONAL URIDYLYLTRANSFERASE_URIDYLYL-REMOVING ENZYME; 1.
DR Pfam; PF01842; ACT; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:OOC08986.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000189177};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:OOC08986.1}.
FT DOMAIN 446..568
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 688..770
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 797..873
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 864..889
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OOC08986.1"
SQ SEQUENCE 889 AA; 101196 MW; 54AC9B49799AF0D8 CRC64;
ELSRHPGDIA RFREYRRGIV EQQYRGFHDG VAIEDLIFGH ARRIDDLLRL IWAQFGLAAD
PNLCLVAVGG YGRGELHPAS DIDIQILVTG EHDATRSERI GEFVTFLWDI GIEVGHSVRS
IEDCTREARD DITVVTNLIE SRYVSGSLAL FNDFRATIEA DRVWDSRSFY AAKLAEQQAR
HRRFGETAYR LEPNVKEGPG GLRDIQMIGW VTKRHFGAER IEELVSLGFL REGEFQEMVE
GQNFLWRVRF ALHMLTGRRE DRLLFDLQRQ LASTFGFVDQ NHNRAVEQFM QRYFRTINDL
ERLNELLLQH FNEAILDDPE QLQQPERIHP RFQVRGGYLE VAHDQVFMIY PPALLEVFRI
LQQHPEIQGI RASTVRLIRA HRHLIDGHFR RNRLNRELFM AILRAPRGIT SQLRRMNRYG
VLGNYLPAFG RIIGRMQYDL FHVYTVDEHT LHVVRNARRL ALPEFAHEHP LASEIHAGLE
RPERLVLAAL FHDIAKGRGG DHSELGAQDA LHFCQQHGLS DADAALVAWL VRSHLLMSLT
AQRRDISDPD VVMEFAREVR SPERLDFLYL LTIADIRGTN PEMWNSWKDS LLQTLYHATR
NVLDRGLDRP PDMEEQIRQT RRETLELLAP QGIGGEDAAV LWGRLDDEYF LRHSPDEIAW
HTQALLNNDL EDLPLVLVRP RTSRGSTEVF VYAEDHPRLF ARTTAALAQL GLDIVDARII
STADGHSLDT FLVLENAGQT VESGYRTQEI CATLNRALRD GAVGAAPVQR QLPRRLKHFD
VDTRVEFEEG SPGGATRMRI RALDRPGLLS TVGHVLAEHD TDIRTARIAT AGEQVEDSFT
LTGSDRRPLT AAERERLRAA LLEAIRESEP PSSNAGPNGS PNAADAGPA
//
