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Conserved domains on  [gi|1560336878|gb|RXA25306|]
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phenylpropionate dioxygenase ferredoxin reductase subunit [Escherichia coli]

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: 723.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80
Cdd:PRK09754    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELA 160
Cdd:PRK09754   81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK09754  161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 241 ANEQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320
Cdd:PRK09754  241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336878 321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 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: 723.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80
Cdd:PRK09754    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELA 160
Cdd:PRK09754   81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK09754  161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 241 ANEQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320
Cdd:PRK09754  241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336878 321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
Cdd:PRK09754  321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
4-400 2.85e-105

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 316.31  E-value: 2.85e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKT 83
Cdd:COG1251     2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  84 LGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASA 163
Cdd:COG1251    82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 164 TQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGISAN 242
Cdd:COG1251   162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTgVRLADGEELPADLVVVAIGVRPN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 243 EQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAML-GLPLPLLPPPWFWS 321
Cdd:COG1251   242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARVAAANLAgGPAAYEGSVPSTKL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 322 DQYSDNLQFIGDMRGDD-WLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIALKSL 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 1.17e-53

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: 180.21  E-value: 1.17e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   6 IIIVGGGQAAAMAAASLRQQGftGELHLFSDERHLPYERPPLSKSML---------LEDSPQLQQVLPANWWQENNVHLH 76
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLgaaeapeiaSLWADLYKRKEEVVKKLNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  77 SGVTIKTLGRDTRELVLT-----NGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERsVVIIG 151
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKR-VVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 152 AGTIGLELAASATQRRCKVTVIElAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQSGETLQA 230
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIE-ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIgDGDGVEVILKDGTEIDA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1560336878 231 DVVIYGIGISANEQLAREANL--DTANGIVIDEACRTCDPAIFAGGDVAITRLD 282
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLelDERGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 30-277 2.25e-33

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 132.26  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  30 ELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATG 109
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 110 AAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQ 189
Cdd:TIGR02374 106 SYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 190 RYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANEQLAREANLDTANGIVIDEACRTCDP 268
Cdd:TIGR02374 186 RLLQRELEQKGLTFLLEkDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDP 265


                  ....*....
gi 1560336878 269 AIFAGGDVA 277
Cdd:TIGR02374 266 DIYAVGECA 274
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 110-177 2.30e-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: 39.61  E-value: 2.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560336878 110 AAARPLPLLDALGercftlrhagdAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAA 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: 723.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80
Cdd:PRK09754    1 MKEKTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELA 160
Cdd:PRK09754   81 IKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIVGAGTIGLELA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240
Cdd:PRK09754  161 ASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGIS 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 241 ANEQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320
Cdd:PRK09754  241 ANDQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAMLGLPLPLLPPPWFW 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560336878 321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
Cdd:PRK09754  321 SDQYSDNLQFIGDMRGDDWLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
4-400 2.85e-105

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 316.31  E-value: 2.85e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   4 KTIIIVGGGQAAAMAAASLRQQGFTGELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKT 83
Cdd:COG1251     2 MRIVIIGAGMAGVRAAEELRKLDPDGEITVIGAEPHPPYNRPPLSKVLAGETDEEDLLLRPADFYEENGIDLRLGTRVTA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  84 LGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASA 163
Cdd:COG1251    82 IDRAARTVTLADGETLPYDKLVLATGSRPRVPPIPGADLPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAAAAL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 164 TQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVE-LTLQSGETLQADVVIYGIGISAN 242
Cdd:COG1251   162 RKRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEALGVEVRLGTGVTEIEGDDRVTgVRLADGEELPADLVVVAIGVRPN 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 243 EQLAREANLDTANGIVIDEACRTCDPAIFAGGDVAITRLDNGALHRCESWENANNQAQIAAAAML-GLPLPLLPPPWFWS 321
Cdd:COG1251   242 TELARAAGLAVDRGIVVDDYLRTSDPDIYAAGDCAEHPGPVYGRRVLELVAPAYEQARVAAANLAgGPAAYEGSVPSTKL 321

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 322 DQYSDNLQFIGDMRGDD-WLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIALKSL 400
Cdd:COG1251   322 KVFGVDVASAGDAEGDEeVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALRQLIKNGRPLPPRALLDAALPLKEL 401
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 24-292 2.09e-63

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: 206.20  E-value: 2.09e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  24 QQGFTGELHLFSDERHLPYERPPLSKSMLLE-DSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWD 102
Cdd:COG0446     1 RLGPDAEITVIEKGPHHSYQPCGLPYYVGGGiKDPEDLLVRTPESFERKGIDVRTGTEVTAIDPEAKTVTLRDGETLSYD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 103 QLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPE--RSVVIIGAGTIGLELAASATQRRCKVTVIELAATVM 180
Cdd:COG0446    81 KLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREALKEFkgKRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 181 GRnAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANEQLAREANLDT--ANGIV 258
Cdd:COG0446   161 GV-LDPEMAALLEEELREHGVELRLGETVVAIDGDDKVAVTLTDGEEIPADLVVVAPGVRPNTELAKDAGLALgeRGWIK 239

