UniProt: A0A0K0Y6B5

Database: UniProt
Entry: A0A0K0Y6B5_9RHOB

LinkDB:  A0A0K0Y6B5_9RHOB 
Original site:  A0A0K0Y6B5_9RHOB

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
DNA sequence (2)   
   EMBL (2)   
Protein domain (6)   
   InterPro (4)   
   Pfam (2)   
Literature (1)   
   PubMed (1)   
All databases (14)   

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ID   A0A0K0Y6B5_9RHOB        Unreviewed;      1075 AA.
AC   A0A0K0Y6B5;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Glutamate-ammonia-ligase adenylyltransferase {ECO:0000313|EMBL:AKS46441.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:AKS46441.1};
GN   Name=glnE {ECO:0000313|EMBL:AKS46441.1};
GN   ORFNames=OSB_19010 {ECO:0000313|EMBL:AKS46441.1}, SAMN05444287_1557
GN   {ECO:0000313|EMBL:SIO14095.1};
OS   Octadecabacter temperatus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Octadecabacter.
OX   NCBI_TaxID=1458307 {ECO:0000313|EMBL:AKS46441.1, ECO:0000313|Proteomes:UP000067444};
RN   [1] {ECO:0000313|EMBL:AKS46441.1, ECO:0000313|Proteomes:UP000067444}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB1 {ECO:0000313|EMBL:AKS46441.1,
RC   ECO:0000313|Proteomes:UP000067444};
RX   PubMed=26358607;
RA   Voget S., Billerbeck S., Simon M., Daniel R.;
RT   "Closed Genome Sequence of Octadecabacter temperatus SB1, the First
RT   Mesophilic Species of the Genus Octadecabacter.";
RL   Genome Announc. 3:e01051-15(2015).
RN   [2] {ECO:0000313|Proteomes:UP000184809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26878 {ECO:0000313|Proteomes:UP000184809};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:SIO14095.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DSM 26878 {ECO:0000313|EMBL:SIO14095.1};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012160; AKS46441.1; -; Genomic_DNA.
DR   EMBL; FSRP01000001; SIO14095.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K0Y6B5; -.
DR   STRING; 1458307.OSB_19010; -.
DR   KEGG; otm:OSB_19010; -.
DR   PATRIC; fig|1458307.3.peg.1914; -.
DR   Proteomes; UP000067444; Chromosome.
DR   Proteomes; UP000184809; 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   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; 1.
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:AKS46441.1};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000313|EMBL:AKS46441.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067444};
KW   Transferase {ECO:0000313|EMBL:AKS46441.1}.
FT   DOMAIN          196..430
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          452..592
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          676..917
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
SQ   SEQUENCE   1075 AA;  115727 MW;  3456C0F0133C82FF CRC64;
     MTRCAAGCED FVEFRQPRIP ECADRVQVSD GGDPANSEPR LFADQGSVGL AQRFARDVAG
     FGGVDFVTAR CDEQNGLTRG FAKKDDRLGD LVQMTACCIR RLLRGTGFAG HFQWCDVVAC
     IRQRTGDSFQ TFTHVFKMPK RVAIDQNEPE AQCQDMTFSS RITRSPTPFD AALGADAASA
     FGDFDASVRE LVAGAAGCSP YLSGLLTRDG DWLRNAFDDP DAALEAELAE IGGLALPELQ
     SGLRQAKRRI ALLTGLADLG GVWSLEQVTR ALARLADGAV DVALKRLVGA EIARGKVPGQ
     VEADAETAAG MCSIAMGKGG AFELNYSSDI DLICLFDETR FDPDDFHDAR AAFVRVTRKM
     AALLSDLTGD GYVFRTDLRL RPDPSVTPVC LSMEAAERYY ESVGRTWERA AYIKARASAG
     DIEAGEGFLR TLTPFVWRKH LDFVAIQDAH DMRLRIREHK GLGGPISLPG HNMKLGRGGI
     REIEFFTQTR QLIAGGRDPE LRCRGTVDGL AALANAGWVP QDDANVLTDH YRYHREVEHR
     LQMLNDAQTH DLPNTDEGFA RLAAFVGIED KALRVELNDR LEAVHALTEG FFAPSEAAPV
     SDFGESITQR WLTYPALRSD RAVEIFDRLK PRLLDALQEA AKPDEALLAF DGFLSGLPAG
     VQVFSLFEAN PQLTQMMVDI AATAPALAQY LGRNAAVFDA VIGGDFFSDW PQVDGLLDAL
     NAVLSQANDY ETQLDAARRW QKEWHFRIGV HHLRGLVDAE TAGRQYADLA QTVLSALFPV
     VVDHFATKHG QPPGRGAVVV GMGSLGAGRL HAASDLDLIV IYDGQDVDSS DGKQPLATRP
     YYARLTQALV TAMTVPMAEG RLYEVDMRLR PSGGQGPVAT SFSGFESYQM NEAWTWEHLA
     LSRARVVAGG VDLAADVEAV RARVLAAKAS GETVAGDVGD MRRRIADAKA PDGAWDAKIG
     AGRLQDVELA GQMVALQAGK TARSTTDQVA SGGLDAADST ALLDAAGLCW SVQAAAQLLL
     GSGLNAEKLG EGGKRFVLRE TGADSLDALA TQLNDVSGKA AAVIAKLVGD NNGKG
//

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