GLND_RHILV
ID GLND_RHILV Reviewed; 944 AA.
AC Q9RAE4;
DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 08-DEC-2000, sequence version 2.
DT 25-MAY-2022, entry version 96.
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};
OS Rhizobium leguminosarum bv. viciae.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=387;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, ACTIVITY REGULATION,
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=VF39;
RX PubMed=11065377; DOI=10.1099/00221287-146-11-2987;
RA Schluter A., Nohlen M., Kramer M., Defez R., Priefer U.B.;
RT "The Rhizobium leguminosarum bv. viciae glnD gene, encoding a
RT uridylyltransferase/uridylyl-removing enzyme, is expressed in the root
RT nodule but is not essential for nitrogen fixation.";
RL Microbiology 146:2987-2996(2000).
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory proteins GlnB and GlnK, in response to the nitrogen status
CC of the cell that GlnD senses through the glutamine level. Under low
CC glutamine levels, catalyzes the conversion of the PII proteins and UTP
CC to PII-UMP and PPi, while under higher glutamine levels, GlnD likely
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 metabolism.
CC {ECO:0000269|PubMed:11065377}.
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 likely activates uridylyl-removing (UR)
CC activity. {ECO:0000269|PubMed:11065377}.
CC -!- INDUCTION: Is constitutively expressed, irrespective of the nitrogen
CC content of the medium. {ECO:0000269|PubMed:11065377}.
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 -!- DISRUPTION PHENOTYPE: Deletions in the 5'-region of this gene appear to
CC be lethal. Insertion mutations in the central part of this gene
CC abolishes the ability to use nitrate as a sole nitrogen source but not
CC glutamine. In addition, neither uridylylation of PII nor induction of
CC the ntr-regulated glnII gene (encoding glutamine synthetase II) under
CC ammonium deficiency can be observed in mutant strains.
CC {ECO:0000269|PubMed:11065377}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF17352.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF155830; AAF17352.1; ALT_INIT; Genomic_DNA.
DR AlphaFoldDB; Q9RAE4; -.
DR SMR; Q9RAE4; -.
DR PRIDE; Q9RAE4; -.
DR BRENDA; 2.7.7.59; 5343.
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 2: Evidence at transcript level;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nucleotidyltransferase;
KW Repeat; Transferase.
FT CHAIN 1..944
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192758"
FT DOMAIN 488..604
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 728..809
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 839..918
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..371
FT /note="Uridylyltransferase"
FT REGION 372..727
FT /note="Uridylyl-removing"
FT REGION 911..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 106218 MW; B164E74FF9E6DF2E CRC64;
MRDLDFTNIL DVELLQKQCD AVAEANRNRP DVLRADLLAV LKKASTEGRQ KAREALMADG
GGLNCAYRIS WLQDQITTVL YNFATAHIFP QQKDKFAVTA VGGYGRDTLA PGSDIDLLFL
FLPRPAEETH KAVEFMLYVL WDMGFKVGHA TRTVEECIAL SKSDMTIRTA ILEMRYICGL
QRLETELETR FDKEIVTGTG PEFIAAKLAE RDERHRKAGD TRYLVEPNVK EGKGGLRDLH
TLFWISKYYY HVRDQAELVK LGVLSKHEYR LLEKADDFLW AVRCHMHFLT GKAEERLSFD
IQREIAEAFG YHTRPGLSAV ERFMKHYFLV AKDVGDLTRI LCAALEDQQA KSIPGLTGVI
SRFTHRNRKI AGSVEFVEDR GRIALADPEV FKRDPVNIIR LFHVADINGL EFHPDALKRV
TRSLALIDNA LRENDEANRL FMSILTSKRD PALILRRMNE AGVLGRFIPE FGKIVAMMQF
NMYHHYTVDE HLIRTVDILS EIDKGRAEDL HPLANKLMPG IEDREALYVA VLLHDIAKGR
QEDHSIAGAR VARKLCVRFG LSQKQTEIVV WLIEEHLTMS MVAQTRDLTD RKTITDFADR
VQSLDRLKML LILTICDIRA VGPGVWNGWK GQLLRTLYYE TELLLAGGFS EVSRKERANA
AAEALHSALA DWSQKDRNTY TKLHYQPYLL SVPLEDQIRH AHFIRQADKA GQALATMVRT
DSFHAITEIT VLSPDHPRLL AVIAGACAAA GANIVDAQIF TTSDGRALDT IHVSREFTDD
ADELRRAATI GRMIEDVLSG RKRLPEVIAT RARNRKKSKA FVIPPSVNIT NSLSNKFTVI
EVECLDRPGL LSEITAVLSD LSLDIQSARI TTFGEKVIDT FYVTDLVGQK ISGDSKRANI
TARMKAVMAE EEDELRERMP SGIIAPAATA RTPPASEKKA GSPI
