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Conserved domains on  [gi|511524224|gb|AGN81765|]
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(2Fe-2S)-binding protein [Pseudomonas putida H8234]

Protein Classification

(2Fe-2S)-binding protein( domain architecture ID 11449880)

(2Fe-2S)-binding protein is the small subunit of a dehydrogenase or oxidoreductase enzyme complex such as carbon monoxide dehydrogenase and isoquinoline 1-oxidoreductase; contains a a 2Fe-2S ferredoxin-type domain which binds 2Fe-2S clusters

Gene Ontology:  GO:0046872|GO:0051536|GO:0051537
PubMed:  11734195
SCOP:  3000113

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 12-165 3.19e-89

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


:

Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 257.33  E-value: 3.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  12 HPIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASD 91
Cdd:COG2080    2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511524224  92 GELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLMKD 165
Cdd:COG2080   82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRAAAALRG 155
 
Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 12-165 3.19e-89

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 257.33  E-value: 3.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  12 HPIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASD 91
Cdd:COG2080    2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511524224  92 GELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLMKD 165
Cdd:COG2080   82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRAAAALRG 155
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 5-159 5.77e-75

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 223.88  E-value: 5.77e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   5 APEGVVEHPIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVT 84
Cdd:PRK11433  43 ATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  85 IEGLASDGELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHE------GHAD---------SREAIREQMSGNLCRCGAY 149
Cdd:PRK11433 123 IEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEikdgipSHVTvdltaapelTADEIRERMSGNICRCGAY 202

                        170
                 ....*....|
gi 511524224 150 GNIVAAVEEA 159
Cdd:PRK11433 203 SNILEAIEDV 212
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
14-165 3.63e-56

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 174.21  E-value: 3.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  14 IHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDGE 93
Cdd:NF041020  11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGK 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511524224  94 LHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLMKD 165
Cdd:NF041020  91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEASQKMKA 162
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 13-159 2.58e-47

xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.


Pssm-ID: 132242 [Multi-domain]  Cd Length: 151  Bit Score: 151.16  E-value: 2.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   13 PIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDg 92
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAEN- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511524224   93 ELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEA 159
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSACRI 148
Fer2_2 pfam01799
[2Fe-2S] binding domain;
84-156 3.13e-35

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 117.92  E-value: 3.13e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511524224   84 TIEGLASDGElHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREA-IREQMSGNLCRCGAYGNIVAAV 156
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPPPPTEAeIREALSGNLCRCTGYRRIVDAV 73
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 14-74 1.36e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 44.31  E-value: 1.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511524224  14 IHLTLNGQPRSLQVQPWTTLLDLLREQLdlIGTKKGCDHGQCGACTV------------------LRDGKRINACLTLA 74
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAG--IDIPYSCRAGACGTCKVevvegevdqsdpslldeeEAEGGYVLACQTRV 77
 
Name Accession Description Interval E-value
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 12-165 3.19e-89

Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and conversion]; Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441683 [Multi-domain]  Cd Length: 155  Bit Score: 257.33  E-value: 3.19e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  12 HPIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASD 91
Cdd:COG2080    2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511524224  92 GELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLMKD 165
Cdd:COG2080   82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDENPNPTEEEIREALSGNLCRCTGYVRIVRAVKRAAAALRG 155
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 5-159 5.77e-75

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 223.88  E-value: 5.77e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   5 APEGVVEHPIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVT 84
Cdd:PRK11433  43 ATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLHLTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  85 IEGLASDGELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHE------GHAD---------SREAIREQMSGNLCRCGAY 149
Cdd:PRK11433 123 IEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVAVLKEikdgipSHVTvdltaapelTADEIRERMSGNICRCGAY 202

                        170
                 ....*....|
gi 511524224 150 GNIVAAVEEA 159
Cdd:PRK11433 203 SNILEAIEDV 212
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
14-165 3.63e-56

