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 25-MAY-2022, entry version 85.
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; Proteobacteria; 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; 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; 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 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
