protein-disulfide reductase DsbD [Klebsiella quasipneumoniae]
Protein Classification
protein-disulfide reductase DsbD( domain architecture ID 11478463)
protein-disulfide reductase DsbD facilitates the formation of correct disulfide bonds in some periplasmic proteins and is required for the assembly of the periplasmic c-type cytochromes
List of domain hits
| Name | Accession | Description | Interval | E-value | |||||||||
| dipZ | PRK00293 | thiol:disulfide interchange protein precursor; Provisional |
4-598 | 0e+00 | |||||||||
thiol:disulfide interchange protein precursor; Provisional : Pssm-ID: 234717 [Multi-domain] Cd Length: 571 Bit Score: 952.35 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | |||||||||
| dipZ | PRK00293 | thiol:disulfide interchange protein precursor; Provisional |
4-598 | 0e+00 | |||||||||
thiol:disulfide interchange protein precursor; Provisional Pssm-ID: 234717 [Multi-domain] Cd Length: 571 Bit Score: 952.35 E-value: 0e+00
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| DsbD | COG4232 | Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
198-598 | 1.06e-143 | |||||||||
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 422.29 E-value: 1.06e-143
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| DsbDgamma | cd02953 | DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
489-594 | 1.18e-42 | |||||||||
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes. Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 148.52 E-value: 1.18e-42
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| DsbC | pfam11412 | Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ... |
30-138 | 2.85e-38 | |||||||||
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD. Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 137.09 E-value: 2.85e-38
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| thioredoxin | TIGR01068 | thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
488-589 | 3.06e-07 | |||||||||
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport] Pssm-ID: 200072 [Multi-domain] Cd Length: 101 Bit Score: 48.82 E-value: 3.06e-07
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| Name | Accession | Description | Interval | E-value | |||||||||
| dipZ | PRK00293 | thiol:disulfide interchange protein precursor; Provisional |
4-598 | 0e+00 | |||||||||
thiol:disulfide interchange protein precursor; Provisional Pssm-ID: 234717 [Multi-domain] Cd Length: 571 Bit Score: 952.35 E-value: 0e+00
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| DsbD | COG4232 | Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, ... |
198-598 | 1.06e-143 | |||||||||
Thiol:disulfide interchange protein DsbD [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 443376 [Multi-domain] Cd Length: 416 Bit Score: 422.29 E-value: 1.06e-143
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| DsbDgamma | cd02953 | DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein ... |
489-594 | 1.18e-42 | |||||||||
DsbD gamma family; DsbD gamma is the C-terminal periplasmic domain of the bacterial protein DsbD. It contains a CXXC motif in a TRX fold and shuttles the reducing potential from the membrane domain (DsbD beta) to the N-terminal periplasmic domain (DsbD alpha). DsbD beta, a transmembrane domain comprising of eight helices, acquires its reducing potential from the cytoplasmic thioredoxin. DsbD alpha transfers the acquired reducing potential from DsbD gamma to target proteins such as the periplasmic protein disulphide isomerases, DsbC and DsbG. This flow of reducing potential from the cytoplasm through DsbD allows DsbC and DsbG to act as isomerases in the oxidizing environment of the bacterial periplasm. DsbD also transfers reducing potential from the cytoplasm to specific reductases in the periplasm which are involved in the maturation of cytochromes. Pssm-ID: 239251 [Multi-domain] Cd Length: 104 Bit Score: 148.52 E-value: 1.18e-42
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| DsbC | pfam11412 | Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a ... |
30-138 | 2.85e-38 | |||||||||
Disulphide bond corrector protein DsbC; This entry represents the N-terminal domain of DsbD, a transmembrane electron transporter. DsbD binds to a DsbC dimer and selectively activates it using electrons from the cytoplasm. The N-terminal domain of DsbD (DsbDN) is capable of forming disulfides with oxidized DsbC, DsbE, or DsbG as well as with reduced DsbD. Pssm-ID: 463273 [Multi-domain] Cd Length: 115 Bit Score: 137.09 E-value: 2.85e-38