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1560336878 259 IDEACRTCDPAIFAGGDVA-ITRLDNGALHRCESW 292
Cdd:COG0446   240 VDETLQTSDPDVYAAGDCAeVPHPVTGKTVYIPLA 274
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 6-282 1.17e-53

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: 180.21  E-value: 1.17e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   6 IIIVGGGQAAAMAAASLRQQGftGELHLFSDERHLPYERPPLSKSML---------LEDSPQLQQVLPANWWQENNVHLH 76
Cdd:pfam07992   3 VVVIGGGPAGLAAALTLAQLG--GKVTLIEDEGTCPYGGCVLSKALLgaaeapeiaSLWADLYKRKEEVVKKLNNGIEVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  77 SGVTIKTLGRDTRELVLT-----NGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERsVVIIG 151
Cdd:pfam07992  81 LGTEVVSIDPGAKKVVLEelvdgDGETITYDRLVIATGARPRLPPIPGVELNVGFLVRTLDSAEALRLKLLPKR-VVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 152 AGTIGLELAASATQRRCKVTVIElAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQSGETLQA 230
Cdd:pfam07992 160 GGYIGVELAAALAKLGKEVTLIE-ALDRLLRAFDEEISAALEKALEKNGVEVRLGTSVKEIIgDGDGVEVILKDGTEIDA 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1560336878 231 DVVIYGIGISANEQLAREANL--DTANGIVIDEACRTCDPAIFAGGDVAITRLD 282
Cdd:pfam07992 239 DLVVVAIGRRPNTELLEAAGLelDERGGIVVDEYLRTSVPGIYAAGDCRVGGPE 292
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
6-277 3.47e-36

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 135.81  E-value: 3.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   6 IIIVGGGQAAAMAAASLRQQGFTGELHLFS----DErhlpYERPPLSKSMLLEDSPQ-LQQVLPANWWQENNVHLHSGVT 80
Cdd:PRK04965    5 IVIIGSGFAARQLVKNIRKQDAHIPITLITadsgDE----YNKPDLSHVFSQGQRADdLTRQSAGEFAEQFNLRLFPHTW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  81 IKTLGRDTReLVLTNGESWHWDQLFIATGAAARPLPLLDalGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELA 160
Cdd:PRK04965   81 VTDIDAEAQ-VVKSQGNQWQYDKLVLATGASAFVPPIPG--RELMLTLNSQQEYRAAETQLRDAQRVLVVGGGLIGTELA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 161 ---ASATQRrckVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSGETLQADVVIYG 236
Cdd:PRK04965  158 mdlCRAGKA---VTLVDNAASLLASLMPPEVSSRLQHRLTEMGVHLLLKSQLQGLeKTDSGIRATLDSGRSIEVDAVIAA 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1560336878 237 IGISANEQLAREANLDTANGIVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK04965  235 AGLRPNTALARRAGLAVNRGIVVDSYLQTSAPDIYALGDCA 275
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 30-277 2.25e-33

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 132.26  E-value: 2.25e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  30 ELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPANWWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHWDQLFIATG 109
Cdd:TIGR02374  26 EITIFGEEPHPNYNRILLSSVLQGEADLDDITLNSKDWYEKHGITLYTGETVIQIDTDQKQVITDAGRTLSYDKLILATG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 110 AAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGRNAPPPVQ 189
Cdd:TIGR02374 106 SYPFILPIPGADKKGVYVFRTIEDLDAIMAMAQRFKKAAVIGGGLLGLEAAVGLQNLGMDVSVIHHAPGLMAKQLDQTAG 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 190 RYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANEQLAREANLDTANGIVIDEACRTCDP 268
Cdd:TIGR02374 186 RLLQRELEQKGLTFLLEkDTVEIVGATKADRIRFKDGSSLEADLIVMAAGIRPNDELAVSAGIKVNRGIIVNDSMQTSDP 265


                  ....*....
gi 1560336878 269 AIFAGGDVA 277
Cdd:TIGR02374 266 DIYAVGECA 274
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 71-277 4.86e-27

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: 111.72  E-value: 4.86e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  71 NNVHLHSGVtiktlGR--DTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRhagDAARLREVlqPERsVV 148
Cdd:COG1249   104 NGVDVIRGR-----ARfvDPHTVEVTGGETLTADHIVIATGSRPRVPPIPGLDEVRVLTSD---EALELEEL--PKS-LV 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 149 IIGAGTIGLELAASAtqRR--CKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV-VDGEKVELTLQSG 225
Cdd:COG1249   173 VIGGGYIGLEFAQIF--ARlgSEVTLVERGDRLL-PGEDPEISEALEKALEKEGIDILTGAKVTSVeKTGDGVTVTLEDG 249

