GLND_MYCTU
ID GLND_MYCTU Reviewed; 808 AA.
AC P9WN29; L0TB10; Q10961;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 48.
DE RecName: Full=Bifunctional uridylyltransferase/uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase/UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional [protein-PII] modification enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE AltName: Full=Bifunctional nitrogen sensor protein {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII] uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=PII uridylyltransferase {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UTase {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=2.7.7.59 {ECO:0000255|HAMAP-Rule:MF_00277};
DE Includes:
DE RecName: Full=[Protein-PII]-UMP uridylyl-removing enzyme {ECO:0000255|HAMAP-Rule:MF_00277};
DE Short=UR {ECO:0000255|HAMAP-Rule:MF_00277};
DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_00277};
GN Name=glnD {ECO:0000255|HAMAP-Rule:MF_00277}; OrderedLocusNames=Rv2918c;
GN ORFNames=MTCY338.07c;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=17303474; DOI=10.1016/j.tube.2006.12.003;
RA Read R., Pashley C.A., Smith D., Parish T.;
RT "The role of GlnD in ammonia assimilation in Mycobacterium tuberculosis.";
RL Tuberculosis 87:384-390(2007).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
CC -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC regulatory protein (GlnB), in response to the nitrogen status of the
CC cell that GlnD senses through the glutamine level. Under low glutamine
CC levels, catalyzes the conversion of the PII protein and UTP to PII-UMP
CC and PPi, while under higher glutamine levels, GlnD hydrolyzes PII-UMP
CC to PII and UMP (deuridylylation). Thus, controls uridylylation state
CC and activity of the PII protein, and plays an important role in the
CC regulation of nitrogen assimilation and metabolism (Probable).
CC {ECO:0000305|PubMed:17303474}.
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:0000255|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:0000255|HAMAP-Rule:MF_00277};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00277};
CC -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is inhibited
CC by glutamine, while glutamine activates uridylyl-removing (UR)
CC activity. {ECO:0000255|HAMAP-Rule:MF_00277}.
CC -!- INDUCTION: Slightly up-regulated in a low ammonia medium.
CC {ECO:0000269|PubMed:17303474}.
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:0000255|HAMAP-Rule:MF_00277}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene have no growth defect in
CC media containing different nitrogen sources. Total glutamine synthetase
CC (GS) activity in culture filtrates is markedly reduced in the mutant,
CC although activity in cell-free extracts remains normal. Virulence is
CC unaffected in both in vitro and in vivo model systems of infection.
CC {ECO:0000269|PubMed:17303474}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
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DR EMBL; AL123456; CCP45720.1; -; Genomic_DNA.
DR PIR; F70747; F70747.
DR RefSeq; NP_217434.1; NC_000962.3.
DR RefSeq; WP_003899539.1; NZ_NVQJ01000006.1.
DR AlphaFoldDB; P9WN29; -.
DR SMR; P9WN29; -.
DR STRING; 83332.Rv2918c; -.
DR PaxDb; P9WN29; -.
DR GeneID; 888621; -.
DR KEGG; mtu:Rv2918c; -.
DR TubercuList; Rv2918c; -.
DR eggNOG; COG2844; Bacteria.
DR OMA; WIAKYVY; -.
DR PhylomeDB; P9WN29; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0005886; C:plasma membrane; HDA:MTBBASE.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IMP:CACAO.
DR GO; GO:0070566; F:adenylyltransferase activity; IMP:CACAO.
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; cd00077; HDc; 1.
DR Gene3D; 3.30.460.10; -; 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; PTHR47320; 2.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; SSF55021; 1.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nucleotidyltransferase;
KW Reference proteome; Repeat; Transferase.
FT CHAIN 1..808
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192745"
FT DOMAIN 430..544
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 610..686
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 730..805
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..315
FT /note="Uridylyltransferase"
FT REGION 316..609
FT /note="Uridylyl-removing"
SQ SEQUENCE 808 AA; 86438 MW; 9B1F14D01C29F0B0 CRC64;
MEAESPCAAS DLAVARRELL SGNHRELDPV GLRQTWLDLH ESWLIDKADE IGIADASGFA
IVGVGGLGRR ELLPYSDLDV LLLHDGKPAD ILRPVADRLW YPLWDANIRL DHSVRTVSEA
LTIANSDLMA ALGMLEARHI AGDQQLSFAL IDGVRRQWRN GIRSRMGELV EMTYARWRRC
GRIAQRAEPD LKLGRGGLRD VQLLDALALA QLIDRHGIGH TDLPAGSLDG AYRTLLDVRT
ELHRVSGRGR DHLLAQFADE ISAALGFGDR FDLARTLSSA GRTIGYHAEA GLRTAANALP
RRGISALVRR PKRRPLDEGV VEYAGEIVLA RDAEPEHDPG LVLRVAAASA DTGLPIGAAT
LSRLAASVPD LPTPWPQEAL DDLLVVLSAG PTTVATIEAL DRTGLWGRLL PEWEPIRDLP
PRDVAHKWTV DRHVVETAVH AAPLATRVAR PDLLALGALL HDIGKGRGTD HSVLGAELVI
PVCTRLGLSP PDVRTLSKLV RHHLLLPITA TRRDLNDPKT IEAVSEALGG DPQLLEVLHA
LSEADSKATG PGVWSDWKAS LVDDLVRRCR MVMAGESLPQ AEPTAPHYLS LAADHGVHVE
ISPRDGERID AVIVAPDERG LVSKAAAVLA LNSLRVHSAS VNVHQGVAIT EFVVSPLFGS
PPAAELVRQQ FVGALNGDVD VLGMLQKRDS DAASLVSARA GDVQAGVPVT RTAAPPRILW
LDTAAPAKLI LEVRAMDRAG LLALLAGALE GAGAGIVWAK VNTFGSTAAD VFCVTVPAEL
DARAAVEQHL LEVLGASVDV VVDEPVGD