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 174.21  E-value: 3.63e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  14 IHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDGE 93
Cdd:NF041020  11 IRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLSKDGK 90

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 511524224  94 LHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLMKD 165
Cdd:NF041020  91 LHPIQEAFWENHALQCGYCTPGMIMQAYFLLKENPNPTEEEIRDGIHGNLCRCTGYQNIVKAVKEASQKMKA 162
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
 14-159 2.80e-55

Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and metabolism];


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 181.10  E-value: 2.80e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  14 IHLTLNGQPRSLQ-VQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTV----LRDGKR----INACLTLAIMCDGAELVT 84
Cdd:COG4630    1 IRFLLNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVvvgeLDDGGLryraVNACILFLPQLDGKALVT 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511524224  85 IEGLAS-DGELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEA 159
Cdd:COG4630   81 VEGLAGpDGALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYERGPAPDRADIEDALSGNLCRCTGYRPIIDAARAM 156
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 13-159 2.58e-47

xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the Iron-sulfur cluster binding-subunit of xanthine dehydrogenase (pucE), acting in conjunction with pucC, the FAD-binding subunit and pucD, the molybdopterin binding subunit. The more common XDH complex (GenProp0640) includes the xdhA gene as the Fe-S cluster binding component.


Pssm-ID: 132242 [Multi-domain]  Cd Length: 151  Bit Score: 151.16  E-value: 2.58e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   13 PIHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDg 92
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGIAEN- 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 511524224   93 ELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEA 159
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRETPQPSDEDMEEGLSGNLCRCTGYGGIIRSACRI 148
4hydroxCoAred TIGR03193
4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts ...
 14-159 5.27e-45

4-hydroxybenzoyl-CoA reductase, gamma subunit; 4-hydroxybenzoyl-CoA reductase converts 4-hydroxybenzoyl-CoA to benzoyl-CoA, a common intermediate in the degradation of aromatic compounds. This protein family represents the gamma chain of this three-subunit enzyme.


Pssm-ID: 132237 [Multi-domain]  Cd Length: 148  Bit Score: 145.40  E-value: 5.27e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   14 IHLTLNGQPRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDGE 93
Cdd:TIGR03193   2 LRLTVNGRWREDAVADNMLLVDYLRDTVGLTGTKQGCDGGECGACTVLVDGRPRLACSTLAHRVAGRKVETVEGLATNGR 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511524224   94 LHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEA 159
Cdd:TIGR03193  82 LSRLQQAFHERLGTQCGFCTPGMIMAAEALLRRNPSPSRDEIRAALAGNLCRCTGYVKIIESVEAA 147
xanthine_xdhA TIGR02963
xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit ...
 18-170 2.13e-42

xanthine dehydrogenase, small subunit; Members of this protein family are the small subunit (or, in eukaryotes, the N-terminal domain) of xanthine dehydrogenase, an enzyme of purine catabolism via urate. The small subunit contains both an FAD and a 2Fe-2S cofactor. Aldehyde oxidase (retinal oxidase) appears to have arisen as a neofunctionalization among xanthine dehydrogenases in eukaryotes and [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 274365 [Multi-domain]  Cd Length: 467  Bit Score: 147.04  E-value: 2.13e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   18 LNGQPRSLQ-VQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTV----LRDGKRI-----NACLTLAIMCDGAELVTIEG 87
Cdd:TIGR02963   5 LNGETVTLSdVDPTRTLLDYLREDAGLTGTKEGCAEGDCGACTVvvgeLVDGGKLryrsvNACIQFLPSLDGKAVVTVED 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   88 LAS-DGELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVaaveEAMPLMKDV 166
Cdd:TIGR02963  85 LRQpDGRLHPVQQAMVECHGSQCGFCTPGFVMSLYALYKNSPAPSRADIEDALQGNLCRCTGYRPIL----DAAEAAFDY 160


                  ....
gi 511524224  167 PRQQ 170
Cdd:TIGR02963 161 PCSD 164
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
14-156 2.50e-40

