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Database: UniProt
Entry: GLND_AZOBR
LinkDB: GLND_AZOBR
Original site: GLND_AZOBR 
ID   GLND_AZOBR              Reviewed;         933 AA.
AC   Q8RQD1;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   13-SEP-2023, entry version 89.
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   Azospirillum brasilense.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Azospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RA   Van Dommelen A., Keijers V., Somers E., Vanderleyden J.;
RT   "Cloning and characterization of the Azospirillum brasilense glnD gene and
RT   analysis of a glnD mutant.";
RL   Mol. Gen. Genet. 266:813-820(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND ACTIVITY REGULATION.
RC   STRAIN=FP2;
RX   PubMed=18392451; DOI=10.1590/s0100-879x2008000400006;
RA   Araujo L.M., Huergo L.F., Invitti A.L., Gimenes C.I., Bonatto A.C.,
RA   Monteiro R.A., Souza E.M., Pedrosa F.O., Chubatsu L.S.;
RT   "Different responses of the GlnB and GlnZ proteins upon in vitro
RT   uridylylation by the Azospirillum brasilense GlnD protein.";
RL   Braz. J. Med. Biol. Res. 41:289-294(2008).
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins GlnB and GlnZ, 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
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:0000269|PubMed:18392451}.
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         ECO:0000269|PubMed:18392451};
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         ECO:0000269|PubMed:18392451};
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. Uridylylation process is dependent on ATP and 2-oxoglutarate,
CC       which are effector molecules that likely bind to PII proteins and
CC       control their activity. {ECO:0000255|HAMAP-Rule:MF_00277,
CC       ECO:0000269|PubMed:18392451}.
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; AF149716; AAL87737.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8RQD1; -.
DR   SMR; Q8RQD1; -.
DR   BRENDA; 2.7.7.59; 611.
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-KW.
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; 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; 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   1: Evidence at protein level;
KW   Hydrolase; Magnesium; Multifunctional enzyme; Nitrogen fixation;
KW   Nucleotidyltransferase; Repeat; Transferase.
FT   CHAIN           1..933
FT                   /note="Bifunctional uridylyltransferase/uridylyl-removing
FT                   enzyme"
FT                   /id="PRO_0000192716"
FT   DOMAIN          506..628
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   DOMAIN          746..829
FT                   /note="ACT 1"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   DOMAIN          859..933
FT                   /note="ACT 2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT   REGION          1..390
FT                   /note="Uridylyltransferase"
FT   REGION          391..745
FT                   /note="Uridylyl-removing"
SQ   SEQUENCE   933 AA;  104602 MW;  35E692E0411BB9E7 CRC64;
     MLSTRAASAD ASDAKDAGTA NIPNKRAILS RRKLAEDLET LVAEHGTGDK LRPALIARLR
     GALNDGRAEV RARFEAKGSG EDCVRQNCYL ADGVVRSLAD LTVTHIFPTP NPTSGEVFDI
     VATGGYGRGE LAPFSDIDLL FLLPYKRTPR VEQVVEYMLY ILWDLGLKVG HAVRSVDDCI
     RQSKADVTIR TAILESRYLW GPRKLFHRLR RRFDREVVAG TGPEFVEAKL AERDNRHLKL
     GDSAYVLEPN LKDGKGGLRD LQTLFWIAKY LYRVEDVDDL VGKKVLLPEE AHGFAKAQNF
     LWTARCHLHY LTGRMEDRMT FDVQTSIGNR MGYTDHAGTK GVERFMKHYF LVAKDVGDLT
     RIFCAALEAE SKRPPKFNIL RLAALARRKD VDGFVVDGER LNVRSDRQFK DEPLDMIRLF
     HTAQQNDIDI HPNALRAITR SLSVVGPKLR ADPEANRLFL EILTGRKDPE ITLRRMNEAG
     VLARFIPDFG RVVAQMQYDM YHVYTVDEHT LFALGILHKI EMGELTDELP LSSEVIHKVV
     SRRALYVAVL LHDIAKGRGG DHSILGARVA EKLCPRLGLT AEETETVAWL VRWHLAMSYT
     AFKRDLEDDK TVRDFVSLVQ SPERLRLLLV LTVADIRAVG PQRWNNWKAT LLRELYNRSE
     EVMSGGLSVE GRGRRIQAAQ AALRDELSDF DAADFERHLA LGYPAYWLAF DAETLGRQAR
     LVRGRLRDER PLTVNTRIDR GRAITEVTIF ATDHHGLFSR LAGALAAAGA DIVDARIFTM
     TNGMALDVFT VQDAAGGGAF ESGDKLAKLS VMIEKVLSGQ LKPLHDLTKR KAPHASRTRV
     FHVPPRVLID NNASTTHTVI EVNGRDRPGL LYDLTRALTN LTLQISSAKI STYGEKAIDV
     FYVKDVFGLK VTHENKLAQI RERLLHALAD PSA
//
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