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560336878 226 ---ETLQADVVIYGIGISAN-EQLareaNLDTAN-------GIVIDEACRTCDPAIFAGGDVA 277
Cdd:COG1249   250 ggeEAVEADKVLVATGRRPNtDGL----GLEAAGveldergGIKVDEYLRTSVPGIYAIGDVT 308
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
69-277 5.44e-26

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 107.91  E-value: 5.44e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  69 QENNVHLHSGvTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPlLDALGERCFTLRHAGDAARLRE-----VLQP 143
Cdd:COG1252    67 RRAGVRFIQG-EVTGIDPEARTVTLADGRTLSYDYLVIATGSVTNFFG-IPGLAEHALPLKTLEDALALRErllaaFERA 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 144 ER----SVVIIGAGTIGLELA---ASATQRRC----------KVTVIELAATVMGRnAPPPVQRYLLQRHQQAGVRILLN 206
Cdd:COG1252   145 ERrrllTIVVVGGGPTGVELAgelAELLRKLLrypgidpdkvRITLVEAGPRILPG-LGEKLSEAAEKELEKRGVEVHTG 223

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560336878 207 NAIEHvVDGEKVelTLQSGETLQADVVIYGIGISANEqLAREANLDT--ANGIVIDEACRTCD-PAIFAGGDVA 277
Cdd:COG1252   224 TRVTE-VDADGV--TLEDGEEIPADTVIWAAGVKAPP-LLADLGLPTdrRGRVLVDPTLQVPGhPNVFAIGDCA 293
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 100-277 3.31e-24

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 103.58  E-value: 3.31e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 100 HWDQLFIATGAAA--RPLPLLDAlgERCFTLRHAGDAARLREVLQPER--SVVIIGAGTIGLELAASATQRRCKVTVIEL 175
Cdd:PRK09564  103 TYDKLMIATGARPiiPPIKNINL--ENVYTLKSMEDGLALKELLKDEEikNIVIIGAGFIGLEAVEAAKHLGKNVRIIQL 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 176 AATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANEQLAREANLDT-A 254
Cdd:PRK09564  181 EDRILPDSFDKEITDVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTDKGEYEADVVIVATGVKPNTEFLEDTGLKTlK 260

                         170       180
                  ....*....|....*....|....
gi 1560336878 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 2.42e-22

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: 89.93  E-value: 2.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 318 WFWSDQYSDNLQFIGDMRGDD-WLCRGNPETQKAIWFNLQNGVLIGAVTLNQGREIRPIRKWIQSGKTFDAKLLIDENIA 396
Cdd:pfam14759   1 WFWSDQYDLKLQIAGLPTGADeVVLRGDPEDGAFSVFYLRDGRLVAVDAVNRPRDFMAARRLIARGASVDPAALADPAVD 80


                  ...
gi 1560336878 397 LKS 399
Cdd:pfam14759  81 LKA 83
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 1-277 6.72e-22

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 97.88  E-value: 6.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878   1 MKEKTIIIVGGGQAAAMAAASLRQQGFTG--ELHLFSDERHLPYERPPLSKSMLLEDSPQLQQVLPAnWWQENNVHLHSG 78
Cdd:PRK14989    1 MSKVRLAIIGNGMVGHRFIEDLLDKADAAnfDITVFCEEPRIAYDRVHLSSYFSHHTAEELSLVREG-FYEKHGIKVLVG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  79 VTIKTLGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLDALGERCFTLRHAGDAARLREVLQPERSVVIIGAGTIGLE 158
Cdd:PRK14989   80 ERAITINRQEKVIHSSAGRTVFYDKLIMATGSYPWIPPIKGSETQDCFVYRTIEDLNAIEACARRSKRGAVVGGGLLGLE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 159 LAASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLN-NAIEHVVDGEKVELTLQ--SGETLQADVVIY 235
Cdd:PRK14989  160 AAGALKNLGVETHVIEFAPMLMAEQLDQMGGEQLRRKIESMGVRVHTSkNTLEIVQEGVEARKTMRfaDGSELEVDFIVF 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1560336878 236 GIGISANEQLAREANLDTA--NGIVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK14989  240 STGIRPQDKLATQCGLAVAprGGIVINDSCQTSDPDIYAIGECA 283
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 92-276 1.43e-19

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 90.24  E-value: 1.43e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  92 VLTNGESWHWDQLFIATGAAARPLP-LLDALGERCFTLRhagDAARLREVlqPErSVVIIGAGTIGLELaASATQRR-CK 169
Cdd:PRK06292  122 VEVNGERIEAKNIVIATGSRVPPIPgVWLILGDRLLTSD---DAFELDKL--PK-SLAVIGGGVIGLEL-GQALSRLgVK 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 170 VTVIELAATVMGrNAPPPVQRYlLQRHQQAGVRILLNNAIEHV--VDGEKVELTLQSGE--TLQADVVIYGIGISAN-EQ 244
Cdd:PRK06292  195 VTVFERGDRILP-LEDPEVSKQ-AQKILSKEFKIKLGAKVTSVekSGDEKVEELEKGGKteTIEADYVLVATGRRPNtDG 272

