A0KQJ4
Gene name |
cysG3 |
Protein name |
Siroheme synthase 3 |
Names |
|
Species |
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) |
KEGG Pathway |
aha:AHA_4121 |
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 A0KQJ4
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A0KQJ4-F1 | Predicted | AlphaFoldDB |
No variants for A0KQJ4
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0KQJ4 | |||||
No associated diseases with A0KQJ4
7 regional properties for A0KQJ4
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Tetrapyrrole methylase | 218 - 427 | IPR000878 |
| conserved_site | Uroporphiryn-III C-methyltransferase, conserved site | 221 - 235 | IPR003043-1 |
| conserved_site | Uroporphiryn-III C-methyltransferase, conserved site | 296 - 329 | IPR003043-2 |
| domain | Uroporphyrin-III C-methyltransferase | 216 - 448 | IPR006366 |
| domain | Sirohaem synthase, N-terminal | 4 - 203 | IPR006367 |
| domain | Sirohaem synthase, dimerisation domain | 150 - 207 | IPR019478 |
| domain | Siroheme synthase, central domain | 119 - 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 |
| MDYLPIFCRL | DNKPVLLVGG | GEVAERKARL | LLDAGAQLTV | VAPELDPELA | ELAANGSIEW |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LAGEFAPQQL | TGKWLVVAAT | DRREVNALVY | QSANQARIFA | NVVDDPKRSS | FIMPSIIDRS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PLMVAISSGG | KAPVLARLLR | EKLEALLPQH | LGAVAAFAGS | LRERVKARFA | SMGERRRFWE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RLLGADRLGQ | ALARGDSASA | NQLADSLFAD | ESQSGGEVVL | VGAGPGDPGL | LTLHALRQMQ |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QADVVVYDRL | VSDEVMALVR | RDARRIFVGK | QAGNHCVPQE | GINQLLLDEA | KKGQRVVRLK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GGDPFIFGRG | GEELETLVGS | GIGFQVVPGI | TAASGCAAYA | GIPLTHRDHA | QSVRFVTAHG |
| 370 | 380 | 390 | 400 | 410 | 420 |
| KGGAQDLDWP | LLAKDKQTLV | FYMGLSSCTT | IREQLLTHGK | AGDTPVALIE | RGTQPSQRVI |
| 430 | 440 | 450 | 460 | ||
| RGTLAQLPEL | ALGVESPALI | MVGSVVTLAD | QLAWFGQGGA | ADAALASA |