Glutamate-1-semialdehyde 2,1-aminomutase
Details
- Name
- Glutamate-1-semialdehyde 2,1-aminomutase
- Synonyms
- 5.4.3.8
- Glutamate-1-semialdehyde aminotransferase
- gsa
- GSA-AT
- Gene Name
- hemL
- Organism
- Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1)
- Amino acid sequence
>lcl|BSEQ0003099|Glutamate-1-semialdehyde 2,1-aminomutase MVTSSPFKTIKSDEIFAAAQKLMPGGVSSPVRAFKSVGGQPIVFDRVKDAYAWDVDGNRY IDYVGTWGPAICGHAHPEVIEALKVAMEKGTSFGAPCALENVLAEMVIDAVPSIEMVRFV NSGTEACMAVLRLMRAYTGRDKIIKFEGCYHGHADMFLVKAGSGVATLGLPDSPGVPKST TANTLTAPYNDLEAVKALFAENPGEIAGVILEPIVGNSGFIVPDAGFLEGLREITLEHDA LLVFDEVMTGFRIAYGGVQEKFGVTPDLTTLGKIIGGGLPVGAYGGKREIMQLVAPAGPM YQAGTLSGNPLAMTAGIKTLELLRQPATYEYLDQITKRLSDGLLAIAQETGHAACGGQVS GMFGFFFTEGPVHNYEDAKKSDLQKFSRFHRGMLEQGIYLAPSQFEAGFTSLAHTEEDID ATLAAARTVMSAL
- Number of residues
- 433
- Molecular Weight
- 46115.52
- Theoretical pI
- 4.95
- GO Classification
- Functionsglutamate-1-semialdehyde 2,1-aminomutase activity / pyridoxal phosphate binding / transaminase activityProcesseschlorophyll biosynthetic process / protoporphyrinogen IX biosynthetic processComponentscytoplasm
- General Function
- Transaminase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Aminotran_3 (PF00202)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasm
- Gene sequence
>lcl|BSEQ0037143|Glutamate-1-semialdehyde 2,1-aminomutase (hemL) ATGCCGGGTGGCGTCAGTTCGCCGGTGCGCGCTTTTAAATCCGTTGGCGGTCAACCCATC GTCTTCGATCGCGTGAAAGATGCCTACGCCTGGGATGTGGACGGCAATCGCTACATCGAC TACGTCGGCACCTGGGGCCCCGCCATCTGCGGGCATGCGCATCCAGAAGTCATCGAAGCC CTCAAAGTTGCCATGGAAAAGGGCACAAGCTTTGGGGCACCCTGTGCATTGGAAAACGTC CTCGCCGAAATGGTGATCGATGCAGTGCCTAGCATCGAGATGGTGCGCTTCGTCAATTCC GGCACCGAAGCCTGTATGGCGGTGCTGCGCTTGATGCGGGCTTATACGGGCCGCGACAAA ATCATCAAGTTCGAAGGCTGCTACCACGGCCACGCTGACATGTTCTTGGTCAAGGCGGGG TCTGGGGTGGCGACCCTCGGCCTGCCAGACTCGCCCGGCGTACCCAAGAGCACCACGGCC AATACCCTGACCGCGCCCTACAACGATCTCGAGGCAGTCAAGGCACTGTTCGCGGAAAAT CCCGGTGAGATTGCTGGGGTCATTCTTGAGCCGATCGTCGGTAACTCGGGCTTCATCGTC CCAGATGCTGGCTTCTTGGAAGGATTGCGGGAAATCACGCTGGAGCATGATGCCCTGCTG GTCTTTGATGAAGTGATGACTGGCTTCCGGATTGCTTACGGTGGCGTGCAAGAAAAGTTT GGCGTTACGCCTGACCTGACCACCTTGGGCAAAATCATCGGTGGCGGCCTACCGGTGGGT GCCTACGGCGGTAAACGCGAGATCATGCAGCTGGTCGCGCCGGCTGGCCCGATGTACCAA GCGGGTACTCTGTCGGGGAACCCCTTGGCGATGACGGCTGGGATTAAAACCCTGGAGCTG CTGCGCCAGCCTGCCACCTACGAATATCTTGACCAGATCACCAAGCGCCTGAGTGATGGT TTGTTGGCGATCGCCCAAGAAACCGGTCATGCGGCTTGCGGTGGTCAGGTGAGTGGTATG TTCGGCTTCTTCTTCACGGAAGGCCCTGTGCACAACTACGAAGACGCCAAAAAGTCGGAC TTGCAAAAGTTCAGTCGCTTCCATCGCGGCATGCTGGAGCAAGGCATCTACCTTGCCCCC TCGCAGTTTGAGGCGGGCTTTACCTCGTTGGCTCACACTGAAGAGGACATTGATGCCACG CTGGCAGCTGCTCGTACGGTGATGAGTGCGCTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P24630 UniProtKB Entry Name GSA_SYNP6 GenBank Protein ID 581789 GenBank Gene ID X53695 - General References
- Grimm B, Bull A, Breu V: Structural genes of glutamate 1-semialdehyde aminotransferase for porphyrin synthesis in a cyanobacterium and Escherichia coli. Mol Gen Genet. 1991 Jan;225(1):1-10. [Article]
- Grimm B, Smith AJ, Kannangara CG, Smith M: Gabaculine-resistant glutamate 1-semialdehyde aminotransferase of Synechococcus. Deletion of a tripeptide close to the NH2 terminus and internal amino acid substitution. J Biol Chem. 1991 Jul 5;266(19):12495-501. [Article]
- Sugita C, Ogata K, Shikata M, Jikuya H, Takano J, Furumichi M, Kanehisa M, Omata T, Sugiura M, Sugita M: Complete nucleotide sequence of the freshwater unicellular cyanobacterium Synechococcus elongatus PCC 6301 chromosome: gene content and organization. Photosynth Res. 2007 Jul-Sep;93(1-3):55-67. Epub 2007 Jan 9. [Article]
- Grimm B, Bull A, Welinder KG, Gough SP, Kannangara CG: Purification and partial amino acid sequence of the glutamate 1-semialdehyde aminotransferase of barley and synechococcus. Carlsberg Res Commun. 1989;54(2):67-79. [Article]
- Hennig M, Grimm B, Contestabile R, John RA, Jansonius JN: Crystal structure of glutamate-1-semialdehyde aminomutase: an alpha2-dimeric vitamin B6-dependent enzyme with asymmetry in structure and active site reactivity. Proc Natl Acad Sci U S A. 1997 May 13;94(10):4866-71. [Article]