(data stored in ACNUC7421 zone)

SWISSPROT: C6AYD2_RHILS

ID   C6AYD2_RHILS            Unreviewed;       968 AA.
AC   C6AYD2;
DT   01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   01-SEP-2009, sequence version 1.
DT   30-AUG-2017, entry version 69.
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=Rleg_0045 {ECO:0000313|EMBL:ACS54356.1};
OS   Rhizobium leguminosarum bv. trifolii (strain WSM1325).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=395491 {ECO:0000313|EMBL:ACS54356.1, ECO:0000313|Proteomes:UP000002256};
RN   [1] {ECO:0000313|EMBL:ACS54356.1, ECO:0000313|Proteomes:UP000002256}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WSM1325 {ECO:0000313|EMBL:ACS54356.1,
RC   ECO:0000313|Proteomes:UP000002256};
RX   PubMed=21304718;
RA   Reeve W., O'Hara G., Chain P., Ardley J., Brau L., Nandesena K.,
RA   Tiwari R., Copeland A., Nolan M., Han C., Brettin T., Land M.,
RA   Ovchinikova G., Ivanova N., Mavromatis K., Markowitz V., Kyrpides N.,
RA   Melino V., Denton M., Yates R., Howieson J.;
RT   "Complete genome sequence of Rhizobium leguminosarum bv. trifolii
RT   strain WSM1325, an effective microsymbiont of annual Mediterranean
RT   clovers.";
RL   Stand. Genomic Sci. 2:347-356(2010).
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 fixation and metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CATALYTIC ACTIVITY: UTP + [protein-PII] = diphosphate + uridylyl-
CC       [protein-PII]. {ECO:0000256|HAMAP-Rule:MF_00277,
CC       ECO:0000256|SAAS:SAAS00300567}.
CC   -!- CATALYTIC ACTIVITY: Uridylyl-[protein-PII] + H(2)O = UMP +
CC       [protein-PII]. {ECO:0000256|HAMAP-Rule:MF_00277,
CC       ECO:0000256|SAAS:SAAS00300537}.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00277, ECO:0000256|SAAS:SAAS00609838};
CC   -!- ENZYME 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:SAAS00554649}.
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; CP001622; ACS54356.1; -; Genomic_DNA.
DR   RefSeq; WP_012755789.1; NC_012850.1.
DR   ProteinModelPortal; C6AYD2; -.
DR   EnsemblBacteria; ACS54356; ACS54356; Rleg_0045.
DR   KEGG; rlg:Rleg_0045; -.
DR   HOGENOM; HOG000261779; -.
DR   KO; K00990; -.
DR   OMA; ARICGYF; -.
DR   OrthoDB; POG091H04HO; -.
DR   Proteomes; UP000002256; Chromosome.
DR   GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008081; F:phosphoric diester hydrolase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-HAMAP.
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; IPR002934; Polymerase_NTP_transf_dom.
DR   InterPro; IPR010043; UTase/UR.
DR   PANTHER; PTHR13734:SF52; PTHR13734:SF52; 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   TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR   PROSITE; PS51671; ACT; 2.
PE   3: Inferred from homology;
DR   PRODOM; C6AYD2.
DR   SWISS-2DPAGE; C6AYD2.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002256};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440795};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00504093};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00677267};
KW   Nitrogen fixation {ECO:0000256|HAMAP-Rule:MF_00277};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00504094, ECO:0000313|EMBL:ACS54356.1};
KW   Repeat {ECO:0000256|SAAS:SAAS00448599};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00504096, ECO:0000313|EMBL:ACS54356.1}.
FT   DOMAIN      752    833       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      863    942       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    395       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
SQ   SEQUENCE   968 AA;  108722 MW;  EEAC4EA7F3BBF4E5 CRC64;
     MQTKQAAGRE PAVRHEQETA PAIAMRDLDF SNILDVELLQ KQCDAVAEAN RNRPDVLRAD
     LLAVLKKAST EGRQKAREAL MADGGGLNCA YRISWLQDQI TTVLYNFATA HIFPQQKDKF
     AVTAVGGYGR DTLAPGSDID LLFLFLPRPA EETHKAVEFM LYVLWDMGFK VGHATRTVEE
     CIALSKSDMT IRTAILEMRY ICGLQRLETE LESRFDKEIV TGTGPEFIAA KLAERDERHR
     KAGDTRYLVE PNVKEGKGGL RDLHTLFWIS KYYYHVRDQA ELIKLGVLSK HEYRLLEKAD
     DFLWAVRCHM HFLTGKAEER LSFDIQREIA EAFGYHTRPG LSAVERFMKH YFLVAKDVGD
     LTRILCAALE DQQAKSIPGL TGVISRFTHR NRKIAGSVEF VEDRGRIALA DPEVFKRDPV
     NIIRLFHVAD INGLEFHPDA LKRVTRSLAL IDTSLRENDE ANRLFMSILT SKRDPALILR
     RMNEAGVLGR FIPEFGKIVA MMQFNMYHHY TVDEHLIRTV DILSEIDKGR AEDLHPLANK
     LMPGIEDREA LYVAVLLHDI AKGRQEDHSI AGARVARKLC ARFGLSQKQT EIVVWLIEEH
     LTMSMVAQTR DLTDRKTITD FADRVQSLDR LKMLLILTIC DIRAVGPGVW NGWKGQLLRT
     LYYETELLLA GGFSEVSRKE RANAAAEALH SALADWSQKD RNTYTKLHYQ PYLLSVPLED
     QIRHAHFIRQ SDKAGQALAT TVRTDSFHAI TEITVLSPDH PRLLAVIAGA CAAAGANIVD
     AQIFTTSDGR ALDTIHVSRE FTDDADELRR AATIGRMIED VLSGRKRLPE VIATRARNRK
     KSKAFVIPPS VNITNSLSNK FTVIEVECLD RPGLLSEITA VLSDLSLDIQ SARITTFGEK
     VIDTFYVTDL VGQKISGDSK RANITARMKA VMAEEEDELR ERMPSGIIAP AATARTPPAA
     EKKAGSPI
//

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