Detailed information of ANN22002-RA in Montipora grisea

Genomic Location: Scaffold_20__1_contigs__length_3961929:3427849...3429502
NR annotation: MXV82570.1, glutamine-hydrolyzing GMP synthase [Candidatus Poribacteria bacterium]


 Gene Structure
More details in Jbrowse  Sequence
CDS
Transcript
Protein
 Uniprot
Uniprot termDescription
C4XSN8GMP synthase [glutamine-hydrolyzing] OS=Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1) OX=573370 GN=guaA PE=3 SV=1
A6Q4N8GMP synthase [glutamine-hydrolyzing] OS=Nitratiruptor sp. (strain SB155-2) OX=387092 GN=guaA PE=3 SV=1
B9L0W3GMP synthase [glutamine-hydrolyzing] OS=Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2) OX=309801 GN=guaA PE=3 SV=1

 Pfam domain
Pfam accessionPfam nameDescriptionTypeSource
PF00117GATaseGlutamine amidotransferase class-IDomainInterproscan
PF00958GMP_synt_CGMP synthase C terminal domainDomainInterproscan

 InterPro
InterPro termTypeDescriptionSource
IPR017926DomainGlutamine amidotransferaseInterproscan
IPR001674DomainGMP synthase, C-terminalInterproscan
IPR025777DomainGMP synthetase ATP pyrophosphatase domainInterproscan
IPR014729Homologous_superfamilyRossmann-like alpha/beta/alpha sandwich foldInterproscan
IPR004739DomainGMP synthase, glutamine amidotransferaseInterproscan
IPR029062Homologous_superfamilyClass I glutamine amidotransferase-likeInterproscan
IPR022955FamilyGMP synthaseInterproscan

 PANTHER
PANTHER termDescriptionSource
PTHR11922GMP SYNTHASE-RELATEDInterproscan

 Gene Ontology
GO termsCategoryDescriptionSource
GO:0003922Molecular FunctionGMP synthase (glutamine-hydrolyzing) activityInterproscan
GO:0005524Molecular FunctionATP bindingInterproscan
GO:0006164Biological Processpurine nucleotide biosynthetic processInterproscan
GO:0006177Biological ProcessGMP biosynthetic processInterproscan
GO:0003921Molecular FunctionGMP synthase activityInterproscan
GO:0005829Cellular ComponentcytosolInterproscan

 KEGG pathway
KOEnzymeEnzyme IDpathwaymapIDSource
K01951guaA, GMPS; GMP synthase (glutamine-hydrolysing)EC:6.3.5.2
Peptidases and inhibitorsko01002deepkoala

TOP