| General Information |
| MoonProt ID | 4 |
| First appeared in release | 1.0 |
| Name(s) | FdGOGAT Glutamate synthase
Ferredoxin-dependent glutamate synthase, chloroplastic
Fd-GOGAT |
| UniProt ID | Q43155 (GLTB_SPIOL), Reviewed |
| GO terms | GO:0006537 glutamate biosynthetic process
GO:0006541 glutamine metabolic process
GO:0006807 nitrogen compound metabolic process
GO:0008152 metabolic process
GO:0008652 cellular amino acid biosynthetic process
GO:0055114 oxidation-reduction process
GO:0097054 L-glutamate biosynthetic process
GO:0003824 catalytic activity
GO:0015930 glutamate synthase activity
GO:0016041 glutamate synthase (ferredoxin) activity
GO:0016491 oxidoreductase activity
GO:0016638 oxidoreductase activity, acting on the CH-NH2 group of donors
GO:0046872 metal ion binding
GO:0051536 iron-sulfur cluster binding
GO:0051538 3 iron, 4 sulfur cluster binding
GO:0009507 chloroplast
GO:0009536 plastid
GO:0009570 chloroplast stroma |
| Organisms for which functions have been demonstrated | Spinacia oleracea (Spinach, a plant) |
| Sequence length | 1517 |
| FASTA sequence | >sp|Q9CW03|SMC3_MOUSE Structural maintenance of chromosomes protein 3 OS=Mus musculus GN=Smc3 PE=1 SV=2
MYIKQVIIQGFRSYRDQTIVDPFSSKHNVIVGRNGSGKSNFFYAIQFVLSDEFSHLRPEQRLALLHEGTGPRVISAFVEIIFDNSDNRLPIDKEEVSLRRVIGAKKDQYFLDKKMVTKNDVMNLLESAGFSRSNPYYIVKQGKINQMATAPDSQRLKLLREVAGTRVYDERKEESISLMKETEGKREKINELLKYIEERLHTLEEEKEELAQYQKWDKMRRALEYTIYNQELNETRAKLDELSAKRETSGEKSRQLRDAQQDARDKMEDIERQVRELKTKISAMKEEKEQLSAERQEQIKQRTKLELKAKDLQDELAGNSEQRKRLLKERQKLLEKIEEKQKELAETEPKFNSVKEKEERGIARLAQATQERTDLYAKQGRGSQFTSKEERDKWIKKELKSLDQAINDKKRQIAAIHKDLEDTEANKEKNLEQYNKLDQDLNEVKARVEELDRKYYEVKNKKDELQSERNYLWREENAEQQALAAKREDLEKKQQLLRAATGKAILNGIDSINKVLEHFRRKGINQHVQNGYHGIVMNNFECEPAFYTCVEVTAGNRLFYHIVDSDEVSTKILMEFNKMNLPGEVTFLPLNKLDVRDTAYPETNDAIPMISKLRYNPRFDKAFKHVFGKTLICRSMEVSTQLARAFTMDCITLEGDQVSHRGALTGGYYDTRKSRLELQKDVRKAEEELGELEAKLNENLRRNIERINNEIDQLMNQMQQIETQQRKFKASRDSILSEMKMLKEKRQQSEKTFMPKQRSLQSLEASLHAMESTRESLKAELGTDLLSQLSLEDQKRVDALNDEIRQLQQENRQLLNERIKLEGIITRVETYLNENLRKRLDQVEQELNELRETEGGTVLTATTSELEAINKRVKDTMARSEDLDNSIDKTEAGIKELQKSMERWKNMEKEHMDAINHDTKELEKMTNRQGMLLKKKEECMKKIRELGSLPQEAFEKYQTLSLKQLFRKLEQCNTELKKYSHVNKKALDQFVNFSEQKEKLIKRQEELDRGYKSIMELMNVLELRKYEAIQLTFKQVSKNFSEVFQKLVPGGKATLVMKKGDVEGSQSQDEGEGSGESERGSGSQSSVPSVDQFTGVGIRVSFTGKQGEMREMQQLSGGQKSLVALALIFAIQKCDPAPFYLFDEIDQALDAQHRKAVSDMIMELAVHAQFITTTFRPELLESADKFYGVKFRNKVSHIDVITAEMAKDFVEDDTTHG |
| Structure Information |
| PDB ID | Closest homologue is 1LLW with 59.32% identity |
| Quaternary structure | |
| SCOP | NA |
| CATH | NA |
| TM Helix Prediction | no TM helices |
| DisProt Annotation | Not in DisProt |
| Predicted Disorder Regions | 435-441,689-693, 873-875,891-900,901-902, 917-930,967-972,1229-1238,1501-1517 |
| Connections to Disease |
| OMIM ID | |
| Function 1 |
| Function description | FdGOGAT Glutamate synthase, enzyme
2 L-glutamate + 2 oxidized ferredoxin => L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+.
amino acid biosynthesis, L-glutamate biosynthesis |
| References for function | |
| E.C. number | 1.4.7.1 |
| Location of functional site(s) | |
| Cellular location of function | chloroplast |
| Comments | |
| Function 2 |
| Function description | Subunit of UDP-sulfoquinovose synthase |
| References for function | Shimojima M, HoffmannBenning S, Garavito RM, Benning C. Ferredoxin-dependent glutamate synthase moonlights in plant sulfolipid biosynthesis by forming a complex with SQD1. Arch Biochem Biophys. 2005 Apr 1;436(1):206-14. PMID: 15752726 |
| E.C. number | N/A |
| Location of functional site(s) | |
| Cellular location of function | chloroplast |
| Comments | |