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Conserved domains on  [gi|15829570|ref|NP_308343|]
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xanthine dehydrogenase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

PRK11433 family protein( domain architecture ID 11485345)

PRK11433 family protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 12-228 3.61e-142

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


:

Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 396.07  E-value: 3.61e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   12 RVGKHEPHDLSLTRRDLIKVSAATAAAAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDALRENLH 91
Cdd:PRK11433   1 RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   92 LIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVA 171
Cdd:PRK11433  81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15829570  172 VLKEIQDGIPSHVTVDLVSPPERTADEIRERMSGNICRCGAYANILAAIEDAAGEIK 228
Cdd:PRK11433 161 VLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIEDVAGEIA 217
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 12-228 3.61e-142

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 396.07  E-value: 3.61e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   12 RVGKHEPHDLSLTRRDLIKVSAATAAAAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDALRENLH 91
Cdd:PRK11433   1 RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   92 LIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVA 171
Cdd:PRK11433  81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15829570  172 VLKEIQDGIPSHVTVDLVSPPERTADEIRERMSGNICRCGAYANILAAIEDAAGEIK 228
Cdd:PRK11433 161 VLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 61-228 3.19e-91

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: 264.65  E-value: 3.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  61 MPLTLKVNGKTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSP 140
Cdd:COG2080   2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570 141 DNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEIqdgipshvtvdlvspPERTADEIRERMSGNICRCGAYANILAAI 220
Cdd:COG2080  82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDEN---------------PNPTEEEIREALSGNLCRCTGYVRIVRAV 146


                ....*...
gi 15829570 221 EDAAGEIK 228
Cdd:COG2080 147 KRAAAALR 154
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
59-229 6.74e-54

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 170.36  E-value: 6.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   59 EIMPLTLKVNGKTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 138
Cdd:NF041020   7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  139 SPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvsPPERTADEIRERMSGNICRCGAYANILA 218
Cdd:NF041020  87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE---------------NPNPTEEEIRDGIHGNLCRCTGYQNIVK 151

                        170
                 ....*....|.
gi 15829570  219 AIEDAAGEIKS 229
Cdd:NF041020 152 AVKEASQKMKA 162
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 62-226 3.35e-40

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: 134.98  E-value: 3.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570    62 PLTLKVNGKTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLgSPD 141
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGI-AEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   142 NLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvsPPERTADEIRERMSGNICRCGAYANILAAIE 221
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRE---------------TPQPSDEDMEEGLSGNLCRCTGYGGIIRSAC 146


                  ....*
gi 15829570   222 DAAGE 226
Cdd:TIGR03198 147 RIRRG 151
Fer2_2 pfam01799
[2Fe-2S] binding domain;
133-220 6.13e-34

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 116.38  E-value: 6.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   133 TIEGLGSPDNlHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvSPPERTADEIRERMSGNICRCGA 212
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65


                  ....*...
gi 15829570   213 YANILAAI 220
Cdd:pfam01799  66 YRRIVDAV 73
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 63-112 3.10e-09

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: 52.40  E-value: 3.10e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15829570  63 LTLKVNGKTEQLEVDTRTTLLDALRENLhlIGTKKGCDHGQCGACTVLVN 112
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAG--IDIPYSCRAGACGTCKVEVV 48
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 12-228 3.61e-142

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 396.07  E-value: 3.61e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   12 RVGKHEPHDLSLTRRDLIKVSAATAAAAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDALRENLH 91
Cdd:PRK11433   1 RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   92 LIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVA 171
Cdd:PRK11433  81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 15829570  172 VLKEIQDGIPSHVTVDLVSPPERTADEIRERMSGNICRCGAYANILAAIEDAAGEIK 228
Cdd:PRK11433 161 VLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 61-228 3.19e-91

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: 264.65  E-value: 3.19e-91
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  61 MPLTLKVNGKTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSP 140
Cdd:COG2080   2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570 141 DNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEIqdgipshvtvdlvspPERTADEIRERMSGNICRCGAYANILAAI 220
Cdd:COG2080  82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDEN---------------PNPTEEEIREALSGNLCRCTGYVRIVRAV 146


