GLND_CORGL
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 03-AUG-2022, entry version 126.
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; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196627;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB
RC 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 / NCIMB
RC 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 / NCIMB
RC 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 OMA; CAAQSIR; -.
DR BRENDA; 2.7.7.59; 960.
DR Proteomes; UP000000582; 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 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; PTHR47320; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF81301; SSF81301; 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
