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Conserved domains on  [gi|15832662|ref|NP_311435|]
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phenylpropionate dioxygenase ferredoxin reductase subunit [Escherichia coli O157:H7 str. Sakai]

Protein Classification

phenylpropionate dioxygenase ferredoxin reductase subunit( domain architecture ID 11484472)

phenylpropionate dioxygenase ferredoxin reductase subunit is part of the multicomponent 3-phenylpropionate dioxygenase, that converts 3-phenylpropionic acid (PP) and cinnamic acid (CI) into 3-phenylpropionate-dihydrodiol (PP-dihydrodiol) and cinnamic acid-dihydrodiol (CI-dihydrodiol), respectively

EC:  1.18.1.3|1.14.12.19
Gene Symbol:  hcaD
Gene Ontology:  GO:0050660|GO:0008860|GO:0008695

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 1-396 0e+00

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


:

Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 743.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVT 80
Cdd:PRK09754   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   81 IKTLGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160
Cdd:PRK09754  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK09754 161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  241 ANDQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNHAQIAAAAMLGLPLPLLPPPWFW 320
Cdd:PRK09754 241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832662  321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIA 396
Cdd:PRK09754 321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
 
Name Accession Description Interval E-value
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 1-396 0e+00

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 743.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVT 80
Cdd:PRK09754   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   81 IKTLGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160
Cdd:PRK09754  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK09754 161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  241 ANDQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNHAQIAAAAMLGLPLPLLPPPWFW 320
Cdd:PRK09754 241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832662  321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIA 396
Cdd:PRK09754 321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
4-400 1.28e-116

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 345.20  E-value: 1.28e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVTIKT 83
Cdd:COG1251   2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  84 LGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASA 163
Cdd:COG1251  82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 164 TQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGISAN 242
Cdd:COG1251 162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTgVRLADGEELPADLVVVAIGVRPN 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 243 DQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNHAQIAAAAML-GLPLPLLPPPWFWS 321
Cdd:COG1251 242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARVAAANLAgGPAAYEGSVPSTKL 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 322 DQYSDNLQFIGDMRGDD-WLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIALKSL 400
Cdd:COG1251 322 KVFGVDVASAGDAEGDEeVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKEL 401
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-282 5.07e-54

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 180.98  E-value: 5.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662     6 IIIVGGGQAAAMAAASLRQQGftGELHLFSDEQHLPYERPPLSKSML--------LEDSPQLQSVLPAHWWQ-ENNVHLH 76
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLgaaeapeiASLWADLYKRKEEVVKKlNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    77 SGVTIKTLGRDTRELVLA-----NGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERsVVIVG 151
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKR-VVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   152 AGTIGLELAASATQRRCKVTVIElAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQSGETLQA 230
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIE-ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIgDGDGVEVILKDGTEIDA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15832662   231 DVVIYGIGISANDQLAREANL--DTTNGIVIDEACRTCDPAIFAGGDVAITRLD 282
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLelDERGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 30-277 4.41e-34

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 134.18  E-value: 4.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    30 ELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVTIKTLGRDTRELVLANGESWHWDQLFIATG 109
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   110 AAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQ 189
Cdd:TIGR02374 106 SYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   190 RYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTTNGIVIDEACRTCDP 268
Cdd:TIGR02374 186 RLLQRELEQKGLTFLLEkDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDP 265


                  ....*....
gi 15832662   269 AIFAGGDVA 277
Cdd:TIGR02374 266 DIYAVGECA 274
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 110-177 4.23e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.84  E-value: 4.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832662 110 AAARPLPLLDALGercftlrhagdAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAA 177
Cdd:cd05188 112 AALLPEPLATAYH-----------ALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSD 168
 
Name Accession Description Interval E-value
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 1-396 0e+00

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 743.28  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVT 80
Cdd:PRK09754   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   81 IKTLGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160
Cdd:PRK09754  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK09754 161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  241 ANDQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNHAQIAAAAMLGLPLPLLPPPWFW 320
Cdd:PRK09754 241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832662  321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIA 396
Cdd:PRK09754 321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
4-400 1.28e-116

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 345.20  E-value: 1.28e-116
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVTIKT 83
Cdd:COG1251   2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  84 LGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASA 163
Cdd:COG1251  82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 164 TQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGISAN 242
Cdd:COG1251 162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTgVRLADGEELPADLVVVAIGVRPN 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 243 DQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNHAQIAAAAML-GLPLPLLPPPWFWS 321
Cdd:COG1251 242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARVAAANLAgGPAAYEGSVPSTKL 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 322 DQYSDNLQFIGDMRGDD-WLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIALKSL 400
Cdd:COG1251 322 KVFGVDVASAGDAEGDEeVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKEL 401
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 24-335 2.20e-74

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 234.32  E-value: 2.20e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  24 QQGFTGELHLFSDEQHLPYERPPLSKSMLLE-DSPQLQSVLPAHWWQENNVHLHSGVTIKTLGRDTRELVLANGESWHWD 102
Cdd:COG0446   1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGiKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 103 QLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPE--RSVVIVGAGTIGLELAASATQRRCKVTVIELAATVM 180
Cdd:COG0446  81 KLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLL 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 181 GRnAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDT--TNGIV 258
Cdd:COG0446 161 GV-LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALgeRGWIK 239

