A1JJS8
Gene name |
cysG1 |
Protein name |
Siroheme synthase 1 |
Names |
|
Species |
Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 / 8081) |
KEGG Pathway |
yen:YE0761 |
EC number |
1.3.1.76: With NAD(+) or NADP(+) as acceptor |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for A1JJS8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1JJS8-F1 | Predicted | AlphaFoldDB |
No variants for A1JJS8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1JJS8 | |||||
No associated diseases with A1JJS8
7 regional properties for A1JJS8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Tetrapyrrole methylase | 217 - 426 | IPR000878 |
| conserved_site | Uroporphiryn-III C-methyltransferase, conserved site | 220 - 234 | IPR003043-1 |
| conserved_site | Uroporphiryn-III C-methyltransferase, conserved site | 295 - 328 | IPR003043-2 |
| domain | Uroporphyrin-III C-methyltransferase | 215 - 448 | IPR006366 |
| domain | Sirohaem synthase, N-terminal | 4 - 206 | IPR006367 |
| domain | Sirohaem synthase, dimerisation domain | 150 - 206 | IPR019478 |
| domain | Siroheme synthase, central domain | 120 - 145 | IPR028281 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.3.1.76 | With NAD(+) or NADP(+) as acceptor |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| precorrin-2 dehydrogenase activity | Catalysis of the reaction: NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin. |
| sirohydrochlorin ferrochelatase activity | Catalysis of the reaction: siroheme + 2 H+ = Fe(2+) + sirohydrochlorin. |
| uroporphyrin-III C-methyltransferase activity | Catalysis of the reaction: 2 S-adenosyl-L-methionine + uroporphyrin III = 2 S-adenosyl-L-homocysteine + precorrin-2. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cobalamin biosynthetic process | The chemical reactions and pathways resulting in the formation of cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. |
| methylation | The process in which a methyl group is covalently attached to a molecule. |
| siroheme biosynthetic process | The chemical reactions and pathways resulting in the formation of siroheme, a tetrahydroporphyrin with adjacent, reduced pyrrole rings. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDYLPLFADL | KRRPVLVVGG | GEVAARKIDL | LHRAGAQVRV | VAQTLSSELE | QLHQDGRIHW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LALDFLPEQL | DEVFLVIAAT | NDTALNAAVF | AAADQRHLLA | NVVDDQPRCS | FIFPSIVDRS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLVVAISSAG | QAPVLARILR | EKLEALLPSS | LGDMAAVAGR | WRGRVKQHIA | SMGERRRFWE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| NAFSGRFASL | ISRGQLAQAE | EELQLSLEGQ | NRNQGEVALV | GAGPGDPGLL | TLRGLQVIQQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| ADVVLYDHLV | SPEVLDLVRR | DAQRICVGKR | AGAHSVAQEE | TNQLLVTLAQ | RGKRVVRLKG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GDPFIFGRGG | EELQVVARAG | IPFHIVPGVT | AASGATAYAG | IPLTHRDYAQ | SVTFITGHCR |
| 370 | 380 | 390 | 400 | 410 | 420 |
| ADGDDVDWQA | LARGRQTLAI | YMGTVKAAEI | SQQLIAHGRA | STTPVAVIGR | GTRADQQVLT |
| 430 | 440 | 450 | 460 | 470 | |
| GTLAELELLA | HQAPTPALLV | IGEVVDLHHQ | IAWFGQQPQT | EQAISPSVVN | LA |