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Database: UniProt
Entry: A0A0Q4ZA30_9RHIZ
LinkDB: A0A0Q4ZA30_9RHIZ
Original site: A0A0Q4ZA30_9RHIZ 
ID   A0A0Q4ZA30_9RHIZ        Unreviewed;       929 AA.
AC   A0A0Q4ZA30;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   08-MAY-2019, entry version 27.
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   ORFNames=ASF49_05245 {ECO:0000313|EMBL:KQP38612.1};
OS   Methylobacterium sp. Leaf104.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=1736254 {ECO:0000313|EMBL:KQP38612.1, ECO:0000313|Proteomes:UP000052064};
RN   [1] {ECO:0000313|EMBL:KQP38612.1, ECO:0000313|Proteomes:UP000052064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf104 {ECO:0000313|EMBL:KQP38612.1,
RC   ECO:0000313|Proteomes:UP000052064};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KQP38612.1, ECO:0000313|Proteomes:UP000052064}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Leaf104 {ECO:0000313|EMBL:KQP38612.1,
RC   ECO:0000313|Proteomes:UP000052064};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) 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 metabolism. {ECO:0000256|HAMAP-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       ECO:0000256|SAAS:SAAS01174765}.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KQP38612.1}.
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DR   EMBL; LMMZ01000012; KQP38612.1; -; Genomic_DNA.
DR   RefSeq; WP_056472705.1; NZ_LMMZ01000012.1.
DR   EnsemblBacteria; KQP38612; KQP38612; ASF49_05245.
DR   Proteomes; UP000052064; Unassembled WGS sequence.
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; 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   TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000052064};
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:KQP38612.1};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:KQP38612.1}.
FT   DOMAIN      485    607       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      725    802       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      836    919       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    367       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
FT   COILED        5     25       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   929 AA;  104159 MW;  46521C0305C6824F CRC64;
     MFDAVAALND ILQNLDRDAR EATRLRAVLV PELRRVIELG RADAEERLLE ERDGIACARR
     LSRLTDAVIR TIHDAVVWRL YPNDNPSTGE QLAVVATGGY GRGTMAPGSD IDLLFLLPYK
     QTAWSESVVE AMLYVLWDLK LKVGHATRSV EECLREGRAD MTIRTSLLEA RYLFGTRALF
     EELVTRFDTE LVMWTAPEFV EAKLRERDAR VSKAGASRYL VEPNVKDGKG GLRDLNTLFW
     IAKYTYRVRD QSELVAAGLF TPEEYRVFER CDELLWRVRC HMHFVTGRAE ERLSFGLQPR
     IAERFGYEPR GGLSGVERFM KAYFLIAKEV GDLTAIVCAA LEARHAKRTP VLDRWIGRFR
     DRFRATAIEA EDFVDDHGRI NLRDADAFSR DPVNLIRLFW LADRHNLPIH PDATRAANRA
     LRLIGHSLRA DEEANRLFLD ILTSKNSPET ILRLMNEAGV LGRFIPDFGR IVAMMQFNMY
     HHFTVDEHLL RAIGVLSAIE SGRAEEEHPL ASRLIDTISH RRALYVTVLL HDIAKGRPED
     HSIAGAAIAE KLGPRFGLTA AETEMVAWLV EHHLLMSMTA QSRDLSDPKT IEKFAGVVQT
     LERLKLLTIL TVADIKAVGP GVWTAWKGTL IRTLYDETEV VLSGGHSEIA RTDRVRLIQM
     ALREQLSDWQ SEAFDAYAAR HNQAYWLKVD TTRQFKHAGF VKALTAEGRT VATVAETDPV
     RGVTELTIYS PDHPRLLAIV TGACAASGGN IVDAQIFTTT DGFALDSIFV SRAFERDEDE
     LRRASRITTA IEKALRGEIR IADLVADKHP PSERARTFLV PPDMAIDNAL SSRETVIEIT
     GLDRPGLLYE LTTALSRLSL NITSAHVATF GERAVDVFYV TDLTGTRVTQ PDRQVAIRTA
     VMEVFAGDVA ALRAEGLDAL IDSPPPREA
//
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