ID   GLND_CORGL              Reviewed;         692 AA.
AC   Q9X706;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   27-MAR-2024, entry version 134.
DE   RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme;
DE            Short=UTase/UR;
DE   AltName: Full=Bifunctional [protein-PII] modification enzyme;
DE   AltName: Full=Bifunctional nitrogen sensor protein;
DE   Includes:
DE     RecName: Full=[Protein-PII] uridylyltransferase;
DE              Short=PII uridylyltransferase;
DE              Short=UTase;
DE              EC=2.7.7.59;
DE   Includes:
DE     RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme;
DE              Short=UR;
DE              EC=3.1.4.-;
GN   Name=glnD; OrderedLocusNames=Cgl2059, cg2258;
OS   Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 /
OS   JCM 1318 / LMG 3730 / NCIMB 10025).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=196627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=10227160; DOI=10.1111/j.1574-6968.1999.tb13518.x;
RA   Jakoby M.J., Kraemer R., Burkovski A.;
RT   "Nitrogen regulation in Corynebacterium glutamicum: isolation of genes
RT   involved and biochemical characterization of corresponding proteins.";
RL   FEMS Microbiol. Lett. 173:303-310(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=12743753; DOI=10.1007/s00253-003-1328-1;
RA   Ikeda M., Nakagawa S.;
RT   "The Corynebacterium glutamicum genome: features and impacts on
RT   biotechnological processes.";
RL   Appl. Microbiol. Biotechnol. 62:99-109(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 /
RC   NCIMB 10025;
RX   PubMed=12948626; DOI=10.1016/s0168-1656(03)00154-8;
RA   Kalinowski J., Bathe B., Bartels D., Bischoff N., Bott M., Burkovski A.,
RA   Dusch N., Eggeling L., Eikmanns B.J., Gaigalat L., Goesmann A.,
RA   Hartmann M., Huthmacher K., Kraemer R., Linke B., McHardy A.C., Meyer F.,
RA   Moeckel B., Pfefferle W., Puehler A., Rey D.A., Rueckert C., Rupp O.,
RA   Sahm H., Wendisch V.F., Wiegraebe I., Tauch A.;
RT   "The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its
RT   impact on the production of L-aspartate-derived amino acids and vitamins.";
RL   J. Biotechnol. 104:5-25(2003).
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 (By similarity). {ECO:0000250}.
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   -!- 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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC       by glutamine, while glutamine activates uridylyl-removing (UR)
CC       activity. {ECO:0000250}.
CC   -!- DOMAIN: Has two distinct domains: an N-terminal nucleotidyltransferase
CC       (NT) domain responsible for UTase activity, and a HD domain that
CC       encodes UR activity (By similarity). Lacks the two C-terminal ACT
CC       domains found in GlnD orthologs, that seem to have a role in glutamine
CC       sensing. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000305}.
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DR   EMBL; AJ010319; CAB39374.1; -; Genomic_DNA.
DR   EMBL; BA000036; BAB99452.1; -; Genomic_DNA.
DR   EMBL; BX927154; CAF20397.1; -; Genomic_DNA.
DR   RefSeq; NP_601262.1; NC_003450.3.
DR   RefSeq; WP_011014852.1; NC_006958.1.
DR   AlphaFoldDB; Q9X706; -.
DR   SMR; Q9X706; -.
DR   STRING; 196627.cg2258; -.
DR   KEGG; cgb:cg2258; -.
DR   KEGG; cgl:Cgl2059; -.
DR   PATRIC; fig|196627.13.peg.1997; -.
DR   eggNOG; COG2844; Bacteria.
DR   HOGENOM; CLU_012833_2_0_11; -.
DR   OrthoDB; 9758038at2; -.
DR   BioCyc; CORYNE:G18NG-11651-MONOMER; -.
DR   BRENDA; 2.7.7.59; 960.
DR   Proteomes; UP000000582; Chromosome.
DR   Proteomes; UP000001009; Chromosome.
DR   GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
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   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR002934; Polymerase_NTP_transf_dom.
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; PF01966; HD; 1.
DR   Pfam; PF01909; NTP_transf_2; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Magnesium; Multifunctional enzyme; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..692
FT                   /note="Bifunctional uridylyltransferase/uridylyl-removing
FT                   enzyme"
FT                   /id="PRO_0000192730"
FT   DOMAIN          383..484
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..270
FT                   /note="Uridylyltransferase"
FT   REGION          271..692
FT                   /note="Uridylyl-removing"
SQ   SEQUENCE   692 AA;  75970 MW;  A7AC19614C133676 CRC64;
     MNNPAQLRQD TEKEVLALLG SLVLPAGTAL AATGSLARSE LTPYSDLDLI LIHPPGATPD
     GVEDLWYPIW DAKKRLDYSV RTPDECVAMI SADSTAALAM LDLRFVAGDE DLCAKTRRRI
     VEKWRQELNK NFDAVVDTAI ARWRRSGPVV AMTRPDLKHG RGGLRDFELI KALALGHLCN
     LPQLDAQHQL LLDARTLLHV HARRSRDVLD PEFAVDVAMD LGFVDRYHLG REIADAARAI
     DDGLTTALAT ARGILPRRTG FAFRNASRRP LDLDVVDANG TIELSKKPDL NDPALPLRVA
     AAAATTGLPV AESTWVRLNE CPPLPEPWPA NAAGDFFRIL SSPKNSRRVV KNMDRHGLWS
     RFVPEWDRIK GLMPREPSHI STIDEHSLNT VAGCALETVT VARPDLLVLG ALYHDIGKGF
     PRPHEQVGAE MVARAASRMG LNLRDRASVQ TLVAEHTAVA KIAARLDPSS EGAVDKLLDA
     VRYDLVTLNL LEVLTEADAK ATGPGVWTAR LEHALRIVCK RARDRLTDIR PVAPMIAPRS
     EIGLVERDGV FTVQWHGEDL HRILGVIYAK GWTITAARML ANGQWSAEFD VRANGPQDFD
     PQHFLQAYQS GVFSEVPIPA LGITATFWHG NTLEVRTELR TGAIFALLRT LPDALWINAV
     TRGATLIIQA ALKPGFDRAT VERSVVRSLA GS
//