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832662 259 IDEACRTCDPAIFAGGDVA-ITRLDNGALHRCESWENANNHAQIAAAAMLGLPLPLLPPPWFWSDQYSDNLQFIGDMR 335
Cdd:COG0446 240 VDETLQTSDPDVYAAGDCAeVPHPVTGKTVYIPLASAANKQGRVAAENILGGPAPFPGLGTFISKVFDLCIASTGTGR 317
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-282 5.07e-54

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 180.98  E-value: 5.07e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662     6 IIIVGGGQAAAMAAASLRQQGftGELHLFSDEQHLPYERPPLSKSML--------LEDSPQLQSVLPAHWWQ-ENNVHLH 76
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLgaaeapeiASLWADLYKRKEEVVKKlNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    77 SGVTIKTLGRDTRELVLA-----NGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERsVVIVG 151
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKR-VVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   152 AGTIGLELAASATQRRCKVTVIElAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQSGETLQA 230
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIE-ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIgDGDGVEVILKDGTEIDA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 15832662   231 DVVIYGIGISANDQLAREANL--DTTNGIVIDEACRTCDPAIFAGGDVAITRLD 282
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLelDERGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
6-277 1.73e-36

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 136.59  E-value: 1.73e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    6 IIIVGGGQAAAMAAASLRQQGFTGELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPA-HWWQENNVHLHSGVTIKTL 84
Cdd:PRK04965   5 IVIIGSGFAARQLVKNIRKQDAHIPITLITADSGDEYNKPDLSHVFSQGQRADDLTRQSAgEFAEQFNLRLFPHTWVTDI 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   85 GRDTReLVLANGESWHWDQLFIATGAAARPLPLLDalGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA---A 161
Cdd:PRK04965  85 DAEAQ-VVKSQGNQWQYDKLVLATGASAFVPPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELAmdlC 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  162 SATQRrckVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK04965 162 RAGKA---VTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLeKTDSGIRATLDSGRSIEVDAVIAAAGLR 238

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 15832662  241 ANDQLAREANLDTTNGIVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK04965 239 PNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCA 275
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 30-277 4.41e-34

nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen metabolism]


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 134.18  E-value: 4.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    30 ELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAHWWQENNVHLHSGVTIKTLGRDTRELVLANGESWHWDQLFIATG 109
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   110 AAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQ 189
Cdd:TIGR02374 106 SYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   190 RYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTTNGIVIDEACRTCDP 268
Cdd:TIGR02374 186 RLLQRELEQKGLTFLLEkDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDP 265


                  ....*....
gi 15832662   269 AIFAGGDVA 277
Cdd:TIGR02374 266 DIYAVGECA 274
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 71-277 2.52e-26

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 109.79  E-value: 2.52e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  71 NNVHLHSGVtiktlGR--DTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRhagDAARLREVlqPERsVV 148
Cdd:COG1249 104 NGVDVIRGR-----ARfvDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSD---EALELEEL--PKS-LV 172

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 149 IVGAGTIGLELAASAtqRR--CKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSG 225
Cdd:COG1249 173 VIGGGYIGLEFAQIF--ARlgSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVeKTGDGVTVTLEDG 249

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15832662 226 ---ETLQADVVIYGIGISAN-DQLAREA---NLDTTNGIVIDEACRTCDPAIFAGGDVA 277
Cdd:COG1249 250 ggeEAVEADKVLVATGRRPNtDGLGLEAagvELDERGGIKVDEYLRTSVPGIYAIGDVT 308
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
4-277 5.48e-24

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 102.13  E-value: 5.48e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   4 KTIIIVGGGQAAAMAAASLRQQGFTG-ELHLFSDEQHLPYerPPL-----SKSMLLED-SPQLQSVLPAHwwqenNVHLH 76
Cdd:COG1252   2 KRIVIVGGGFAGLEAARRLRKKLGGDaEVTLIDPNPYHLF--QPLlpevaAGTLSPDDiAIPLRELLRRA-----GVRFI 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  77 SGvTIKTLGRDTRELVLANGESWHWDQLFIATGAAARPLPlLDALGERCFTLRHAGDAARLRE-----VLQPER----SV 147
Cdd:COG1252  75 QG-EVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG-IPGLAEHALPLKTLEDALALRErllaaFERAERrrllTI 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 148 VIVGAGTIGLELA---ASATQRRC----------KVTVIELAATVMGRnAPPPVQRYLLQRHQQAGVRILLNNAIEHvVD 214
Cdd:COG1252 153 VVVGGGPTGVELAgelAELLRKLLrypgidpdkvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTGTRVTE-VD 230

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15832662 215 GEKVelTLQSGETLQADVVIYGIGISANDqLAREANLDTT--NGIVIDEACRTCD-PAIFAGGDVA 277
Cdd:COG1252 231 ADGV--TLEDGEEIPADTVIWAAGVKAPP-LLADLGLPTDrrGRVLVDPTLQVPGhPNVFAIGDCA 293
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 100-277 1.26e-23

