C5W865
Gene name |
cysI |
Protein name |
Sulfite reductase [NADPH] hemoprotein beta-component |
Names |
SiR-HP, SiRHP |
Species |
Escherichia coli (strain B / BL21-DE3) |
KEGG Pathway |
ebl:ECD_02608 |
EC number |
1.8.1.2: 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 C5W865
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-C5W865-F1 | Predicted | AlphaFoldDB |
No variants for C5W865
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C5W865 | |||||
No associated diseases with C5W865
5 regional properties for C5W865
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Nitrite/Sulfite reductase ferredoxin-like domain | 81 - 138 | IPR005117-1 |
| domain | Nitrite/Sulfite reductase ferredoxin-like domain | 355 - 417 | IPR005117-2 |
| binding_site | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | 429 - 447 | IPR006066-1 |
| binding_site | Nitrite/sulphite reductase iron-sulphur/sirohaem-binding site | 477 - 495 | IPR006066-2 |
| domain | Nitrite/sulphite reductase 4Fe-4S domain | 173 - 331 | IPR006067 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.8.1.2 | With NAD(+) or NADP(+) as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| 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. |
5 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. |
| 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. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
| sulfite reductase (NADPH) activity | Catalysis of the reaction: hydrogen sulfide + 3 NADP+ + 3 H2O = sulfite + 3 NADPH + 3 H+. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| cysteine biosynthetic process | The chemical reactions and pathways resulting in the formation of cysteine, 2-amino-3-mercaptopropanoic acid. |
| hydrogen sulfide biosynthetic process | The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S. |
| sulfate assimilation | The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSEKHPGPLV | VEGKLTDAER | MKLESNYLRG | TIAEDLNDGL | TGGFKGDNFL | LIRFHGMYQQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DDRDIRAERA | EQKLEPRHAM | LLRCRLPGGV | ITTKQWQAID | KFAGENTIYG | SIRLTNRQTF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QFHGILKKNV | KPVHQMLHSV | GLDALATAND | MNRNVLCTSN | PYESQLHAEA | YEWAKKISEH |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLPRTRAYAE | IWLDQEKVAT | TDEEPILGQT | YLPRKFKTTV | VIPPQNDIDL | HANDMNFVAI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AENGKLVGFN | LLVGGGLSIE | HGNKKTYART | ASEFGYLPLE | HTLAVAEAVV | TTQRDWGNRT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| DRKNAKTKYT | LERVGVETFK | AEVERRAGIK | FEPIRPYEFT | GRGDRIGWVK | GIDDNWHLTL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| FIENGRILDY | PARPLKTGLL | EIAKIHKGDF | RITANQNLII | AGVPESEKAK | IEKIAKESGL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| MNAVTPQREN | SMACVSFPTC | PLAMAEAERF | LPSFIDNIDN | LMAKHGVSDE | HIVMRVTGCP |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NGCGRAMLAE | VGLVGKAPGR | YNLHLGGNRI | GTRIPRMYKE | NITEPEILAS | LDELIGRWAK |
| 550 | 560 | ||||
| EREAGEGFGD | FTVRAGIIRP | VLDPARDLWD |