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Database: UniProt
Entry: D6ZH01_MOBCV
LinkDB: D6ZH01_MOBCV
Original site: D6ZH01_MOBCV 
ID   D6ZH01_MOBCV            Unreviewed;      1066 AA.
AC   D6ZH01;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
DE   SubName: Full=[glutamate--ammonia-ligase] adenylyltransferase {ECO:0000313|EMBL:ADI67909.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:ADI67909.1};
GN   Name=glnE {ECO:0000313|EMBL:ADI67909.1};
GN   OrderedLocusNames=HMPREF0573_11590 {ECO:0000313|EMBL:ADI67909.1};
OS   Mobiluncus curtisii (strain ATCC 43063 / DSM 2711 / V125) (Falcivibrio
OS   vaginalis).
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Mobiluncus.
OX   NCBI_TaxID=548479 {ECO:0000313|EMBL:ADI67909.1, ECO:0000313|Proteomes:UP000006742};
RN   [1] {ECO:0000313|Proteomes:UP000006742}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43063 / DSM 2711 / V125
RC   {ECO:0000313|Proteomes:UP000006742};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R., Gibbs R.;
RT   "Complete sequence of Mobiluncus curtisii ATCC 43063.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP001992; ADI67909.1; -; Genomic_DNA.
DR   RefSeq; WP_013189491.1; NC_014246.1.
DR   AlphaFoldDB; D6ZH01; -.
DR   STRING; 548479.HMPREF0573_11590; -.
DR   GeneID; 55565691; -.
DR   KEGG; mcu:HMPREF0573_11590; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   OMA; EFMVQYA; -.
DR   Proteomes; UP000006742; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
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   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; 3.
DR   SUPFAM; SSF81301; Nucleotidyltransferase; 2.
DR   SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 2.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Ligase {ECO:0000313|EMBL:ADI67909.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000313|EMBL:ADI67909.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006742};
KW   Transferase {ECO:0000313|EMBL:ADI67909.1}.
FT   DOMAIN          85..330
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          353..491
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          598..777
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          803..890
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          938..1064
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1066 AA;  116384 MW;  CF3ED57993905031 CRC64;
     MAREYSETVA LLTSGVEDVE RAKTRLTAIT QAAPQVDIPQ LIENLGQTAD PDLVLLGLDR
     IFSEDAAHPS GITETLSVRQ IGNRTLQLLG ASEFFASYLA THPAALELLE QEPEPETYSA
     RLLRAVGAKN LGTVKNPCWV ADPQAHDLEL RRVYYALLAQ LAAEDLAHAG ETAAKAEFQA
     TSRRISDLVD AALEASLALA RRDHDPEGLI AFSVVAMGKT GARELNYISD VDVIYVGQAQ
     EDADLDPAEV NRRATAMAQA LGSYCSATGP EPALWILDAA LRPEGKDGAL VRNLESHLDY
     YQRWAKTWEF QALLKARPAA GDRELGARYL STIRPFVWSA VEREGFVEDT RAMRRRVEKL
     LDPKKAGREI KLGAGGLRDV EFTVQLLQLV HGRVDESLRV RGTLDALQAL IAGGYIGRDQ
     GEEMADYYRF LRVIEHRTQL DRMRRTHLFP QDAQLRRVAR SIDVTRFSEG AKLTQAWQEV
     RHKVRGLHEE IYYRPLLPAM AKLSAGVAAL DSVAAQSRLQ AIGYRDPKRA LEHIEALTSG
     MSRRAAIQRQ LLPVLLDWLA DGVDPDGGLL AFRQVSDALG DTHWYLGLLR DSGTAARSLT
     RLLSSSPLVA GLLPANPDAI KWLDDESQLR GRTREELERE ILATFERQPD LDKQAARLRA
     VRGRELLRAA MVDVLQGIDP LRTAQRLTDV GEAVLAGAFD LALRKLKAQL PPTAPGHKGG
     GEPPSAQVAL ASPATRALAS AGYYADHLIV GMGRFGGGES GYPSDADVVF YYRPWQEPGN
     PAGGYLRATP ADLPVVGTEA DSATSEIRKR AVMEATSLVN TVSSILSGSQ AGAWRVDTDL
     RPEGRSGAVS KDLDLLKDYY ARWASAWERQ ALLRARPVVG SSTLRTDFAE IVDPVRFDTP
     PEDKELKEIR RLKARMESER IGGGQVSGAG KTGAAVRHVK LGPGGLSDVE WSVQLLQMCH
     AHTVPGLRCV STGDALRAAV SAGLIPASDA EILRTAWMMA MSIRAANVLG SGRTTGKKLD
     VLPVDRLLVT TAALLGYPEG THQDLTDDWM RAARLARGVV EQIFYS
//
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