(data stored in ACNUC7421 zone)

SWISSPROT: A0LFI3_SYNFM

ID   A0LFI3_SYNFM            Unreviewed;       864 AA.
AC   A0LFI3;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE            Short=UTase/UR {ECO:0000256|HAMAP-Rule:MF_00277};
DE   AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE   AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000256|HAMAP-Rule:MF_00277};
DE   Includes:
DE     RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=PII uridylyltransferase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=UTase {ECO:0000256|HAMAP-Rule:MF_00277};
DE              EC=2.7.7.59 {ECO:0000256|HAMAP-Rule:MF_00277};
DE   Includes:
DE     RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00277};
DE              Short=UR {ECO:0000256|HAMAP-Rule:MF_00277};
DE              EC=3.1.4.- {ECO:0000256|HAMAP-Rule:MF_00277};
GN   Name=glnD {ECO:0000256|HAMAP-Rule:MF_00277};
GN   OrderedLocusNames=Sfum_0485 {ECO:0000313|EMBL:ABK16185.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16185.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16185.1, ECO:0000313|Proteomes:UP000001784}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10017 / MPOB {ECO:0000313|Proteomes:UP000001784};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.G.,
RA   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Boone D.R., Brockman F., Culley D., Ferry J., Gunsalus R.,
RA   McInerney M.J., Morrison M., Plugge C., Rohlin L., Scholten J.,
RA   Sieber J., Stams A.J.M., Worm P., Henstra A.M., Richardson P.;
RT   "Complete sequence of Syntrophobacter fumaroxidans MPOB.";
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the
CC       nitrogen status of the cell that GlnD senses through the glutamine
CC       level. Under low glutamine levels, catalyzes the conversion of the
CC       PII proteins and UTP to PII-UMP and PPi, while under higher
CC       glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP
CC       (deuridylylation). Thus, controls uridylylation state and activity
CC       of the PII proteins, and plays an important role in the regulation
CC       of nitrogen assimilation and metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-
CC         L-tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:46858, ChEBI:CHEBI:90602;
CC         EC=2.7.7.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-
CC         L-tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:90602; Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00277, ECO:0000256|SAAS:SAAS00609838};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is
CC       inhibited by glutamine, while glutamine activates uridylyl-
CC       removing (UR) activity. {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- DOMAIN: Has four distinct domains: an N-terminal
CC       nucleotidyltransferase (NT) domain responsible for UTase activity,
CC       a central HD domain that encodes UR activity, and two C-terminal
CC       ACT domains that seem to have a role in glutamine sensing.
CC       {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
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DR   EMBL; CP000478; ABK16185.1; -; Genomic_DNA.
DR   STRING; 335543.Sfum_0485; -.
DR   EnsemblBacteria; ABK16185; ABK16185; Sfum_0485.
DR   KEGG; sfu:Sfum_0485; -.
DR   eggNOG; COG2844; LUCA.
DR   KO; K00990; -.
DR   BioCyc; SFUM335543:G1G7I-496-MONOMER; -.
DR   Proteomes; UP000001784; 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:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR   InterPro; IPR002912; ACT_dom.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   InterPro; IPR010043; UTase/UR.
DR   PANTHER; PTHR47320; PTHR47320; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 1.
DR   Pfam; PF01966; HD; 1.
DR   PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LFI3.
DR   SWISS-2DPAGE; A0LFI3.
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000313|EMBL:ABK16185.1};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00204441};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00677267};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440786, ECO:0000313|EMBL:ABK16185.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:ABK16185.1}.
FT   DOMAIN      455    558       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      676    757       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      787    864       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    321       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
FT   COILED      600    620       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   864 AA;  96982 MW;  0DC692E5B98AC62A CRC64;
     MHSISESLRK QREQVLSDSS EDALIRHTSL LEIAIISLYN RLVNRLSQDT EHFRSSAAVI
     GLDGFARGVI GPGQPVRILF LMTDSALWNA SWLDEITVPL TEAGWTVDLR RETIDSLMIA
     LEGDFEAFLE LLEMRYVSGN RQLLEQAEKG IEGFIEARRE ELLSRLYGTV KAREGRLQKP
     ESWLEPDLQD NPGALSDIVA IRLACRIASN IRSLDDAIFM GYLVRREVDF IRHAEKSYMR
     LLGLLRSLSD KSSGVLHFDE QGLLADKLGY AERAGYLPVE SLMQEVFQLF HGVGVVSAEF
     WERLRESREN LPAAGEMRGE PLEEGLFVLN GKIHIQTDRY PATPGHLVHL FRLAAEGGLG
     FANVTRQWVH HHRNALNSSS GDPLVKEELF ALIRADSEDL PAFRRFCDNG LFTALIPELA
     AVYGLAQHDA FHLYPIHEHH LRTLSELKKI RAGFYSAAEP ELTQIARGIE DPVWLYLAGL
     LHDIGKSSGR GHAAKGGEMI PAIARRLGLE PEETSKVRFL VAQHLLLMDS ASLRDLADQE
     MLAGCAAAVG SSELLDLLVL LSYADMLSTG PKARQKWRDT PVLALYNSIR HLLEKGEPSA
     RAITERIERL RNQVRNEVLD LVDEAQLDSY FSQLVPRYLL SMQPKAVARH LRMWRHLQSS
     DTPFVWEVES SGDTAEITIV SWEKPGLLSR CAGLLTLHSM NILGAQVFTM HNGLILLIFQ
     CRLPGGAGGG MDWNAVRLDV ERLLLGKMAL DYRIAEHARR RPASQVPMRT APSQVLVDNQ
     SSAMYTILEV YTVDRVGLLY TIGRTLFELQ IRISVAKITT KIDQVADVFY VRTHQGEKVS
     DPEQIDELKR ALLFWLDGPA EMPA
//

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