GLND_VIBA3
ID GLND_VIBA3 Reviewed; 873 AA.
AC B7VIS0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 79.
DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase/UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=PII uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=2.7.7.59 {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_00277};
GN Name=glnD {ECO:0000255|HAMAP-Rule:MF_00277}; OrderedLocusNames=VS_2355;
OS Vibrio atlanticus (strain LGP32) (Vibrio splendidus (strain Mel32)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=575788;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LGP32;
RA Mazel D., Le Roux F.;
RT "Vibrio splendidus str. LGP32 complete genome.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory proteins (GlnB and homologs), in response to the nitrogen
CC status of the cell that GlnD senses through the glutamine level. Under
CC low glutamine levels, catalyzes the conversion of the PII proteins and
CC UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC uridylylation state and activity of the PII proteins, and plays an
CC important role in the regulation of nitrogen assimilation and
CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-
CC tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:90602; EC=2.7.7.59;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-
CC tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:57865, ChEBI:CHEBI:90602;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC by glutamine, while glutamine activates uridylyl-removing (UR)
CC activity. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- DOMAIN: Has four distinct domains: an N-terminal nucleotidyltransferase
CC (NT) domain responsible for UTase activity, a central HD domain that
CC encodes UR activity, and two C-terminal ACT domains that seem to have a
CC role in glutamine sensing. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
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DR EMBL; FM954972; CAV19516.1; -; Genomic_DNA.
DR RefSeq; WP_012604606.1; NC_011753.2.
DR AlphaFoldDB; B7VIS0; -.
DR SMR; B7VIS0; -.
DR STRING; 575788.VS_2355; -.
DR PRIDE; B7VIS0; -.
DR EnsemblBacteria; CAV19516; CAV19516; VS_2355.
DR KEGG; vsp:VS_2355; -.
DR PATRIC; fig|575788.5.peg.3618; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_0_0_6; -.
DR OMA; WIAKYVY; -.
DR OrthoDB; 162558at2; -.
DR Proteomes; UP000009100; Chromosome 1.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 1.
DR Gene3D; 3.30.460.10; -; 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 PANTHER; PTHR47320; PTHR47320; 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; SSF55021; 2.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..873
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_1000132531"
FT DOMAIN 451..573
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 693..777
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 800..873
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..332
FT /note="Uridylyltransferase"
FT REGION 333..692
FT /note="Uridylyl-removing"
SQ SEQUENCE 873 AA; 100638 MW; F87E5B8C89D7356D CRC64;
MPYQCPITFN DEQLEICELK NQLEIFTQYQ KSEFLNHHPV TDLVLLRSEY MDLLLNRLWE
HFGFSKLPHI ALVAVGGYGR GELHPLSDID ILIVSQRTLP SALGEKVSQF ITLLWDLKLE
VGHAVRTIAE CIEIGSDDLT VATNLQESRL LCGSEDTFQE LKLKIHSDSF WPSETFYKAK
IQEQRERHAR YHDTTYNLEP DIKSTPGGLR DIHTLSWVAR RHFGATSLLE MSKYGFLTDA
EYRELVECQD FLWRVRFALH IELRRYDNRL TFAHQAQVAE HLGYTGEGNR GVEMMMKEFY
RTLRRVAELN KMLLKLFDQA IINGGQTQEA EILDNDFQRR GSLIEARKPA LFQARPETIL
DMFIHIANDS TIEGVSPPTL RQLRTARRRL NRFLHTIPEA RDKFMDLVRH PNALHKAFSL
MHKLGVLSAY LPQWSQIVGQ MQFDLFHVYT VDEHSIRLLK HINRFSQVEN HDKHPICCEV
YPRVQKKELL ILAAIFHDIG KGRGGDHSEI GAVEAYSFCI EHGLSKPEAK QVAWLVQNHL
LMSVTAQRRD IYDPDVITEF AKKVRDEESL ELLVCLTVAD ICATNPELWN SWKRTLLAEL
FHSTQRALRR GLENPVDVRD RIRHNQQMAS ALLRKEGFSA REIEVLWQRF KADYFLRHTH
TQIAWHCEHL LRLEDPSQPL VLISKKATRG GTEVFVYCKD QAALFATVVA ELDRRNFNVH
DAQVMVSKDG HVLDTFIVLD QHGEAIDEAR HKAVAKHLTH VLADGRPTKI KTRRTPRNLQ
HFKVKTRVEF LPTKSKKRTL MELRALDTPG LLAQVGATFA ELDINLHGAK ITTIGERAED
LFILTSDAGG RLSEEQEQAL RERLTEHVSE LAP
