UniProt: S4XIU7

Database: UniProt
Entry: S4XIU7_9CORY

LinkDB:  S4XIU7_9CORY 
Original site:  S4XIU7_9CORY

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Ontology (2)   
   GO (2)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (1)   
   KEGG GENES (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (6)   
   InterPro (4)   
   Pfam (2)   
All databases (12)   

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ID   S4XIU7_9CORY            Unreviewed;      1055 AA.
AC   S4XIU7;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Bifunctional glutamine-synthetase adenylyltransferase/deadenyltransferase {ECO:0000313|EMBL:AGP30518.1};
DE            EC=2.7.7.42 {ECO:0000313|EMBL:AGP30518.1};
GN   ORFNames=A606_04345 {ECO:0000313|EMBL:AGP30518.1};
OS   Corynebacterium terpenotabidum Y-11.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC   Corynebacteriaceae; Corynebacterium.
OX   NCBI_TaxID=1200352 {ECO:0000313|EMBL:AGP30518.1, ECO:0000313|Proteomes:UP000014809};
RN   [1] {ECO:0000313|EMBL:AGP30518.1, ECO:0000313|Proteomes:UP000014809}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y-11 {ECO:0000313|EMBL:AGP30518.1,
RC   ECO:0000313|Proteomes:UP000014809};
RA   Ruckert C., Albersmeier A., Al-Dilaimi A., Szczepanowski R., Kalinowski J.;
RT   "Complete genome sequence of Corynebacterium terpenotabidum Y-11 (=DSM
RT   44721).";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP003696; AGP30518.1; -; Genomic_DNA.
DR   RefSeq; WP_020440880.1; NC_021663.1.
DR   AlphaFoldDB; S4XIU7; -.
DR   STRING; 1200352.A606_04345; -.
DR   KEGG; cter:A606_04345; -.
DR   PATRIC; fig|1200352.3.peg.879; -.
DR   eggNOG; COG1391; Bacteria.
DR   HOGENOM; CLU_006233_1_0_11; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000014809; 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:AGP30518.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000014809};
KW   Transferase {ECO:0000313|EMBL:AGP30518.1}.
FT   DOMAIN          212..349
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          374..520
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          625..879
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          901..1043
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1055 AA;  115743 MW;  D0684041EEB2DBD8 CRC64;
     MSQPRTSRRG VPSAASLGLS RPHAAADLAA LGWDDEAHLD LLWTLAATGH PDQALNNIVR
     LIQATEGSEV PAAASATELQ ARLDTDHEFR VRLLALLGAS SLLGDHVVAH PEIWPQLGDD
     LPGRVEMMDT MLASVDAASV DGQDADGNPL HTGDSLLRRA GMTGPAADRA MRTAYRTLLA
     RIAAIDLAGT FVPRRGEAPT AKGRTGYPDF VPFEVIADRL ADAADAALSA ALAVATAVVY
     PSGPVDARIA VLAMGKCGAL ELNYISDVDV IFVAEPADAR TTRLAGEFIN IGCRCFFEVD
     AALRPEGKHG ALVRTLDSHL AYYRKWAHTW EFQALLKARP MTGDLALGEA YVEELAPMVW
     TASQREDFVP DVQAMRRRVV DNVPEDLQAR ELKLGPGGLR DVEFAVQLLQ MVHGRADVSL
     RVRSTVDALN ALVAGGYVSR EDGRTLIGNY SFMRLLEHRM QLHHLRRTHL LPEDSDLPER
     TWLARVSGLV AEGTRTLAEE LEAQVRSTGR QIRQLHNKLF YRPLLSSVVA MSVDELRLTP
     EAAQRQLAAL GYRYPDRAMD HLTALASDTT RRARVQAVLL PSLLEWLSET VDPDAGLLAY
     RKLSEAAVDR AWFLRLLRDE NIVGQRLMKI LGTSPYVTDL FLAAPDAVKM LSDGAMKPKL
     LEKSASVISH SLVAAAGRHT DPDKAISVAR SLRRTELARV AAADLLGMMD LPEVAQSLSL
     VWDAVLEAAL SAEIRAWEDA HSRNAPAVIS VIGMGRLGGA ELSYRSDADV LFVCEPVAGD
     GIEGMDIDRD GEPGTDQDAV AWAIGICDRL RSRLAKPSQD PPLEVDLDLR PEGRSGPAVR
     TLESYRAYYE RWGETWEYQA LLRATWVAGD KDLGIRFLRS IDPFRYPEGG ADEKTVQEVR
     RMKARVDGER LPRGANRATH TKLGRGGLAD VEWTVQLLTM QHSHLFESLH NTSTLEVLEE
     IRTAGLLSEF DVETLREAWI TASHARNALV LSNAKTTDQL PPPGAQLVHV AAAAGWDPED
     SQGYLDDYLK KTRRARRVVD RVFWGEEVVD ARYDD
//

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