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Conserved domains on  [gi|445992844|ref|WP_000070699|]
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MULTISPECIES: aldehyde dehydrogenase iron-sulfur subunit [Enterobacteriaceae]

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 4.35e-139

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


:

Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 388.36  E-value: 4.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  12 RVGKHEPHDLSLTRRDLIKVSAATAATAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLH 91
Cdd:PRK11433   1 RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  92 LIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVA 171
Cdd:PRK11433  81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445992844 172 ALKEIQDGIPSHVTVDLVSAPETTADEIRERMSGNICRCGAYANILAAIEDAAGEIK 228
Cdd:PRK11433 161 VLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIEDVAGEIA 217
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 12-228 4.35e-139

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 388.36  E-value: 4.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  12 RVGKHEPHDLSLTRRDLIKVSAATAATAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLH 91
Cdd:PRK11433   1 RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  92 LIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVA 171
Cdd:PRK11433  81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445992844 172 ALKEIQDGIPSHVTVDLVSAPETTADEIRERMSGNICRCGAYANILAAIEDAAGEIK 228
Cdd:PRK11433 161 VLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 61-228 2.98e-90

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: 262.34  E-value: 2.98e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  61 MPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSP 140
Cdd:COG2080    2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 141 DNLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEIqdgipshvtvdlvsaPETTADEIRERMSGNICRCGAYANILAAI 220
Cdd:COG2080   82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDEN---------------PNPTEEEIREALSGNLCRCTGYVRIVRAV 146


                 ....*...
gi 445992844 221 EDAAGEIK 228
Cdd:COG2080  147 KRAAAALR 154
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
59-229 3.87e-54

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 171.13  E-value: 3.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  59 EIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 138
Cdd:NF041020   7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 139 SPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvsAPETTADEIRERMSGNICRCGAYANILA 218
Cdd:NF041020  87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE---------------NPNPTEEEIRDGIHGNLCRCTGYQNIVK 151

                        170
                 ....*....|.
gi 445992844 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 1.30e-39

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: 133.44  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844   62 PLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLgSPD 141
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGI-AEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  142 NLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvsAPETTADEIRERMSGNICRCGAYANILAAIE 221
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRE---------------TPQPSDEDMEEGLSGNLCRCTGYGGIIRSAC 146


                  ....*
gi 445992844  222 DAAGE 226
Cdd:TIGR03198 147 RIRRG 151
Fer2_2 pfam01799
[2Fe-2S] binding domain;
133-220 3.72e-34

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 117.15  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  133 TIEGLGSPDNlHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvSAPETTADEIRERMSGNICRCGA 212
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65


                  ....*...
gi 445992844  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 3.76e-08

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: 49.32  E-value: 3.76e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 445992844  63 LTLKVNGKTEQLEVDTRTTLLDTLRENLhlIGTKKGCDHGQCGACTVLVN 112
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAG--IDIPYSCRAGACGTCKVEVV 48
 
Name Accession Description Interval E-value
PRK11433 PRK11433
aldehyde oxidoreductase 2Fe-2S subunit; Provisional
 12-228 4.35e-139

aldehyde oxidoreductase 2Fe-2S subunit; Provisional


Pssm-ID: 236910 [Multi-domain]  Cd Length: 217  Bit Score: 388.36  E-value: 4.35e-139
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  12 RVGKHEPHDLSLTRRDLIKVSAATAATAVVYPHSTLAASVPAATPAPEIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLH 91
Cdd:PRK11433   1 RVGMHEPHDLSLTRRDLLKVSAATAATAAAYPHSTLAASVPAATPAPEISPVTLKVNGKTEQLEVDTRTTLLDALREHLH 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  92 LIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVA 171
Cdd:PRK11433  81 LTGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSPDNLHPMQAAFVKHDGFQCGYCTPGQICSSVA 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 445992844 172 ALKEIQDGIPSHVTVDLVSAPETTADEIRERMSGNICRCGAYANILAAIEDAAGEIK 228
Cdd:PRK11433 161 VLKEIKDGIPSHVTVDLTAAPELTADEIRERMSGNICRCGAYSNILEAIEDVAGEIA 217
CutS COG2080
Aldehyde, CO, or xanthine dehydrogenase, Fe-S subunit, CoxS/CutS family [Energy production and ...
 61-228 2.98e-90

