Q1LTP1
Gene name |
cysJ |
Protein name |
Sulfite reductase [NADPH] flavoprotein alpha-component |
Names |
SiR-FP |
Species |
Baumannia cicadellinicola subsp Homalodisca coagulata |
KEGG Pathway |
bci:BCI_0218 |
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 Q1LTP1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q1LTP1-F1 | Predicted | AlphaFoldDB |
No variants for Q1LTP1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q1LTP1 | |||||
No associated diseases with Q1LTP1
15 regional properties for Q1LTP1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Flavodoxin-like | 60 - 73 | IPR001094-1 |
| domain | Flavodoxin-like | 108 - 119 | IPR001094-2 |
| domain | Flavodoxin-like | 140 - 150 | IPR001094-3 |
| domain | Flavodoxin-like | 164 - 183 | IPR001094-4 |
| domain | Oxidoreductase FAD/NAD(P)-binding | 453 - 559 | IPR001433 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 266 - 276 | IPR001709-1 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 382 - 389 | IPR001709-2 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 452 - 471 | IPR001709-3 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 477 - 486 | IPR001709-4 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 490 - 501 | IPR001709-5 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 521 - 537 | IPR001709-6 |
| domain | Flavoprotein pyridine nucleotide cytochrome reductase | 544 - 552 | IPR001709-7 |
| domain | Sulfite reductase [NADPH] flavoprotein alpha-component-like, FAD-binding | 229 - 420 | IPR003097 |
| domain | Flavodoxin/nitric oxide synthase | 59 - 197 | IPR008254 |
| domain | FAD-binding domain, ferredoxin reductase-type | 230 - 444 | IPR017927 |
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 | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| FMN binding | Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
| 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 |
| MTQQNAPKDL | PPLSAEQLDR | LQAISSDLSN | LQLAWASGYL | WNKASHSIPI | DYTASQQVIT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| VLSASQTGNA | RRLAVQLYED | LLAAQLSVVI | INAGDYKFKQ | IAQEKWLLIV | TSTQGDGDPP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| EEAIALYKYL | FSKKAPVLNN | IQFAIFGLGD | SSYTYFAKIG | KDFDSRLAEL | GAQRLYDRVD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ADVDYQEKAD | IWRREIVKIL | QTKLVTVNAK | QQLSVINNRI | EVKNNLYTKE | EPFTAHLVVK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QKITSRSSKK | DIRHLEIDIA | GSGLNYQPGD | ALGVWYENDP | VLISEILELL | GLTGNELVQV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KEKNIPLNEA | LQKHYELTNN | TAEIVKSYAY | ITRNSSLLAL | VDDQQQLKQF | AFSTPFIDMI |
| 370 | 380 | 390 | 400 | 410 | 420 |
| QRIPVELHPK | QLLTLLRPLM | PRLYSIASSQ | AEVGDEVHLT | VSVVRYEIDG | KIRTGGASSY |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LAYRLQESEP | IRVFIEHNDN | FRLPNNPNTA | IIMIGSGTGI | APFRGFMQQR | EATTAKGKNW |
| 490 | 500 | 510 | 520 | 530 | 540 |
| LFFGNQHLTD | DFLYQVEWQR | YIKNGLLNKI | DVAWSQDQNK | KIYVQDRLLE | KGIELWNWIQ |
| 550 | 560 | 570 | 580 | 590 | |
| DGAHIYVCGN | ANLMARDVEK | ALVKLIAIHG | RMDYEQADEF | LSELRIARRF | QRDTY |