GLND_PECAS
ID GLND_PECAS Reviewed; 904 AA.
AC Q6D8E5;
DT 08-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, 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=ECA1029;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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 fixation and metabolism.
CC {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX950851; CAG73940.1; -; Genomic_DNA.
DR RefSeq; WP_011092628.1; NC_004547.2.
DR AlphaFoldDB; Q6D8E5; -.
DR SMR; Q6D8E5; -.
DR STRING; 218491.ECA1029; -.
DR EnsemblBacteria; CAG73940; CAG73940; ECA1029.
DR GeneID; 57207858; -.
DR KEGG; eca:ECA1029; -.
DR PATRIC; fig|218491.5.peg.1037; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_0_0_6; -.
DR OMA; WIAKYVY; -.
DR OrthoDB; 162558at2; -.
DR Proteomes; UP000007966; 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:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 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; 2.
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; Nitrogen fixation;
KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..904
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192731"
FT DOMAIN 479..601
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 720..801
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 827..904
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..360
FT /note="Uridylyltransferase"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 361..719
FT /note="Uridylyl-removing"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 904 AA; 104412 MW; 1A6A4DEF5361ED32 CRC64;
MTDKRFSPDN TPPDASSPDS PIDTIAAAQP PVSPLTYADD MLNCQALKQQ LELFQLWLGS
EFRSGVSAEK LIDARTLFID RLLQRLWYCH GFENIAQTAL VAVGGYGRGE LHPLSDIDVL
VLSQTELSDE HSQRVGQFIT LLWDLKLEVG HSVRTLEECL QEGRADISVA TNLIESRMIC
GDVALFLTLQ KHVFSDEFWP SPTFFPAKIT EQQERHQRYH STSYNLEPDI KSSPGGLRDI
HTLLWVARRH FGATSLNEMV GFGFLTEAER KELNECQSFL WRIRFALHLI LPRYDNRLLF
DRQLNVAQLL QYQGEGNTPV ERMMKDFYRM TRRVSELNQM LLQLFDEAIL ALDASEKPRP
IDDEFQLRGN LVDLRDENLF IKKPEAIMRM FYLMVRNRDI SGIYSTTLRQ LRHARRHLAS
PLCTIPEARQ LFMNILRHPY AVSRALLPMH RHSVLWAYMP LWGNIVGQMQ FDLFHAYTVD
EHTIRVLLKL ESFADEDTRP QHPLCVELYP RLPQPELLLL AALFHDIAKG RGGDHSELGA
LDVLEFAALH GLNSREAQLV SWLVRCHLLM SVTAQRRDIQ DPTVIQQFAT EVQSETRLRY
LVSLTVADIC ATNETLWNSW KQSLLRELYF ATEKQLRRGM QNTPDLRERV RHHRLQALAL
LRMDNIDEEA LHHIWSRCRA DYFLRHSPNQ IAWHARHLLE HDTNKPLVLI SHQASRGGTE
IFIWSPDRPY LFAAVAGELD RRNLSVHDAQ IFTSRDGMAM DTFIVLEPDG SPLAQDRHEM
IRHALEQALT QRHYQHPRVR RTSPKLRHFS VPTEVNFLPT HTDRRSYMEL SALDQPGLLA
RIGEIFSDLN LSLHGARIST IGERVEDLFI LADSDRRALK PELRLKLQER LTEALNPNDK
VPLS