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1560336878 245 LAREA---NLDTANGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK06292  273 LGLENtgiELDERGRPVVDEHTQTSVPGIYAAGDV 307
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 106-277 1.81e-18

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 86.74  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 106 IATGAAARPLPLLDALGERCFTLRHAgdaarlrevLQPER---SVVIIGAGTIGLELAASATQRRCKVTVIELAATVMG- 181
Cdd:PRK06416  140 LATGSRPRELPGIEIDGRVIWTSDEA---------LNLDEvpkSLVVIGGGYIGVEFASAYASLGAEVTIVEALPRILPg 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 182 --RNAPPPVQRYLLQRhqqaGVRILLNNAIEHVVDGE-KVELTLQSG---ETLQADVVIYGIGISAN-EQLARE-ANLDT 253
Cdd:PRK06416  211 edKEISKLAERALKKR----GIKIKTGAKAKKVEQTDdGVTVTLEDGgkeETLEADYVLVAVGRRPNtENLGLEeLGVKT 286

                         170       180
                  ....*....|....*....|....*
gi 1560336878 254 ANG-IVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK06416  287 DRGfIEVDEQLRTNVPNIYAIGDIV 311
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
76-277 1.34e-17

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 82.48  E-value: 1.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  76 HSGVTIKT-------LGRDTRELVLTNGESWHWDQLFIATGAAARPLPLLdalGERCFTLR--HAG---DAARLREvlqp 143
Cdd:COG0492    69 RFGAEILLeevtsvdKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKLGLP---GEEEFEGRgvSYCatcDGFFFRG---- 141

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 144 eRSVVIIGAGTIGLELAASATQRRCKVTVI----ELAATvmgrnapppvqRYLLQR-HQQAGVRILLNNAIEHVVDGEKV 218
Cdd:COG0492   142 -KDVVVVGGGDSALEEALYLTKFASKVTLIhrrdELRAS-----------KILVERlRANPKIEVLWNTEVTEIEGDGRV 209

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1560336878 219 E-LTLQSGET-----LQADVVIYGIGISANEQLAREANLDT-ANG-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 2.89e-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: 73.01  E-value: 2.89e-16
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560336878 146 SVVIIGAGTIGLELAASATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLN---NAIEHVVDGEKVELT 221
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVERRDRLL-PGFDPEIAKILQEKLEKNGIEFLLNttvEAIEGNGDGVVVVLT 78
PRK07251 PRK07251
FAD-containing oxidoreductase;
102-276 3.99e-16

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 79.79  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 102 DQLFIATGAAAR--PLPLLDalgercfTLRHAGDAARLREV-LQPERsVVIIGAGTIGLELAASATQRRCKVTVIELAAT 178
Cdd:PRK07251  120 ETIVINTGAVSNvlPIPGLA-------DSKHVYDSTGIQSLeTLPER-LGIIGGGNIGLEFAGLYNKLGSKVTVLDAAST 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 179 VMGRnAPPPVQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQsGETLQADVVIYGIGISAN-EQLAREaNLDTA-- 254
Cdd:PRK07251  192 ILPR-EEPSVAALAKQYMEEDGITFLLNAHTTEVKnDGDQVLVVTE-DETYRFDALLYATGRKPNtEPLGLE-NTDIElt 268

                         170       180
                  ....*....|....*....|....
gi 1560336878 255 --NGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK07251  269 erGAIKVDDYCQTSVPGVFAVGDV 292
PRK06116 PRK06116
glutathione reductase; Validated
 71-276 2.87e-13

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 70.96  E-value: 2.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  71 NNVHLHSG----VTIKTlgrdtrelVLTNGESWHWDQLFIATGAAARPLPLLDAlgERCFTlrhAGDAARLREvlQPERs 146
Cdd:PRK06116  106 NGVDLIEGfarfVDAHT--------VEVNGERYTADHILIATGGRPSIPDIPGA--EYGIT---SDGFFALEE--LPKR- 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 147 VVIIGAGTIGLELAASATQRRCKVTVIelaatVMG----RNAPPPVQRYLLQRHQQAGVRILLNNAIEHVV---DGeKVE 219
Cdd:PRK06116  170 VAVVGAGYIAVEFAGVLNGLGSETHLF-----VRGdaplRGFDPDIRETLVEEMEKKGIRLHTNAVPKAVEknaDG-SLT 243

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560336878 220 LTLQSGETLQADVVIYGIGisaneqlaREANLD-----------TANG-IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK06116  244 LTLEDGETLTVDCLIWAIG--------REPNTDglglenagvklNEKGyIIVDEYQNTNVPGIYAVGDV 304
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 78-277 3.23e-13

