Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2740891456 13 NCAPCLNSKRLLDAKKHPYEFVSVADsvedgkpvlNEAVIDELEALVGtRRMTMPQIFHDGKHVGGFDQL 82
Cdd:cd03418    9 NCPYCVRAKALLDKKGVDYEEIDVDG---------DPALREEMINRSG-GRRTVPQIFIGDVHIGGCDDL 68

Glutaredoxin-family domain; This C-terminal domain with homology to glutaredoxin is fused to an N-terminal peroxiredoxin-like domain.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2740891456 14 CAPCLNSKRLLdaKKHPYEFVSVadsvedgkPVLNEAVIDELEALVGtrRMTMPQIFHDGKHVGGFDQLREY 85
Cdd:TIGR02190 18 CPFCAKAKATL--KEKGYDFEEI--------PLGNDARGRSLRAVTG--ATTVPQVFIGGKLIGGSDELEAY 77

Glutaredoxin (GRX) family, GRX bacterial class 1 and 3 (b_1_3)-like subfamily; composed of bacterial GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including E. coli GRX1 and GRX3, which are members of this subfamily.

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2740891456 13 NCAPCLNSKRLLDAKKHPYEFVSVADsvedgkpvlNEAVIDELEALVGtRRMTMPQIFHDGKHVGGFDQL 82
Cdd:cd03418    9 NCPYCVRAKALLDKKGVDYEEIDVDG---------DPALREEMINRSG-GRRTVPQIFIGDVHIGGCDDL 68

glutaredoxin 3; Provisional

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2740891456 14 CAPCLNSKRLLDAKKHPYEFVSVadsveDGKPVLNEAVIDElealvgTRRMTMPQIFHDGKHVGGFDQL 82
Cdd:PRK10638  12 CPFCHRAKALLNSKGVSFQEIPI-----DGDAAKREEMIKR------SGRTTVPQIFIDAQHIGGCDDL 69

Glutaredoxin, GrxC family; Glutaredoxins are thioltransferases (disulfide reductases) which utilize glutathione and NADPH as cofactors. Oxidized glutathione is regenerated by glutathione reductase. Together these components compose the glutathione system. Glutaredoxins utilize the CXXC motif common to thioredoxins and are involved in multiple cellular processes including protection from redox stress, reduction of critical enzymes such as ribonucleotide reductase and the generation of reduced sulfur for iron sulfur cluster formation. Glutaredoxins are capable of reduction of mixed disulfides of glutathione as well as the formation of glutathione mixed disulfides. This family of glutaredoxins includes the E. coli protein GrxC (Grx3) which appears to have a secondary role in reducing ribonucleotide reductase (in the absence of GrxA) possibly indicating a role in the reduction of other protein disulfides. [Energy metabolism, Electron transport]

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2740891456 13 NCAPCLNSKRLLDAKKHPYEFVSVADsvedgkpvlNEAVIDELEALVGtrRMTMPQIFHDGKHVGGFDQL 82
Cdd:TIGR02181  8 YCPYCTRAKALLSSKGVTFTEIRVDG---------DPALRDEMMQRSG--RRTVPQIFIGDVHVGGCDDL 66

Glutaredoxin;

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2740891456 14 CAPCLNSKRLLDAKKHPYEFVSVADsvedgkpvlNEAVIDELEALVGtrRMTMPQIFHDGKHV 76
Cdd:pfam00462  9 CPFCKRAKRLLKSLGVDFEEIDVDE---------DPEIREELKELSG--WPTVPQVFIDGEHI 60

Glutaredoxin (GRX) family, GRX human class 1 and 2 (h_1_2)-like subfamily; composed of proteins similar to human GRXs, approximately 10 kDa in size, and proteins containing a GRX or GRX-like domain. GRX is a glutathione (GSH) dependent reductase, catalyzing the disulfide reduction of target proteins such as ribonucleotide reductase. It contains a redox active CXXC motif in a TRX fold and uses a similar dithiol mechanism employed by TRXs for intramolecular disulfide bond reduction of protein substrates. Unlike TRX, GRX has preference for mixed GSH disulfide substrates, in which it uses a monothiol mechanism where only the N-terminal cysteine is required. The flow of reducing equivalents in the GRX system goes from NADPH -> GSH reductase -> GSH -> GRX -> protein substrates. By altering the redox state of target proteins, GRX is involved in many cellular functions including DNA synthesis, signal transduction and the defense against oxidative stress. Different classes are known including human GRX1 and GRX2, which are members of this subfamily. Also included in this subfamily are the N-terminal GRX domains of proteins similar to human thioredoxin reductase 1 and 3.

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2740891456 14 CAPCLNSKRLLDAKKHPYEFVSVaDSVEDGKpvlneAVIDELEALVGTRrmTMPQIFHDGKHVGGFDQL 82
Cdd:cd03419   10 CPYCKRAKSLLKELGVKPAVVEL-DQHEDGS-----EIQDYLQELTGQR--TVPNVFIGGKFIGGCDDL 70

Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins including the transcriptional regulator, Spx. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX), through a single catalytic cysteine. This family of predominantly bacterial enzymes is unrelated to two other families of arsenate reductases which show similarity to low-molecular-weight acid phosphatases and phosphotyrosyl phosphatases. Spx is a general regulator that exerts negative and positive control over transcription initiation by binding to the C-terminal domain of the alpha subunit of RNA polymerase.

                          10        20        30
                  ....*....|....*....|....*....|..
gi 2740891456   3 KIYGYiPsvyNCAPCLNSKRLLDAKKHPYEFV 34
Cdd:cd02977     2 TIYGN-P---NCSTSRKALAWLEEHGIEYEFI 29