C5Y3V8

PR
Gene name
GATB
Protein name
Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial
Names
Glu-AdT subunit B
Species
Sorghum bicolor (Sorghum) (Sorghum vulgare)
KEGG Pathway
sbi:8057007
EC number
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

1-90 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for C5Y3V8

Entry ID Method Resolution Chain Position Source
AF-C5Y3V8-F1 Predicted AlphaFoldDB

No variants for C5Y3V8

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for C5Y3V8

No associated diseases with C5Y3V8

3 regional properties for C5Y3V8

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 72 - 359 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 213 - 227 IPR017958
domain Asn/Gln amidotransferase 398 - 545 IPR018027

Functions

Description
EC Number
Subcellular Localization
  • Mitochondrion
  • Plastid, chloroplast
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

3 GO annotations of cellular component

Name Definition
chloroplast A chlorophyll-containing plastid with thylakoids organized into grana and frets, or stroma thylakoids, and embedded in a stroma.
glutamyl-tRNA(Gln) amidotransferase complex A protein complex that possesses glutamyl-tRNA(Gln) amidotransferase activity, and therefore creates Gln-tRNA by amidating Glu-tRNA; usually composed of 3 subunits: A, B, and C. Note that the C subunit may not be required in all organisms.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

2 GO annotations of molecular function

Name Definition
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + glutamyl-tRNA(Gln) + ATP = L-glutamate + glutaminyl-tRNA(Gln) + phosphate + ADP.

2 GO annotations of biological process

Name Definition
glutaminyl-tRNAGln biosynthesis via transamidation A tRNA aminoacylation process in which glutaminyl-tRNAGln is formed by a tRNA-dependent two-step pathway. In the first step a non-discriminating glutamyl-tRNAGlx synthetase generates the misacylated L-glutamyl-tRNAGln species, and in the second step it is amidated to the correctly charged L-glutaminyl-tRNAGln by a glutamyl-tRNAGln amidotransferase.
mitochondrial translation The chemical reactions and pathways resulting in the formation of a protein in a mitochondrion. This is a ribosome-mediated process in which the information in messenger RNA (mRNA) is used to specify the sequence of amino acids in the protein; the mitochondrion has its own ribosomes and transfer RNAs, and uses a genetic code that differs from the nuclear code.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P33893 PET112 Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
Q2R2Z0 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Oryza sativa subsp japonica (Rice) PR
Q9FV81 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MALTLLRGMR TPVSSGSNPG LFFAVLRPRL SRFTARAESA QATEPKAAPP PRSIQLATKE
70 80 90 100 110 120
AAEQKTQGFE AVIGIETHVQ LSTVTKAFCS CPYSYGAQPN STVCPTCMGH PGTLPVLNEK
130 140 150 160 170 180
VVECAVKLGL ALNCEISMTS KFDRKQYFYP DLPKGYQISQ FDIPIAKKGH VDLDLPVEFG
190 200 210 220 230 240
GGHRKFGITR VHMEEDAGKL LHSESSSYSQ VDLNRAGVPL LEIVSEPDMR TGIEAAEYGA
250 260 270 280 290 300
ELQRIVRYLG VSNGNMQEGS LRCDVNVSIR PVGQSEFGTK VEIKNMNSFS AINRAIDYEI
310 320 330 340 350 360
SRQILLHKEG QADQIVQETR LWDESSQKTF TMRKKEGLAD YRYFPEPDLP EVVLTSDYIN
370 380 390 400 410 420
EISKSMPELP EAKRRRYENM GLSMQDVLFL ANDDNIGHFY DSTLEHGADA KLAANWIMGD
430 440 450 460 470 480
IAAYLKDEKV SIDEIKLTPL ELSELIASIK NGTISGKIGK EILAELIAKG GTVKGVIEEK
490 500 510 520 530 540
DLVQIADPAA IEAMVDKVIA DNPKQLEQYR AGKTKLQGFF AGQVMKASKG KANPVLLNKI
LGEKLNAN