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 70.72  E-value: 3.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  78 GVTIKTLGRDTRELVLtngeswhwDQLFIATGAAARPLPLLDALGERcfTLRHAGdAARLREVlqPERsVVIIGAGTIGL 157
Cdd:PRK06327  131 GYEIKVTGEDETVITA--------KHVIIATGSEPRHLPGVPFDNKI--ILDNTG-ALNFTEV--PKK-LAVIGAGVIGL 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 158 ELAAsaTQRR--CKVTVIELAATVMGRNAPPpVQRYLLQRHQQAGVRILLNNAIEHVVDGEK---VELTLQSGE--TLQA 230
Cdd:PRK06327  197 ELGS--VWRRlgAEVTILEALPAFLAAADEQ-VAKEAAKAFTKQGLDIHLGVKIGEIKTGGKgvsVAYTDADGEaqTLEV 273

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1560336878 231 DVVIYGIGISANEQ-LAREA---NLDTANGIVIDEACRTCDPAIFAGGDVA 277
Cdd:PRK06327  274 DKLIVSIGRVPNTDgLGLEAvglKLDERGFIPVDDHCRTNVPNVYAIGDVV 324
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
145-276 3.86e-12

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 67.49  E-value: 3.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 145 RSVVIIGAGTIGLELAASATQRRCKVTVIELAATVMGrnapppvqrYL-------LQRH-QQAGVRILLNNAIEHVVDGE 216
Cdd:PRK05249  176 RSLIIYGAGVIGCEYASIFAALGVKVTLINTRDRLLS---------FLddeisdaLSYHlRDSGVTIRHNEEVEKVEGGD 246

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560336878 217 -KVELTLQSGETLQADVVIYGIGISAN-EQLAREANLDTANG---IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK05249  247 dGVIVHLKSGKKIKADCLLYANGRTGNtDGLNLENAGLEADSrgqLKVNENYQTAVPHIYAVGDV 311
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 80-279 4.25e-12

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 67.12  E-value: 4.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  80 TIKTLGRDTRELVLTngeswHWDQLFIATGAAARPLPLLDALgerCFTLRHAGDAARLREVLQPE--RSVVIIGAGTIGL 157
Cdd:PRK13512   90 TVTVLNRKTNEQFEE-----SYDKLILSPGASANSLGFESDI---TFTLRNLEDTDAIDQFIKANqvDKALVVGAGYISL 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 158 ELAASATQRRCKVTVIELAATV---MGRNAPPPVQRYLLQRHqqagVRILLNNAIEHVvDGEKVelTLQSGETLQADVVI 234
Cdd:PRK13512  162 EVLENLYERGLHPTLIHRSDKInklMDADMNQPILDELDKRE----IPYRLNEEIDAI-NGNEV--TFKSGKVEHYDMII 234

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1560336878 235 YGIGISANEQLAREAN--LDTANGIVIDEACRTCDPAIFAGGDVAIT 279
Cdd:PRK13512  235 EGVGTHPNSKFIESSNikLDDKGFIPVNDKFETNVPNIYAIGDIITS 281
PRK06370 PRK06370
FAD-containing oxidoreductase;
92-276 4.29e-12

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 67.15  E-value: 4.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  92 VLTNGESWHWDQLFIATGAAAR--PLPLLDALG----ERCFTLRHagdaarlrevlQPERsVVIIGAGTIGLELAASAtq 165
Cdd:PRK06370  125 VRVGGETLRAKRIFINTGARAAipPIPGLDEVGyltnETIFSLDE-----------LPEH-LVIIGGGYIGLEFAQMF-- 190

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 166 RR--CKVTVIELAATVMGRNAPPPVQryLLQRHQQA-GVRILLNNAIEHV-VDGEKVELTL---QSGETLQADVVIYGIG 238
Cdd:PRK06370  191 RRfgSEVTVIERGPRLLPREDEDVAA--AVREILEReGIDVRLNAECIRVeRDGDGIAVGLdcnGGAPEITGSHILVAVG 268

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1560336878 239 ISAN-EQLAREA---NLDTANGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK06370  269 RVPNtDDLGLEAagvETDARGYIKVDDQLRTTNPGIYAAGDC 310
PRK07846 PRK07846
mycothione reductase; Reviewed
 87-276 2.69e-10

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 61.89  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  87 DTRELVLTNGESWHWDQLFIATGAaaRP-LPllDALGERCFTLRHAGDAARLREvlQPERsVVIIGAGTIGLELAASATQ 165
Cdd:PRK07846  115 GPKTLRTGDGEEITADQVVIAAGS--RPvIP--PVIADSGVRYHTSDTIMRLPE--LPES-LVIVGGGFIAAEFAHVFSA 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 166 RRCKVTVIElAATVMGRNAPPPV-QRYLLQRHQQAGVRiLLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIG-ISANE 243
Cdd:PRK07846  188 LGVRVTVVN-RSGRLLRHLDDDIsERFTELASKRWDVR-LGRNVVGVSQDGSGVTLRLDDGSTVEADVLLVATGrVPNGD 265

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1560336878 244 QL-AREANLDTANG--IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK07846  266 LLdAAAAGVDVDEDgrVVVDEYQRTSAEGVFALGDV 301
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 101-277 9.03e-10