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 133.89  E-value: 2.50e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  14 IHLTLNGQPRSLQVQPWTTLLDLLREQlDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDGE 93
Cdd:PRK09908   9 IECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEAKGGK 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 511524224  94 LHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHAD--SREAIREQMSGNLCRCGAYGNIVAAV 156
Cdd:PRK09908  88 LSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPREKplTITEIRRGLAGNLCRCTGYQMIVNTV 152
Fer2_2 pfam01799
[2Fe-2S] binding domain;
84-156 3.13e-35

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 117.92  E-value: 3.13e-35
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511524224   84 TIEGLASDGElHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREA-IREQMSGNLCRCGAYGNIVAAV 156
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLERNPPPPTEAeIREALSGNLCRCTGYRRIVDAV 73
Se_dep_XDH TIGR03311
selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional ...
 16-170 5.09e-34

selenium-dependent xanthine dehydrogenase; Members of this protein resemble conventional xanthine dehydrogenase enzymes, which depend on molybdenum cofactor - molybdopterin bound to molybdate with two sulfur atoms as ligands. But all members of this family occur in species that contain markers for the biosynthesis of enzymes with a selenium-containing form of molybdenum cofactor. The member of this family from Enterococcus faecalis has been shown to act as a xanthine dehydrogenenase, and its activity if dependent on SelD (selenophosphate synthase), selenium, and molybdenum. [Purines, pyrimidines, nucleosides, and nucleotides, Other]


Pssm-ID: 132354 [Multi-domain]  Cd Length: 848  Bit Score: 126.49  E-value: 5.09e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   16 LTLNGqpRSLQVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLaSDGELH 95
Cdd:TIGR03311   3 FIVNG--REVDVNEEKKLLEFLREDLRLTGVKNGCGEGACGACTVIVNGKAVRACRFTTAKLAGKEITTVEGL-TEREKD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511524224   96 PLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLM---KDVPRQQ 170
Cdd:TIGR03311  80 VYAWAFAKAGAVQCGFCIPGMVISAKALLDKNPNPTEAEIKKALKGNICRCTGYVKIIKAVRLAAKAFreeIEPPRGE 157
PLN02906 PLN02906
xanthine dehydrogenase
 32-155 3.99e-30

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 115.18  E-value: 3.99e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   32 TLLDLLREqLDLIGTKKGCDHGQCGACTVL-----RDGKR-----INACLTLAIMCDGAELVTIEGLAS--DGeLHPLQR 99
Cdd:PLN02906    3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVMvshydRKTGKcvhyaVNACLAPLYSVEGMHVITVEGIGNrrDG-LHPVQE 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 511524224  100 AFIRHDAFQCGYCTPGQICSAVGLVH-EGHADSREAIREQMSGNLCRCGAYGNIVAA 155
Cdd:PLN02906   81 ALASMHGSQCGFCTPGFIMSMYALLRsSKTPPTEEQIEECLAGNLCRCTGYRPILDA 137
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
 26-155 9.99e-28

aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, closely related to xanthine dehydrogenase/oxidase.


Pssm-ID: 132014 [Multi-domain]  Cd Length: 1330  Bit Score: 108.56  E-value: 9.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224    26 QVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVL-----RDGKRI-----NACLTLAIMCDGAELVTIEGLASD-GEL 94
Cdd:TIGR02969   16 NVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMisrynPSTKSIrhhpvNACLTPICSLYGAAVTTVEGIGSTrTRL 95

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 511524224    95 HPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAA 155
Cdd:TIGR02969   96 HPVQERIAKCHGTQCGFCTPGMVMSMYALLRNHPEPTLDQLTDALGGNLCRCTGYRPIIDA 156
PLN00192 PLN00192
aldehyde oxidase
 10-155 1.30e-22