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 102.04  E-value: 1.26e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  100 HWDQLFIATGAAA--RPLPLLDAlgERCFTLRHAGDAARLREVLQPER--SVVIVGAGTIGLELAASATQRRCKVTVIEL 175
Cdd:PRK09564 103 TYDKLMIATGARPiiPPIKNINL--ENVYTLKSMEDGLALKELLKDEEikNIVIIGAGFIGLEAVEAAKHLGKNVRIIQL 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  176 AATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANDQLAREANLDTT- 254
Cdd:PRK09564 181 EDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTLk 260

                        170       180
                 ....*....|....*....|....
gi 15832662  255 NG-IVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK09564 261 NGaIIVDEYGETSIENIYAAGDCA 284
Reductase_C pfam14759
Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, ...
 318-399 6.82e-23

Reductase C-terminal; This domain occurs at the C-terminus of various reductase enzymes, including putidaredoxin reductase, ferredoxin reductase, 3-phenylpropionate/cinnamic acid dioxygenase ferredoxin--NAD(+) reductase component, benzene 1,2-dioxygenase system ferredoxin--NAD(+) reductase subunit, rhodocoxin reductase, biphenyl dioxygenase system ferredoxin--NAD(+) reductase component, rubredoxin-NAD(+) reductase and toluene 1,2-dioxygenase system ferredoxin--NAD(+) reductase component. In putidaredoxin reductase this domain is involved in dimerization. In the FAD-containing NADH-ferredoxin reductase (BphA4) it is responsible for interaction with the Rieske-type [2Fe-2S] ferredoxin (BphA3).


Pssm-ID: 434185 [Multi-domain]  Cd Length: 83  Bit Score: 91.47  E-value: 6.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   318 WFWSDQYSDNLQFIGDMRGDD-WLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRSIRKWIQSGKTFDAKQLTDENIA 396
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADeVVLRGDPEDGAFSVFYLRDGRLVAVDAVNRPRDFMAARRLIARGASVDPAALADPAVD 80


                  ...
gi 15832662   397 LKS 399
Cdd:pfam14759  81 LKA 83
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 1-294 5.29e-22

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 98.27  E-value: 5.29e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTG--ELHLFSDEQHLPYERPPLSKSMLLEDSPQLQSVLPAhWWQENNVHLHSG 78
Cdd:PRK14989   1 MSKVRLAIIGNGMVGHRFIEDLLDKADAAnfDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREG-FYEKHGIKVLVG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   79 VTIKTLGRDTRELVLANGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLE 158
Cdd:PRK14989  80 ERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  159 LAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQ--SGETLQADVVIY 235
Cdd:PRK14989 160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSkNTLEIVQEGVEARKTMRfaDGSELEVDFIVF 239

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832662  236 GIGISANDQLAREANLDTT--NGIVIDEACRTCDPAIFAGGDvaitrldngalhrCESWEN 294
Cdd:PRK14989 240 STGIRPQDKLATQCGLAVAprGGIVINDSCQTSDPDIYAIGE-------------CASWNN 287
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 92-303 7.11e-20

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 91.01  E-value: 7.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   92 VLANGESWHWDQLFIATGAAARPLP-LLDALGERCFTLRhagDAARLREVlqPErSVVIVGAGTIGLELaASATQRR-CK 169
Cdd:PRK06292 122 VEVNGERIEAKNIVIATGSRVPPIPgVWLILGDRLLTSD---DAFELDKL--PK-SLAVIGGGVIGLEL-GQALSRLgVK 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  170 VTVIELAATVMGrNAPPPVQRYlLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGE--TLQADVVIYGIGISAN-DQ 244
Cdd:PRK06292 195 VTVFERGDRILP-LEDPEVSKQ-AQKILSKEFKIKLGAKVTSVekSGDEKVEELEKGGKteTIEADYVLVATGRRPNtDG 272

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15832662  245 LAREA---NLDTTNGIVIDEACRTCDPAIFAGGDVaitrldNGA---LHrcesweNANNHAQIAA 303
Cdd:PRK06292 273 LGLENtgiELDERGRPVVDEHTQTSVPGIYAAGDV------NGKpplLH------EAADEGRIAA 325
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 106-277 2.54e-18

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 86.35  E-value: 2.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  106 IATGAAARPLPLLDALGERCFTLRHAgdaarlrevLQPER---SVVIVGAGTIGLELAASATQRRCKVTVIELAATVMG- 181
Cdd:PRK06416 140 LATGSRPRELPGIEIDGRVIWTSDEA---------LNLDEvpkSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPg 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  182 --RNAPPPVQRYLLQRhqqaGVRILLNNAIEHVVDGE-KVELTLQSG---ETLQADVVIYGIGISAN-DQLARE-ANLDT 253
Cdd:PRK06416 211 edKEISKLAERALKKR----GIKIKTGAKAKKVEQTDdGVTVTLEDGgkeETLEADYVLVAVGRRPNtENLGLEeLGVKT 286

                        170       180
                 ....*....|....*....|....*
gi 15832662  254 TNG-IVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK06416 287 DRGfIEVDEQLRTNVPNIYAIGDIV 311
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
76-277 3.21e-18