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 60.17  E-value: 9.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 101 WDQLFIATGAaaRPLPL-LDALGERCFTLRHAGDAARLREVL---------------QPER--SVVIIGAGTIGLELAAS 162
Cdd:PTZ00318  114 YDKLVVAHGA--RPNTFnIPGVEERAFFLKEVNHARGIRKRIvqcieraslpttsveERKRllHFVVVGGGPTGVEFAAE 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 163 ATQ------RR--------CKVTVIELAATVMGrNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVeltLQSGETL 228
Cdd:PTZ00318  192 LADffrddvRNlnpelveeCKVTVLEAGSEVLG-SFDQALRKYGQRRLRRLGVDIRTKTAVKEVLDKEVV---LKDGEVI 267

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1560336878 229 QADVVIYGIGISANEqLAREANLD-TANG-IVIDEACRTCD-PAIFAGGDVA 277
Cdd:PTZ00318  268 PTGLVVWSTGVGPGP-LTKQLKVDkTSRGrISVDDHLRVKPiPNVFALGDCA 318
PRK13748 PRK13748
putative mercuric reductase; Provisional
 23-275 4.56e-09

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 58.24  E-value: 4.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  23 RQQGFTGELhlfsdeRHLPYERpplsksmLLEDSPQLQQVLPANWWQENN---VHLHSGvtiktlgrDTRELvltngesw 99
Cdd:PRK13748  181 QQQARVDEL------RHAKYEG-------ILDGNPAITVLHGEARFKDDQtliVRLNDG--------GERVV-------- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 100 HWDQLFIATGAAARpLPLLDALGERCF-TLRHAGDAARLrevlqPERSVVIiGAGTIGLELAASATQRRCKVTVieLAAT 178
Cdd:PRK13748  232 AFDRCLIATGASPA-VPPIPGLKETPYwTSTEALVSDTI-----PERLAVI-GSSVVALELAQAFARLGSKVTI--LARS 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 179 VMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHV--VDGEKVeLTLQSGEtLQADVVIYGIGISAN-EQLAREA---NLD 252
Cdd:PRK13748  303 TLFFREDPAIGEAVTAAFRAEGIEVLEHTQASQVahVDGEFV-LTTGHGE-LRADKLLVATGRAPNtRSLALDAagvTVN 380

                         250       260
                  ....*....|....*....|...
gi 1560336878 253 TANGIVIDEACRTCDPAIFAGGD 275
Cdd:PRK13748  381 AQGAIVIDQGMRTSVPHIYAAGD 403
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
147-278 5.94e-07

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 50.89  E-value: 5.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 147 VVIIGAGTIGLELAASATQRRCKVTVIE-------LAATVMGRN---APPPVQ-RYLLQR-HQQA---GVRILLNNAIEH 211
Cdd:COG0492     3 VVIIGAGPAGLTAAIYAARAGLKTLVIEggepggqLATTKEIENypgFPEGISgPELAERlREQAerfGAEILLEEVTSV 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560336878 212 VVDGEKVELTLQSGETLQADVVIYGIGISANE-QLAREANLdTANGIVideACRTCDPAIFAGGDVAI 278
Cdd:COG0492    83 DKDDGPFRVTTDDGTEYEAKAVIIATGAGPRKlGLPGEEEF-EGRGVS---YCATCDGFFFRGKDVVV 146
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 78-277 1.14e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.56  E-value: 1.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  78 GVTIKT---LGRDtrelvLTngeswhWDQL-------FIATGAAArPlPLLDALGErcfTLRHAGDA----ARLREV--- 140
Cdd:PRK11749  204 GVEIRTnteVGRD-----IT------LDELragydavFIGTGAGL-P-RFLGIPGE---NLGGVYSAvdflTRVNQAvad 267

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 141 --LQPERSVVIIGAG-------TIGLEL-AASATQ--RRCK-----------------VTVIELAATVmgrnapppvqRY 191
Cdd:PRK11749  268 ydLPVGKRVVVIGGGntamdaaRTAKRLgAESVTIvyRRGReempaseeevehakeegVEFEWLAAPV----------EI 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 192 LLQRHQQAGVRILLNNAIEHVVDGEKVELTLQSGETLQADVVIYGIGISANE---QLAREANLDTANGIVIDEA-CRTCD 267
Cdd:PRK11749  338 LGDEGRVTGVEFVRMELGEPDASGRRRVPIEGSEFTLPADLVIKAIGQTPNPlilSTTPGLELNRWGTIIADDEtGRTSL 417

                         250
                  ....*....|
gi 1560336878 268 PAIFAGGDVA 277
Cdd:PRK11749  418 PGVFAGGDIV 427
PLN02507 PLN02507
glutathione reductase
 77-276 6.33e-06

glutathione reductase


Pssm-ID: 215281 [Multi-domain]  Cd Length: 499  Bit Score: 48.27  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  77 SGVTI-----KTLGRDTRELVLTNGESWHW--DQLFIATGAAARPLPLLDAlgERCFTlrhAGDAARLREVlqPERsVVI 149
Cdd:PLN02507  137 AGVKLyegegKIVGPNEVEVTQLDGTKLRYtaKHILIATGSRAQRPNIPGK--ELAIT---SDEALSLEEL--PKR-AVV 208

