ID GLND_NITWN Reviewed; 925 AA.
AC Q3SWE0;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 27-MAR-2024, entry version 118.
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=Nwi_0133;
OS Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS NCIMB 11846 / Nb-255).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Nitrobacter.
OX NCBI_TaxID=323098;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA Hickey W.J.;
RT "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT Nitrobacter winogradskyi Nb-255.";
RL Appl. Environ. Microbiol. 72:2050-2063(2006).
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; CP000115; ABA03401.1; -; Genomic_DNA.
DR RefSeq; WP_011313470.1; NC_007406.1.
DR AlphaFoldDB; Q3SWE0; -.
DR SMR; Q3SWE0; -.
DR STRING; 323098.Nwi_0133; -.
DR KEGG; nwi:Nwi_0133; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_1_0_5; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000002531; 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; cd04899; ACT_ACR-UUR-like_2; 1.
DR CDD; cd04900; ACT_UUR-like_1; 1.
DR CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR Gene3D; 3.30.70.260; -; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 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; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 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..925
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000231682"
FT DOMAIN 498..621
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 739..820
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 849..925
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..382
FT /note="Uridylyltransferase"
FT REGION 383..738
FT /note="Uridylyl-removing"
SQ SEQUENCE 925 AA; 104377 MW; 9B4D8076280C0070 CRC64;
MVLPTTKDAT AAGAGFDTVR IIGDIDALAE KHAGHEDVFR SAVSRLLKAE LAKVRDAAQA
KLLRDRHGRH CAEWLCFVQD EIIRLSFSAA TRHLYHSPIP SDGERMAVVA TGGYGRGLMA
PESDIDLLFI LPYKQTAWGE QVAEAILYCL WDMGLNVGHA TRSVNESIRQ ARRDMTVRTG
ILEARFLTGD RALYDELISR FDTEVVQGTA AEFVAAKLAE REERHHRAGQ SRYLVEPNVK
DGKGGLRDLH TLFWIAKYVY RVRESHELLR RNVFDVREYR TFRRCADFLW SVRCNLHFAT
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLT AKDVGDLTAI LCAKLEDQQA
KPAPVLSRAM SKPPGAEVRR VPDSDDFIID NNRINLAAPD LFKRDPVNLI RLFRLAQKNN
LAFHPDALRM VRRSRRLINA QLREDPESNR LFIEILTSND AETVLRRMNE TGVLGEFIRA
FGKIVSMMQF NMYHHYTVDE HLIRCIGILQ DIERGDNDEV ALAGELMRTI NPEHRPVIYI
ATLLHDVAKG RPEDHSIAGA RVARRLCPRL GFNAADTELV AWLIEQHLTM SKVAQSRDLS
DRKTIENFAA VVQSVERMKL LTILTTADIR GVGPGVWNGW KAQLLRTLYY ETEPVLTGGF
SEVNRAQRMA AAEAEFRAAF TEWSGHELNA YIARHYPAYW LKVDLEHKIR HARFLRASEQ
SGRKLNINVG FDEARGVTEL TILAADHPWL LSIIAGACAS AGANIVDAQI YTTTDGQALD
TIAISREYER DEDEGRRAAR IAEIIEQVLE GRLRLPDVMP SRAAGKRLRP FVVEPKVTIN
NQWSDRHTMI EVSGLDRPGL LFQLTTAISK LNLNIASAHV ATFGERARDV FYVTDLLGAR
ITAPTRQAAI KRALVHLLAS GNTAE
//