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 84.40  E-value: 3.21e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  76 HSGVTIKT-------LGRDTRELVLANGESWHWDQLFIATGAAARPLPLLdalGERCFTLR--HAG---DAARLREvlqp 143
Cdd:COG0492  69 RFGAEILLeevtsvdKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLP---GEEEFEGRgvSYCatcDGFFFRG---- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 144 eRSVVIVGAGTIGLELAASATQRRCKVTVI----ELAATvmgrnapppvqRYLLQR-HQQAGVRILLNNAIEHVVDGEKV 218
Cdd:COG0492 142 -KDVVVVGGGDSALEEALYLTKFASKVTLIhrrdELRAS-----------KILVERlRANPKIEVLWNTEVTEIEGDGRV 209

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15832662 219 E-LTLQSGET-----LQADVVIYGIGISANDQLAREANLDTTNG--IVIDEACRTCDPAIFAGGDVA 277
Cdd:COG0492 210 EgVTLKNVKTgeekeLEVDGVFVAIGLKPNTELLKGLGLELDEDgyIVVDEDMETSVPGVFAAGDVR 276
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 146-221 1.98e-16

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 73.39  E-value: 1.98e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832662   146 SVVIVGAGTIGLELAASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLN---NAIEHVVDGEKVELT 221
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNttvEAIEGNGDGVVVVLT 78
PRK07251 PRK07251
FAD-containing oxidoreductase;
102-276 3.28e-15

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 76.71  E-value: 3.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  102 DQLFIATGAAAR--PLPLLDalgercfTLRHAGDAARLREV-LQPERsVVIVGAGTIGLELAASATQRRCKVTVIELAAT 178
Cdd:PRK07251 120 ETIVINTGAVSNvlPIPGLA-------DSKHVYDSTGIQSLeTLPER-LGIIGGGNIGLEFAGLYNKLGSKVTVLDAAST 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  179 VMGRnAPPPVQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQsGETLQADVVIYGIGISANDQLAREANLD---TT 254
Cdd:PRK07251 192 ILPR-EEPSVAALAKQYMEEDGITFLLNAHTTEVKnDGDQVLVVTE-DETYRFDALLYATGRKPNTEPLGLENTDielTE 269

                        170       180
                 ....*....|....*....|...
gi 15832662  255 NG-IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK07251 270 RGaIKVDDYCQTSVPGVFAVGDV 292
PRK06116 PRK06116
glutathione reductase; Validated
 71-276 2.25e-13

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 71.34  E-value: 2.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   71 NNVHLHSG----VTIKTlgrdtrelVLANGESWHWDQLFIATGAAARPLPLLDAlgERCFTlrhAGDAARLREvlQPERs 146
Cdd:PRK06116 106 NGVDLIEGfarfVDAHT--------VEVNGERYTADHILIATGGRPSIPDIPGA--EYGIT---SDGFFALEE--LPKR- 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  147 VVIVGAGTIGLELAASATQRRCKVTVIelaatVMG----RNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV---DGeKVE 219
Cdd:PRK06116 170 VAVVGAGYIAVEFAGVLNGLGSETHLF-----VRGdaplRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEknaDG-SLT 243

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832662  220 LTLQSGETLQADVVIYGIGISAN-DQLAREA---NLDTTNGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK06116 244 LTLEDGETLTVDCLIWAIGREPNtDGLGLENagvKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 78-277 1.02e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 69.18  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   78 GVTIKTLGRDTRELVLangeswhwDQLFIATGAAARPLPLLDALGERcfTLRHAGdAARLREVlqPERSVVIvGAGTIGL 157
Cdd:PRK06327 131 GYEIKVTGEDETVITA--------KHVIIATGSEPRHLPGVPFDNKI--ILDNTG-ALNFTEV--PKKLAVI-GAGVIGL 196

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  158 ELAAsaTQRR--CKVTVIELAATVMGRNAPPpVQRYLLQRHQQAGVRILLNNAIEHVVDGEK---VELTLQSGE--TLQA 230
Cdd:PRK06327 197 ELGS--VWRRlgAEVTILEALPAFLAAADEQ-VAKEAAKAFTKQGLDIHLGVKIGEIKTGGKgvsVAYTDADGEaqTLEV 273

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15832662  231 DVVIYGIGISAN-DQLAREA---NLDTTNGIVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK06327 274 DKLIVSIGRVPNtDGLGLEAvglKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
PRK06370 PRK06370
FAD-containing oxidoreductase;
92-276 2.72e-12

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 67.92  E-value: 2.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   92 VLANGESWHWDQLFIATGAAAR--PLPLLDALG----ERCFTLRHagdaarlrevlQPERsVVIVGAGTIGLELAASAtq 165
Cdd:PRK06370 125 VRVGGETLRAKRIFINTGARAAipPIPGLDEVGyltnETIFSLDE-----------LPEH-LVIIGGGYIGLEFAQMF-- 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  166 RR--CKVTVIELAATVMGRNAPPPVQryLLQRHQQA-GVRILLNNAIEHV-VDGEKVELTL---QSGETLQADVVIYGIG 238
Cdd:PRK06370 191 RRfgSEVTVIERGPRLLPREDEDVAA--AVREILEReGIDVRLNAECIRVeRDGDGIAVGLdcnGGAPEITGSHILVAVG 268

