2TRX,1AUC,1DBY,1EP7,1ERT,1F6M,1F9M,1FAA,1FB0,1GH2,1NW2,1R26,1SYR,1THX,1TI3,1XFL,1XWC,1ZMA


Conserved Protein Domain Family
TRX_family
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cd02947: TRX_family 
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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.
Links
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Statistics
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PSSM-Id: 239245
Aligned: 515 rows
Threshold Bit Score: 37.5377
Created: 22-Nov-2004
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
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catalytic
Conserved site includes 2 residues -Click on image for an interactive view with Cn3D
Feature 1:catalytic residues [active site]
Evidence:
  • Comment:CXXC motif
  • Comment:Disulfide bond reduction by thioredoxin is initiated by deprotonation of the solvent-exposed N-terminal cysteine in the CXXC motif to form a thiolate. The pKa of this thiol must be near physiological pH to achieve maximal catalysis.
  • Citation:PMID 9099998
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Sequence Alignment
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Format: Row Display: Color Bits: Type Selection: 
Feature 1                              #  #                                                     
2TRX_A       10 DSFDTDVlka-dgaILVDFWAEWCGPCKMIAPILDEIadey---qgkLTVAKLNIDq----nPGTAPKYgirgIPTLLLF 81  Escherichia coli
NP_215331    42 ARTAELGlsg-agpTVVHFRAPGCAPCDRVRRGVGDVcad----lgdVAHIEVDLDs----nPQAARRFsvlsLPTTLIF 112 Mycobacterium tu...
ZP_00130771   8 ADFEQVLaat--asGVVIFFKKQCPHCKNMEKVLEKFaak----npdVALFSMDSEe----nPATVERLeaerAPTIIVI 77  Desulfovibrio de...
NP_716047    76 DALAPLKkvt-eptEIVVIIGTWCPDCHRETPRFIRIieev--anpnIKVTYIGVDrskqdpEGLAAKYefkrIPTFIVQ 152 Shewanella oneid...
BAC69193     42 AELGEGLge---raTLVQFSSAFCAPCRATRRVLTEVagl----vpgVTHVEIDAEd----rLELVRELdiikTPTVLVL 110 Streptomyces ave...
YP_009602    14 AHFEGLSd------AIVFFHKNLCPHCKNMEKVLDKFgar----apqVAISSVDSEa----rPELMKELgferVPTLVFI 79  Desulfovibrio vu...
ZP_00129721  24 GDLDARIeqt--aqGIVLFHKELCPHCKNMEKVLAKFgak----npdVELLAVDSEa----dPAVMEAYgverVPSLVIV 93  Desulfovibrio de...
ZP_00348854  28 AALETAAtg----pRIVFFKGDDSASCQAIARIVEEAeary---agrVGVTRVDWSp----eNPLIQAYkvrfLPTVVFV 96  Dechloromonas ar...
YP_116805    41 AGLLAAAgvtgtgpAVLHFSAEWCGPCAAVRRVVAGVtadlaaephpPQDIEIDIDa----ePALARELnvlsLPTTFVF 116 Nocardia farcini...
ZP_00545738  37 AEFASLGetmgeraTLLQFSTAFCAPCRSTRRVLAGVaev----vpgVRHVEVDAEa----hLDLVRRLgirrTPTVLIV 108 Frankia sp. CcI3

Feature 1                                    
2TRX_A       82 KNge-vaATKVGALsk-----gQLKEFLD 104 Escherichia coli
NP_215331   113 DVdgrqrYRTSGVPka-----aDLRSALK 136 Mycobacterium tuberculosis H37Rv
ZP_00130771  78 KNga-vaARKAGLMnp-----kEMKAFFA 100 Desulfovibrio desulfuricans G20
NP_716047   153 QQgk-eiGRIVERPtvs--lekDLAEILK 178 Shewanella oneidensis MR-1
BAC69193    111 DAegrivRRATGQPrk-----aDVIAALG 134 Streptomyces avermitilis MA-4680
YP_009602    80 RDgk-vaKVFSGIMnp-----rELQALYA 102 Desulfovibrio vulgaris subsp. vulgaris str. Hildenborough
ZP_00129721  94 RGgr-avYTRTGLMnp-----kELTTLYH 116 Desulfovibrio desulfuricans G20
ZP_00348854  97 DGagrerKRIIGESaav---qaALRQSLA 122 Dechloromonas aromatica RCB
YP_116805   117 DAagrerFRISGVPka-----gDLRSALA 140 Nocardia farcinica IFM 10152
ZP_00545738 109 DGhgrevRRASGAPptraavfaTLEEIVS 137 Frankia sp. CcI3

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