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: 262.34  E-value: 2.98e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  61 MPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLGSP 140
Cdd:COG2080    2 MMITLTVNGKPVEVDVDPDTPLLDVLRDDLGLTGTKFGCGHGQCGACTVLVDGKAVRSCLTLAVQADGKEITTIEGLAED 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 141 DNLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEIqdgipshvtvdlvsaPETTADEIRERMSGNICRCGAYANILAAI 220
Cdd:COG2080   82 GELHPLQQAFIEHGALQCGYCTPGMIMAAVALLDEN---------------PNPTEEEIREALSGNLCRCTGYVRIVRAV 146


                 ....*...
gi 445992844 221 EDAAGEIK 228
Cdd:COG2080  147 KRAAAALR 154
glyceraldDH_gamma NF041020
glyceraldehyde dehydrogenase subunit gamma;
59-229 3.87e-54

glyceraldehyde dehydrogenase subunit gamma;


Pssm-ID: 468949 [Multi-domain]  Cd Length: 162  Bit Score: 171.13  E-value: 3.87e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  59 EIMPLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 138
Cdd:NF041020   7 EKVKIRVKVNGVWYEAEVEPRKLLVHFLRDDLGFTGTHVGCDTSTCGACTVIMNGKSVKSCTVLAVQADGAEITTIEGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 139 SPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvsAPETTADEIRERMSGNICRCGAYANILA 218
Cdd:NF041020  87 KDGKLHPIQEAFWENHALQCGYCTPGMIMQAYFLLKE---------------NPNPTEEEIRDGIHGNLCRCTGYQNIVK 151

                        170
                 ....*....|.
gi 445992844 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 4.07e-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: 4.07e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  67 VNGKTEQLE-VDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLV----NGRR----LNACLTLAVMHQGAEITTIEGL 137
Cdd:COG4630    5 LNGELVELSdVPPTTTLLDWLREDRGLTGTKEGCAEGDCGACTVVVgeldDGGLryraVNACILFLPQLDGKALVTVEGL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 138 GSPD-NLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvsAPETTADEIRERMSGNICRCGAYANI 216
Cdd:COG4630   85 AGPDgALHPVQQAMVDHHGSQCGFCTPGFVMSLFALYER---------------GPAPDRADIEDALSGNLCRCTGYRPI 149


                 ....*....
gi 445992844 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 1.30e-39

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: 133.44  E-value: 1.30e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844   62 PLTLKVNGKTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLgSPD 141
Cdd:TIGR03198   3 QFRFTVNGQAWEVAAVPTTRLSDLLRKELQLTGTKVSCGIGRCGACSVLIDGKLANACLTMAYQADGHEITTIEGI-AEN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  142 NLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvsAPETTADEIRERMSGNICRCGAYANILAAIE 221
Cdd:TIGR03198  82 ELDPCQTAFLEEGGFQCGYCTPGMVVALKALFRE---------------TPQPSDEDMEEGLSGNLCRCTGYGGIIRSAC 146


                  ....*
gi 445992844  222 DAAGE 226
Cdd:TIGR03198 147 RIRRG 151
Fer2_2 pfam01799
[2Fe-2S] binding domain;
133-220 3.72e-34

[2Fe-2S] binding domain;


Pssm-ID: 460336 [Multi-domain]  Cd Length: 73  Bit Score: 117.15  E-value: 3.72e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  133 TIEGLGSPDNlHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEiqdgipshvtvdlvSAPETTADEIRERMSGNICRCGA 212
Cdd:pfam01799   1 TIEGLAESGG-EPVQQAFAEAGAVQCGYCTPGMIMSAYALLER--------------NPPPPTEAEIREALSGNLCRCTG 65


                  ....*...
gi 445992844  213 YANILAAI 220
Cdd:pfam01799  66 YRRIVDAV 73
PRK09908 PRK09908
xanthine dehydrogenase iron sulfur-binding subunit XdhC;
59-222 8.23e-34

xanthine dehydrogenase iron sulfur-binding subunit XdhC;