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 15832662  239 ISAN-DQLAREA---NLDTTNGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK06370 269 RVPNtDDLGLEAagvETDARGYIKVDDQLRTTNPGIYAAGDC 310
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
71-276 3.56e-12

Si-specific NAD(P)(+) transhydrogenase;


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 67.49  E-value: 3.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   71 NNVHLHSGvTIKTLGRDTRELVLANGES--WHWDQLFIATGA-AARPlPLLDALGERCFtlrhagDAARLREVLQPERSV 147
Cdd:PRK05249 107 NRVDLIQG-RARFVDPHTVEVECPDGEVetLTADKIVIATGSrPYRP-PDVDFDHPRIY------DSDSILSLDHLPRSL 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  148 VIVGAGTIGLELAASATQRRCKVTVIELAATVMGrnapppvqrYL-------LQRH-QQAGVRILLNNAIEHVVDGE-KV 218
Cdd:PRK05249 179 IIYGAGVIGCEYASIFAALGVKVTLINTRDRLLS---------FLddeisdaLSYHlRDSGVTIRHNEEVEKVEGGDdGV 249

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832662  219 ELTLQSGETLQADVVIYGIGISAN-DQLARE-ANLDTTN-G-IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK05249 250 IVHLKSGKKIKADCLLYANGRTGNtDGLNLEnAGLEADSrGqLKVNENYQTAVPHIYAVGDV 311
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 80-279 3.88e-12

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 67.50  E-value: 3.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   80 TIKTLGRDTRELVLAngeswHWDQLFIATGAAARPLPLLDALgerCFTLRHAGDAARLREVLQPE--RSVVIVGAGTIGL 157
Cdd:PRK13512  90 TVTVLNRKTNEQFEE-----SYDKLILSPGASANSLGFESDI---TFTLRNLEDTDAIDQFIKANqvDKALVVGAGYISL 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  158 ELAASATQRRCKVTVIELAATV---MGRNAPPPVQRYLLQRHqqagVRILLNNAIEHVvDGEKVelTLQSGETLQADVVI 234
Cdd:PRK13512 162 EVLENLYERGLHPTLIHRSDKInklMDADMNQPILDELDKRE----IPYRLNEEIDAI-NGNEV--TFKSGKVEHYDMII 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 15832662  235 YGIGISANDQLAREAN--LDTTNGIVIDEACRTCDPAIFAGGDVAIT 279
Cdd:PRK13512 235 EGVGTHPNSKFIESSNikLDDKGFIPVNDKFETNVPNIYAIGDIITS 281
PRK07846 PRK07846
mycothione reductase; Reviewed
 87-276 6.67e-12

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 66.52  E-value: 6.67e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   87 DTRELVLANGESWHWDQLFIATGAaaRP-LPllDALGERCFTLRHAGDAARLREvlQPERsVVIVGAGTIGLELAASATQ 165
Cdd:PRK07846 115 GPKTLRTGDGEEITADQVVIAAGS--RPvIP--PVIADSGVRYHTSDTIMRLPE--LPES-LVIVGGGFIAAEFAHVFSA 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  166 RRCKVTVIElAATVMGRNAPPPV-QRYLLQRHQQAGVRiLLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIG-ISAND 243
Cdd:PRK07846 188 LGVRVTVVN-RSGRLLRHLDDDIsERFTELASKRWDVR-LGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGrVPNGD 265

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 15832662  244 QL-AREANLDTTNG--IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK07846 266 LLdAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGDV 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 101-277 1.20e-10

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 62.86  E-value: 1.20e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  101 WDQLFIATGAaaRPLPL-LDALGERCFTLRHAGDAARLREVL---------------QPER--SVVIVGAGTIGLELAAS 162
Cdd:PTZ00318 114 YDKLVVAHGA--RPNTFnIPGVEERAFFLKEVNHARGIRKRIvqcieraslpttsveERKRllHFVVVGGGPTGVEFAAE 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  163 ATQ------RR--------CKVTVIELAATVMGrNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVeltLQSGETL 228
Cdd:PTZ00318 192 LADffrddvRNlnpelveeCKVTVLEAGSEVLG-SFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVV---LKDGEVI 267

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 15832662  229 QADVVIYGIGISANdQLAREANLD-TTNG-IVIDEACRTCD-PAIFAGGDVA 277
Cdd:PTZ00318 268 PTGLVVWSTGVGPG-PLTKQLKVDkTSRGrISVDDHLRVKPiPNVFALGDCA 318
PRK13748 PRK13748
putative mercuric reductase; Provisional
 86-275 2.10e-08

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 55.93  E-value: 2.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   86 RDTRELVLANGESW----HWDQLFIATGAAARpLPLLDALGERCF-TLRHAGDAARLrevlqPERSVVIvGAGTIGLELA 160
Cdd:PRK13748 214 KDDQTLIVRLNDGGervvAFDRCLIATGASPA-VPPIPGLKETPYwTSTEALVSDTI-----PERLAVI-GSSVVALELA 286