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 150 IGAGTIGLELAASATQRRCKVTVI---ELAATVMGRNAPPPVQRYLLQR----HQQAGVrillnNAIEHVVDGEKVelTL 222
Cdd:PLN02507  209 LGGGYIAVEFASIWRGMGATVDLFfrkELPLRGFDDEMRAVVARNLEGRginlHPRTNL-----TQLTKTEGGIKV--IT 281

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1560336878 223 QSGETLQADVVIYGIGISANEQ-LAREA---NLDTANGIVIDEACRTCDPAIFAGGDV 276
Cdd:PLN02507  282 DHGEEFVADVVLFATGRAPNTKrLNLEAvgvELDKAGAVKVDEYSRTNIPSIWAIGDV 339
trypano_reduc TIGR01423
trypanothione-disulfide reductase; Trypanothione, a glutathione-modified derivative of ...
 69-276 1.35e-05

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: 46.89  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  69 QENNVhlhsgVTIKTlGRDTRELVLtngESWHWDQLFIATGAAARPLPLLDAlgERCFTlrhAGDAARLREvlqPERSVV 148
Cdd:TIGR01423 129 EDKNV-----VLVRE-SADPKSAVK---ERLQAEHILLATGSWPQMLGIPGI--EHCIS---SNEAFYLDE---PPRRVL 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 149 IIGAGTIGLELAA---SATQRRCKVTVIELAATVMgRNAPPPVQRYLLQRHQQAGVRILLNN---AIEHVVDGEKvELTL 222
Cdd:TIGR01423 192 TVGGGFISVEFAGifnAYKPRGGKVTLCYRNNMIL-RGFDSTLRKELTKQLRANGINIMTNEnpaKVTLNADGSK-HVTF 269

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1560336878 223 QSGETLQADVVIYGIGI---SANEQLAREA-NLDTANGIVIDEACRTCDPAIFAGGDV 276
Cdd:TIGR01423 270 ESGKTLDVDVVMMAIGRvprTQTLQLDKVGvELTKKGAIQVDEFSRTNVPNIYAIGDV 327
PRK08010 PRK08010
pyridine nucleotide-disulfide oxidoreductase; Provisional
 86-276 3.06e-05

pyridine nucleotide-disulfide oxidoreductase; Provisional


Pssm-ID: 181196 [Multi-domain]  Cd Length: 441  Bit Score: 45.77  E-value: 3.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  86 RDTRELVLtngeswHWDQLFIATGAAArPLPLLDALGercfTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQ 165
Cdd:PRK08010  111 RPEGNLEI------HGEKIFINTGAQT-VVPPIPGIT----TTPGVYDSTGLLNLKELPGHLGILGGGYIGVEFASMFAN 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 166 RRCKVTVIELAATVM---GRNAPPPVQRYLlqrhQQAGVRILLNNAIEHVVDGE---KVE----------LTLQSG-ETL 228
Cdd:PRK08010  180 FGSKVTILEAASLFLpreDRDIADNIATIL----RDQGVDIILNAHVERISHHEnqvQVHsehaqlavdaLLIASGrQPA 255

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1560336878 229 QADVVIYGIGISANEQlareanldtaNGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK08010  256 TASLHPENAGIAVNER----------GAIVVDKYLHTTADNIWAMGDV 293
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 78-277 3.85e-05

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: 45.51  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  78 GVTIKT---LGRDtrelvLTngeswhWDQL-------FIATGA-AARPLPL--------LDALGercFtLRHAGDAARLR 138
Cdd:COG0493   185 GVEFRTnveVGKD-----IT------LDELleefdavFLATGAgKPRDLGIpgedlkgvHSAMD---F-LTAVNLGEAPD 249

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 139 EVLQPERSVVIIGAGTIGLELAASAtqRRC---KVTVIELaatvMGRNAPPpvQRYLLQRH-QQAGVRILLNNAIEHVV- 213
Cdd:COG0493   250 TILAVGKRVVVIGGGNTAMDCARTA--LRLgaeSVTIVYR----RTREEMP--ASKEEVEEaLEEGVEFLFLVAPVEIIg 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 214 --DGEKVELTLQ---------SG-----------ETLQADVVIYGIGISANEQLAREAN---LDTANGIVIDEAC-RTCD 267
Cdd:COG0493   322 deNGRVTGLECVrmelgepdeSGrrrpvpiegseFTLPADLVILAIGQTPDPSGLEEELgleLDKRGTIVVDEETyQTSL 401

