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.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//