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  161 ASATQRRCKVTVieLAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVeLTLQSGEtLQADVVIYGIG 238
Cdd:PRK13748 287 QAFARLGSKVTI--LARSTLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVahVDGEFV-LTTGHGE-LRADKLLVATG 362

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 15832662  239 ISAND-QLAREA---NLDTTNGIVIDEACRTCDPAIFAGGD 275
Cdd:PRK13748 363 RAPNTrSLALDAagvTVNAQGAIVIDQGMRTSVPHIYAAGD 403
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 102-276 2.38e-06

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 49.47  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  102 DQLFIATGAAARPLPLLDALGERCFTLRHAGDaarLREVlqPERSVViVGAGTIGLELAASATQRRCKVTVI-------- 173
Cdd:PRK07845 141 DVVLIATGASPRILPTAEPDGERILTWRQLYD---LDEL--PEHLIV-VGSGVTGAEFASAYTELGVKVTLVssrdrvlp 214

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  174 ---ELAATVmgrnapppVQRYLLQRhqqaGVRILLNNAIEHVV-DGEKVELTLQSGETLQADVVIYGIGISANDQ---LA 246
Cdd:PRK07845 215 gedADAAEV--------LEEVFARR----GMTVLKRSRAESVErTGDGVVVTLTDGRTVEGSHALMAVGSVPNTAglgLE 282

                        170       180       190
                 ....*....|....*....|....*....|..
gi 15832662  247 rEANLDTTNG--IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK07845 283 -EAGVELTPSghITVDRVSRTSVPGIYAAGDC 313
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 78-277 2.59e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 49.41  E-value: 2.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   78 GVTIKT---LGRD-TRELVLANgeswhWDQLFIATGAAArPlPLLDALGErcfTLRHAGDA----ARLREV-----LQPE 144
Cdd:PRK11749 204 GVEIRTnteVGRDiTLDELRAG-----YDAVFIGTGAGL-P-RFLGIPGE---NLGGVYSAvdflTRVNQAvadydLPVG 273

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  145 RSVVIVGAG-------TIGLEL-AASATQ--RRCK-----------------VTVIELAATVmgrnapppvqRYLLQRHQ 197
Cdd:PRK11749 274 KRVVVIGGGntamdaaRTAKRLgAESVTIvyRRGReempaseeevehakeegVEFEWLAAPV----------EILGDEGR 343

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  198 QAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISAND---QLAREANLDTTNGIVIDEA-CRTCDPAIFAG 273
Cdd:PRK11749 344 VTGVEFVRMELGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPlilSTTPGLELNRWGTIIADDEtGRTSLPGVFAG 423


                 ....
gi 15832662  274 GDVA 277
Cdd:PRK11749 424 GDIV 427
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
147-278 6.50e-06

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 47.42  E-value: 6.50e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 147 VVIVGAGTIGLELAASATQRRCKVTVIE-------LAATVMGRN---APPPVQ-RYLLQR-HQQA---GVRILLNNAIEH 211
Cdd:COG0492   3 VVIIGAGPAGLTAAIYAARAGLKTLVIEggepggqLATTKEIENypgFPEGISgPELAERlREQAerfGAEILLEEVTSV 82

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832662 212 VVDGEKVELTLQSGETLQADVVIYGIGISAND-QLAREANLdTTNGIVideACRTCDPAIFAGGDVAI 278
Cdd:COG0492  83 DKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKlGLPGEEEF-EGRGVS---YCATCDGFFFRGKDVVV 146
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 69-276 7.28e-06

trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of spermidine, is (in its reduced form) an important antioxidant found in trypanosomatids (Crithidia, Leishmania, Trypanosoma). This model describes trypanothione reductase, a possible antitrypanosomal drug target closely related to some forms of glutathione reductase.


Pssm-ID: 200098 [Multi-domain]  Cd Length: 486  Bit Score: 48.05  E-value: 7.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662    69 QENNVhlhsgVTIKTlGRDTRELVLangESWHWDQLFIATGAAARPLPLLDAlgERCFTlrhAGDAARLREvlqPERSVV 148
Cdd:TIGR01423 129 EDKNV-----VLVRE-SADPKSAVK---ERLQAEHILLATGSWPQMLGIPGI--EHCIS---SNEAFYLDE---PPRRVL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   149 IVGAGTIGLELAA---SATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNN---AIEHVVDGEKvELTL 222
Cdd:TIGR01423 192 TVGGGFISVEFAGifnAYKPRGGKVTLCYRNNMIL-RGFDSTLRKELTKQLRANGINIMTNEnpaKVTLNADGSK-HVTF 269

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832662   223 QSGETLQADVVIYGIGI---SANDQLAREA-NLDTTNGIVIDEACRTCDPAIFAGGDV 276
Cdd:TIGR01423 270 ESGKTLDVDVVMMAIGRvprTQTLQLDKVGvELTKKGAIQVDEFSRTNVPNIYAIGDV 327
PLN02507 PLN02507
glutathione reductase
 77-276 1.11e-05

