GLND_NOVAD
ID GLND_NOVAD Reviewed; 912 AA.
AC Q2GAJ4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2006, sequence version 1.
DT 25-MAY-2022, entry version 105.
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=Saro_0682;
OS Novosphingobium aromaticivorans (strain ATCC 700278 / DSM 12444 / CCUG
OS 56034 / CIP 105152 / NBRC 16084 / F199).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=279238;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700278 / DSM 12444 / CCUG 56034 / CIP 105152 / NBRC 16084 /
RC F199;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chain P., Malfatti S., Shin M.,
RA Vergez L., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N.,
RA Fredrickson J., Balkwill D., Romine M.F., Richardson P.;
RT "Complete sequence of Novosphingobium aromaticivorans DSM 12444.";
RL Submitted (JAN-2006) 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; CP000248; ABD25129.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2GAJ4; -.
DR SMR; Q2GAJ4; -.
DR STRING; 279238.Saro_0682; -.
DR EnsemblBacteria; ABD25129; ABD25129; Saro_0682.
DR KEGG; nar:Saro_0682; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_1_0_5; -.
DR OMA; WIAKYVY; -.
DR Proteomes; UP000009134; Chromosome.
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; IPR010043; UTase/UR.
DR PANTHER; PTHR47320; PTHR47320; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 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..912
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_1000078807"
FT DOMAIN 486..608
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 723..802
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 834..912
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..369
FT /note="Uridylyltransferase"
FT REGION 370..722
FT /note="Uridylyl-removing"
SQ SEQUENCE 912 AA; 101972 MW; E81AD196FA1A216A CRC64;
MLPRIANQRA IVDRRALADA VSAAFAEQGD RSRPAVVELL RGALDSGRAE LARRLEARPS
AGTECAHGQA FLVDQLVRVI HDHVVGKVYR ASNRSTGERI AIIAVGGYGR GEMAPHSDVD
IAFVTPIKPT SWCEQVIEAI LYFLWDLGLK VGHSSRSLDE VVRMAKSDLT IRTALLEGRY
VWGDRDLFDA ASARFWNEVV NGTEKQFVAE KLQERNERHK RLGDSRYVVE PNVKEGKGGL
RDLHTLYWIG KYIHKVRDAS ELVDVGLLTA EEYRAFRRAE NFFWAVRCHL HAITRRAEDR
LTFDLQREVA MRMNFADRPG KSAVERFMQY FFLQAKQVGS LTGVFLAQLD GQFARQKRSF
FASLRSRRKK VGPFFIEGGK LGVPAEDTFQ QDPVRLVELF AVAASEKVEI HPEAMRLARR
DAGLIDAAVR KDQRANALFL DVLTSRNDPE TVLRWMNEAG VFGRFVPDFG RVVAQMQFDM
YHHYTVDEHT IRAIGLLASI EKGEAKADHP LASEVVGKVA SRRVLYVATL LHDIAKGRRG
DHSVLGAEVA MKLCPRLGLS AAETELVAWL VRWHLLMSAT AFKRDLADYK TIADFVNTVQ
SQERLRLLLL LTIVDIRAVG PGVWNSWKRQ LLGDLFVSAE EVLRLGHKQH GRAERIIAKK
KAVGAILKER DNLIGTVGRQ LGDAYWIAEP EDIIALNLQQ MDQALGELLS VEAHWYPARG
ATLVTVLAAD HPGLFYRIAG GIHLAGGNII DARIHTARNG TAVDNFLVQD PLGRPLNEAS
QIERLKNAIA DALANRVKLV PQLAARPLAR PRADAFDVRP IVIFDNKASN RFTVIEVGAR
DRPALLNRLA RALFEARLIV HSAHIATYGE RAVDTFYVTD VLGEKVDSEA RMKAVEKRLL
EAAEDRKVKD AA
