Q2S1B9

PR
Gene name
gatB
Protein name
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Names
Asp/Glu-ADT subunit B
Species
Salinibacter ruber (strain DSM 13855 / M31)
KEGG Pathway
sru:SRU_1902
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

91-171 (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 Q2S1B9

Entry ID Method Resolution Chain Position Source
AF-Q2S1B9-F1 Predicted AlphaFoldDB

No variants for Q2S1B9

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q2S1B9

No associated diseases with Q2S1B9

3 regional properties for Q2S1B9

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 6 - 288 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 144 - 158 IPR017958
domain Asn/Gln amidotransferase 328 - 474 IPR018027

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

3 GO annotations of molecular function

Name Definition
asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity Catalysis of the reaction: L-glutamine + aspartyl-tRNA(Asn) + ATP = L-glutamate + asparaginyl-tRNA(Asn) + phosphate + ADP.
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.

1 GO annotations of biological process

Name Definition
translation The cellular metabolic process in which a protein is formed, using the sequence of a mature mRNA or circRNA molecule to specify the sequence of amino acids in a polypeptide chain. Translation is mediated by the ribosome, and begins with the formation of a ternary complex between aminoacylated initiator methionine tRNA, GTP, and initiation factor 2, which subsequently associates with the small subunit of the ribosome and an mRNA or circRNA. Translation ends with the release of a polypeptide chain from the ribosome.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAYERYEPVI GLEVHVQLQT NAKIFSPDAA AFGAAPNTQV DPISLGHPGT LPVLNETVVK
70 80 90 100 110 120
HALRLGVATH CSIADRSAFA RKHYFYPDLP KGYQISQYDT PICYDGYLEV FPGEEEDASP
130 140 150 160 170 180
SAPDSRRVGL TRIHMEEDAG KSVHASAGGT TRLDNNRCGV PLLEMVTEPD LRSPREASLF
190 200 210 220 230 240
LQRLRQLVRY LGISDGNMEE GSLRCDANVS VRPQGREAFG TRTELKNMNS MRHVEQALDY
250 260 270 280 290 300
EIARQIAAEE RGESITQQTL LWDADAGTTR PMRSKEEAHD YRYLPDPDLV EVRIEDATVD
310 320 330 340 350 360
EVRANLPELP RARRRRFVEE VGLPAYDAGV LTEERAVADY FEEALRHLYK RTKGGDTDAQ
370 380 390 400 410 420
AKAVSNFIMT EVMRVLNERD LSVSELGVGP ERLAQLVFLR LQDKVSSNGA QEVFEAMLDA
430 440 450 460 470 480
PDKSAGRIAD ERDLIQVTDR GAIAPVVEDV LNDNPDKVNT YLGGKDGLLG FFIGQVMQRF
490 500
DGSPNPELVR SLLREKLDAR RDTANVDE