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Database: UniProt
Entry: A0A1M7FXL5_9RHOB
LinkDB: A0A1M7FXL5_9RHOB
Original site: A0A1M7FXL5_9RHOB 
ID   A0A1M7FXL5_9RHOB        Unreviewed;       905 AA.
AC   A0A1M7FXL5;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   08-MAY-2019, entry version 16.
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=SAMN05444389_103303 {ECO:0000313|EMBL:SHM08801.1};
OS   Paracoccus solventivorans.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Paracoccus.
OX   NCBI_TaxID=53463 {ECO:0000313|EMBL:SHM08801.1, ECO:0000313|Proteomes:UP000184444};
RN   [1] {ECO:0000313|EMBL:SHM08801.1, ECO:0000313|Proteomes:UP000184444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6637 {ECO:0000313|EMBL:SHM08801.1,
RC   ECO:0000313|Proteomes:UP000184444};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) 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}.
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DR   EMBL; FRCK01000003; SHM08801.1; -; Genomic_DNA.
DR   Proteomes; UP000184444; 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:UP000184444};
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:SHM08801.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184444};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:SHM08801.1}.
FT   DOMAIN      476    599       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      717    799       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      827    905       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    358       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
FT   COILED      624    651       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   905 AA;  102328 MW;  84A9AAA0B376A891 CRC64;
     MFDPDRAIAA LDAGLAGLSD PRDIRARSVA ILSTLRAEAM EDITAGLASH PRKGRETVRA
     IAELTDATIR AIHYVATTRL HPNLAPTEGE RIAVIATGGY GRGEMAPHSD IDLLFLLPWK
     PSGWIESVVE SMLYMLWDLR LKVGHATRSL DDCLRLAEQD FTIRTSLLEH RLVCGDAVLA
     QSLRDRLWPE LFARTIPEFI EAKLTERAER HRRQGGRRYV LEPNVKEGKG GLRDLQTLYW
     IAKYIHQVDR AIELVDLGHF TRAEHTTFWA AEDFLWAVRC HMHLVAGRAV EKLSFDMQLE
     VAERMGYRDA GGRRGVEIFM QTYFRHATKV GELTRVFLTG LEQRHLYRAS FLERLRRPRV
     AAGLRVETGR LAIADPKRYF ADPLNILRLF QEALRTGILI HPEAMRLVTQ NLRRIDDAMR
     NSPEAGRIFL GLLLDHGNPE RALRRMNELG VLGAYIPEFE RIVAMMQFNV YHHYTVDEHL
     IQCVAALSQI ERGELVENLP IVSGIMAEGR IDRTVIYLAT LLHDIGKGRP EDHSIIGARI
     ARRVCQRLGL EPARVELVEW LIRNHLLMSD VAQKRDISDP RTLGDFAKAV RSRQRLDLLT
     VLTVCDIRGV GPNTWNNWKA ELLRNLHRLT AEALENGLEE VNREQQADEA RRDLTLLLTA
     QGWDTAEIDA ETARHDDGYW QGLPGDTHQV FARLLRGIGA GEIRMDLDPD LRRDATRAAF
     VVADQPGLFS RLAGALALAG ANVVDARTYT TRDGYATAVF WVQDAEGRPY SAERMPQLRR
     MIDRTLAGRA VAQAALADRD RVKKRDRGFR FPTHVTFDNE GSDIHTIVEV DTRDRPGLLY
     DLTRTLAEEQ VQIVSAVIAT FGAQVVDAFY VKEADGAKLL SPARQQALER RLREAIREGA
     ERARA
//
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