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Conserved domains on  [gi|495129697|ref|WP_007854508|]
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arsenate reductase (glutaredoxin) [Cronobacter sakazakii]

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
Thioredoxin_like super family cl00388
Protein Disulfide Oxidoreductases and Other Proteins with a Thioredoxin fold; The thioredoxin ...
 1-133 1.03e-78

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 PRK10026:

Pssm-ID: 469754  Cd Length: 141  Bit Score: 228.55  E-value: 1.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   1 MTPITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEA 80
Cdd:PRK10026   1 MSNITIYHNPACGTSRNTLEMIRNSGTEPTIIHYLETPPTRDELVKLIADMGISVRALLRKNVEPYEELGLAEDKFTDDQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495129697  81 LLDAMLAHPILINRPIVVTPLGTRLCRPSEEVLSILPDPQQGPFTKEDGEVVI 133
Cdd:PRK10026  81 LIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLEILPDAQKGAFTKEDGEKVV 133
 
Name Accession Description Interval E-value
PRK10026 PRK10026
arsenate reductase (glutaredoxin);
1-133 1.03e-78

arsenate reductase (glutaredoxin);


Pssm-ID: 182200  Cd Length: 141  Bit Score: 228.55  E-value: 1.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   1 MTPITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEA 80
Cdd:PRK10026   1 MSNITIYHNPACGTSRNTLEMIRNSGTEPTIIHYLETPPTRDELVKLIADMGISVRALLRKNVEPYEELGLAEDKFTDDQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495129697  81 LLDAMLAHPILINRPIVVTPLGTRLCRPSEEVLSILPDPQQGPFTKEDGEVVI 133
Cdd:PRK10026  81 LIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLEILPDAQKGAFTKEDGEKVV 133
ArsC_ArsC cd03034
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ...
 4-115 1.54e-59

Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded by arsC on the R733 plasmid of Escherichia coli. E. coli ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], the first step in the detoxification of arsenic, using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX). ArsC contains a single catalytic cysteine, within a thioredoxin fold, that forms a covalent thiolate-As(V) intermediate, which is reduced by GRX through a mixed GSH-arsenate intermediate. 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.


Pssm-ID: 239332  Cd Length: 112  Bit Score: 178.94  E-value: 1.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLD 83
Cdd:cd03034    1 ITIYHNPRCSKSRNALALLEEAGIEPEIVEYLKTPPTAAELRELLAKLGISPRDLLRTKEAPYKELGLADPELSDEELID 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495129697  84 AMLAHPILINRPIVVTPLGTRLCRPSEEVLSI 115
Cdd:cd03034   81 AMAAHPILIERPIVVTGDGAVLGRPPEAVLEL 112
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 4-117 3.99e-49

Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism];


Pssm-ID: 441003  Cd Length: 115  Bit Score: 152.94  E-value: 3.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLD 83
Cdd:COG1393    2 ITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDKALSEEEALA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495129697  84 AMLAHPILINRPIVVTPLGTRLCRPSEEVLSILP 117
Cdd:COG1393   82 LMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
arsC TIGR00014
arsenate reductase (glutaredoxin); This model describes a distinct clade, including ArsC ...
 4-116 2.21e-47

arsenate reductase (glutaredoxin); This model describes a distinct clade, including ArsC itself, of the broader ArsC family described by Pfam pfam03960. This clade is almost completely restricted to the Proteobacteria. An anion-translocating ATPase has been identified as the product of the arsenical resistance operon of resistance plasmid R773. When expressed in Escherichia coli this ATP-driven oxyanion pump catalyses extrusion of the oxyanions arsenite, antimonite and arsenate. The pump is composed of two polypeptides, the products of the arsA and arsB genes. The pump alone produces resistance to arsenite and antimonite. This protein, ArsC, catalyzes the reduction of arsenate to arsenite, and thus extends resistance to include arsenate. [Cellular processes, Detoxification]


