| Identification |
|---|
| HMDB Protein ID
| HMDBP01952 |
| Secondary Accession Numbers
| |
| Name
| Glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial |
| Synonyms
|
- Cytochrome oxidase assembly factor PET112 homolog
- Glu-ADT subunit B
- Cytochrome c oxidase assembly factor PET112 homolog
|
| Gene Name
| PET112 |
| Protein Type
| Enzyme |
| Biological Properties |
|---|
| General Function
| Involved in carbon-nitrogen ligase activity, with glutamine as amido-N-donor |
| Specific Function
| Allows the formation of correctly charged Gln-tRNA(Gln) through the transamidation of misacylated Glu-tRNA(Gln) in the mitochondria. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln).
|
| Pathways
|
Not Available
|
| Reactions
|
| Adenosine triphosphate + L-glutamyl-tRNA(Gln) + L-Glutamine → ADP + Phosphate + L-glutaminyl-tRNA(Gln) + L-Glutamic acid |
details
|
|
| GO Classification
|
| Biological Process |
| glutaminyl-tRNAGln biosynthesis via transamidation |
| mitochondrial translation |
| Cellular Component |
| mitochondrion |
| glutamyl-tRNA(Gln) amidotransferase complex |
| Function |
| catalytic activity |
| ligase activity |
| carbon-nitrogen ligase activity, with glutamine as amido-n-donor |
| ligase activity, forming carbon-nitrogen bonds |
| Molecular Function |
| ATP binding |
| glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity |
| translation factor activity, nucleic acid binding |
| Process |
| macromolecule biosynthetic process |
| cellular macromolecule biosynthetic process |
| translation |
| metabolic process |
| biosynthetic process |
|
| Cellular Location
|
- Mitochondrion
|
| Gene Properties |
|---|
| Chromosome Location
| 4 |
| Locus
| 4q31.3 |
| SNPs
| PET112L |
| Gene Sequence
|
>1674 bp
ATGGCGGCGCCCATGCTGCGCTGGGGCTGCCGTGGAAGACGTTGGGCTTTCGCCCGGGTT
GACGGTGGTTCTTGCCACCGAAGAGGGGCTCCGACTGGGTCCACATCCAACCAGATTAGG
GGAGAGAGCTCAGTGGCTCAGCAGCCCCTCCACACGGCCCAGAAGACGAGGAAAGGTGAA
CACAAATGGGCTGCTGTGGTAGGTTTGGAAATTCATGCCCAGATTTCCTCCAACTCTAAA
CTCTTCTCTGGATCTCAAGTTCGCTTTTCAGCACCTCCAAATTCTTTGGTTTCTTTTTTT
GATGCATCTCTACCTGGAACTTTGCCGGTTCTCAACAGGAGGTGTGTAGAAGCGGCGGTG
ATGACAGGCCTGGCTCTGAACTGCCACATAAACAAGAAGTCCTTGTTTGACAGGAAGCAC
TACTTCTATGCAGACCTCCCTGCAGGCTACCAAATTACCCAGCAGAGGCTCCCAATTGCT
GTGAATGGGAGCTTGATATATGGCGTCTGTGCAGGGAAGAAGCAGAGTCAGGTGATCCCC
AAGACGGTGAGGATCAAGCAGATCCAGTTGGAGCAAGACAGTGGCAAAAGCCTCCACGAC
AACCTGAGGTCTCAGACGCTCATTGATTTGAACAGGGCAGGAGTGGGCCTTCTGGAGGTG
GTCCTGGAGCCCGACATGTCCTGTGGAGAAGAGGCGGCAACAGCTGTCAGGGAGCTGCAG
CTGATCCTTCAAGCCCTGGGGACCAGCCAGGCGAACATGGCAGAGGGCCAGTTGAGAGTG
GATGCCAATATATCCGTGCATCACCCTGGGGAGCCTTTGGGCGTTCGAACGGAAGTGAAG
AATCTCAACAGCATCAGGTTCCTGGCCAAAGCCATAGACTATGAAATTCAGAGGCAAATC
AATGAACTTGAGAATGGAGGTGAAATTCTGAACGAAACACGCTCATTTCATCACAAGCTG
GGGTGCACCATGTCAATGAGAGACAAAGAAGGAAAACAGGACTACAGGTTCATGCCAGAA