                ....*...
gi 15829570 221 EDAAGEIK 228
Cdd:COG2080 147 KRAAAALR 154
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
59-229 6.74e-54

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 170.36  E-value: 6.74e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   59 EIMPLTLKVNGKTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 138
Cdd:NF041020   7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  139 SPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvsPPERTADEIRERMSGNICRCGAYANILA 218
Cdd:NF041020  87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE---------------NPNPTEEEIRDGIHGNLCRCTGYQNIVK 151

                        170
                 ....*....|.
gi 15829570  219 AIEDAAGEIKS 229
Cdd:NF041020 152 AVKEASQKMKA 162
XdhA COG4630
Xanthine dehydrogenase, Fe-S cluster and FAD-binding subunit XdhA [Nucleotide transport and ...
 67-225 4.61e-42

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


Pssm-ID: 443668 [Multi-domain]  Cd Length: 476  Bit Score: 148.36  E-value: 4.61e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  67 VNGKTEQLE-VDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLV----NGRR----LNACLTLAVMHQGAEITTIEGL 137
Cdd:COG4630   5 LNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVgeldDGGLryraVNACILFLPQLDGKALVTVEGL 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570 138 GSPD-NLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvsPPERTADEIRERMSGNICRCGAYANI 216
Cdd:COG4630  85 AGPDgALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYER---------------GPAPDRADIEDALSGNLCRCTGYRPI 149


                ....*....
gi 15829570 217 LAAIEDAAG 225
Cdd:COG4630 150 IDAARAMAE 158
pucE TIGR03198
xanthine dehydrogenase E subunit; This gene has been characterized in B. subtilis as the ...
 62-226 3.35e-40

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: 134.98  E-value: 3.35e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570    62 PLTLKVNGKTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLgSPD 141
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGI-AEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   142 NLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvsPPERTADEIRERMSGNICRCGAYANILAAIE 221
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRE---------------TPQPSDEDMEEGLSGNLCRCTGYGGIIRSAC 146


                  ....*
gi 15829570   222 DAAGE 226
Cdd:TIGR03198 147 RIRRG 151
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
59-222 1.35e-34

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 121.18  E-value: 1.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   59 EIMPLTLKVNGKTEQLEVDTRTTLLDALRENlHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 138
Cdd:PRK09908   5 ETITIECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  139 SPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvsPPER--TADEIRERMSGNICRCGAYANI 216
Cdd:PRK09908  84 KGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAK---------------PREKplTITEIRRGLAGNLCRCTGYQMI 148


                 ....*.
gi 15829570  217 LAAIED 222
Cdd:PRK09908 149 VNTVLD 154
Fer2_2 pfam01799
[2Fe-2S] binding domain;
133-220 6.13e-34

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 116.38  E-value: 6.13e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   133 TIEGLGSPDNlHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKEiqdgipshvtvdlvSPPERTADEIRERMSGNICRCGA 212
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65


                  ....*...
gi 15829570   213 YANILAAI 220
Cdd:pfam01799  66 YRRIVDAV 73
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
 63-219 3.83e-30

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: 117.42  E-value: 3.83e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570     63 LTLKVNG-KTEQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVLVN-----GRRL-----NACLTLAVMHQGAEI 131
Cdd:TIGR02969    3 LLFYVNGrKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISrynpsTKSIrhhpvNACLTPICSLYGAAV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570    132 TTIEGLGSPDN-LHPMQAAFIKHDGFQCGYCTSGQICSSVAVLKeiqdgipSHvtvdlvspPERTADEIRERMSGNICRC 210
Cdd:TIGR02969   83 TTVEGIGSTRTrLHPVQERIAKCHGTQCGFCTPGMVMSMYALLR-------NH--------PEPTLDQLTDALGGNLCRC 147


