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Database: UniProt
Entry: I4BL24_MYCCN
LinkDB: I4BL24_MYCCN
Original site: I4BL24_MYCCN 
ID   I4BL24_MYCCN            Unreviewed;       991 AA.
AC   I4BL24;
DT   05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT   05-SEP-2012, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   RecName: Full=Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATP:glutamine synthetase adenylyltransferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE   AltName: Full=ATase {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl-L-tyrosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.89 {ECO:0000256|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl removase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AR {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT-N {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Includes:
DE     RecName: Full=Glutamine synthetase adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              EC=2.7.7.42 {ECO:0000256|HAMAP-Rule:MF_00802};
DE     AltName: Full=Adenylyl transferase {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT {ECO:0000256|HAMAP-Rule:MF_00802};
DE              Short=AT-C {ECO:0000256|HAMAP-Rule:MF_00802};
DE   Flags: Precursor;
GN   Name=glnE {ECO:0000256|HAMAP-Rule:MF_00802};
GN   OrderedLocusNames=Mycch_3233 {ECO:0000313|EMBL:AFM17981.1};
OS   Mycolicibacterium chubuense (strain NBB4) (Mycobacterium chubuense).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=710421 {ECO:0000313|EMBL:AFM17981.1, ECO:0000313|Proteomes:UP000006057};
RN   [1] {ECO:0000313|EMBL:AFM17981.1, ECO:0000313|Proteomes:UP000006057}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBB4 {ECO:0000313|EMBL:AFM17981.1,
RC   ECO:0000313|Proteomes:UP000006057};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Teshima H., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Mattes T.,
RA   Holmes A., Rutledge P., Paulsen I., Coleman N., Woyke T.;
RT   "Complete sequence of chromosome of Mycobacterium chubuense NBB4.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in the regulation of glutamine synthetase GlnA, a
CC       key enzyme in the process to assimilate ammonia. When cellular nitrogen
CC       levels are high, the C-terminal adenylyl transferase (AT) inactivates
CC       GlnA by covalent transfer of an adenylyl group from ATP to specific
CC       tyrosine residue of GlnA, thus reducing its activity. Conversely, when
CC       nitrogen levels are low, the N-terminal adenylyl removase (AR)
CC       activates GlnA by removing the adenylyl group by phosphorolysis,
CC       increasing its activity. The regulatory region of GlnE binds the signal
CC       transduction protein PII (GlnB) which indicates the nitrogen status of
CC       the cell. {ECO:0000256|HAMAP-Rule:MF_00802}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[glutamine synthetase]-L-tyrosine + ATP = [glutamine
CC         synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate;
CC         Xref=Rhea:RHEA:18589, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:46858,
CC         ChEBI:CHEBI:83624; EC=2.7.7.42; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00802};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine +
CC         phosphate = [glutamine synthetase]-L-tyrosine + ADP;
CC         Xref=Rhea:RHEA:43716, Rhea:RHEA-COMP:10660, Rhea:RHEA-COMP:10661,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:83624,
CC         ChEBI:CHEBI:456216; EC=2.7.7.89; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00802};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00802};
CC   -!- SIMILARITY: Belongs to the GlnE family. {ECO:0000256|HAMAP-
CC       Rule:MF_00802}.
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DR   EMBL; CP003053; AFM17981.1; -; Genomic_DNA.
DR   RefSeq; WP_014816457.1; NC_018027.1.
DR   AlphaFoldDB; I4BL24; -.
DR   STRING; 710421.Mycch_3233; -.
DR   KEGG; mcb:Mycch_3233; -.
DR   PATRIC; fig|710421.3.peg.3232; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000006057; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0047388; F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0000820; P:regulation of glutamine family amino acid metabolic process; IEA:UniProtKB-UniRule.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 2.
DR   Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 2.
DR   HAMAP; MF_00802; GlnE; 1.
DR   InterPro; IPR023057; GlnE.
DR   InterPro; IPR005190; GlnE_rpt_dom.
DR   InterPro; IPR043519; NT_sf.
DR   InterPro; IPR013546; PII_UdlTrfase/GS_AdlTrfase.
DR   PANTHER; PTHR30621:SF0; BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME; 1.
DR   PANTHER; PTHR30621; GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF08335; GlnD_UR_UTase; 2.
DR   Pfam; PF03710; GlnE; 2.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00802};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00802};
KW   Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_00802};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00802};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695, ECO:0000256|HAMAP-
KW   Rule:MF_00802}; Reference proteome {ECO:0000313|Proteomes:UP000006057};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00802, ECO:0000313|EMBL:AFM17981.1}.
FT   DOMAIN          86..310
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          335..481
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          587..824
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          851..983
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   REGION          1..485
FT                   /note="Adenylyl removase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          495..991
FT                   /note="Adenylyl transferase"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00802"
FT   REGION          759..778
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   991 AA;  107032 MW;  E087586037532844 CRC64;
     MAKPATQRPK LPGVGRLGLV ERQAQADLDA LGWNTDAHVE LLWSLSRAPD ADSALRATVR
     LSEALGRDWA ELDGALLKDR GLRGRLFAVL GSSLALGDHL VANPGSWRLL AGNVTLPVPA
     ELKQMFGECA DGVTSAATAV APLRTLYRDR LLVLAALDVA PTVENEPVLP FTVVAEHLAD
     LADAALAAAL SVVTASVCGD DEAPALAVIA MGKCGARELN YVSDVDVIFV ADDGSHSTLA
     TATRIAGEMM RLAGEAFFEV DAALRPEGKQ GQLVRTLDSH IAYYERWAKT WEFQALMKAR
     PAAGDAGLGD RYIEALMPMV WTACEREDFV PEVQAMRRRV EALVPAGVRN RELKLGTGGL
     RDVEFAVQLL QLVHGRNDES LHVASTVNAL AALGAGGYIG RDDAANMTAS YEFLRLLEHR
     LQMQRLKRTH MLPETDDDEA MRWLARAAHM RPDGRHDALG VLREELKRQS HRVSRLHAKL
     FYQPLMESVG QPPLGFSVGM STEAAERQLA ALGYEGPQSA LTHLAALTGG TGRRGRVQQV
     LLPTLLDWLS DTPDPDAGLL NYRRLSDELA DQRWFLATLR DEGAVAKRLM HVLGTSAYVP
     GLLMRAPEVI QLYADGPNGP KLCDADADAL AGSLVASAAR HSDPLRAIAA ARSLRRRELA
     RIASADLLGM LDVTDVCRQL TAVWVAVLQA ALDAVTRANT PESGPPARIA VIGMGRLGGG
     ELGYGSDADV MFVCEPNSGV EESVAVKWSV TVAEQVRSRL GTPSSDPPLD VDTNLRPEGR
     QGPLVRTLAS YEAYYSQWAQ PWEIQALLRA HRVAGDQELG ERFLLMIDET RYPPGGVSPE
     AVQEIRRIKA RVDAERLPRG ADPNTHTKLG RGGLADIEWT VQLLQLRFAH KIPALHNTST
     LDTLNAIGAA ELIAEGDIEL LREAWLTATR ARNALVLVRG KPTDQLPGPG KLANAVAVAA
     GWPGGDGGEF LDNYLRVTRR AKAVVLRIFG G
//
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