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| CcdA | COG0785 | Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational ... |
200-397 | 3.56e-29 | |||||||||
Cytochrome c biogenesis protein CcdA [Energy production and conversion, Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440548 [Multi-domain] Cd Length: 193 Bit Score: 114.17 E-value: 3.56e-29
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| DsbD | pfam02683 | Cytochrome C biogenesis protein transmembrane region; This family consists of the ... |
204-411 | 4.61e-20 | |||||||||
Cytochrome C biogenesis protein transmembrane region; This family consists of the transmembrane (i.e. non-catalytic) region of Cytochrome C biogenesis proteins also known as disulphide interchange proteins. These proteins posses a protein disulphide isomerase like domain that is not found within the aligned region of this family. Pssm-ID: 280792 [Multi-domain] Cd Length: 213 Bit Score: 89.00 E-value: 4.61e-20
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| SoxW | COG2143 | Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones] ... |
447-594 | 8.96e-19 | |||||||||
Thioredoxin-related protein SoxW [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 441746 [Multi-domain] Cd Length: 146 Bit Score: 83.03 E-value: 8.96e-19
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| Thioredoxin_7 | pfam13899 | Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
492-570 | 1.80e-14 | |||||||||
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Pssm-ID: 433567 [Multi-domain] Cd Length: 84 Bit Score: 68.93 E-value: 1.80e-14
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| Thioredoxin_2 | pfam13098 | Thioredoxin-like domain; |
499-593 | 6.36e-12 | |||||||||
Thioredoxin-like domain; Pssm-ID: 379034 [Multi-domain] Cd Length: 103 Bit Score: 62.06 E-value: 6.36e-12
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| CnoX | COG3118 | Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family ... |
490-595 | 8.24e-12 | |||||||||
Chaperedoxin CnoX, contains thioredoxin-like and TPR-like domains, YbbN/TrxSC family [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 442352 [Multi-domain] Cd Length: 105 Bit Score: 61.76 E-value: 8.24e-12
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| TRX_family | cd02947 | TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a ... |
490-593 | 9.37e-11 | |||||||||
TRX family; composed of two groups: Group I, which includes proteins that exclusively encode a TRX domain; and Group II, which are composed of fusion proteins of TRX and additional domains. Group I TRX is a small ancient protein that alter the redox state of target proteins via the reversible oxidation of an active site dithiol, present in a CXXC motif, partially exposed at the protein's surface. TRX reduces protein disulfide bonds, resulting in a disulfide bond at its active site. Oxidized TRX is converted to the active form by TRX reductase, using reducing equivalents derived from either NADPH or ferredoxins. By altering their redox state, TRX regulates the functions of at least 30 target proteins, some of which are enzymes and transcription factors. It also plays an important role in the defense against oxidative stress by directly reducing hydrogen peroxide and certain radicals, and by serving as a reductant for peroxiredoxins. At least two major types of functional TRXs have been reported in most organisms; in eukaryotes, they are located in the cytoplasm and the mitochondria. Higher plants contain more types (at least 20 TRX genes have been detected in the genome of Arabidopsis thaliana), two of which (types f amd m) are located in the same compartment, the chloroplast. Also included in the alignment are TRX-like domains which show sequence homology to TRX but do not contain the redox active CXXC motif. Group II proteins, in addition to either a redox active TRX or a TRX-like domain, also contain additional domains, which may or may not possess homology to known proteins. Pssm-ID: 239245 [Multi-domain] Cd Length: 93 Bit Score: 58.72 E-value: 9.37e-11
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| TrxA | COG0526 | Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
495-595 | 1.64e-10 | |||||||||
