(data stored in ACNUC7421 zone)

SWISSPROT: C3MEZ9_SINFN

ID   C3MEZ9_SINFN            Unreviewed;       965 AA.
AC   C3MEZ9;
DT   16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT   16-JUN-2009, sequence version 1.
DT   08-MAY-2019, entry version 89.
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:ACP23836.1};
GN   OrderedLocusNames=NGR_c00320 {ECO:0000313|EMBL:ACP23836.1};
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394 {ECO:0000313|EMBL:ACP23836.1, ECO:0000313|Proteomes:UP000001054};
RN   [1] {ECO:0000313|EMBL:ACP23836.1, ECO:0000313|Proteomes:UP000001054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234 {ECO:0000313|Proteomes:UP000001054};
RX   PubMed=19376903; DOI=10.1128/AEM.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of
RT   secretion systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
CC   -!- FUNCTION: Modifies, by uridylylation and deuridylylation, the PII
CC       regulatory proteins (GlnB and homologs), in response to the
CC       nitrogen status of the cell that GlnD senses through the glutamine
CC       level. Under low glutamine levels, catalyzes the conversion of the
CC       PII proteins and UTP to PII-UMP and PPi, while under higher
CC       glutamine levels, GlnD hydrolyzes PII-UMP to PII and UMP
CC       (deuridylylation). Thus, controls uridylylation state and activity
CC       of the PII proteins, and plays an important role in the regulation
CC       of nitrogen fixation and metabolism. {ECO:0000256|HAMAP-
CC       Rule:MF_00277}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-L-tyrosine + UTP = [protein-PII]-uridylyl-
CC         L-tyrosine + diphosphate; Xref=Rhea:RHEA:13673, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:46398, ChEBI:CHEBI:46858, ChEBI:CHEBI:90602;
CC         EC=2.7.7.59; Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
CC         ECO:0000256|SAAS:SAAS01174802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein-PII]-uridylyl-L-tyrosine + H2O = [protein-PII]-
CC         L-tyrosine + H(+) + UMP; Xref=Rhea:RHEA:48600, Rhea:RHEA-
CC         COMP:12147, Rhea:RHEA-COMP:12148, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:57865,
CC         ChEBI:CHEBI:90602; Evidence={ECO:0000256|HAMAP-Rule:MF_00277,
CC         ECO:0000256|SAAS:SAAS01174764};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00277, ECO:0000256|SAAS:SAAS00609838};
CC   -!- ACTIVITY REGULATION: Uridylyltransferase (UTase) activity is
CC       inhibited by glutamine, while glutamine activates uridylyl-
CC       removing (UR) activity. {ECO:0000256|HAMAP-Rule:MF_00277,
CC       ECO:0000256|SAAS:SAAS01174765}.
CC   -!- DOMAIN: Has four distinct domains: an N-terminal
CC       nucleotidyltransferase (NT) domain responsible for UTase activity,
CC       a central HD domain that encodes UR activity, and two C-terminal
CC       ACT domains that seem to have a role in glutamine sensing.
CC       {ECO:0000256|HAMAP-Rule:MF_00277}.
CC   -!- SIMILARITY: Belongs to the GlnD family. {ECO:0000256|HAMAP-
CC       Rule:MF_00277, ECO:0000256|SAAS:SAAS01174767}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00277}.
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DR   EMBL; CP001389; ACP23836.1; -; Genomic_DNA.