Pssm-ID: 272855  Cd Length: 114  Bit Score: 148.37  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697    4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISV-RALLRKNVEPYQALGLDDEKIGDEALL 82
Cdd:TIGR00014   1 VTIYHNPRCSKSRNTLALLEDKGIEPEVVKYLKNPPTKSELEAIFAKLGLTVaREMIRTKEALYKELGLSDPNLSDQELL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 495129697   83 DAMLAHPILINRPIVVTPLGTRLCRPSEEVLSIL 116
Cdd:TIGR00014  81 DAMVAHPILLERPIVVAGDGARIGRPPENVLDIL 114
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 7-115 1.24e-42

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 136.19  E-value: 1.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697    7 YHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLDAML 86
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNLDKEDLSEDELLELIL 80

                          90       100
                  ....*....|....*....|....*....
gi 495129697   87 AHPILINRPIVVTPLGTRLCRPSEEVLSI 115
Cdd:pfam03960  81 EHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
 
Name Accession Description Interval E-value
PRK10026 PRK10026
arsenate reductase (glutaredoxin);
1-133 1.03e-78

arsenate reductase (glutaredoxin);


Pssm-ID: 182200  Cd Length: 141  Bit Score: 228.55  E-value: 1.03e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   1 MTPITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEA 80
Cdd:PRK10026   1 MSNITIYHNPACGTSRNTLEMIRNSGTEPTIIHYLETPPTRDELVKLIADMGISVRALLRKNVEPYEELGLAEDKFTDDQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495129697  81 LLDAMLAHPILINRPIVVTPLGTRLCRPSEEVLSILPDPQQGPFTKEDGEVVI 133
Cdd:PRK10026  81 LIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLEILPDAQKGAFTKEDGEKVV 133
ArsC_ArsC cd03034
Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded ...
 4-115 1.54e-59

Arsenate Reductase (ArsC) family, ArsC subfamily; arsenic reductases similar to that encoded by arsC on the R733 plasmid of Escherichia coli. E. coli ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], the first step in the detoxification of arsenic, using reducing equivalents derived from glutathione (GSH) via glutaredoxin (GRX). ArsC contains a single catalytic cysteine, within a thioredoxin fold, that forms a covalent thiolate-As(V) intermediate, which is reduced by GRX through a mixed GSH-arsenate intermediate. 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.


Pssm-ID: 239332  Cd Length: 112  Bit Score: 178.94  E-value: 1.54e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLD 83
Cdd:cd03034    1 ITIYHNPRCSKSRNALALLEEAGIEPEIVEYLKTPPTAAELRELLAKLGISPRDLLRTKEAPYKELGLADPELSDEELID 80

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495129697  84 AMLAHPILINRPIVVTPLGTRLCRPSEEVLSI 115
Cdd:cd03034   81 AMAAHPILIERPIVVTGDGAVLGRPPEAVLEL 112
ArsC COG1393
Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and ...
 4-117 3.99e-49

Arsenate reductase or related protein, glutaredoxin family [Inorganic ion transport and metabolism];


Pssm-ID: 441003  Cd Length: 115  Bit Score: 152.94  E-value: 3.99e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLD 83
Cdd:COG1393    2 ITIYGNPNCSTSRKALAWLEEAGIEYEFIDYLKTPPTAEELKELLAKLGLGVEELLNTRGTTYRELGLKDKALSEEEALA 81

                         90       100       110
                 ....*....|....*....|....*....|....
gi 495129697  84 AMLAHPILINRPIVVTPLGTRLCRPSEEVLSILP 117
Cdd:COG1393   82 LMLEHPSLIKRPIVVTGDKALVGFPPEEVLALLG 115
arsC TIGR00014
arsenate reductase (glutaredoxin); This model describes a distinct clade, including ArsC ...
 4-116 2.21e-47

arsenate reductase (glutaredoxin); This model describes a distinct clade, including ArsC itself, of the broader ArsC family described by Pfam pfam03960. This clade is almost completely restricted to the Proteobacteria. An anion-translocating ATPase has been identified as the product of the arsenical resistance operon of resistance plasmid R773. When expressed in Escherichia coli this ATP-driven oxyanion pump catalyses extrusion of the oxyanions arsenite, antimonite and arsenate. The pump is composed of two polypeptides, the products of the arsA and arsB genes. The pump alone produces resistance to arsenite and antimonite. This protein, ArsC, catalyzes the reduction of arsenate to arsenite, and thus extends resistance to include arsenate. [Cellular processes, Detoxification]


