GLND_BRADU
ID GLND_BRADU Reviewed; 929 AA.
AC Q89VX9;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 2.
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=bll0916;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
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 -!- SEQUENCE CAUTION:
CC Sequence=BAC46181.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BA000040; BAC46181.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_767556.1; NC_004463.1.
DR RefSeq; WP_038965190.1; NZ_CP011360.1.
DR AlphaFoldDB; Q89VX9; -.
DR SMR; Q89VX9; -.
DR STRING; 224911.27349166; -.
DR PRIDE; Q89VX9; -.
DR EnsemblBacteria; BAC46181; BAC46181; BAC46181.
DR GeneID; 64020780; -.
DR KEGG; bja:bll0916; -.
DR PATRIC; fig|224911.44.peg.305; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_1_0_5; -.
DR InParanoid; Q89VX9; -.
DR OMA; WIAKYVY; -.
DR Proteomes; UP000002526; 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 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 3: Inferred from homology;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nitrogen fixation;
KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase.
FT CHAIN 1..929
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192721"
FT DOMAIN 499..622
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 740..822
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 850..927
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..383
FT /note="Uridylyltransferase"
FT REGION 384..739
FT /note="Uridylyl-removing"
SQ SEQUENCE 929 AA; 105033 MW; E4A270C497C26D5E CRC64;
MDSVTTEHKQ EVDDRFDTAR ITAAVDALAE KHQGREDAFR TAMAQLLKAE LIAARAAAQA
ILLKDRHGRR CAERLCHVQD EIIRILYSAA TRHLYRSPIP SGAERMAVVA TGGYGRGLMA
PESDIDLLFI LPYKQTAWGE QVAEAILYCL WDMGLKVGHA TRSVDESIRQ ARGDMTIRTA
ILETRFLTGD QPLYDELVER FDKEVVQGTA SEFVTAKLAE REERHRRGGQ SRYLVEPNVK
DGKGALRDLH TLFWIAKYVY RVRDTDELVE RGVFDAQEYR TFRRCADFLW SVRCNLHFYS
GRAEERLSFD LQREIAVRLG YTSHPGMQDV ERFMKHYFLV AKEVGNLTAI LCAKLEDQQA
KPAPVLSRMM ARLRPTPAKR RVPDSDDFIV DNNRINVAAP DVFKHDPVNL IRIFRLAQKH
NLAFHPDAMR DVTRSLGLIN AQLRENPEAN RLFMEILTSD NAEIVLRRMN ETGVLGHFIR
AFGKIVSMMQ FNMYHHYTVD EHLIRCVGFL QDIERGGIEE FAVASDLMRK IRPEHRSVIY
IATLLHDVAK GRPEDHSIAG AKVARRLCPR LGFSPADTEL VAWLIEEHLT MSTVAQSRDL
SDRKTIENFA AVVQSVEQMK LLTILTTADI RGVGPGVWNG WKAQLLRSLY YETEPVLTGG
FSEVDRGKRL TAAYAEFRNA FAEWPADELD AYIARHYPAY WLKVELPRKI RHARFVRSSE
QAGHKLAINV GFDEVRGVTE LTIFAADHPW LLSIIAGACA SAGANIVDAQ IYTTTDGRAL
DTISISREYD RDEDEGRRAT RIGEMIEDVL EGKLRLPEVV ARRTVRSKAR PFVIEPEVTI
NNQWSDRYTV IEVSGLDRPG LLYELTTAIS KLNLNIASAH VATFGERARD VFYVTDLLGA
QINAPTRQSA IKSALTHVMA GDKAVQPAA