DR   RefSeq; WP_012706621.1; NC_012587.1.
DR   RefSeq; YP_002824589.1; NC_012587.1.
DR   STRING; 394.NGR_c00320; -.
DR   EnsemblBacteria; ACP23836; ACP23836; NGR_c00320.
DR   GeneID; 7790611; -.
DR   KEGG; rhi:NGR_c00320; -.
DR   PATRIC; fig|394.7.peg.2822; -.
DR   eggNOG; ENOG4105E1P; Bacteria.
DR   eggNOG; COG2844; LUCA.
DR   HOGENOM; HOG000261779; -.
DR   KO; K00990; -.
DR   OMA; HTLFWIA; -.
DR   OrthoDB; 162558at2; -.
DR   Proteomes; UP000001054; Chromosome.
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-UniRule.
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; IPR002912; ACT_dom.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
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; 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   TIGRFAMs; TIGR01693; UTase_glnD; 1.
DR   PROSITE; PS51671; ACT; 2.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
DR   PRODOM; C3MEZ9.
DR   SWISS-2DPAGE; C3MEZ9.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001054};
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS01174769};
KW   Magnesium {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00204441};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00677267};
KW   Nitrogen fixation {ECO:0000256|HAMAP-Rule:MF_00277};
KW   Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440786, ECO:0000313|EMBL:ACP23836.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001054};
KW   Repeat {ECO:0000256|SAAS:SAAS00300508};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00277,
KW   ECO:0000256|SAAS:SAAS00440788, ECO:0000313|EMBL:ACP23836.1}.
FT   DOMAIN      510    626       HD. {ECO:0000259|PROSITE:PS51831}.
FT   DOMAIN      750    832       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   DOMAIN      861    942       ACT. {ECO:0000259|PROSITE:PS51671}.
FT   REGION        1    391       Uridylyltransferase. {ECO:0000256|HAMAP-
FT                                Rule:MF_00277}.
SQ   SEQUENCE   965 AA;  108121 MW;  06330DD44BAE149E CRC64;
     MQRTIRSVGQ DASRHFMARH ETSFPEILDV AALRAKCGFI AAAHAEQREP MRRALLAAFK
     EANNAGRAKA RQLLAADGAG IKCAERISWL QDQLITVLHD FMLNEVFDAA HAPPAARLAV
     TAVGGYGRGT LAPGSDIDLL FLLPSKRAVW AEPAIEFMLY VLWDLGFKVG HATRTIDECI
     RLSRADMTIR TAILECRYIC GSEALAGELE QRFDHEIVRN TGPEFIAAKL AERDGRHRKA
     GDTRYLVEPN VKEGKGGLRD LHTLFWIAKY FYRVKDPADL VKLAVLSRQE YKLFQKSDDF
     LWAVRCHMHF LTGKAEERLS FDIQREIAEA LGYHDHPGLS AVERFMKHYF LVAKDVGDLT
     RIFCAALEDQ QAKDTPGISG VFSRFKHRTR KIAGTLDFVD DGGRIALASP DVFKREPINL
     LRLFHIADIH GLEFHPNALK QVTRSLGLIT PHLRENDEAN RLFLSILTSR RNPELILRRM
     NEAGVLGRFI PDFGKIVSMM QFNMYHHYTV DEHLLRTVDV LSRIDRGLEE EAHPLTAMLM
     PGIEDRSALY VAVLLHDIAK GRPEDHSVAG AKVARKLCPR LGLSPKQTET VVWLVEEHLT
     MSMVAQTRDL NDRKTILDFA ERVQSLDRLK MLLILTVCDI RAVGPGVWNG WKGQLLRTLY
     YETELLLSGG FSELSRKERA KHAAHMLSDA LKDWSKKERD AYVRLHYQPY LLTVALEDQV
     RHAEFIREAD RAGKTLATMV RTHHFHAITE ITVLSPDHPR LLTVIAGACA AAGANIVDAQ
     IHTTSDGRAL DTILVNREFS VDEDEMRRAA SIGKLIEDVL SGRKRLPEVI ASRTRAKKRS
     KAFTVTPEVT ISNTLSNKFT VIEVEGLDRT GLLSEITAVL SDLSLDIASA HITTFGEKVI
     DTFYVTDLVG AKITNENRQG NIAARLKAVL AGEVDEARER MPSGIIAPAH SPRSSHAART
     TKVET
//

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