ID S9S6W0_9RHOB Unreviewed; 472 AA.
AC S9S6W0;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Glutamine synthetase adenylyltransferase {ECO:0000313|EMBL:EPX85930.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:EPX85930.1};
GN ORFNames=ruthe_01651 {ECO:0000313|EMBL:EPX85930.1};
OS Rubellimicrobium thermophilum DSM 16684.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=1123069 {ECO:0000313|EMBL:EPX85930.1, ECO:0000313|Proteomes:UP000015346};
RN [1] {ECO:0000313|EMBL:EPX85930.1, ECO:0000313|Proteomes:UP000015346}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16684 {ECO:0000313|EMBL:EPX85930.1,
RC ECO:0000313|Proteomes:UP000015346};
RX PubMed=24501632; DOI=10.4056/sigs.4247911;
RA Fiebig A., Riedel T., Gronow S., Petersen J., Klenk H.P., Goker M.;
RT "Genome sequence of the reddish-pigmented Rubellimicrobium thermophilum
RT type strain (DSM 16684(T)), a member of the Roseobacter clade.";
RL Stand. Genomic Sci. 8:480-490(2013).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EPX85930.1}.
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DR EMBL; AOLV01000012; EPX85930.1; -; Genomic_DNA.
DR AlphaFoldDB; S9S6W0; -.
DR STRING; 1123069.ruthe_01651; -.
DR PATRIC; fig|1123069.3.peg.1622; -.
DR HOGENOM; CLU_045976_0_0_5; -.
DR Proteomes; UP000015346; Unassembled WGS sequence.
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; 1.
DR Gene3D; 3.30.460.10; Beta Polymerase, domain 2; 1.
DR Gene3D; 1.20.120.330; Nucleotidyltransferases domain 2; 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; 1.
DR Pfam; PF03710; GlnE; 1.
DR SUPFAM; SSF81301; Nucleotidyltransferase; 1.
DR SUPFAM; SSF81593; Nucleotidyltransferase substrate binding subunit/domain; 1.
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:EPX85930.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000015346};
KW Transferase {ECO:0000313|EMBL:EPX85930.1}.
FT DOMAIN 71..307
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 351..421
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 472 AA; 50920 MW; FF522093361C8397 CRC64;
MTARWPDYPA LRSQRAVGIF RRLRPEILRR LREAARPDEA LTSFDAFLSG LPAGVQLFSL
FEANPDLLRL MVEIAATSPA LARYLSRNAG VLDAVIGGDF FAPWPGQQRL AESLGAAMAE
AADYEAQLNA ARRWAREWWF RIGVHHLQGL IDAAEAGQHY ADLAGAVLDR LFPAVTAEFA
RRHGSGPGWG AVVLGMGSLG AGRLNAASDL DLIMIYEAGG EQSDGPAPLA PRAYFARLTQ
ALLTALSAPM ADGRLYAADM RLRPSGRQGP VATSWASFES YQRTEAWTWE HLALTRARVV
AGAGDWQRLA DRVERFRTDL VAGRRGDPRI PPDVAEMRAR LAAHQGGDGP WDAKAGPGRL
RDIELFAQTL ALLAGSPRRG TAAQIGDGLA AGLIGPSEAQ RLTAAADLFW RLQSAGRLLT
EGRLDPAAVG EGGRRFLLRE TGAETLEDLE RRLAAAAADA EAIISTRLEA MP
//
