Q2R2Z0

PR
Gene name
GATB
Protein name
Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial
Names
Glu-AdT subunit B
Species
Oryza sativa subsp japonica (Rice)
KEGG Pathway
osa:4350686
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

1-86 (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 Q2R2Z0

Entry ID Method Resolution Chain Position Source
AF-Q2R2Z0-F1 Predicted AlphaFoldDB

No variants for Q2R2Z0

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2R2Z0

No associated diseases with Q2R2Z0

3 regional properties for Q2R2Z0

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 67 - 354 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 208 - 222 IPR017958
domain Asn/Gln amidotransferase 393 - 540 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
C5Y3V8 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Sorghum bicolor (Sorghum) (Sorghum vulgare) PR
Q9FV81 GATB Glutamyl-tRNA(Gln) amidotransferase subunit B, chloroplastic/mitochondrial Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MALTLLRGMR TPVVARRNAG LFFTTLQSPL LSRFTMRAES ARAAAPKSIQ LATKEAAEQK
70 80 90 100 110 120
AQGFEAVIGI ETHVQLSTVT KAFCSCPYSY GSQPNSTVCP TCMGHPGTLP VLNAKVVECA
130 140 150 160 170 180
VRLGLALNCE IAMTSKFDRK QYFYPDLPKG YQISQFDIPI AKEGYLDLDL PVEFGGGHRR
190 200 210 220 230 240
FGVTRVHMEE DAGKLLHSES GSYSQVDLNR AGVPLLEIVS EPDMRTGIEA AEYGAELQRL
250 260 270 280 290 300
VRYLGVSNGN MQEGSLRCDV NVSVRPIGQS NFGTKVEIKN MNSFSAISRA IDYEISRQIL
310 320 330 340 350 360
LHKEGQADQI VQETRLWDES SQKTFTMRKK EGLADYRYFP EPDLPEVVLT SEYIDEIQNS
370 380 390 400 410 420
MPELPEAKRR RFENMGLSMQ DVLFLANDDN VARFFDSTLE HGADAKLAAN WIMGDIAAYL
430 440 450 460 470 480
KNEKLSIDEI KLTPLELSEL IASIRNGTIS GKIGKEILIE LIAKGGTVKS VIEEKDLVQI
490 500 510 520 530 540
ADPAAIEAMV DQVLADNPKQ LEQYRSGKTK LQGFFAGQVM KASKGKANPV LLNKILGEKL
KANS