ID F8ADY1_THEID Unreviewed; 911 AA.
AC F8ADY1;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=(Glutamate--ammonia-ligase) adenylyltransferase {ECO:0000313|EMBL:AEH44946.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:AEH44946.1};
GN OrderedLocusNames=Thein_1075 {ECO:0000313|EMBL:AEH44946.1};
OS Thermodesulfatator indicus (strain DSM 15286 / JCM 11887 / CIR29812).
OC Bacteria; Thermodesulfobacteriota; Thermodesulfobacteria;
OC Thermodesulfobacteriales; Thermodesulfatatoraceae; Thermodesulfatator.
OX NCBI_TaxID=667014 {ECO:0000313|EMBL:AEH44946.1, ECO:0000313|Proteomes:UP000006793};
RN [1] {ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Pagani I., Ivanova N., Saunders L.,
RA Detter J.C., Tapia R., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schroeder M.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Thermodesulfatator indicus DSM 15286.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AEH44946.1, ECO:0000313|Proteomes:UP000006793}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15286 / JCM 11887 / CIR29812
RC {ECO:0000313|Proteomes:UP000006793};
RX PubMed=22768359; DOI=10.4056/sigs.2665915;
RA Anderson I., Saunders E., Lapidus A., Nolan M., Lucas S., Tice H.,
RA Del Rio T.G., Cheng J.F., Han C., Tapia R., Goodwin L.A., Pitluck S.,
RA Liolios K., Mavromatis K., Pagani I., Ivanova N., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Jeffries C.D., Chang Y.J.,
RA Brambilla E.M., Rohde M., Spring S., Goker M., Detter J.C., Woyke T.,
RA Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA Klenk H.P.;
RT "Complete genome sequence of the thermophilic sulfate-reducing ocean
RT bacterium Thermodesulfatator indicus type strain (CIR29812(T)).";
RL Stand. Genomic Sci. 6:155-164(2012).
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DR EMBL; CP002683; AEH44946.1; -; Genomic_DNA.
DR RefSeq; WP_013907688.1; NC_015681.1.
DR AlphaFoldDB; F8ADY1; -.
DR STRING; 667014.Thein_1075; -.
DR PaxDb; 667014-Thein_1075; -.
DR KEGG; tid:Thein_1075; -.
DR PATRIC; fig|667014.3.peg.1104; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_1_0_0; -.
DR InParanoid; F8ADY1; -.
DR Proteomes; UP000006793; 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 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; 2.
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 Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:AEH44946.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006793};
KW Transferase {ECO:0000313|EMBL:AEH44946.1}.
FT DOMAIN 42..270
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 292..430
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 583..752
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 789..869
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 911 AA; 104672 MW; D3DE2648DB05FD98 CRC64;
MQVNFKCLEP PDSEWASFNL ERLKEAHSDF PWGRIPHENL SLLKNLLGFS PYATNILLRR
KDVLELFCSY PLPKPKGSRN LFREIAQKTD SLKDWKDLAV FLRRIKQREM IKILAHDLAG
REFRKTVFAI TALAEASLKA ILFWLTSTSY PEDFREKFFI LGMGKFGARE LNYSSDIDII
YFFHAPLNEK ERFIALAREI TRIMDTLIEG DRVFRVDLGL RPGGKDGELV YSARAGVNYY
FYQAHPFERL AMVKARPVAG NIKLGKSFLK VLRPVIYPQF LDFAYLEHIK DLKARIEKEA
RKKGAERNIK IGPGGIRSVE FFCQTLQMIF GGKHPYLRTR HTLWALNHLA KYKILPSDEA
LFLKKAYVFL RQVEHRIQTV HFRQTYTLPE EETSLKRLAK SLGYQGEEAH RIFLDELNVL
RQQTERIFLS LLEPEKSKAS NLSGKIDLFF DGEISSKELA GELNLPSHLL KDIKNILVAK
GPLAARRAPL LKDIFKVVLE KAVIWGVKTE TLAKLLSFFE RLGGRLSFYH ALRHDPEKIE
DLLEIFEKSA FLSHLLMEVP GAAEALFELE ISFILPVIPS GMELEQALGL LRMAKNEEIF
RVAYLDLKQK IPFPQVPERL SILAESIIKE TYNLASSSKQ YPPHLLTILG LGKLGGKELG
YRSDLDMVFI APSEEEMVPA TKLVQRFMHY LTTPLPEGPG YEVDTRLRPE GRKGPLVATV
EGFLKYHQED SGLWEKLALL RLKPLAGDLE AGELLLKRLR EVLSSFEFGA SQAEEIRQMR
FKMEKERTTP GRFNPKVSRG GLADIEFVTF WLILKNIREK DLWGGPIPLV LNKLAQKGIV
PSKVAKKLEA NYLFLRRLEQ LLILLLDKSG EEKEYSFSEI KLCESYLGSG LEEKLKQICE
ENRKLFEEWL A
//