Pssm-ID: 182139 [Multi-domain]  Cd Length: 159  Bit Score: 118.87  E-value: 8.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  59 EIMPLTLKVNGKTEQLEVDTRTTLLDTLRENlHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLAVMHQGAEITTIEGLG 138
Cdd:PRK09908   5 ETITIECTINGMPFQLHAAPGTPLSELLREQ-GLLSVKQGCCVGECGACTVLVDGTAIDSCLYLAAWAEGKEIRTLEGEA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 139 SPDNLHPMQAAFIKHDGFQCGYCTSGQICSSVAALKEIQdgipshvtvdlvSAPETTAdEIRERMSGNICRCGAYANILA 218
Cdd:PRK09908  84 KGGKLSHVQQAYAKSGAVQCGFCTPGLIMATTAMLAKPR------------EKPLTIT-EIRRGLAGNLCRCTGYQMIVN 150


                 ....
gi 445992844 219 AIED 222
Cdd:PRK09908 151 TVLD 154
mam_aldehyde_ox TIGR02969
aldehyde oxidase; Members of this family are mammalian aldehyde oxidase (EC 1.2.3.1) isozymes, ...
 63-219 5.46e-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: 117.03  E-value: 5.46e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844    63 LTLKVNG-KTEQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVLVN-----GRRL-----NACLTLAVMHQGAEI 131
Cdd:TIGR02969    3 LLFYVNGrKVVEKNVDPETMLLPYLRKKLRLTGTKYGCGGGGCGACTVMISrynpsTKSIrhhpvNACLTPICSLYGAAV 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844   132 TTIEGLGSPDN-LHPMQAAFIKHDGFQCGYCTSGQICSSVAALKeiqdgipshvtvdlvSAPETTADEIRERMSGNICRC 210
Cdd:TIGR02969   83 TTVEGIGSTRTrLHPVQERIAKCHGTQCGFCTPGMVMSMYALLR---------------NHPEPTLDQLTDALGGNLCRC 147


                   ....*....
gi 445992844   211 GAYANILAA 219
Cdd:TIGR02969  148 TGYRPIIDA 156
PLN02906 PLN02906
xanthine dehydrogenase
 81-219 1.74e-26

xanthine dehydrogenase


Pssm-ID: 215491 [Multi-domain]  Cd Length: 1319  Bit Score: 107.09  E-value: 1.74e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844   81 TLLDTLREnLHLIGTKKGCDHGQCGACTVLV----------NGRRLNACLTLAVMHQGAEITTIEGLGS-PDNLHPMQAA 149
Cdd:PLN02906    3 TLLEYLRD-LGLTGTKLGCGEGGCGACTVMVshydrktgkcVHYAVNACLAPLYSVEGMHVITVEGIGNrRDGLHPVQEA 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  150 FIKHDGFQCGYCTSGQICSSVAALKEIQDgipshvtvdlvsAPetTADEIRERMSGNICRCGAYANILAA 219
Cdd:PLN02906   82 LASMHGSQCGFCTPGFIMSMYALLRSSKT------------PP--TEEQIEECLAGNLCRCTGYRPILDA 137
PLN00192 PLN00192
aldehyde oxidase
 61-227 1.04e-24

aldehyde oxidase


Pssm-ID: 215096 [Multi-domain]  Cd Length: 1344  Bit Score: 101.72  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844   61 MPLTLKVNGKT-EQLEVDTRTTLLDTLRENLHLIGTKKGCDHGQCGACTVL----------VNGRRLNACLTLAVMHQGA 129
Cdd:PLN00192    4 MSLVFAVNGERfELSSVDPSTTLLEFLRTQTPFKSVKLGCGEGGCGACVVLlskydpvldqVEDFTVSSCLTLLCSVNGC 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  130 EITTIEGLG-SPDNLHPMQAAFikhDGF---QCGYCTSGQICSSVAALkeiqdgipshVTVDLVSAPET-------TADE 198
Cdd:PLN00192   84 SITTSEGLGnSKDGFHPIHKRF---AGFhasQCGFCTPGMCISLFSAL----------VNADKTDRPEPpsgfsklTVVE 150

                         170       180
                  ....*....|....*....|....*....
gi 445992844  199 IRERMSGNICRCGAYANILAAIEDAAGEI 227
Cdd:PLN00192  151 AEKAVSGNLCRCTGYRPIVDACKSFAADV 179
PRK09800 PRK09800
putative hypoxanthine oxidase; Provisional
 61-228 2.99e-08

putative hypoxanthine oxidase; Provisional


Pssm-ID: 182084 [Multi-domain]  Cd Length: 956  Bit Score: 53.68  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  61 MPLTLKVNGKTEQLEvdtrTTLLDTLRENLHLIG--TKKGCDHGQ--CGACTVLVNGRRLNACLTLAVMHQGAEITTIEG 136
Cdd:PRK09800   1 MIIHFTLNGAPQELT----VNPGENVQKLLFNMGmhSVRNSDDGFgfAGSDAIIFNGNIVNASLLIAAQLEKADIRTAES 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844 137 LGSPDNLHPMQAAFIKHDGFQCGYctsgqiCSSVAALkeiqdgipshVTVDLVS-APETTADEIRERMSGNICRCGAYAN 215
Cdd:PRK09800  77 LGKWNELSLVQQAMVDVGVVQSGY------NDPAAAL----------IITDLLDrIAAPTREEIDDALSGLFSRDAGWQQ 140