                   ....*....
gi 15829570    211 GAYANILAA 219
Cdd:TIGR02969  148 TGYRPIIDA 156
PLN02906 PLN02906
xanthine dehydrogenase
 81-219 2.06e-27

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 109.79  E-value: 2.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570    81 TLLDALREnLHLIGTKKGCDHGQCGACTVLV----------NGRRLNACLTLAVMHQGAEITTIEGLGS-PDNLHPMQAA 149
Cdd:PLN02906    3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVMVshydrktgkcVHYAVNACLAPLYSVEGMHVITVEGIGNrRDGLHPVQEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   150 FIKHDGFQCGYCTSGQICSSVAVLKEIQDgipshvtvdlvsPPerTADEIRERMSGNICRCGAYANILAA 219
Cdd:PLN02906   82 LASMHGSQCGFCTPGFIMSMYALLRSSKT------------PP--TEEQIEECLAGNLCRCTGYRPILDA 137
PLN00192 PLN00192
aldehyde oxidase
 61-227 6.05e-24

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 99.79  E-value: 6.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570    61 MPLTLKVNGKT-EQLEVDTRTTLLDALRENLHLIGTKKGCDHGQCGACTVL----------VNGRRLNACLTLAVMHQGA 129
Cdd:PLN00192    4 MSLVFAVNGERfELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLlskydpvldqVEDFTVSSCLTLLCSVNGC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   130 EITTIEGLG-SPDNLHPMQAAFikhDGF---QCGYCTSGqICSSV--AVLKeiqdgipSHVTVDLVSPP---ERTADEIR 200
Cdd:PLN00192   84 SITTSEGLGnSKDGFHPIHKRF---AGFhasQCGFCTPG-MCISLfsALVN-------ADKTDRPEPPSgfsKLTVVEAE 152

                         170       180
                  ....*....|....*....|....*..
gi 15829570   201 ERMSGNICRCGAYANILAAIEDAAGEI 227
Cdd:PLN00192  153 KAVSGNLCRCTGYRPIVDACKSFAADV 179
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 63-112 3.10e-09

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: 52.40  E-value: 3.10e-09
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 15829570  63 LTLKVNGKTEQLEVDTRTTLLDALRENLhlIGTKKGCDHGQCGACTVLVN 112
Cdd:cd00207   1 VTINVPGSGVEVEVPEGETLLDAAREAG--IDIPYSCRAGACGTCKVEVV 48
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
 61-228 5.82e-08

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 52.53  E-value: 5.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570   61 MPLTLKVNGKTEQLEvdtrTTLLDALRENLHLIG--TKKGCDHGQ--CGACTVLVNGRRLNACLTLAVMHQGAEITTIEG 136
Cdd:PRK09800   1 MIIHFTLNGAPQELT----VNPGENVQKLLFNMGmhSVRNSDDGFgfAGSDAIIFNGNIVNASLLIAAQLEKADIRTAES 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  137 LGSPDNLHPMQAAFIKHDGFQCGYCTSgqicSSVAVLKEIQDGIPShvtvdlvspPERtaDEIRERMSGNICRCGAYANI 216
Cdd:PRK09800  77 LGKWNELSLVQQAMVDVGVVQSGYNDP----AAALIITDLLDRIAA---------PTR--EEIDDALSGLFSRDAGWQQY 141

                        170
                 ....*....|..
gi 15829570  217 LAAIEDAAGEIK 228
Cdd:PRK09800 142 YQVIELAVARKN 153
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
65-112 9.83e-08

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 47.90  E-value: 9.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15829570    65 LKVNGKTEQLEVDT-RTTLLDALRENLhlIGTKKGCDHGQCGACTVLVN 112
Cdd:pfam00111   1 VTINGKGVTIEVPDgETTLLDAAEEAG--IDIPYSCRGGGCGTCAVKVL 47
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
73-138 9.04e-07

