ID GLND_BRUMB Reviewed; 934 AA.
AC C0RGK0;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 84.
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=BMEA_A0150;
OS Brucella melitensis biotype 2 (strain ATCC 23457).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=546272;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23457;
RA Setubal J.C., Boyle S., Crasta O.R., Gillespie J.J., Kenyon R.W., Lu J.,
RA Mane S., Nagrani S., Shallom J.M., Shallom S., Shukla M., Snyder E.E.,
RA Sobral B.W., Wattam A.R., Will R., Williams K., Yoo H., Munk C., Tapia R.,
RA Han C., Detter J.C., Bruce D., Brettin T.S.;
RT "Brucella melitensis ATCC 23457 whole genome shotgun sequencing project.";
RL Submitted (MAR-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; CP001488; ACN99957.1; -; Genomic_DNA.
DR RefSeq; WP_004686653.1; NC_012441.1.
DR AlphaFoldDB; C0RGK0; -.
DR SMR; C0RGK0; -.
DR KEGG; bmi:BMEA_A0150; -.
DR HOGENOM; CLU_012833_1_0_5; -.
DR PRO; PR:C0RGK0; -.
DR Proteomes; UP000001748; Chromosome I.
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; cd00077; HDc; 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; 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; 2.
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; 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 Repeat; Transferase.
FT CHAIN 1..934
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_1000132526"
FT DOMAIN 496..613
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 737..818
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 848..931
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..379
FT /note="Uridylyltransferase"
FT REGION 380..736
FT /note="Uridylyl-removing"
SQ SEQUENCE 934 AA; 105904 MW; C4F873C09366CF25 CRC64;
MSAHDLKLEE IVNAETLRRK LNELADTADE SYTSLPMRKV VLQTLKDALA SGRANAEDML
MKDGGGTLCA KRLCYLMDTL IDILFEFATT RAYPTRNPSK AENMALVAVG GYGRGGLAQG
SDIDLLFLLP YKQTPWGEQV VEHTLYMLWD MGLKVGHSTR NIDECIRLAR EDMTIRTALL
DARFLTGDKD LFRTLEIRFE EEIVKGTEPE FIQAKLAERD ARHRKAGETR YLVEPNVKEG
KGGQRDLHTL FWITKYFYRV KTKEELVKLG VLSRAELKLF NKAEDFLWAV RCHMHFATLK
AEERLSFDIQ PEIAQRLGYT AHPGQNYVER FMKHYFLVAK DVGDLTRIIC AALEEQQAKH
VPGFNRIFLT FSRRKRKLSD DGAFISENHR INIARPDIFR QDPVNMIRLF HLADRHGLEF
HPEAMQSLTR SLKLINADLR ENPEANRLFL EILTSPRNPE LILRRMNESG VLGKFIPDFG
KIVAMMQFNM YHHYTVDEHL LRCIAVLSEI EHGELKTEHP LSNHLITTIK RDRNLLYVTL
LLHDIAKGRP EDHSIAGARI ARRLCPRFGL TPSETETVEW LVREHLTMSM VAQSRDLNDR
KTIIDFADTV QTMERLKLLL ILTVCDIKAV GPGIWNGWKG QLLRTLFYET ELVLTGGFSE
LSRAARDKQA REALAERLSD WPKEERDAYL ALPYTNYFLT VSLDDQVRHA HFIRDADQQG
RALVTMAKPH AFEAVTEITV LAPDHPRLLS VITGACAAAG GNIVDAQIFT TSDGRALDTI
LISREFDTDD DERRRAERVG KVIEDVLSGK AHLPDMLAKR TKPKKAARAF KVEPRVEINN
TLSNKFTVIE VEGLDRPGLL SELTGLISDL SLDIASAHIT TFGEKVIDSF YVTDLVGHKI
SNATRQGNIK RKLLALLGAE NGARTNGRSP QAAA
//