CCCAACCTGCCTCCCCTGGTGCTCTACGACGCCACATCTCTGCCCGCAGGTGCAGACCCA
CAGCAAGTGATCAATATTGACCAGATTCGGGAGACACTCCCGGAGCTCCCCAGTGTGACC
CGAGAGAAGCTTGTCCAACAGTATGGGATGCTGCTGGAACACAGCTTCACTTTGCTGAAC
GAAGTCGGCCTACTGGAGTTCTTCCAAAATGTGATAAAAGAAACTAGGGCAGAGCCAAAA
AAGGTGACTAGTTGGGTCCTCAACACTTTTCTGGGCTATTTAAAGCAACAGAACCTCGCT
GTCAGTGAGAGTCCTGTCACACCCTCTGCACTCGCTGAGCTTCTTGACCTGCTGGACAGC
AGAACAATTTCTTCATCAGCAGCTAAACAGGTGTTTGAGGAACTGTGGAAGAGGGAAGGC
AAGACTCCAGGGCAGATTGTTTCAGAAAAGCAGCTTGAACTGATGCAGGACCAGGGGGCA
CTGGAGCAGCTCTGCCACTCTGTGATGGAGGCCCATCCTCAAGTGGTAATGGATGTGAAG
AACAGAAACCCCAGAGCTATAAATAAACTGATTGGGTTGGTCCGGAAAGCGACTCAAAGC
CGAGCAGATCCAGTCATGATAAAGGAGATCCTGGAGAAGAAGCTGTCATTGTGA
|
| Protein Properties |
|---|
| Number of Residues
| 557 |
| Molecular Weight
| 61863.57 |
| Theoretical pI
| 8.631 |
| Pfam Domain Function
|
|
| Signals
|
Not Available
|
|
Transmembrane Regions
|
Not Available
|
| Protein Sequence
|
>Probable glutamyl-tRNA(Gln) amidotransferase subunit B, mitochondrial
MAAPMLRWGCRGRRWAFARVDGGSCHRRGAPTGSTSNQIRGESSVAQQPLHTAQKTRKGE
HKWAAVVGLEIHAQISSNSKLFSGSQVRFSAPPNSLVSFFDASLPGTLPVLNRRCVEAAV
MTGLALNCHINKKSLFDRKHYFYADLPAGYQITQQRLPIAVNGSLIYGVCAGKKQSQVIP
KTVRIKQIQLEQDSGKSLHDNLRSQTLIDLNRAGVGLLEVVLEPDMSCGEEAATAVRELQ
LILQALGTSQANMAEGQLRVDANISVHHPGEPLGVRTEVKNLNSIRFLAKAIDYEIQRQI
NELENGGEILNETRSFHHKLGCTMSMRDKEGKQDYRFMPEPNLPPLVLYDATSLPAGADP
QQVINIDQIRETLPELPSVTREKLVQQYGMLLEHSFTLLNEVGLLEFFQNVIKETRAEPK
KVTSWVLNTFLGYLKQQNLAVSESPVTPSALAELLDLLDSRTISSSAAKQVFEELWKREG
KTPGQIVSEKQLELMQDQGALEQLCHSVMEAHPQVVMDVKNRNPRAINKLIGLVRKATQS
RADPVMIKEILEKKLSL
|
| External Links |
|---|
| GenBank ID Protein
| Not Available |
| UniProtKB/Swiss-Prot ID
| O75879 |
| UniProtKB/Swiss-Prot Entry Name
| GATB_HUMAN |
| PDB IDs
|
Not Available |
| GenBank Gene ID
| AF026851 |
| GeneCard ID
| PET112L |
| GenAtlas ID
| PET112L |
| HGNC ID
| HGNC:8849 |
| References |
|---|
| General References
| - Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
- Gevaert K, Goethals M, Martens L, Van Damme J, Staes A, Thomas GR, Vandekerckhove J: Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides. Nat Biotechnol. 2003 May;21(5):566-9. Epub 2003 Mar 31. [PubMed:12665801 ]
- Zhang QH, Ye M, Wu XY, Ren SX, Zhao M, Zhao CJ, Fu G, Shen Y, Fan HY, Lu G, Zhong M, Xu XR, Han ZG, Zhang JW, Tao J, Huang QH, Zhou J, Hu GX, Gu J, Chen SJ, Chen Z: Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells. Genome Res. 2000 Oct;10(10):1546-60. [PubMed:11042152 ]
- Petruzzella V, Tiranti V, Fernandez P, Ianna P, Carrozzo R, Zeviani M: Identification and characterization of human cDNAs specific to BCS1, PET112, SCO1, COX15, and COX11, five genes involved in the formation and function of the mitochondrial respiratory chain. Genomics. 1998 Dec 15;54(3):494-504. [PubMed:9878253 ]
|