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 47.50  E-value: 1.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   77 SGVTI-----KTLGRDTRELVLANGESWHW--DQLFIATGAAARPLPLLDAlgERCFTlrhAGDAARLREVlqPERsVVI 149
Cdd:PLN02507 137 AGVKLyegegKIVGPNEVEVTQLDGTKLRYtaKHILIATGSRAQRPNIPGK--ELAIT---SDEALSLEEL--PKR-AVV 208

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  150 VGAGTIGLELAASATQRRCKVTVI---ELAATVMGRNAPPPVQRYLLQR----HQQAGVrillnNAIEHVVDGEKVelTL 222
Cdd:PLN02507 209 LGGGYIAVEFASIWRGMGATVDLFfrkELPLRGFDDEMRAVVARNLEGRginlHPRTNL-----TQLTKTEGGIKV--IT 281

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 15832662  223 QSGETLQADVVIYGIGISANDQ-LAREA---NLDTTNGIVIDEACRTCDPAIFAGGDV 276
Cdd:PLN02507 282 DHGEEFVADVVLFATGRAPNTKrLNLEAvgvELDKAGAVKVDEYSRTNIPSIWAIGDV 339
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 57-276 7.88e-05

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 44.76  E-value: 7.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   57 PQLQSVLPAHWwQENNVHLHSGVTIKTL--GRDTRELVLANGESWHWDQLFIATGAAARPL--PlldalGERCFtlrhag 132
Cdd:PRK15317 266 PKLAAALEEHV-KEYDVDIMNLQRASKLepAAGLIEVELANGAVLKAKTVILATGARWRNMnvP-----GEDEY------ 333

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  133 daaRLREV---------LQPERSVVIVGAGTIGLE----LAASATqrrcKVTVIELAATVmgrNAPPPVQRYLlqrHQQA 199
Cdd:PRK15317 334 ---RNKGVaycphcdgpLFKGKRVAVIGGGNSGVEaaidLAGIVK----HVTVLEFAPEL---KADQVLQDKL---RSLP 400

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  200 GVRILLNNAIEHVV-DGEKVE-LTLQ---SGE--TLQADVVIYGIGISANDQLAREAnLDTTN-G-IVIDEACRTCDPAI 270
Cdd:PRK15317 401 NVTIITNAQTTEVTgDGDKVTgLTYKdrtTGEehHLELEGVFVQIGLVPNTEWLKGT-VELNRrGeIIVDARGATSVPGV 479


                 ....*.
gi 15832662  271 FAGGDV 276
Cdd:PRK15317 480 FAAGDC 485
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 86-276 8.56e-05

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 44.62  E-value: 8.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   86 RDTRELVLangeswHWDQLFIATGAAArPLPLLDALGercfTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQ 165
Cdd:PRK08010 111 RPEGNLEI------HGEKIFINTGAQT-VVPPIPGIT----TTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFAN 179

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  166 RRCKVTVIELAATVM---GRNAPPPVQRYLlqrhQQAGVRILLNNAIEHVVDGE-KVELtlqsgETLQADVVIYGIGISA 241
Cdd:PRK08010 180 FGSKVTILEAASLFLpreDRDIADNIATIL----RDQGVDIILNAHVERISHHEnQVQV-----HSEHAQLAVDALLIAS 250

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 15832662  242 NDQLArEANLDTTN---------GIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK08010 251 GRQPA-TASLHPENagiavnergAIVVDKYLHTTADNIWAMGDV 293
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 83-275 1.16e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 44.33  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662   83 TLGRDtreLVLANGESWHwDQLFIATGA---AARPLPLLDALGERC---FtLRHAGDAarlrEVLQPERSVVIVGAGTIG 156
Cdd:PRK12814 265 VFGRD---ITLEELQKEF-DAVLLAVGAqkaSKMGIPGEELPGVISgidF-LRNVALG----TALHPGKKVVVIGGGNTA 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  157 LELAASAtqrrckvtvIELAA---TVMGRN--APPPVQRYLLQRHQQAGVRILLNNA---IEHVVDGekVELT---LQSG 225
Cdd:PRK12814 336 IDAARTA---------LRLGAesvTILYRRtrEEMPANRAEIEEALAEGVSLRELAApvsIERSEGG--LELTaikMQQG 404

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  226 E-----------------TLQADVVIYGIGISANDQLAREANLDTT-NGIVI--DEACRTCDPAIFAGGD 275
Cdd:PRK12814 405 EpdesgrrrpvpvegsefTLQADTVISAIGQQVDPPIAEAAGIGTSrNGTVKvdPETLQTSVAGVFAGGD 474
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 142-234 1.33e-04

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 43.39  E-value: 1.33e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 142 QPERSVVIVGAGTIGLELAASATQRRCKVTVIE--------------------------LAATVMGRNAPPP-------- 187
Cdd:COG0654   1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVErappprpdgrgialsprslellrrlgLWDRLLARGAPIRgirvrdgs 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15832662 188 -------------------------VQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQSGETLQADVVI 234
Cdd:COG0654  81 dgrvlarfdaaetglpaglvvpradLERALLEAARALGVELRFGTEVTGLEqDADGVTVTLADGRTLRADLVV 153
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 78-306 2.27e-04