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 93.63  E-value: 1.30e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   10 VEHPIHLTLNGQPRSL-QVQPWTTLLDLLREQLDLIGTKKGCDHGQCGACTVLR----------DGKRINACLTLAIMCD 78
Cdd:PLN00192    2 SNMSLVFAVNGERFELsSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLLskydpvldqvEDFTVSSCLTLLCSVN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224   79 GAELVTIEGLAS--DGeLHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQ------------MSGNLC 144
Cdd:PLN00192   82 GCSITTSEGLGNskDG-FHPIHKRFAGFHASQCGFCTPGMCISLFSALVNADKTDRPEPPSGfskltvveaekaVSGNLC 160

                         170
                  ....*....|.
gi 511524224  145 RCGAYGNIVAA 155
Cdd:PLN00192  161 RCTGYRPIVDA 171
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
 14-165 1.87e-14

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 70.25  E-value: 1.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 511524224  14 IHLTLNGQPRSLQVQPWTTLLDLLReQLDLIGTKKGCD-HGQCGACTVLRDGKRINACLTLAIMCDGAELVTIEGLASDG 92
Cdd:PRK09800   3 IHFTLNGAPQELTVNPGENVQKLLF-NMGMHSVRNSDDgFGFAGSDAIIFNGNIVNASLLIAAQLEKADIRTAESLGKWN 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 511524224  93 ELHPLQRAFIRHDAFQCGYCTPGQICSAVGLVHEGHADSREAIREQMSGNLCRCGAYGNIVAAVEEAMPLMKD 165
Cdd:PRK09800  82 ELSLVQQAMVDVGVVQSGYNDPAAALIITDLLDRIAAPTREEIDDALSGLFSRDAGWQQYYQVIELAVARKNN 154
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 14-74 1.36e-06

2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in electron transfer processes and in various enzymatic reactions. The family includes plant and algal ferredoxins, which act as electron carriers in photosynthesis and ferredoxins, which participate in redox chains (from bacteria to mammals). Fold is ismilar to thioredoxin.


Pssm-ID: 238126 [Multi-domain]  Cd Length: 84  Bit Score: 44.31  E-value: 1.36e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 511524224  14 IHLTLNGQPRSLQVQPWTTLLDLLREQLdlIGTKKGCDHGQCGACTV------------------LRDGKRINACLTLA 74
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAG--IDIPYSCRAGACGTCKVevvegevdqsdpslldeeEAEGGYVLACQTRV 77
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
16-74 4.13e-05

2Fe-2S iron-sulfur cluster binding domain;


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 40.20  E-value: 4.13e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 511524224   16 LTLNGQPRSLQVQPW-TTLLDLLREQLdlIGTKKGCDHGQCGACTV------------------LRDGKRINACLTLA 74
Cdd:pfam00111   1 VTINGKGVTIEVPDGeTTLLDAAEEAG--IDIPYSCRGGGCGTCAVkvlegedqsdqsfleddeLAAGYVVLACQTYP 76
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
21-88 2.74e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 37.04  E-value: 2.74e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 511524224  21 QPRSLQVQPWTTLLDLLR----EQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLA--IMCDGAELVTIEGL 88
Cdd:PRK12576  25 QEYKVKVDRFTQVTEALRrikeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIEPM 98
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 27-88 6.94e-03

2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core structure consisting of beta(2)-alpha-beta(2) which abeta-grasp type fold. The domain is around one hundred amino acids with four conserved cysteine residues to which the 2Fe-2S cluster is ligated.


Pssm-ID: 432963 [Multi-domain]  Cd Length: 107  Bit Score: 34.52  E-value: 6.94e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 511524224   27 VQPWTTLLDLL----REQLDLIGTKKGCDHGQCGACTVLRDGKRINACLTLaIMCDGAELVTIEGL 88
Cdd:pfam13085  25 YEEGMTVLDALnkikEEQDPTLAFRRSCREGICGSCAMNINGKPRLACKTL-IDDLLGQDITLEPL 89
 
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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