Q5HN35

PR
Gene name
gatB
Protein name
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
Names
Asp/Glu-ADT subunit B
Species
Staphylococcus epidermidis (strain ATCC 35984 / RP62A)
KEGG Pathway
ser:SERP1437
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

206-276 (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 Q5HN35

Entry ID Method Resolution Chain Position Source
AF-Q5HN35-F1 Predicted AlphaFoldDB

No variants for Q5HN35

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q5HN35

No associated diseases with Q5HN35

3 regional properties for Q5HN35

Type Name Position InterPro Accession
domain Aspartyl/Glutamyl-tRNA(Gln) amidotransferase, subunit B/E, catalytic 5 - 284 IPR006075
conserved_site Glutamyl-tRNA(Gln) amidotransferase, subunit B, conserved site 141 - 155 IPR017958
domain Asn/Gln amidotransferase 325 - 472 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
MHFETVIGLE VHVELKTDSK MFSPSPAHFG AEPNSNTNVI DLAYPGVLPV VNRRAVDWAM
70 80 90 100 110 120
RASMALNMDI ATNSKFDRKN YFYPDNPKAY QISQFDQPIG ENGYIDIEVD GETKRIGITR
130 140 150 160 170 180
LHMEEDAGKS THKDGYSLVD LNRQGTPLIE IVSEPDIRSP KEAYAYLEKL RSIIQYTGVS
190 200 210 220 230 240
DCKMEEGSLR CDANISLRPY GQKEFGTKTE LKNLNSFNYV KKGLEYEEKR QEEELLNGGE
250 260 270 280 290 300
IGQETRRFDE STGKTILMRV KEGSDDYRYF PEPDIVPLYV DEDWKARVRE TIPELPDERK
310 320 330 340 350 360
AKYVNDLGLP EYDAHVLTLT KEMSDFFEGA IDHGADVKLT SNWLMGGVNE YLNKNQVELK
370 380 390 400 410 420
DTQLTPENLA GMIKLIEDGT MSSKIAKKVF PELAENGGDA KQIMEDKGLV QISDEATLLK
430 440 450 460 470
FVTDALDNNP QSIEDYKNGK GKAMGFLVGQ IMKASKGQAN PQKVNSLLKQ ELDNR