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones]; Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 59.32 E-value: 1.64e-10
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| DsbD_2 | pfam13386 | Cytochrome C biogenesis protein transmembrane region; |
226-404 | 8.95e-09 | |||||||||
Cytochrome C biogenesis protein transmembrane region; Pssm-ID: 463866 Cd Length: 199 Bit Score: 55.70 E-value: 8.95e-09
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| Thioredoxin | pfam00085 | Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
488-595 | 9.34e-08 | |||||||||
Thioredoxin; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond. Some members with only the active site are not separated from the noise. Pssm-ID: 395038 [Multi-domain] Cd Length: 103 Bit Score: 50.31 E-value: 9.34e-08
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| TxlA | cd02950 | TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium ... |
497-575 | 1.12e-07 | |||||||||
TRX-like protein A (TxlA) family; TxlA was originally isolated from the cyanobacterium Synechococcus. It is found only in oxygenic photosynthetic organisms. TRX is a small enzyme that participate in redox reactions, via the reversible oxidation of an active site dithiol present in a CXXC motif. Disruption of the txlA gene suggests that the protein is involved in the redox regulation of the structure and function of photosynthetic apparatus. The plant homolog (designated as HCF164) is localized in the chloroplast and is involved in the assembly of the cytochrome b6f complex, which takes a central position in photosynthetic electron transport. Pssm-ID: 239248 [Multi-domain] Cd Length: 142 Bit Score: 51.18 E-value: 1.12e-07
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| thioredoxin | TIGR01068 | thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of ... |
488-589 | 3.06e-07 | |||||||||
thioredoxin; Several proteins, such as protein disulfide isomerase, have two or more copies of a domain closely related to thioredoxin. This model is designed to recognize authentic thioredoxin, a small protein that should be hit exactly once by this model. Any protein that hits once with a score greater than the second (per domain) trusted cutoff may be taken as thioredoxin. [Energy metabolism, Electron transport] Pssm-ID: 200072 [Multi-domain] Cd Length: 101 Bit Score: 48.82 E-value: 3.06e-07
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| PDI_a_family | cd02961 | Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic ... |
499-578 | 4.68e-07 | |||||||||
Protein Disulfide Isomerase (PDIa) family, redox active TRX domains; composed of eukaryotic proteins involved in oxidative protein folding in the endoplasmic reticulum (ER) by acting as catalysts and folding assistants. Members of this family include PDI and PDI-related proteins like ERp72, ERp57 (or ERp60), ERp44, P5, PDIR, ERp46 and the transmembrane PDIs. PDI, ERp57, ERp72, P5, PDIR and ERp46 are all oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. These proteins usually contain multiple copies of a redox active TRX (a) domain containing a CXXC motif, and may also contain one or more redox inactive TRX-like (b) domains. Only one a domain is required for the oxidase function but multiple copies are necessary for the isomerase function. The different types of PDIs may show different substrate specificities and tissue-specific expression, or may be induced by stress. PDIs are in their reduced form at steady state and are oxidized to the active form by Ero1, which is localized in the ER through ERp44. Some members of this family also contain a DnaJ domain in addition to the redox active a domains; examples are ERdj5 and Pfj2. Also included in the family is the redox inactive N-terminal TRX-like domain of ERp29. Pssm-ID: 239259 [Multi-domain] Cd Length: 101 Bit Score: 48.38 E-value: 4.68e-07
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| TlpA_like_family | cd02966 | TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
496-582 | 9.62e-07 | |||||||||
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases. Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 48.00 E-value: 9.62e-07
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| PDI_a_PDI_a'_C | cd02995 | PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' ... |
504-576 | 1.92e-06 | |||||||||
