GLND_KLEOX
ID GLND_KLEOX Reviewed; 887 AA.
AC P41393;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 25-MAY-2022, entry version 102.
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};
OS Klebsiella oxytoca.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=571;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=M5a1;
RX PubMed=7753028; DOI=10.1007/bf00705649;
RA Edwards R.A., Merrick M.J.;
RT "The role of uridylyltransferase in the control of Klebsiella pneumoniae
RT nif gene regulation.";
RL Mol. Gen. Genet. 247:189-198(1995).
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 fixation and metabolism
CC (Probable). {ECO:0000305|PubMed:7753028}.
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 -!- 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 are unable to uridylylate
CC PII and are altered in adenylation/deadenylation of glutamine
CC synthetase. {ECO:0000269|PubMed:7753028}.
CC -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000255|HAMAP-
CC Rule:MF_00277}.
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DR EMBL; X78685; CAA55353.1; -; Genomic_DNA.
DR PIR; S54756; S43196.
DR AlphaFoldDB; P41393; -.
DR SMR; P41393; -.
DR STRING; 571.MC52_13170; -.
DR eggNOG; COG2844; Bacteria.
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:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:UniProtKB-UniRule.
DR CDD; cd00077; HDc; 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; IPR002934; Polymerase_NTP_transf_dom.
DR InterPro; IPR010043; UTase/UR.
DR PANTHER; PTHR47320; PTHR47320; 1.
DR Pfam; PF01842; ACT; 2.
DR Pfam; PF08335; GlnD_UR_UTase; 1.
DR Pfam; PF01966; HD; 1.
DR Pfam; PF01909; NTP_transf_2; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; SSF55021; 2.
DR SUPFAM; SSF81301; SSF81301; 1.
DR TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Multifunctional enzyme; Nitrogen fixation;
KW Nucleotidyltransferase; Repeat; Transferase.
FT CHAIN 1..887
FT /note="Bifunctional uridylyltransferase/uridylyl-removing
FT enzyme"
FT /id="PRO_0000192739"
FT DOMAIN 465..587
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT DOMAIN 706..786
FT /note="ACT 1"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT DOMAIN 813..887
FT /note="ACT 2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00277"
FT REGION 1..346
FT /note="Uridylyltransferase"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 347..705
FT /note="Uridylyl-removing"
SQ SEQUENCE 887 AA; 102344 MW; 73782E94DA434CAC CRC64;
MSNSLSNTVP PDLSAQPENP GEWPKSDFNC ATIKALIDAF QRWLGEAFDS GIAAERLIEA
RTEFIDQLLQ RLWVEYGFGS INDIALVAVG GYGRGELHPL SDIDLLILSR KKLPDEQAQK
VGERLALLWD IKLEVGHSVR TLEECLLEGL SDLSVATNLI ESRLLIGDVA LFLELQKHIF
SDGFWPSEKF FAAKVEEQND RHQRYHGTSY NLEPDVKSSP GGLRDIHTLQ WIARRHFGAT
SLDEMVGFGF LTEAERNELN ECLHQLWRIR FALHLELNRY DNRLLFDRQF SVARRLRYEG
ESNQPIEHMM KDFFRVTRRV SELNQMLIQL FEEAILALTE DEKPRPIDDD FQLRGTLIDL
RDDTLFIREP QAILRMFYTM VRNSSITGIY STTVRHLRHA RRHLTQPLCY IPEARTLFLS
MLRHQGGLSR GLLPMHRHSV LWAYMPQWSH IVGQMQFDLF HAYTVDEHTI RVLLKLESFA
KEETRSRHPL WLELWPRLTH PELILIAALF HDIAKGAGGD HSILGAQDVL KFAELHGLNC
AQTQLVAWLV RHQLLMSVTA QRRDIQDPEV IKQFAEEVQT ENRLHYLVCL TVADICATNE
NLWNSWKQSL LRELYFATEK QLRRGMQNTP DMRERVRHHQ LQALALLRME NINEQALHQI
WNRCRANYFV RHTPNQLAWH ARNLLKHDLS KPMILLSSHA TRGGTEIFIW SPDRPYLFAA
VSAELDRRNL SVHDAQIFTT RDGMAMDTFI VLEPDGSPLS ADRTQMIRVG LEQTLSQRSW
QPPAPRRQAA KLRHFSVPTE VNFLPTHTDR KSFLELIALD QPGLLARVGQ VFADLGISLH
GARITTIGER VEDLFIIATA DRRALNNELQ QEVQQRLTEA LNPNDKG
