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Database: UniProt
Entry: D1AB20_THECD
LinkDB: D1AB20_THECD
Original site: D1AB20_THECD 
ID   D1AB20_THECD            Unreviewed;       780 AA.
AC   D1AB20;
DT   19-JAN-2010, integrated into UniProtKB/TrEMBL.
DT   19-JAN-2010, sequence version 1.
DT   24-JAN-2024, entry version 90.
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=Tcur_3425 {ECO:0000313|EMBL:ACY98963.1};
OS   Thermomonospora curvata (strain ATCC 19995 / DSM 43183 / JCM 3096 / KCTC
OS   9072 / NBRC 15933 / NCIMB 10081 / Henssen B9).
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=471852 {ECO:0000313|EMBL:ACY98963.1, ECO:0000313|Proteomes:UP000001918};
RN   [1] {ECO:0000313|EMBL:ACY98963.1, ECO:0000313|Proteomes:UP000001918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19995 / DSM 43183 / JCM 3096 / KCTC 9072 / NBRC 15933 /
RC   NCIMB 10081 / Henssen B9 {ECO:0000313|Proteomes:UP000001918};
RX   PubMed=21475583; DOI=10.4056/sigs.1453580;
RA   Chertkov O., Sikorski J., Nolan M., Lapidus A., Lucas S., Del Rio T.G.,
RA   Tice H., Cheng J.F., Goodwin L., Pitluck S., Liolios K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Ovchinnikova G., Pati A., Chen A.,
RA   Palaniappan K., Djao O.D., Land M., Hauser L., Chang Y.J., Jeffries C.D.,
RA   Brettin T., Han C., Detter J.C., Rohde M., Goker M., Woyke T., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Klenk H.P., Kyrpides N.C.;
RT   "Complete genome sequence of Thermomonospora curvata type strain (B9).";
RL   Stand. Genomic Sci. 1:13-22(2011).
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 metabolism.
CC       {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; CP001738; ACY98963.1; -; Genomic_DNA.
DR   AlphaFoldDB; D1AB20; -.
DR   STRING; 471852.Tcur_3425; -.
DR   KEGG; tcu:Tcur_3425; -.
DR   eggNOG; COG2844; Bacteria.
DR   HOGENOM; CLU_012833_2_0_11; -.
DR   OMA; WIAKYVY; -.
DR   OrthoDB; 9758038at2; -.
DR   Proteomes; UP000001918; 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; cd04899; ACT_ACR-UUR-like_2; 1.
DR   CDD; cd00077; HDc; 1.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 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   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; 2.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 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|HAMAP-Rule:MF_00277,
KW   ECO:0000313|EMBL:ACY98963.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001918};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00277}.
FT   DOMAIN          421..522
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
FT   DOMAIN          601..679
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          710..780
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..307
FT                   /note="Uridylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
SQ   SEQUENCE   780 AA;  82998 MW;  51FDD51EEF405C55 CRC64;
     MKETTGRFKA ATAVEGAGAG GLEEARKALA AARARRGAEL DRWLAGLLEA TGAAREVALV
     AVGSHSRGEL TPGGDLDLVL VHRGRPDIAQ IADRIWYPVW DRGLRLDHSV RTVREARKVA
     GSDIKAAMGL LGARLLAGDQ DLADQLRAVV LTDWRAQARR RLAELAELTR RRWADRGELA
     FLLEGDLKEA KGGLRDVYTM QAAAATWAVP GPGERVRAAH DLLLDVRHAL HETTGRAGDR
     LHLQEQDAVA HLLGLPDGAA LLRVIVAAAR TVSYAADNLW RHVDRFCADR PRGIRVARPG
     GRVERRPVGD GAVEHEGEVV LARGADLTDP VLPLCVAAAA AQAGLPLAPA TAEQLAAKVP
     PLPVPWPAEA RDALVSLLGA GPAAIPVWEA LDQAGVIVRE LPEWEQVRNR PQRNPVHRFT
     VDRHLVETAA GAAAMTRDVA RPDLLLVGAL LHDIGKGRPG DHSRTGAALA RTMAARMGFC
     DTDADVLETV VLHHLLLPDT ATRRDLDDPV TIQTVAQKVS AVPGRGRQVL EILAALAVAD
     AQATGPAAWG AWKARLIEEL VRRVDACLAG GAPPRNGLDP TPEQLALARH DGAAVRIAGS
     RVTVAVPDRP GLLWRTAGVL ALHRLVVRTA RVFASAGAGT AVLDFTAVPE YGTPPDPAAL
     EADLRRMLAG RLDVAGLLER RAAAVRRRPG APVPPPRVTI VEDASDTATV VEVRAHDRPG
     LLWRIGQAIG ACGLQVDKAR VDTLGAEAVD VFYVVDAQGR PLREPAALSA LREKVLAALR
//
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