(data stored in ACNUC7421 zone)

SWISSPROT: A0LFS1_SYNFM

ID   A0LFS1_SYNFM            Unreviewed;       864 AA.
AC   A0LFS1;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   08-MAY-2019, entry version 92.
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_0574 {ECO:0000313|EMBL:ABK16273.1};
OS   Syntrophobacter fumaroxidans (strain DSM 10017 / MPOB).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Syntrophobacterales;
OC   Syntrophobacteraceae; Syntrophobacter.
OX   NCBI_TaxID=335543 {ECO:0000313|EMBL:ABK16273.1, ECO:0000313|Proteomes:UP000001784};
RN   [1] {ECO:0000313|EMBL:ABK16273.1, 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         ECO:0000256|SAAS:SAAS01174802};
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         ECO:0000256|SAAS:SAAS01174764};
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, ECO:0000256|SAAS:SAAS01174767}.
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; ABK16273.1; -; Genomic_DNA.
DR   RefSeq; WP_011697446.1; NC_008554.1.
DR   STRING; 335543.Sfum_0574; -.
DR   EnsemblBacteria; ABK16273; ABK16273; Sfum_0574.
DR   KEGG; sfu:Sfum_0574; -.
DR   eggNOG; ENOG4105E1P; Bacteria.
DR   eggNOG; COG2844; LUCA.
DR   HOGENOM; HOG000261779; -.
DR   KO; K00990; -.
DR   OMA; HTLFWIA; -.
DR   OrthoDB; 162558at2; -.
DR   BioCyc; SFUM335543:G1G7I-589-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   CDD; cd00077; HDc; 1.
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   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; A0LFS1.
DR   SWISS-2DPAGE; A0LFS1.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001784};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS01174769};
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:ABK16273.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001784};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:ABK16273.1}.
FT   DOMAIN      439    562       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      679    769       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      791    864       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    322       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
SQ   SEQUENCE   864 AA;  99583 MW;  BC598C8633945F0B CRC64;
     MHLRPQLSRK LKDLRETFQQ MCREDVPGVL AARTYAHQFH ESLRKAFPET VVPEDGWGLL
     AVGGFGRGEL GFASDIDLLL LYRNRLVKSH EALFKELVYC LWDSGFEVGH ATASLSSMKR
     MAQDDFTVLT NILEARLIAG DPKLFSEWRE SFFNGFGRQS RKKFLQNLVG YREERQQQYG
     GSSYLQEPHV KEGVGAMRDV HILRWAGHVF LRDPSFAAMV RKELMTNQEK LWLEQAYDFL
     WRVRLQLHRL TGRRQDQLLF MEQEQIAERF GCMAGQQGSA VEVFMRLYYR HTSRIRRTAS
     FFLERVGETQ KSFPGLRPRR RILPGPFLLE GKHLNFMEPE WIKKDPRLLM RFFWQAALSD
     AHFHHQAGQI IRENLAVFTD EARRDPEVVK QFFDILLDSE HAFSVVNVML ETGFLEVFIP
     EFAAVRYRVQ NDVYHLYTVD EHLLRTVWQM HQMERGDDEV AGELNPSDIF VHVKSRRVLY
     LAALVHDIGK GDGRNHAVRG GAMAGPIAER LGLDTHETGL LRFLVEHHLI LAETALKRDL
     MDEKPIAQCA IQIKDRERLQ MLYLLTIADS RATGPGAWST WKASLVRELF VKVDRVLARG
     DLQGQDLEQR SGEVQENVLD LVSDPAERER VRHWLERVSY RYLLSQAPTA IVEHHRMERA
     LGNKPLVLAS SPAEGEMWQL TVVTADRPGL FALITGVLWA RGLNILSADI FTWESGVALD
     VLIVERLPDP LHPRELWERV EADLGRALEH RGYLDELLSN KRKPSILQQK NLPRKDDIVL
     VDEEASDFYT IIEVYTWDRP GVLHCITDTL YHLDVSIQLA KISTPGAQVA DVFYVTDLSG
     NKLMDYEMHE KIRVSLLDSL TRVG
//

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