Home/GT Families/GT7/mig-22
mig-22
Caenorhabditis elegans · Chondroitin sulfate synthase mig-22 (EC 2.4.1.175; 2.4.1.226)
GT7Model organism · annotation ≥ 4Fold GT-AInverting
External resources
Identification and annotation
| CAZy family | GT7 · CAZy entry |
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| Gene symbol | mig-22 |
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| Synonyms / alternate names | - pfc-1
- Abnormal cell migration
- Chondroitin-polymerizing factor
- N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 1
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| UniProt accession | P45895 |
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| NCBI Gene ID | 176231 |
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| Source species | Caenorhabditis elegans |
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| Taxonomic domain | Eukaryota |
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| UniProt annotation level | 5 |
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Function and localisation
| Enzyme function | Chondroitin sulfate synthase mig-22 (EC 2.4.1.175; 2.4.1.226) |
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| Subcellular location | - Golgi apparatus
- Golgi stack membrane
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Structure and mechanism
| Fold type | GT-A |
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| Catalytic mechanism | Inverting |
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| Cation dependence | Yes (Mn2+) |
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| Oligomeric state | Interacts with sqv-5 |
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| PDB structures | not curated |
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Donor and acceptor specificity
| Sugar nucleotide donor | - UDP-N-acetyl-alpha-D-galactosamine
- UDP-alpha-D-glucuronate
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| Donor CCD code(s) | UD2, UGA |
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| Acceptor substrate(s) | - 3-O-(beta-D-GlcA-(1->3)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein]
- 3-O-{beta-D-GlcA-(1->3)-[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein]
- 3-O-(beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein]
- 3-O-{[beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)](n)-beta-D-GalNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl}-L-seryl-[protein]
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| Acceptor CCD / GlycoCT | not curated |
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Protein sequences
Full protein sequence
804 aa
MVGGGRTGIHLLLGFLIGAALALFFFSSTPSIDLTSSLAAFTSCQNQETETNVLEPSALEKGRVYKDLSEHWIVHQDDMPAPPHNQDATPKVTRTRFAATELGTRERVMAAVMAESALALSINATLGRHVPRVHLFADSSRIDNDLAQLTNLSPYKLNGQKTHSMVLGLLFNMTVHNNYDWFLLAKDSTYINPFVLLRMIDTMNWNEPVVMGEAAEDGSGRCRLDTGMLLSQPAMHALMNNRNACNNFALAADDDQLAFEKCIQIATNLTCKPLHQGVRYEVWRGAERADSPAAHDSIEDWKHSPAFKRALAVPRLLSDADASALHDYFVRVEMQRADREIIKMEAELSRLAEQEARETGEAISWPPALPPYAKPPNRYQVSTWEYFTMTELFRSEPNQNVRRLEGKDFDDVAEVVVAARQQVESEEPELEFVQLRNGYRVFDPRRGMDYMVDLTYRKTVNEMPEVDNRFESDNEAAHEESLKEIVVERRVHVSRMIASTQLMNQAPYVKEDTDVTVVIPVASEKDVLPARKLLARQARLCLFPTEEARKTRMVVAVFPLIESRSVTAITNDMEELKRRCKRSLLETDVLPVHPAVSTEGKGTAAAAALDDAVDRYGANTIYLLLSPHADVQKEFFDRARINTIKHYQVFFPVPFVEYHPTISGMEMTEKEEKETPTEQAREAALSRLRDGVEPKRKRTLIVQKEHGRFDSQDFSCFAVYGVDYVTARAKFGQNERRNDLISAFLGQDSIHVLRAVEPTLRIRYHKRSCDMESIDTEDIARCLDSKKENVAAKDQLAKLLFHEK
Catalytic domain sequence
555 aa
RNACNNFALAADDDQLAFEKCIQIATNLTCKPLHQGVRYEVWRGAERADSPAAHDSIEDWKHSPAFKRALAVPRLLSDADASALHDYFVRVEMQRADREIIKMEAELSRLAEQEARETGEAISWPPALPPYAKPPNRYQVSTWEYFTMTELFRSEPNQNVRRLEGKDFDDVAEVVVAARQQVESEEPELEFVQLRNGYRVFDPRRGMDYMVDLTYRKTVNEMPEVDNRFESDNEAAHEESLKEIVVERRVHVSRMIASTQLMNQAPYVKEDTDVTVVIPVASEKDVLPARKLLARQARLCLFPTEEARKTRMVVAVFPLIESRSVTAITNDMEELKRRCKRSLLETDVLPVHPAVSTEGKGTAAAAALDDAVDRYGANTIYLLLSPHADVQKEFFDRARINTIKHYQVFFPVPFVEYHPTISGMEMTEKEEKETPTEQAREAALSRLRDGVEPKRKRTLIVQKEHGRFDSQDFSCFAVYGVDYVTARAKFGQNERRNDLISAFLGQDSIHVLRAVEPTLRIRYHKRSCDMESIDTEDIARCLDSKKENVAAKDQL
