Q9JUD9
Gene name |
cysI |
Protein name |
Sulfite reductase [NADPH] hemoprotein beta-component |
Names |
SiR-HP, SiRHP |
Species |
Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 / Z2491) |
KEGG Pathway |
nma:NMA1362 |
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 Q9JUD9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9JUD9-F1 | Predicted | AlphaFoldDB |
No variants for Q9JUD9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9JUD9 | |||||
No associated diseases with Q9JUD9
1 regional properties for Q9JUD9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Phosphoadenosine phosphosulphate reductase | 29 - 257 | IPR002500 |
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 |
| MTVQTKTKGL | AWQEKPLSDN | ERLKTESNFL | RGTILDDLKD | PLTGGFKGDN | FQLIRFHGMY |
| 70 | 80 | 90 | 100 | 110 | 120 |
| EQDDRDIRAE | RAEAKLEPLK | FMLLRCRLPG | GIIKPSQWIE | LDKFARENSH | YRSIRLTNRQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TFQFHGVPKA | KLQTMHRLLH | KLGLDSIATA | ADMNRNVLCT | SNPIESELHR | QAYEYAKKIS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| EHLLPRTRGY | LDVWVDGKKV | QSSDDFLQED | EPILGKTYLP | RKFKTAVVIP | PLNDVDCYGN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DLDFVAISDG | NGQLAGFNVL | AGGGLSMEHG | NTKTYPNISL | ELGFVPPEHA | LKAAEAVVTT |
| 310 | 320 | 330 | 340 | 350 | 360 |
| QRDFGNRSDR | KNARTRYTIQ | NMGLDNFRAE | VERRMGMPFE | PIRPFKFTGR | GDRIGWVKGI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DGNWHLTLFI | ESGRLVDEGG | KQLLTGVLEI | AKIHKGDFRI | TANQNLIVAN | VPEGGKARIE |
| 430 | 440 | 450 | 460 | 470 | 480 |
| QLARSYGLIH | DGVSKLRENA | MSCVSFPTCP | LAMAEAERVL | PDFIGELDKI | MAKHGTSDDY |
| 490 | 500 | 510 | 520 | 530 | 540 |
| IVTRITGCPN | GCGRAMLAEI | GLVGKAVGRY | NLHIGGDREG | VRIPRLYKEN | ITLPEILAEL |
| 550 | 560 | 570 | 580 | ||
| DDLIGKWAAE | RNIGEGFGDF | AIRTGIVKPV | LNAPVDFWDA | SKAVAIARA |