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 48.59  E-value: 9.04e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15829570   73 QLEVDTRTTLLDALR----ENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLA--VMHQGAEITTIEGLG 138
Cdd:PRK12576  28 KVKVDRFTQVTEALRrikeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIEPMD 99
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 61-122 3.45e-06

Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440247 [Multi-domain]  Cd Length: 230  Bit Score: 46.28  E-value: 3.45e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570  61 MPLTLKV---NGKTE--------QLEVDTRTTLLDALrenLHLIGTKKG-------CDHGQCGACTVLVNGR-RLnACLT 121
Cdd:COG0479   1 MTVTLKIwrqDPETDskprfqtyEVPVSPGMTVLDAL---DYIKEEQDPtlafrrsCREGICGSCAMVINGRpRL-ACQT 76


                .
gi 15829570 122 L 122
Cdd:COG0479  77 H 77
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 73-138 1.15e-05

succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase and fumarate reductase are reverse directions of the same enzymatic interconversion, succinate + FAD+ = fumarate + FADH2 (EC 1.3.11.1). In E. coli, the forward and reverse reactions are catalyzed by distinct complexes: fumarate reductase operates under anaerobic conditions and succinate dehydrogenase operates under aerobic conditions. This model also describes a region of the B subunit of a cytosolic archaeal fumarate reductase. [Energy metabolism, Aerobic, Energy metabolism, Anaerobic, Energy metabolism, TCA cycle]


Pssm-ID: 273049 [Multi-domain]  Cd Length: 220  Bit Score: 44.73  E-value: 1.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829570    73 QLEVDTRTTLLDALRE-NLHLIGT---KKGCDHGQCGACTVLVNGRRLNACLTlAVMHQGAEITTIEGLG 138
Cdd:TIGR00384  18 EVPADEGMTVLDALNYiKDEQDPSlafRRSCRNGICGSCAMNVNGKPVLACKT-KVEDLGQPVMKIEPLP 86
Fer2_3 pfam13085
2Fe-2S iron-sulfur cluster binding domain; The 2Fe-2S ferredoxin family have a general core ...
 73-122 3.89e-05

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: 41.45  E-value: 3.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15829570    73 QLEVDTRTTLLDALRE-NLHLIGT---KKGCDHGQCGACTVLVNGR-RLnACLTL 122
Cdd:pfam13085  22 EVPYEEGMTVLDALNKiKEEQDPTlafRRSCREGICGSCAMNINGKpRL-ACKTL 75
Fdx COG0633
Ferredoxin [Energy production and conversion];
61-111 1.76e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440398 [Multi-domain]  Cd Length: 87  Bit Score: 36.36  E-value: 1.76e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15829570  61 MPlTLKVNGKTEQLEVDTRTTLLDALREN-LHLIGtkkGCDHGQCGACTVLV 111
Cdd:COG0633   1 MP-KVTFIPEGHTVEVPAGESLLEAALRAgIDLPY---SCRSGACGTCHVRV 48
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 62-111 2.28e-03

Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and conversion]; Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF is part of the Pathway/BioSystem: Na+-translocating NADH dehydrogenase


Pssm-ID: 442118 [Multi-domain]  Cd Length: 396  Bit Score: 38.30  E-value: 2.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 15829570  62 PLTLKVNGKTEQLEVDTRTTLLDAL-RENLHLIGtkkGCD-HGQCGACTVLV 111
Cdd:COG2871  34 EVKITINGDGKEIEVEEGQTLLDALlRQGIFLPS---ACGgGGTCGQCKVKV 82
PRK12577 PRK12577
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
70-119 5.73e-03

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 183605 [Multi-domain]  Cd Length: 329  Bit Score: 36.98  E-value: 5.73e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15829570   70 KTEQLEVDTRTTLLDAL-RENLHLIGT---KKGCDHGQCGACTVLVNGRRLNAC 119
Cdd:PRK12577  19 QTYTLEVEPGNTILDCLnRIKWEQDGSlafRKNCRNTICGSCAMRINGRSALAC 72
 
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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