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Conserved domains on  [gi|1199442632|ref|WP_087182815|]
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thioredoxin family protein [Gemmiger sp. An50]

Protein Classification

thioredoxin domain-containing protein( domain architecture ID 144)

thioredoxin domain-containing protein may function as a thiol disulfide oxidoreductase that catalyzes the oxidation or reduction of protein disulfide bonds using an active site dithiol, present in a CXXC motif

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HemE super family cl43134
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
 59-122 8.22e-11

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


The actual alignment was detected with superfamily member COG0407:

Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 61.01  E-value: 8.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199442632  59 AKAITDRyNVVIGGNIPLTSIMLHGTQQDNMKYVVDLLDQLPEYRNFIVAPGCDMPYSVPVENA 122
Cdd:COG0407   263 AKERLGD-KVALQGNLDPALLLLNGTPEEVEAEVKRILDAGGGGPGHIFNLGHGIPPDTPPENV 325
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 171-248 2.39e-04

Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin (TRX)-like superfamily is a large, diverse group of proteins containing a TRX fold. Many members contain a classic TRX domain with a redox active CXXC motif. They function as protein disulfide oxidoreductases (PDOs), altering the redox state of target proteins via the reversible oxidation of their active site dithiol. The PDO members of this superfamily include the families of TRX, protein disulfide isomerase (PDI), tlpA, glutaredoxin, NrdH redoxin, and bacterial Dsb proteins (DsbA, DsbC, DsbG, DsbE, DsbDgamma). Members of the superfamily that do not function as PDOs but contain a TRX-fold domain include phosducins, peroxiredoxins, glutathione (GSH) peroxidases, SCO proteins, GSH transferases (GST, N-terminal domain), arsenic reductases, TRX-like ferredoxins and calsequestrin, among others.


The actual alignment was detected with superfamily member pfam13192:

Pssm-ID: 469754 [Multi-domain]  Cd Length: 71  Bit Score: 38.35  E-value: 2.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199442632 171 SASCAACTYMMGAAAAAKEQFGDTIDMVEYKFTQKeniarFRKMGVKKLPSIYINGQPKFSSIIPSREEledaIREIL 248
Cdd:pfam13192   2 GPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPE-----IAKYGVMSTPALVINGKVVSSGKVPSEEE----IRKLL 70
HemE super family cl43134
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
 1-56 4.44e-03

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


The actual alignment was detected with superfamily member COG0407:

Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 37.89  E-value: 4.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1199442632   1 MTPKELLFATLRHEATPRAPWAPFSGIHSGFLTGADATRILTDEDALVEALLAVNR 56
Cdd:COG0407     1 MTPKERLLRALRGEPVDRVPVWPLTTAALMRQAGRYLPEYCYDPELAAEVTLQPVR 56
 
Name Accession Description Interval E-value
HemE COG0407
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
 59-122 8.22e-11

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 61.01  E-value: 8.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199442632  59 AKAITDRyNVVIGGNIPLTSIMLHGTQQDNMKYVVDLLDQLPEYRNFIVAPGCDMPYSVPVENA 122
Cdd:COG0407   263 AKERLGD-KVALQGNLDPALLLLNGTPEEVEAEVKRILDAGGGGPGHIFNLGHGIPPDTPPENV 325
URO-D_like cd03465
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ...
 67-121 1.47e-05

The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane.


Pssm-ID: 239548  Cd Length: 330  Bit Score: 45.40  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1199442632  67 NVVIGGNIPLTSIMLHGTQQDNMKYVVDLLDQLPEY-RNFIVAPGCDMPYSVPVEN 121
Cdd:cd03465   265 KACLMGNLDPIDVLLNGSPEEIKEEVKELLEKLLKGgGGYILSSGCEIPPDTPIEN 320
Thioredoxin_3 pfam13192
Thioredoxin domain;
171-248 2.39e-04

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 38.35  E-value: 2.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199442632 171 SASCAACTYMMGAAAAAKEQFGDTIDMVEYKFTQKeniarFRKMGVKKLPSIYINGQPKFSSIIPSREEledaIREIL 248
Cdd:pfam13192   2 GPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPE-----IAKYGVMSTPALVINGKVVSSGKVPSEEE----IRKLL 70
HemE COG0407
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
 1-56 4.44e-03

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 37.89  E-value: 4.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1199442632   1 MTPKELLFATLRHEATPRAPWAPFSGIHSGFLTGADATRILTDEDALVEALLAVNR 56
Cdd:COG0407     1 MTPKERLLRALRGEPVDRVPVWPLTTAALMRQAGRYLPEYCYDPELAAEVTLQPVR 56
 
Name Accession Description Interval E-value
HemE COG0407
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
 59-122 8.22e-11

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 61.01  E-value: 8.22e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1199442632  59 AKAITDRyNVVIGGNIPLTSIMLHGTQQDNMKYVVDLLDQLPEYRNFIVAPGCDMPYSVPVENA 122
Cdd:COG0407   263 AKERLGD-KVALQGNLDPALLLLNGTPEEVEAEVKRILDAGGGGPGHIFNLGHGIPPDTPPENV 325
URO-D_like cd03465
The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen ...
 67-121 1.47e-05

The URO-D _like protein superfamily includes bacterial and eukaryotic uroporphyrinogen decarboxylases (URO-D), coenzyme M methyltransferases and other putative bacterial methyltransferases. Uroporphyrinogen decarboxylase (URO-D) decarboxylates the four acetate side chains of uroporphyrinogen III (uro-III) to create coproporphyrinogen III, an important branching point of the tetrapyrrole biosynthetic pathway. The methyltransferases represented here are important for ability of methanogenic organisms to use other compounds than carbon dioxide for reduction to methane.


Pssm-ID: 239548  Cd Length: 330  Bit Score: 45.40  E-value: 1.47e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1199442632  67 NVVIGGNIPLTSIMLHGTQQDNMKYVVDLLDQLPEY-RNFIVAPGCDMPYSVPVEN 121
Cdd:cd03465   265 KACLMGNLDPIDVLLNGSPEEIKEEVKELLEKLLKGgGGYILSSGCEIPPDTPIEN 320
Thioredoxin_3 pfam13192
Thioredoxin domain;
171-248 2.39e-04

Thioredoxin domain;


Pssm-ID: 433026 [Multi-domain]  Cd Length: 71  Bit Score: 38.35  E-value: 2.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1199442632 171 SASCAACTYMMGAAAAAKEQFGDTIDMVEYKFTQKeniarFRKMGVKKLPSIYINGQPKFSSIIPSREEledaIREIL 248
Cdd:pfam13192   2 GPGCPKCPQLEKAVKEAAAELGIDAEVEKVTDFPE-----IAKYGVMSTPALVINGKVVSSGKVPSEEE----IRKLL 70
HemE COG0407
Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; ...
 1-56 4.44e-03

Uroporphyrinogen-III decarboxylase HemE [Coenzyme transport and metabolism]; Uroporphyrinogen-III decarboxylase HemE is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440176 [Multi-domain]  Cd Length: 336  Bit Score: 37.89  E-value: 4.44e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1199442632   1 MTPKELLFATLRHEATPRAPWAPFSGIHSGFLTGADATRILTDEDALVEALLAVNR 56
Cdd:COG0407     1 MTPKERLLRALRGEPVDRVPVWPLTTAALMRQAGRYLPEYCYDPELAAEVTLQPVR 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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