ID   C1F3D2_ACIC5            Unreviewed;       896 AA.
AC   C1F3D2;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   04-NOV-2026, entry version 97.
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   ECO:0000313|EMBL:ACO31556.1};
GN   OrderedLocusNames=ACP_0921 {ECO:0000313|EMBL:ACO31556.1};
OS   Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / BCRC 80197 / JCM
OS   7670 / NBRC 15755 / NCIMB 13165 / 161).
OC   Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Terriglobales;
OC   Acidobacteriaceae; Acidobacterium.
OX   NCBI_TaxID=240015 {ECO:0000313|EMBL:ACO31556.1, ECO:0000313|Proteomes:UP000002207};
RN   [1] {ECO:0000313|EMBL:ACO31556.1, ECO:0000313|Proteomes:UP000002207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51196 / DSM 11244 / BCRC 80197 / JCM 7670 / NBRC 15755 /
RC   NCIMB 13165 / 161 {ECO:0000313|Proteomes:UP000002207};
RX   PubMed=19201974; DOI=10.1128/AEM.02294-08;
RA   Ward N.L., Challacombe J.F., Janssen P.H., Henrissat B., Coutinho P.M.,
RA   Wu M., Xie G., Haft D.H., Sait M., Badger J., Barabote R.D., Bradley B.,
RA   Brettin T.S., Brinkac L.M., Bruce D., Creasy T., Daugherty S.C.,
RA   Davidsen T.M., DeBoy R.T., Detter J.C., Dodson R.J., Durkin A.S.,
RA   Ganapathy A., Gwinn-Giglio M., Han C.S., Khouri H., Kiss H., Kothari S.P.,
RA   Madupu R., Nelson K.E., Nelson W.C., Paulsen I., Penn K., Ren Q.,
RA   Rosovitz M.J., Selengut J.D., Shrivastava S., Sullivan S.A., Tapia R.,
RA   Thompson L.S., Watkins K.L., Yang Q., Yu C., Zafar N., Zhou L., Kuske C.R.;
RT   "Three genomes from the phylum Acidobacteria provide insight into the
RT   lifestyles of these microorganisms in soils.";
RL   Appl. Environ. Microbiol. 75:2046-2056(2009).
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 + UMP + H(+); 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; Evidence={ECO:0000256|HAMAP-
CC         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; CP001472; ACO31556.1; -; Genomic_DNA.
DR   AlphaFoldDB; C1F3D2; -.
DR   FunCoup; C1F3D2; 224.
DR   STRING; 240015.ACP_0921; -.
DR   KEGG; aca:ACP_0921; -.
DR   eggNOG; COG2844; Bacteria.
DR   HOGENOM; CLU_012833_1_0_0; -.
DR   InParanoid; C1F3D2; -.
DR   OMA; AACFCIT; -.
DR   Proteomes; UP000002207; 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:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR   CDD; cd04899; ACT_ACR-UUR-like_2; 1.
DR   CDD; cd04900; ACT_UUR-like_1; 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; IPR010043; GlnD.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
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; 1.
DR   SUPFAM; SSF55021; ACT-like; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   SUPFAM; SSF81891; Poly A polymerase C-terminal region-like; 1.
DR   PROSITE; PS51671; ACT; 2.
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:UP000002207};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00277}.
FT   DOMAIN          709..790
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   DOMAIN          821..896
FT                   /note="ACT"
FT                   /evidence="ECO:0000259|PROSITE:PS51671"
FT   REGION          1..358
FT                   /note="Uridylyltransferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
SQ   SEQUENCE   896 AA;  101759 MW;  93A41B8F30F5EBCB CRC64;
     MSVVPAAAPQ ADAAASFITF TSGISFSSME IAPPLLAQCR QRVSQDADSL RQSFERTGDG
     SAVARRRATS VSLRLKELWQ LLFPAASPAP VALVATGGFG RSELFPYSDV DVLYLCENDK
     AAATYANELR IFSQAMWDIG LRASPMTRTL KECDRIEADN LEFTIALLDR RFLAGQEALY
     DQLANKLLPD LCLREWQPIV QNLAEIARAR HEKFGHTIFH LEPNVKESPG GLRDYHLAQW
     LTLLNKLHAD RAWPQNSASH FYATHSELES AYDFLSATRC FLHYRSKRDD NALDWYGQDE
     AAARSIGLET AGTSDPAYWM RTYYRQARTI FRRAQLLLDE IPPARRSFYK TLRRKRTPIA
     GTDFYVEHGR IGLAEGAMVT SAEDMLAVFG YMAQHGHRLN QYAEDSIAEA LPVLAVQLPE
     GPYLWNALRG VLMGPWAADA LRTMHALGLL ELLIPEFHGI DSLVIRDAYH RYTVDEHTFV
     VIDNVHKLRQ PHEDWERRLA TLLPEIERLD LFFLALLMHD TGKARRTGDH AVQSVEFCES
     LFSRLLFDNE ERETVRRLIR LHLEMSAAMR RDIFDEETVR RFAEKIGSPQ PLKMLTLMTY
     ADIGGVSPDA LTPWKAEQLW QLYISTSNVL DRSVDETRYH VEADPTVLER ILVRMPQHAE
     RLKAFLEGLP QRYLQTRLPE QVEKHVTMSF ALRQEPVQLS YRRVRQLHEI TLITQDRPLL
     FADMAGVLAA WGMNIVKADA FANAAGLIVD TFQFTDPYRT LELNPSEIER FVAEVREVIS
     HRTQLETLLK ARRHRLKRTA SKLKVETRIQ FDNVASSHST LLQLTTQDTP GLLRQIALAL
     ATEGCNIEVA LIDTEGEIAI DVFYLTENGA KLDEARQKSL RTALMDSLAE ETEAAS
//