ID D5ALT3_RHOCB Unreviewed; 923 AA.
AC D5ALT3;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:ADE86144.1};
DE EC=2.7.7.42 {ECO:0000313|EMBL:ADE86144.1};
GN Name=glnE {ECO:0000313|EMBL:ADE86144.1};
GN OrderedLocusNames=RCAP_rcc02414 {ECO:0000313|EMBL:ADE86144.1};
OS Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodobacter.
OX NCBI_TaxID=272942 {ECO:0000313|EMBL:ADE86144.1, ECO:0000313|Proteomes:UP000002361};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SB1003;
RA Strnad H., Lapidus A., Vlcek C., Ulbrich P., Paces J., Maltsev N.,
RA Kumar V., Kogan Y., Milgram A., Rebrekov D., Mazur M., Cox R., Kyrpides N.,
RA Kolar M., Sachova J., Ridl J., Ivanova N., Kapatral V., Los T., Lykidis A.,
RA Mikhailova N., Reznik G., Vasieva O., Fonstein M., Paces V., Haselkorn R.;
RT "Complete genome sequence of Rhodobacter capsulatus SB1003.";
RL Submitted (DEC-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADE86144.1, ECO:0000313|Proteomes:UP000002361}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003
RC {ECO:0000313|Proteomes:UP000002361};
RX PubMed=20418398; DOI=10.1128/JB.00366-10;
RA Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA Haselkorn R.;
RT "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT Rhodobacter capsulatus SB 1003.";
RL J. Bacteriol. 192:3545-3546(2010).
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DR EMBL; CP001312; ADE86144.1; -; Genomic_DNA.
DR RefSeq; WP_013068123.1; NC_014034.1.
DR AlphaFoldDB; D5ALT3; -.
DR STRING; 272942.RCAP_rcc02414; -.
DR GeneID; 31491245; -.
DR KEGG; rcp:RCAP_rcc02414; -.
DR eggNOG; COG1391; Bacteria.
DR HOGENOM; CLU_006233_0_0_5; -.
DR OrthoDB; 9759366at2; -.
DR Proteomes; UP000002361; 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; 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 Ligase {ECO:0000313|EMBL:ADE86144.1};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ADE86144.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002361};
KW Transferase {ECO:0000313|EMBL:ADE86144.1}.
FT DOMAIN 42..276
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 298..439
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
FT DOMAIN 527..768
FT /note="Glutamate-ammonia ligase adenylyltransferase
FT repeated"
FT /evidence="ECO:0000259|Pfam:PF03710"
FT DOMAIN 807..920
FT /note="PII-uridylyltransferase/Glutamine-synthetase
FT adenylyltransferase"
FT /evidence="ECO:0000259|Pfam:PF08335"
SQ SEQUENCE 923 AA; 100135 MW; 857EEA06CA131596 CRC64;
MSLASRLTRT PVPLDPARGA DVVARYGDFP PEIRGLIAGT AGCSPYLAGL LEREADWARA
ALSSPVEAAF DAEIARLQGI ELEALGAELR RAKRRLALLI ALADLGGVWA LEQVTGALTT
LADTAVDLAL RRLVADEIRR GKLPGKGPDD AARAGGMVAL AMGKMGAHEL NYSSDIDLIC
LFDETQFAPD DRMEARAAFI RVTRKMSALI NDITAEGYVF RTDLRLRPDA SVTPVCISMG
AAELYYEAEG RTWERAAYIK ARPCAGDIAA GEKFLRALTP FVWRKHLDFA AIQDAHDMRL
RIRAHKGLGG AIEVAGHNLK LGQGGIREIE FFTQTRQLIA GGRDAELRDR TTLGGLAKLA
AKGWVPADVA CELTDHYREH REIEHRIQMV NDAQTQLMPT TPEGIDRIAR LMGAGDTAAW
TARLKDRLTR VEALTGAFFA PAEAAARPDL SPEAEAIVGA WTRYPALRSD RAQAIFRRIE
PEILKRMERA ASPEEALRQF DGFLARLPAG VQLFSLFEAN PSLIDLIVDI CATAPGLAAH
LSRNPGVFDA VIGGSFFAAW PGAEALAESF RTTLAAVPDY EKKLDAARRW AKEFRFRVGV
HHLRGLIDAA EAARFYADIA GTAVTGLWPE VVAEFARRHG SQPGRGAVVL GMGSLGAERL
NAASDLDLII IYDALGVEQS EGPKPLATRQ YFARLTQAFI TALTAPMPEG RLYEVDMRLR
PSGRGGPVAV SLDSFRDYQR TEAWTWEHLA LTRARVLAGD AGLGADVEAA RLAVLAEKGG
DPKVMPDLAE MRARIFAAKA PDGAWEAKIG PGRLQDIELL AQSFALRAGE PARKVEAQLR
IGPRRGFVTK AEGETLASAY RFLWRLQAGG RLLTDRPLDL QALGEGGRAF LLRELGEDSL
DALAERLART TSEVAALVEK ALG
//