Pssm-ID: 272855  Cd Length: 114  Bit Score: 148.37  E-value: 2.21e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697    4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISV-RALLRKNVEPYQALGLDDEKIGDEALL 82
Cdd:TIGR00014   1 VTIYHNPRCSKSRNTLALLEDKGIEPEVVKYLKNPPTKSELEAIFAKLGLTVaREMIRTKEALYKELGLSDPNLSDQELL 80

                          90       100       110
                  ....*....|....*....|....*....|....
gi 495129697   83 DAMLAHPILINRPIVVTPLGTRLCRPSEEVLSIL 116
Cdd:TIGR00014  81 DAMVAHPILLERPIVVAGDGARIGRPPENVLDIL 114
ArsC pfam03960
ArsC family; This family is related to glutaredoxins pfam00462.
 7-115 1.24e-42

ArsC family; This family is related to glutaredoxins pfam00462.


Pssm-ID: 427617  Cd Length: 109  Bit Score: 136.19  E-value: 1.24e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697    7 YHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLDAML 86
Cdd:pfam03960   1 YGSPNCSTCRKALAWLEEHGIEYQEIDYLETPPSKEELKDILAKLGDGVEALLNTRGTTYRELNLDKEDLSEDELLELIL 80

                          90       100
                  ....*....|....*....|....*....
gi 495129697   87 AHPILINRPIVVTPLGTRLCRPSEEVLSI 115
Cdd:pfam03960  81 EHPSLIRRPIVVDGGKLLVGFNEEEIRAF 109
ArsC_family cd02977
Arsenate Reductase (ArsC) family; composed of TRX-fold arsenic reductases and similar proteins ...
 4-107 1.29e-39

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.


Pssm-ID: 239275  Cd Length: 105  Bit Score: 128.38  E-value: 1.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEK-IGDEALL 82
Cdd:cd02977    1 ITIYGNPNCSTSRKALAWLEEHGIEYEFIDYLKEPPTKEELKELLAKLGLGVEDLFNTRGTPYRKLGLADKDeLSDEEAL 80

                         90       100
                 ....*....|....*....|....*
gi 495129697  83 DAMLAHPILINRPIVVTPLGTRLCR 107
Cdd:cd02977   81 ELMAEHPKLIKRPIVVDGDRLLVGF 105
arsC_related TIGR01617
transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins ...
 4-100 9.62e-14

transcriptional regulator, Spx/MgsR family; This model represents a portion of the proteins within the larger set covered by pfam03960. That larger family includes a glutaredoxin-dependent arsenate reductase (TIGR00014). Characterized members of this family include Spx and MgsR from Bacillus subtili. Spx is a global regulator for response to thiol-specific oxidative stress. It interacts with RNA polymerase. MgsR (modulator of the general stress response, also called YqgZ) provides a second level of regulation for more than a third of the proteins in the B. subtilis general stress regulon controlled by Sigma-B. [Regulatory functions, DNA interactions]


Pssm-ID: 273720  Cd Length: 117  Bit Score: 62.83  E-value: 9.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697    4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEK--IGDEAL 81
Cdd:TIGR01617   1 IKVYGSPNCTTCKKARRWLEANGIEYQFIDIGEDGPTREELLDILSLLEDGIDPLLNTRGQSYRALNTSNTFldLSDKEA 80

                          90
                  ....*....|....*....
gi 495129697   82 LDAMLAHPILINRPIVVTP 100
Cdd:TIGR01617  81 LELLAEDPALLRRPLIVDT 99
ArsC_like cd03036
Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a ...
 4-100 6.54e-10

Arsenate Reductase (ArsC) family, unknown subfamily; uncharacterized proteins containing a CXXC motif with similarity to thioredoxin (TRX)-fold arsenic reductases, ArsC. Proteins containing a redox active CXXC motif like TRX and glutaredoxin (GRX) function as protein disulfide oxidoreductases, altering the redox state of target proteins via the reversible oxidation of the active site dithiol. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via GRX, through a single catalytic cysteine.