PDIa family, C-terminal TRX domain (a') subfamily; composed of the C-terminal redox active a' domains of PDI, ERp72, ERp57 (or ERp60) and EFP1. PDI, ERp72 and ERp57 are endoplasmic reticulum (ER)-resident eukaryotic proteins involved in oxidative protein folding. They are oxidases, catalyzing the formation of disulfide bonds of newly synthesized polypeptides in the ER. They also exhibit reductase activity in acting as isomerases to correct any non-native disulfide bonds, as well as chaperone activity to prevent protein aggregation and facilitate the folding of newly synthesized proteins. PDI and ERp57 have the abb'a' domain structure (where a and a' are redox active TRX domains while b and b' are redox inactive TRX-like domains). PDI also contains an acidic region (c domain) after the a' domain that is absent in ERp57. ERp72 has an additional a domain at the N-terminus (a"abb'a' domain structure). ERp57 interacts with the lectin chaperones, calnexin and calreticulin, and specifically promotes the oxidative folding of glycoproteins, while PDI shows a wider substrate specificity. ERp72 associates with several ER chaperones and folding factors to form complexes in the ER that bind nascent proteins. EFP1 is a binding partner protein of thyroid oxidase, which is responsible for the generation of hydrogen peroxide, a crucial substrate of thyroperoxidase, which functions to iodinate thyroglobulin and synthesize thyroid hormones. Pssm-ID: 239293 [Multi-domain] Cd Length: 104 Bit Score: 46.78 E-value: 1.92e-06
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| SoxW | cd02951 | SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, ... |
487-595 | 5.28e-05 | |||||||||
SoxW family; SoxW is a bacterial periplasmic TRX, containing a redox active CXXC motif, encoded by a genetic locus (sox operon) involved in thiosulfate oxidation. Sulfur bacteria oxidize sulfur compounds to provide reducing equivalents for carbon dioxide fixation during autotrophic growth and the respiratory electron transport chain. It is unclear what the role of SoxW is, since it has been found to be dispensable in the oxidation of thiosulfate to sulfate. SoxW is specifically kept in the reduced state by SoxV, which is essential in thiosulfate oxidation. Pssm-ID: 239249 [Multi-domain] Cd Length: 125 Bit Score: 43.07 E-value: 5.28e-05
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| ER_PDI_fam | TIGR01130 | protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide ... |
504-576 | 4.94e-04 | |||||||||
protein disulfide isomerase, eukaryotic; This model represents eukaryotic protein disulfide isomerases retained in the endoplasmic reticulum (ER) and closely related forms. Some members have been assigned alternative or additional functions such as prolyl 4-hydroxylase and dolichyl-diphosphooligosaccharide-protein glycotransferase. Members of this family have at least two protein-disulfide domains, each similar to thioredoxin but with the redox-active disulfide in the motif PWCGHCK, and an ER retention signal at the extreme C-terminus (KDEL, HDEL, and similar motifs). Pssm-ID: 273457 [Multi-domain] Cd Length: 462 Bit Score: 42.74 E-value: 4.94e-04
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| PTZ00443 | PTZ00443 | Thioredoxin domain-containing protein; Provisional |
476-569 | 6.64e-04 | |||||||||
Thioredoxin domain-containing protein; Provisional Pssm-ID: 185622 [Multi-domain] Cd Length: 224 Bit Score: 41.53 E-value: 6.64e-04
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| PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
496-585 | 6.67e-04 | |||||||||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 42.43 E-value: 6.67e-04
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| PDI_a_P5 | cd03001 | PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related ... |
503-587 | 1.62e-03 | |||||||||
PDIa family, P5 subfamily; composed of eukaryotic proteins similar to human P5, a PDI-related protein with a domain structure of aa'b (where a and a' are redox active TRX domains and b is a redox inactive TRX-like domain). Like PDI, P5 is located in the endoplasmic reticulum (ER) and displays both isomerase and chaperone activities, which are independent of each other. Compared to PDI, the isomerase and chaperone activities of P5 are lower. The first cysteine in the CXXC motif of both redox active domains in P5 is necessary for isomerase activity. The P5 gene was first isolated as an amplified gene from a hydroxyurea-resistant hamster cell line. The zebrafish P5 homolog has been implicated to play a critical role in establishing left/right asymmetries in the embryonic midline. Some members of this subfamily are P5-like proteins containing only one redox active TRX domain. Pssm-ID: 239299 [Multi-domain] Cd Length: 103 Bit Score: 38.42 E-value: 1.62e-03
