Q9AWB2
Gene name |
SIR (DCP68) |
Protein name |
Sulfite reductase [ferredoxin], chloroplastic |
Names |
GmSiR, Nucleoid DNA-compacting protein of 68 kDa |
Species |
Glycine max (Soybean) (Glycine hispida) |
KEGG Pathway |
|
EC number |
1.8.7.1: With an iron-sulfur protein 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 Q9AWB2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9AWB2-F1 | Predicted | AlphaFoldDB |
No variants for Q9AWB2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9AWB2 | |||||
No associated diseases with Q9AWB2
5 regional properties for Q9AWB2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Nitrite/Sulfite reductase ferredoxin-like domain | 124 - 178 | IPR005117-1 |
| domain | Nitrite/Sulfite reductase ferredoxin-like domain | 414 - 467 | IPR005117-2 |
| binding_site | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | 492 - 510 | IPR006066-1 |
| binding_site | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | 541 - 559 | IPR006066-2 |
| domain | Nitrite/sulphite reductase 4Fe-4S domain | 218 - 396 | IPR006067 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.8.7.1 | With an iron-sulfur protein as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| chloroplast nucleoid | The region of a chloroplast to which the DNA is confined. |
| chloroplast stroma | The space enclosed by the double membrane of a chloroplast but excluding the thylakoid space. It contains DNA, ribosomes and some temporary products of photosynthesis. |
| sulfite reductase complex (NADPH) | A multisubunit iron flavoprotein, which in yeast is composed of 2 alpha and 2 beta subunits. Catalyzes the reduction of sulfite to sulfide. |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| DNA binding | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| metal ion binding | Binding to a metal ion. |
| sulfite reductase (ferredoxin) activity | Catalysis of the reaction: hydrogen sulfide + 3 oxidized ferredoxin + 3 H2O = sulfite + 3 reduced ferredoxin. |
| sulfite reductase activity | Catalysis of the reaction: hydrogen sulfide + acceptor + 3 H2O = sulfite + reduced acceptor. |
5 GO annotations of biological process
| Name | Definition |
|---|---|
| DNA replication | The cellular metabolic process in which a cell duplicates one or more molecules of DNA. DNA replication begins when specific sequences, known as origins of replication, are recognized and bound by initiation proteins, and ends when the original DNA molecule has been completely duplicated and the copies topologically separated. The unit of replication usually corresponds to the genome of the cell, an organelle, or a virus. The template for replication can either be an existing DNA molecule or RNA. |
| negative regulation of DNA-templated transcription | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. |
| plastid chromosome packaging | A process in which plastidial DNA and associated proteins organize into a compact, orderly structure. |
| sulfate assimilation | The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds. |
| sulfide oxidation, using siroheme sulfite reductase | A sulfide oxidation process that proceeds via the reaction catalyzed by siroheme sulfite reductase. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9LZ66 | SIR | Assimilatory sulfite reductase (ferredoxin), chloroplastic | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTTSFGPATT | SAPLKDHKVQ | IPSFHGLRSS | SASALPRNAL | SLPSSTRSLS | LIRAVSTPAQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SETATVKRSK | VEIFKEQSNF | IRYPLNEDIL | TDAPNISEAA | TQLIKFHGSY | QQYNREERGS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RSYSFMIRTK | NPCGKVSNQL | YLTMDDLADQ | FGIGTLRLTT | RQTFQLHGVL | KKDLKTVMGT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IIRNMGSTLG | ACGDLNRNVL | APAAPLARKD | YLFAQQTAEN | IAALLAPQSG | FYYDIWVDGE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KILTSEPPEV | VQARNDNSHG | TNFPDSPEPI | YGTQFLPRKF | KIAVTVPTDN | SVDILTNDIG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| VVVVTDDDGE | PQGFNIYVGG | GMGRTHRLET | TFPRLAEPIG | YVPKEDILYA | VKAIVVTQRE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NGRRDDRKYS | RLKYLISSWG | IEKFRSVVEQ | YYGKKFEPFR | ALPEWEFKSY | LGWHEQGDGK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LFYGLHVDNG | RIGGNMKKTL | REVIEKYNLN | VRITPNQNII | LTDVRAAWKR | PITTTLAQAG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LLQPRFVDPL | NITAMACPAF | PLCPLAITEA | ERGIPNILKR | IRDVFDKVGL | KYSESVVVRI |
| 550 | 560 | 570 | |||
| TGCPNGCARP | YMAELGLVGD | GPNSYQIWLG | GTP |