Pssm-ID: 239334  Cd Length: 111  Bit Score: 52.63  E-value: 6.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDD--EKIGDEAL 81
Cdd:cd03036    1 LKFYEYPKCSTCRKAKKWLDEHGVDYTAIDIVEEPPSKEELKKWLEKSGLPLKKFFNTSGKSYRELGLKDklPSLSEEEA 80

                         90
                 ....*....|....*....
gi 495129697  82 LDAMLAHPILINRPIVVTP 100
Cdd:cd03036   81 LELLSSDGMLIKRPFVVDD 99
ArsC_Spx cd03032
Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding ...
 4-98 2.49e-05

Arsenate Reductase (ArsC) family, Spx subfamily; Spx is a unique RNA polymerase (RNAP)-binding protein present in bacilli and some mollicutes. It inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP, disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA. In response to oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation. Spx has been shown to exert redox-sensitive transcriptional control over genes like trxA (TRX) and trxB (TRX reductase), genes that function in thiol homeostasis. This redox-sensitive activity is dependent on the presence of a CXXC motif, present in some members of the Spx subfamily, that acts as a thiol/disulfide switch. Spx has also been shown to repress genes in a sulfate-dependent manner independent of the presence of the CXXC motif.


Pssm-ID: 239330  Cd Length: 115  Bit Score: 40.69  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISVRALLRKNVEPYQALGLDDEKIGDEALLD 83
Cdd:cd03032    2 IKLYTSPSCSSCRKAKQWLEEHQIPFEERNLFKQPLTKEELKEILSLTENGVEDIISTRSKAFKNLNIDIDELSLSELIR 81

                         90
                 ....*....|....*
gi 495129697  84 AMLAHPILINRPIVV 98
Cdd:cd03032   82 LISEHPSLLRRPIII 96
ArsC_15kD cd03033
Arsenate Reductase (ArsC) family, 15kD protein subfamily; composed of proteins of unknown ...
 4-95 1.57e-04

Arsenate Reductase (ArsC) family, 15kD protein subfamily; composed of proteins of unknown function with similarity to thioredoxin-fold arsenic reductases, ArsC. It is encoded by an ORF present in a gene cluster associated with nitrogen fixation that also encodes dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase activating glycohydrolase (DRAG). ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from glutathione via glutaredoxin, through a single catalytic cysteine.


Pssm-ID: 239331  Cd Length: 113  Bit Score: 38.42  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISV---RALLR-KNVEpyqalgLDDEKIGDE 79
Cdd:cd03033    2 IIFYEKPGCANNARQKALLEAAGHEVEVRDLLTEPWTAETLRPFFGDLPVAEwfnPAAPRvKSGE------VVPEALDEE 75

                         90
                 ....*....|....*.
gi 495129697  80 ALLDAMLAHPILINRP 95
Cdd:cd03033   76 EALALMIADPLLIRRP 91
ArsC_Yffb cd03035
Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein ...
 4-100 1.28e-03

Arsenate Reductase (ArsC) family, Yffb subfamily; Yffb is an uncharacterized bacterial protein encoded by the yffb gene, related to the thioredoxin-fold arsenic reductases, ArsC. The structure of Yffb and the conservation of the catalytic cysteine suggest that it is likely to function as a glutathione (GSH)-dependent thiol reductase. ArsC catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)], using reducing equivalents derived from GSH via glutaredoxin, through a single catalytic cysteine.


Pssm-ID: 239333  Cd Length: 105  Bit Score: 36.03  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495129697   4 ITIYHNPACGTSRNTLGLIRNSGVEPAIILYLETPPTRDALKTLISDMGISvrALLRKNVEPYQALglDDEkigDEALLD 83
Cdd:cd03035    1 ITLYGIKNCDTVKKARKWLEARGVAYTFHDYRKDGLDAATLERWLAKVGWE--TLLNKRGTTWRKL--DDA---QKAALD 73

                         90       100
                 ....*....|....*....|...
gi 495129697  84 A------MLAHPILINRPIVVTP 100
Cdd:cd03035   74 AakaialMLEHPSLIKRPVLETG 96
 
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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