                        170
                 ....*....|...
gi 445992844 216 ILAAIEDAAGEIK 228
Cdd:PRK09800 141 YYQVIELAVARKN 153
fer2 cd00207
2Fe-2S iron-sulfur cluster binding domain. Iron-sulfur proteins play an important role in ...
 63-112 3.76e-08

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: 49.32  E-value: 3.76e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 445992844  63 LTLKVNGKTEQLEVDTRTTLLDTLRENLhlIGTKKGCDHGQCGACTVLVN 112
Cdd:cd00207    1 VTINVPGSGVEVEVPEGETLLDAAREAG--IDIPYSCRAGACGTCKVEVV 48
Fer2 pfam00111
2Fe-2S iron-sulfur cluster binding domain;
65-112 1.47e-06

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


Pssm-ID: 395061 [Multi-domain]  Cd Length: 77  Bit Score: 44.82  E-value: 1.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 445992844   65 LKVNGKTEQLEVDT-RTTLLDTLRENLhlIGTKKGCDHGQCGACTVLVN 112
Cdd:pfam00111   1 VTINGKGVTIEVPDgETTLLDAAEEAG--IDIPYSCRGGGCGTCAVKVL 47
PRK12576 PRK12576
succinate dehydrogenase/fumarate reductase iron-sulfur subunit;
73-138 5.94e-06

succinate dehydrogenase/fumarate reductase iron-sulfur subunit;


Pssm-ID: 237143 [Multi-domain]  Cd Length: 279  Bit Score: 45.90  E-value: 5.94e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 445992844  73 QLEVDTRTTLLDTLR----ENLHLIGTKKGCDHGQCGACTVLVNGRRLNACLTLA--VMHQGAEITTIEGLG 138
Cdd:PRK12576  28 KVKVDRFTQVTEALRrikeEQDPTLSYRASCHMAVCGSCGMKINGEPRLACKTLVldVAKKYNSVITIEPMD 99
SdhB/FrdB COG0479
Succinate dehydrogenase/fumarate reductase, Fe-S protein subunit [Energy production and ...
 61-122 4.67e-05

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: 43.20  E-value: 4.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844  61 MPLTLKV---NGKTE--------QLEVDTRTTLLDTLrenLHLIGTKKG-------CDHGQCGACTVLVNGR-RLnACLT 121
Cdd:COG0479    1 MTVTLKIwrqDPETDskprfqtyEVPVSPGMTVLDAL---DYIKEEQDPtlafrrsCREGICGSCAMVINGRpRL-ACQT 76


                 .
gi 445992844 122 L 122
Cdd:COG0479   77 H 77
dhsB TIGR00384
succinate dehydrogenase and fumarate reductase iron-sulfur protein; Succinate dehydrogenase ...
 73-138 8.83e-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: 42.03  E-value: 8.83e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 445992844   73 QLEVDTRTTLLDTLRE-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 3.29e-04

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: 38.76  E-value: 3.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 445992844   73 QLEVDTRTTLLDTLRE-NLHLIGT---KKGCDHGQCGACTVLVNGR-RLnACLTL 122
Cdd:pfam13085  22 EVPYEEGMTVLDALNKiKEEQDPTlafRRSCREGICGSCAMNINGKpRL-ACKTL 75
NqrF COG2871
Na+-transporting NADH:ubiquinone oxidoreductase, subunit NqrF [Energy production and ...
 62-111 2.94e-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: 2.94e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 445992844  62 PLTLKVNGKTEQLEVDTRTTLLDTL-RENLHLIGtkkGCD-HGQCGACTVLV 111
Cdd:COG2871   34 EVKITINGDGKEIEVEEGQTLLDALlRQGIFLPS---ACGgGGTCGQCKVKV 82
 
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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