GLND_AZOVI
ID GLND_AZOVI Reviewed; 899 AA.
AC P36223;
DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1994, sequence version 1.
DT 25-MAY-2022, entry version 95.
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}; Synonyms=nfrX;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, COMPLEMENTATION OF E.COLI GLND
RP MUTANT, AND ROLE IN NITROGEN FIXATION.
RC STRAIN=OP / UW136;
RX PubMed=1683868; DOI=10.1128/jb.173.24.7741-7749.1991;
RA Contreras A., Drummond M., Bali A., Blanco G., Garcia E., Bush G.,
RA Kennedy C., Merrick M.;
RT "The product of the nitrogen fixation regulatory gene nfrX of Azotobacter
RT vinelandii is functionally and structurally homologous to the
RT uridylyltransferase encoded by glnD in enteric bacteria.";
RL J. Bacteriol. 173:7741-7749(1991).
RN [2]
RP FUNCTION AS PII URIDYLYLTRANSFERASE, AND DISRUPTION PHENOTYPE.
RC STRAIN=OP / UW136;
RX PubMed=11320130; DOI=10.1099/00221287-147-5-1267;
RA Colnaghi R., Rudnick P., He L., Green A., Yan D., Larson E., Kennedy C.;
RT "Lethality of glnD null mutations in Azotobacter vinelandii is suppressible
RT by prevention of glutamine synthetase adenylylation.";
RL Microbiology 147:1267-1276(2001).
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory protein GlnK, in response to the nitrogen status of the cell
CC that GlnD senses through the glutamine level. Under low glutamine
CC levels, catalyzes the conversion of the PII protein and UTP to PII-UMP
CC and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP
CC to PII and UMP (deuridylylation). Thus, controls uridylylation state
CC and activity of the PII protein, and plays an important role in the
CC regulation of nitrogen fixation and metabolism.
CC {ECO:0000269|PubMed:11320130, ECO:0000269|PubMed:1683868}.
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 -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not viable unless a
CC second mutation occurs, either spontaneously or by design, resulting in
CC the inability of glutamine synthetase (GS) to be adenylylated.
CC {ECO:0000269|PubMed:11320130}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
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DR EMBL; X59610; CAA42173.1; -; Genomic_DNA.
DR PIR; S24223; S24223.
DR RefSeq; WP_012702416.1; NZ_FPKM01000003.1.
DR AlphaFoldDB; P36223; -.
DR SMR; P36223; -.
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; 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; 1.
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..899
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192717"
FT DOMAIN 461..583
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 706..789
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 816..899
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..342
FT /note="Uridylyltransferase"
FT REGION 343..705
FT /note="Uridylyl-removing"
SQ SEQUENCE 899 AA; 102580 MW; 96AF63BC5EDE3C9D CRC64;
MPQVDPDLFD PGQFQAELAL KSSPIPAYKK ALRCAREVLD ARFQEGRDIR RLIEDRAWFV
DQILALAWNR FDWSEDADIA LIAVGGYGRG ELHPYSDIDL LILMDGADHE VFREPIEGFL
TLLWDIGLEV GQSVRSLAEC AEEAQADLTV ITNLMESRTI AGPEHLRQRM QEVTSAQRMW
PSRAFFLAKR DEQKTRHARY NDTEYNLEPN VKGSPGGLRD IQTLLWIARR QFGTINLHAM
VGQGFLLESE YTLLASSQEF LWKVRYALHM LAGRAEDRLL FDLQRQIAGL LGYEDSDAKL
AVERFMQKYY RVVLGIAELT ELVFQHFEEV ILPGDAAGRV EPLNERFQVR DGYLEVTHAG
VFQETPSALL EIFVLLARRP EIRGVRADTI RLLRDHRYLI DDAFRRDPHN TGLFIELFKS
RQGIHRNLRR MNRYGILGRY LPEFGHIVGQ MQHDLFHIYT VDAHTLNLIK NLRKLFWPEL
AEKYPLASKL IEKLPKPELI YLAGLYHDIG KGRGGDHSEL GAADALAFCQ RHDLPAMDTQ
LIVWLVRNHL LMSTTAQRKD LSDPQVIFDF AQKVRDQTYL DYLYVLTVAD INATNPTLWN
SWRASLLRQL YTETKHALRR GLEQPVGREE QIRQTQKAAL DILVRSGTDP DDAEHLWTQL
GDDYFLRHTS SDIAWHTEAI LQHPSSGGPL VLIKETTQRE FEGATQIFIY APDQHDFFAV
TVAAMDQLNL SIHDARVITS TSQFTLDTYI VLDADGGSIG NNPARIQEIR QGLVEALRNP
ADYPTIIQRR VPRQLKHFAF APQVTIQNDA LRPVTILEII APDRPGLLAR IGKIFLDFDL
SLQNAKIATL GERVEDVFFV TDAHNQPLSD PELCARLQLA IAEQLADGDS YIQPSRISI