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| PTZ00102 | PTZ00102 | disulphide isomerase; Provisional |
504-589 | 3.67e-03 | |||||||||
disulphide isomerase; Provisional Pssm-ID: 240266 [Multi-domain] Cd Length: 477 Bit Score: 40.12 E-value: 3.67e-03
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| ERp19 | cd02959 | Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein ... |
496-577 | 4.91e-03 | |||||||||
Endoplasmic reticulum protein 19 (ERp19) family; ERp19 is also known as ERp18, a protein located in the ER containing one redox active TRX domain. Denaturation studies indicate that the reduced form is more stable than the oxidized form, suggesting that the protein is involved in disulfide bond formation. In vitro, ERp19 has been shown to possess thiol-disulfide oxidase activity which is dependent on the presence of both active site cysteines. Although described as protein disulfide isomerase (PDI)-like, the protein does not complement for PDI activity. ERp19 shows a wide tissue distribution but is most abundant in liver, testis, heart and kidney. Pssm-ID: 239257 [Multi-domain] Cd Length: 117 Bit Score: 37.11 E-value: 4.91e-03
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| PDI_a_ERp38 | cd02998 | PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar ... |
501-577 | 6.07e-03 | |||||||||
PDIa family, endoplasmic reticulum protein 38 (ERp38) subfamily; composed of proteins similar to the P5-like protein first isolated from alfalfa, which contains two redox active TRX (a) domains at the N-terminus, like human P5, and a C-terminal domain with homology to the C-terminal domain of ERp29, unlike human P5. The cDNA clone of this protein (named G1) was isolated from an alfalfa cDNA library by screening with human protein disulfide isomerase (PDI) cDNA. The G1 protein is constitutively expressed in all major organs of the plant and its expression is induced by treatment with tunicamycin, indicating that it may be a glucose-regulated protein. The G1 homolog in the eukaryotic social amoeba Dictyostelium discoideum is also described as a P5-like protein, which is located in the endoplasmic reticulum (ER) despite the absence of an ER-retrieval signal. G1 homologs from Aspergillus niger and Neurospora crassa have also been characterized, and are named TIGA and ERp38, respectively. Also included in the alignment is an atypical PDI from Leishmania donovani containing a single a domain, and the C-terminal a domain of a P5-like protein from Entamoeba histolytica. Pssm-ID: 239296 [Multi-domain] Cd Length: 105 Bit Score: 36.84 E-value: 6.07e-03
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| PDI_a_APS_reductase | cd02993 | PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS ... |
502-568 | 7.00e-03 | |||||||||
PDIa family, 5'-Adenylylsulfate (APS) reductase subfamily; composed of plant-type APS reductases containing a C-terminal redox active TRX domain and an N-terminal reductase domain which is part of a superfamily that includes N type ATP PPases. APS reductase catalyzes the reduction of activated sulfate to sulfite, a key step in the biosynthesis of sulfur-containing metabolites. Sulfate is first activated by ATP sulfurylase, forming APS, which can be phosphorylated to 3'-phosphoadenosine-5'-phosphosulfate (PAPS). Depending on the organism, either APS or PAPS can be used for sulfate reduction. Prokaryotes and fungi use PAPS, whereas plants use both APS and PAPS. Since plant-type APS reductase uses glutathione (GSH) as its electron donor, the C-terminal domain may function like glutaredoxin, a GSH-dependent member of the TRX superfamily. The flow of reducing equivalents goes from GSH -> C-terminal TRX domain -> N-terminal reductase domain -> APS. Plant-type APS reductase shows no homology to that of dissimilatory sulfate-reducing bacteria, which is an iron-sulfur flavoenzyme. Also included in the alignment is EYE2 from Chlamydomonas reinhardtii, a protein required for eyespot assembly. Pssm-ID: 239291 [Multi-domain] Cd Length: 109 Bit Score: 36.66 E-value: 7.00e-03
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