ID A0KHG1_AERHH Unreviewed; 884 AA.
AC A0KHG1;
DT 12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT 12-DEC-2006, sequence version 1.
DT 24-JAN-2024, entry version 120.
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:ABK36708.1};
GN OrderedLocusNames=AHA_1171 {ECO:0000313|EMBL:ABK36708.1};
OS Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK36708.1, ECO:0000313|Proteomes:UP000000756};
RN [1] {ECO:0000313|EMBL:ABK36708.1, ECO:0000313|Proteomes:UP000000756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC KCTC 2358 / NCIMB 9240 / NCTC 8049
RC {ECO:0000313|Proteomes:UP000000756};
RX PubMed=16980456; DOI=10.1128/JB.00621-06;
RA Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL J. Bacteriol. 188:8272-8282(2006).
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 + 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:0000256|HAMAP-Rule:MF_00277};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=guanosine 3',5'-bis(diphosphate) + H2O = diphosphate + GDP +
CC H(+); Xref=Rhea:RHEA:14253, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58189, ChEBI:CHEBI:77828; EC=3.1.7.2;
CC Evidence={ECO:0000256|ARBA:ARBA00024273};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-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; CP000462; ABK36708.1; -; Genomic_DNA.
DR RefSeq; WP_011705092.1; NC_008570.1.
DR RefSeq; YP_855712.1; NC_008570.1.
DR AlphaFoldDB; A0KHG1; -.
DR STRING; 380703.AHA_1171; -.
DR EnsemblBacteria; ABK36708; ABK36708; AHA_1171.
DR KEGG; aha:AHA_1171; -.
DR PATRIC; fig|380703.7.peg.1178; -.
DR eggNOG; COG2844; Bacteria.
DR HOGENOM; CLU_012833_0_0_6; -.
DR OMA; WIAKYVY; -.
DR OrthoDB; 9758038at2; -.
DR Proteomes; UP000000756; Chromosome.
DR GO; GO:0008773; F:[protein-PII] uridylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008893; F:guanosine-3',5'-bis(diphosphate) 3'-diphosphatase activity; IEA:RHEA.
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; cd04899; ACT_ACR-UUR-like_2; 1.
DR CDD; cd04900; ACT_UUR-like_1; 1.
DR CDD; cd00077; HDc; 1.
DR CDD; cd05401; NT_GlnE_GlnD_like; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.10.3090.10; cca-adding enzyme, domain 2; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases 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; 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 NCBIfam; TIGR01693; UTase_glnD; 1.
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 Pfam; PF01909; NTP_transf_2; 1.
DR PIRSF; PIRSF006288; PII_uridyltransf; 1.
DR SMART; SM00471; HDc; 1.
DR SUPFAM; SSF55021; ACT-like; 2.
DR SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
DR PROSITE; PS51671; ACT; 2.
DR PROSITE; PS51831; HD; 1.
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|HAMAP-Rule:MF_00277,
KW ECO:0000313|EMBL:ABK36708.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00277}.
FT DOMAIN 452..574
FT /note="HD"
FT /evidence="ECO:0000259|PROSITE:PS51831"
FT DOMAIN 694..775
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT DOMAIN 802..877
FT /note="ACT"
FT /evidence="ECO:0000259|PROSITE:PS51671"
FT REGION 1..334
FT /note="Uridylyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00277"
SQ SEQUENCE 884 AA; 101382 MW; C1043C4E9C65A6DD CRC64;
MDASLLSPHL LPDAQLTREN CKEYLSRFLG WLHARFDAGD NIIELVATRS EYMDELLTRL
WQKFGFDKTE LTLIAVGGYG RGELHPHSDI DLLILYEGDE LDEVLGLRIG EFITLLWDLK
LEVGQAVRNV AECLEQGRGD ITVATNLIEA RYITGREAGF QQLKEATGPQ HFWPSEQFFK
AKREEQAQRH QQFLGTAYKL EPDLKSNPGG LRDIQTLAWV ARRHFGATTL FEMTSHGFLN
RAEYRELLDC QNFLWKVRFA LHMAINKGDN RLLFDRQRTV AQMLGFEGEG NAPVEQMMKR
FYQTVRRVSE LNEMLLQLFD EAILGNTAMD VRRLSDEFQL RGRLIDAVDS ELFGREPAAI
LRLFYQIAQH PEIAGIHSAT LRQLREARRK LNCWLQDLPD CRRLFMALLR HPNGIGQPLT
LMHKYGILAA YLPQWNLIVG QMQFDMFHAY TVDEHTHRLL KNIHQFPNPA SRQTHPLCHE
VFTRLRKPEL LSIAALFHDI AKGRRGDHSE LGAVDALEFC QLHGLDRYES RLVAWLVRHH
LLMSVTAQRR DIYDPEVVTD FAQKVRDEQH LDLLYCLTVA DICATNDTLW NDWKGTLLRE
LYFATQKALR QGLENPPDMR LKIRENQRQA KQILAQRDVP EAAINQLWSD FKADYFLRHT
PEQIAWHCRK IIEHGDNPAP LVIIGKHPTR GGSEVFIYCR DTPNLFATVA SALDQKNLNI
HDAQIMNSRS DYVLDTFVVL EPNGEPISPN RTATIKKALE KALQEPGKLV LRSKPLSRRH
RQFSVPTRVV FLPHKGETRH TLLELTALDT PGLLARIGAV FQQCGLSLHA AKITTIGERV
EDFFSLTTLA GEPLTQAEQH ALEERLVNQL NPQESADDEG RPGQ
//