ID D0LAL9_GORB4 Unreviewed; 860 AA.
AC D0LAL9;
DT 15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT 15-DEC-2009, sequence version 1.
DT 27-MAR-2024, 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=Gbro_2080 {ECO:0000313|EMBL:ACY21332.1};
OS Gordonia bronchialis (strain ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198
OS / KCTC 3076 / NBRC 16047 / NCTC 10667) (Rhodococcus bronchialis).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=526226 {ECO:0000313|EMBL:ACY21332.1, ECO:0000313|Proteomes:UP000001219};
RN [1] {ECO:0000313|Proteomes:UP000001219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kyrpides N., Mavromatis K., Ivanova N.,
RA Ovchinnikova G., Saunders E., Brettin T., Detter J.C., Han C., Larimer F.,
RA Land M., Hauser L., Markowitz V., Cheng J.-F., Hugenholtz P., Woyke T.,
RA Wu D., Jando M., Schneider S., Goeker M., Klenk H.-P., Eisen J.A.;
RT "The complete chromosome of Gordonia bronchialis DSM 43247.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACY21332.1, ECO:0000313|Proteomes:UP000001219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25592 / DSM 43247 / BCRC 13721 / JCM 3198 / KCTC 3076 /
RC NBRC 16047 / NCTC 10667 {ECO:0000313|Proteomes:UP000001219};
RX PubMed=21304674;
RA Ivanova N., Sikorski J., Jando M., Lapidus A., Nolan M., Lucas S.,
RA Del Rio T.G., Tice H., Copeland A., Cheng J.F., Chen F., Bruce D.,
RA Goodwin L., Pitluck S., Mavromatis K., Ovchinnikova G., Pati A., Chen A.,
RA Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA Saunders E., Han C., Detter J.C., Brettin T., Rohde M., Goker M.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P.,
RA Kyrpides N.C.;
RT "Complete genome sequence of Gordonia bronchialis type strain (3410).";
RL Stand. Genomic Sci. 2:19-28(2010).
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory proteins (GlnB and homologs), in response to the nitrogen
CC status of the cell that GlnD senses through the glutamine level. Under
CC low glutamine levels, catalyzes the conversion of the PII proteins and
CC UTP to PII-UMP and PPi, while under higher glutamine levels, GlnD
CC hydrolyzes PII-UMP to PII and UMP (deuridylylation). Thus, controls
CC uridylylation state and activity of the PII proteins, and plays an
CC important role in the regulation of nitrogen assimilation and
CC metabolism. {ECO:0000256|HAMAP-Rule:MF_00277}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-L-
CC tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019, ChEBI:CHEBI:46398,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:90602; EC=2.7.7.59;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-L-
CC tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-COMP:12147,
CC Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:46858, ChEBI:CHEBI:57865, ChEBI:CHEBI:90602;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00277};
CC -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC by glutamine, while glutamine activates uridylyl-removing (UR)
CC activity. {ECO:0000256|HAMAP-Rule:MF_00277}.
CC -!- DOMAIN: Has four distinct domains: an N-terminal nucleotidyltransferase
CC (NT) domain responsible for UTase activity, a central HD domain that
CC encodes UR activity, and two C-terminal ACT domains that seem to have a
CC role in glutamine sensing. {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 of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
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DR EMBL; CP001802; ACY21332.1; -; Genomic_DNA.
DR RefSeq; WP_012833889.1; NC_013441.1.
DR AlphaFoldDB; D0LAL9; -.
DR STRING; 526226.Gbro_2080; -.
DR KEGG; gbr:Gbro_2080; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_2_0_11; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000001219; 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; cd04873; ACT_UUR-ACR-like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR HAMAP; MF_00277; PII_uridylyl_transf; 1.
DR InterPro; IPR045865; ACT-like_dom_sf.
DR InterPro; IPR002912; ACT_dom.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR043519; NT_sf.
DR InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR InterPro; IPR010043; UTase/UR.
DR NCBIfam; TIGR01693; UTase_glnD; 1.
DR PANTHER; PTHR47320; BIFUNCTIONAL URIDYLYLTRANSFERASE/URIDYLYL-REMOVING ENZYME; 1.
DR PANTHER; PTHR47320:SF1; BIFUNCTIONAL URIDYLYLTRANSFERASE_URIDYLYL-REMOVING ENZYME; 1.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 2.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; ACT-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00277};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00277};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268, ECO:0000256|HAMAP-
KW Rule:MF_00277};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW Rule:MF_00277}; Reference proteome {ECO:0000313|Proteomes:UP000001219};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00277}.
FT DOMAIN 453..554
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 633..709
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 765..837
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..338
FT /note="Uridylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
FT REGION 1..29
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 829..860
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 91647 MW; CFD76A9C9EF76B4B CRC64;
MPFLNTTHGP ASDDESGAGP RSSTPDNPVA ATDLAKTRRQ LTESAKAGRL DSAGLRQVLV
DLHEFWLTSK GAELGIKPYS GFAIVAVGGL GRGELLPHSD LDLILLHDDL PAARVSEVAD
GLWYPLWDAN IPLDHSVRTV PQALQVAAED ITAALGLLEA RHIAGDEDLS ALLIGGVRQQ
WRNDIRDRFA GVVEHAQDRW RRAGDIAHRA EPDLKNGRGG LRDVQLLGAL AIAQLTDGMA
SLRPDSPGAG PQLAYMRLLD IRTELHRIAG RAREQVQAQD ADEIGAALRI GDRFDLARVI
SDSARTISYS IDVGLRTAGN ALPRRGLAKL RRSPIRRPLD EGVVEHNGEI VLARSAIPSK
DPGLILRVAS ASARTGLPIS ASTLSRLGDY APELREPWPA EALSDLLVLL SSGHHMVDAI
EALDRTGLWG RLLPEWGAVR DLPPRDAIHT WTVDRHLVET AAHASSMTTR VSRPDLLVLG
ALIHDLGKGR GADHSIVGAE LAIQVGNRVG LWPQDVEILS VMVRHHLLLP AVATRRDLDD
PATAESVVQT LGYNRVLLEL LAALAEADSK ATGPGVWGEW KASLILDLVR RSMRLIDAGE
LPVPEPLTAE QIALAESAEY AVRMTPAEGH MIDVTMVAPD QPGLLSKMAG VLALGGLRSN
SVNARSHGAK AVNTFVVIPV FGSPPEAGLV RQQMIAAVEG KIDVLARLDA RERDSPIPTI
ATVATTPGAA EPVVEAGHPR NAVPALFAVA PPRALWIDGP SGEALLELRT DDRIGLLSRV
SAVLERHGAD IRWARVATLG STVVDTFGLR LSDETESARA ALADAVLAVC PPPQPRSDDE
DGDSGPTSYG GTGRSGVPIS
//