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 43.20  E-value: 2.27e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  78 GVTIKT---LGRDTrelvlangeswHWDQL-------FIATGA-AARPLPL--------LDALGercFtLRHAGDAARLR 138
Cdd:COG0493 185 GVEFRTnveVGKDI-----------TLDELleefdavFLATGAgKPRDLGIpgedlkgvHSAMD---F-LTAVNLGEAPD 249

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 139 EVLQPERSVVIVGAGTIGLELAASAtqRRC---KVTVIELaatvMGRNAPPpvQRYLLQRH-QQAGVRILLNNAIEHVV- 213
Cdd:COG0493 250 TILAVGKRVVVIGGGNTAMDCARTA--LRLgaeSVTIVYR----RTREEMP--ASKEEVEEaLEEGVEFLFLVAPVEIIg 321

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 214 --DGEKVELTLQ---------SG-----------ETLQADVVIYGIGISANDQLAREAN---LDTTNGIVIDEAC-RTCD 267
Cdd:COG0493 322 deNGRVTGLECVrmelgepdeSGrrrpvpiegseFTLPADLVILAIGQTPDPSGLEEELgleLDKRGTIVVDEETyQTSL 401

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 15832662 268 PAIFAGGDVaitrldngalHRCES---WenANNHAQIAAAAM 306
Cdd:COG0493 402 PGVFAGGDA----------VRGPSlvvW--AIAEGRKAARAI 431
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 148-280 6.86e-04

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 41.73  E-value: 6.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  148 VIVGAGTIGLELAASATQRRCKVTVIELAATVMG--RNAPPPVQRYLlqrhQQAGVRIL---LNNAIEHVVDGEKVELTl 222
Cdd:PTZ00052 186 LIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGfdRQCSEKVVEYM----KEQGTLFLegvVPINIEKMDDKIKVLFS- 260

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15832662  223 qSGETLQADVVIYGIGISAN-DQLAREA---NLDTTNGIVIDEACrTCDPAIFAGGDVAITR 280
Cdd:PTZ00052 261 -DGTTELFDTVLYATGRKPDiKGLNLNAigvHVNKSNKIIAPNDC-TNIPNIFAVGDVVEGR 320
trkA PRK09496
Trk system potassium transporter TrkA;
134-174 8.00e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 41.26  E-value: 8.00e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15832662  134 AARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIE 174
Cdd:PRK09496 221 MSEFGRLEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIE 261
PTZ00058 PTZ00058
glutathione reductase; Provisional
 141-275 8.61e-04

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 41.52  E-value: 8.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  141 LQPERSVVIVGAGTIGLELaASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVEL 220
Cdd:PTZ00058 234 IKEAKRIGIAGSGYIAVEL-INVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNL 312

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15832662  221 TL---QSGETLQADVVIYGIGISAN-DQLAREANLDTT--NGIVIDEACRTCDPAIFAGGD 275
Cdd:PTZ00058 313 TIylsDGRKYEHFDYVIYCVGRSPNtEDLNLKALNIKTpkGYIKVDDNQRTSVKHIYAVGD 373
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 145-276 1.29e-03

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 40.88  E-value: 1.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662  145 RSVVIVGAGTIGLElaASATQRRCKVtviELAATVMGRN-APPPVQRYLLQRHQQAGVRIL-LNNAIEHVVD--GEKVEL 220
Cdd:PRK12778 571 KKVAVVGGGNTAMD--SARTAKRLGA---ERVTIVYRRSeEEMPARLEEVKHAKEEGIEFLtLHNPIEYLADekGWVKQV 645

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15832662  221 TLQ---------SG-----------ETLQADVVIYGIGISANDQLAR---EANLDTTNGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK12778 646 VLQkmelgepdaSGrrrpvaipgstFTVDVDLVIVSVGVSPNPLVPSsipGLELNRKGTIVVDEEMQSSIPGIYAGGDI 724
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 110-177 4.23e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 38.84  E-value: 4.23e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15832662 110 AAARPLPLLDALGercftlrhagdAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIELAA 177
Cdd:cd05188 112 AALLPEPLATAYH-----------ALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSD 168
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 141-234 6.75e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 38.20  E-value: 6.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15832662 141 LQPERSVVIVGAGTIGLELAASATQRRCKvTVIelaatVMGRNAPPpvqrylLQRHQQAGVRILLNNAIEHVVDGEKvEL 220
Cdd:COG1063 159 VKPGDTVLVIGAGPIGLLAALAARLAGAA-RVI-----VVDRNPER------LELARELGADAVVNPREEDLVEAVR-EL 225

                        90
                ....*....|....
gi 15832662 221 TLQSGetlqADVVI 234
Cdd:COG1063 226 TGGRG----ADVVI 235
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 126-174 8.07e-03

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 37.74  E-value: 8.07e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 15832662 126 FTLRHAGDAARLREVLQPERSVVIVGAGTIGLELAASATQRRCKVTVIE 174
Cdd:COG0569  77 GLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
190-234 8.51e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 37.64  E-value: 8.51e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15832662 190 RYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQSGETLQADVVI 234
Cdd:COG0644  90 RWLAEQAEEAGAEVRTGtRVTDVLRDDGRVVVRTGDGEEIRADYVV 135
 
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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