UniProt: A0A0M5KVH6

Database: UniProt
Entry: A0A0M5KVH6_9MICC

LinkDB:  A0A0M5KVH6_9MICC 
Original site:  A0A0M5KVH6_9MICC

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

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ID   A0A0M5KVH6_9MICC        Unreviewed;      1013 AA.
AC   A0A0M5KVH6;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=Glutamine-synthetase {ECO:0000313|EMBL:ALE05486.1};
GN   ORFNames=AL755_08365 {ECO:0000313|EMBL:ALE05486.1};
OS   Arthrobacter sp. ERGS1:01.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Arthrobacter.
OX   NCBI_TaxID=1704044 {ECO:0000313|EMBL:ALE05486.1, ECO:0000313|Proteomes:UP000060433};
RN   [1] {ECO:0000313|EMBL:ALE05486.1, ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|EMBL:ALE05486.1,
RC   ECO:0000313|Proteomes:UP000060433};
RX   PubMed=26415659; DOI=10.1016/j.jbiotec.2015.09.025;
RA   Kumar R., Singh D., Swarnkar M.K., Singh A.K., Kumar S.;
RT   "Complete genome sequence of Arthrobacter sp. ERGS1:01, a putative novel
RT   bacterium with prospective cold active industrial enzymes, isolated from
RT   East Rathong glacier in India.";
RL   J. Biotechnol. 214:139-140(2015).
RN   [2] {ECO:0000313|Proteomes:UP000060433}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ERGS1:01 {ECO:0000313|Proteomes:UP000060433};
RA   Kumar R., Swarnkar M.K., Singh A.K., Singh D.;
RT   "Complete Genome Sequencing of Arthrobacter sp. ERGS1:01.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; CP012479; ALE05486.1; -; Genomic_DNA.
DR   RefSeq; WP_054010610.1; NZ_CP012479.1.
DR   AlphaFoldDB; A0A0M5KVH6; -.
DR   SMR; A0A0M5KVH6; -.
DR   STRING; 1704044.AL755_08365; -.
DR   KEGG; are:AL755_08365; -.
DR   PATRIC; fig|1704044.3.peg.903; -.
DR   OrthoDB; 9759366at2; -.
DR   Proteomes; UP000060433; Chromosome.
DR   GO; GO:0008882; F:[glutamate-ammonia-ligase] adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   CDD; cd05401; NT_GlnE_GlnD_like; 2.
DR   Gene3D; 1.20.120.1510; -; 1.
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   Reference proteome {ECO:0000313|Proteomes:UP000060433};
KW   Transferase {ECO:0000256|ARBA:ARBA00022695}.
FT   DOMAIN          82..336
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          358..501
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
FT   DOMAIN          606..846
FT                   /note="Glutamate-ammonia ligase adenylyltransferase
FT                   repeated"
FT                   /evidence="ECO:0000259|Pfam:PF03710"
FT   DOMAIN          886..1011
FT                   /note="PII-uridylyltransferase/Glutamine-synthetase
FT                   adenylyltransferase"
FT                   /evidence="ECO:0000259|Pfam:PF08335"
SQ   SEQUENCE   1013 AA;  109718 MW;  D1982365D453EEEE CRC64;
     MSSLTRALIT NGFSDLEKTE RFLGFAELAE LDQAELLAAL RVANNPDLAV QSLVRLLSAA
     PAVYAKLTVT DKESGRQEPN EALFRLLGAS EALADFLIRH PEHVDVLDTP TSPEPAPVDA
     GELRASLLSA VGADPASAMP VAAETGTAAR LALRTRYRRH LAVLAIRDLC AASPQDVMPL
     VGAELADLAA AALDAALAVA RAEVAAVFAP DAVAGVRLAV IGMGKCGARE LNYISDVDVM
     YVIETADGGP DDADAVAIGN ALASAVSQAI YAPEREPGLW EVDANLRPEG KDGPLVRTLD
     SFLNYYGRWA QSWEFQALLK ARALGGDREL GRRFEQAVSP LIWTSSEREG FVASVQGMRR
     RVTANIPDAE AGRQIKLGKG GLRDVEFTVQ LLQLVHGKND ESIRVKATTA AIGALMKAGY
     IGRTDAAHLD EAYRYLRVLE HRIQLVHMRR THLMPTAPEQ LRALARAVAG PLSIKRPSAE
     SLLADWAKVK RQVSSLHERI FYRPILATAA HLSAADAALT TDAARARLAA LGYRDAAGAQ
     RHIEALTAGV SRRAALQRQL LPVLLNWLAD GVDPDAGLLA FRRVSEALGT SHWYLGMLRD
     HQAAAERLCH VLSSSRLVTD LLEVSPEATA WFGNDKELVP LSFETQWAEI QSKMSRHPEP
     GEAIRLIRLI RQREILRIAI ADCSGLLGQD DVASALSDAD RAAVLGALLV AESAVYAGEP
     PLTRVLVVAM GRQGGREIAY GSDADVLFVH RPVQDGPGAE EAAGEQARAI VAKLTAMLTQ
     PVRPAIQAER VLSVDADLRP EGKSGPLVRS LEAYREYYSR WSSPWEAQAL LRARPLAGSD
     DLAADFVAMA DPIRYPAVLP DAALREIKLL KARMESERLP RGADPARHVK LGRGGLSDVE
     WLVQLWQLQH AHHHEGLRTT ATLPALHAAT ELGLVEADDA ELLEAAWRLA GKIRNANVIW
     TGKTSDLLPS ARGDLEAVAR WCGYEPGHAA RFEEDYLGLT RRCRAVFERL FYG
//

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