                         250
                  ....*....|
gi 1560336878 268 PAIFAGGDVA 277
Cdd:COG0493   402 PGVFAGGDAV 411
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 83-275 8.67e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 44.72  E-value: 8.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878  83 TLGRDtrelVLTNGESWHWDQLFIATGA---AARPLPLLDALGERC---FtLRHAGDAarlrEVLQPERSVVIIGAGTIG 156
Cdd:PRK12814  265 VFGRD----ITLEELQKEFDAVLLAVGAqkaSKMGIPGEELPGVISgidF-LRNVALG----TALHPGKKVVVIGGGNTA 335

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 157 LELAASAtqrrckvtvIELAA---TVMGRN--APPPVQRYLLQRHQQAGVRILLNNA---IEHVVDGekVELT---LQSG 225
Cdd:PRK12814  336 IDAARTA---------LRLGAesvTILYRRtrEEMPANRAEIEEALAEGVSLRELAApvsIERSEGG--LELTaikMQQG 404

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 226 E-----------------TLQADVVIYGIGISANEQLAREANLDTA-NGIVI--DEACRTCDPAIFAGGD 275
Cdd:PRK12814  405 EpdesgrrrpvpvegsefTLQADTVISAIGQQVDPPIAEAAGIGTSrNGTVKvdPETLQTSVAGVFAGGD 474
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 142-234 1.38e-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: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 142 QPERSVVIIGAGTIGLELAASATQRRCKVTVIE--------------------------LAATVMGRNAPPP-------- 187
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVErappprpdgrgialsprslellrrlgLWDRLLARGAPIRgirvrdgs 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560336878 188 -------------------------VQRYLLQRHQQAGVRILLNNAIEHVV-DGEKVELTLQSGETLQADVVI 234
Cdd:COG0654    81 dgrvlarfdaaetglpaglvvpradLERALLEAARALGVELRFGTEVTGLEqDADGVTVTLADGRTLRADLVV 153
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 147-276 4.18e-04

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 42.45  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 147 VVIIGAGTIGLE----LAASATqrrcKVTVIELAATVmgrNAPPPVQRYLlqrHQQAGVRILLNNAIEHVV-DGEKVE-L 220
Cdd:PRK15317  354 VAVIGGGNSGVEaaidLAGIVK----HVTVLEFAPEL---KADQVLQDKL---RSLPNVTIITNAQTTEVTgDGDKVTgL 423

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560336878 221 TLQ---SGE--TLQADVVIYGIGISANEQLAREANLDTANG-IVIDEACRTCDPAIFAGGDV 276
Cdd:PRK15317  424 TYKdrtTGEehHLELEGVFVQIGLVPNTEWLKGTVELNRRGeIIVDARGATSVPGVFAAGDC 485
trkA PRK09496
Trk system potassium transporter TrkA;
134-174 7.20e-04

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 41.65  E-value: 7.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1560336878 134 AARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIE 174
Cdd:PRK09496  221 MSEFGRLEKPVKRVMIVGGGNIGYYLAKLLEKEGYSVKLIE 261
PTZ00058 PTZ00058
glutathione reductase; Provisional
 141-275 1.08e-03

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 41.14  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 141 LQPERSVVIIGAGTIGLELaASATQRRCKVTVIELAATVMGRNAPPPVQRYLLQRHQQAGVRILLNNAIEHVVDGEKVEL 220
Cdd:PTZ00058  234 IKEAKRIGIAGSGYIAVEL-INVVNRLGAESYIFARGNRLLRKFDETIINELENDMKKNNINIITHANVEEIEKVKEKNL 312

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1560336878 221 TL---QSGETLQADVVIYGIGISAN-EQLAREA-NLDTANG-IVIDEACRTCDPAIFAGGD 275
Cdd:PTZ00058  313 TIylsDGRKYEHFDYVIYCVGRSPNtEDLNLKAlNIKTPKGyIKVDDNQRTSVKHIYAVGD 373
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 145-276 1.15e-03

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 41.27  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 145 RSVVIIGAGTIGLElaASATQRRCKVtviELAATVMGRN-APPPVQRYLLQRHQQAGVRIL-LNNAIEHVVD--GEKVEL 220
Cdd:PRK12778  571 KKVAVVGGGNTAMD--SARTAKRLGA---ERVTIVYRRSeEEMPARLEEVKHAKEEGIEFLtLHNPIEYLADekGWVKQV 645

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1560336878 221 TLQ---------SG-----------ETLQADVVIYGIGISANEQLAR---EANLDTANGIVIDEACRTCDPAIFAGGDV 276
Cdd:PRK12778  646 VLQkmelgepdaSGrrrpvaipgstFTVDVDLVIVSVGVSPNPLVPSsipGLELNRKGTIVVDEEMQSSIPGIYAGGDI 724
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 110-177 2.30e-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: 39.61  E-value: 2.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560336878 110 AAARPLPLLDALGercftlrhagdAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIELAA 177
Cdd:cd05188   112 AALLPEPLATAYH-----------ALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSD 168
HI0933_like pfam03486
HI0933-like protein;
147-174 3.39e-03

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 39.49  E-value: 3.39e-03
                          10        20
                  ....*....|....*....|....*...
gi 1560336878 147 VVIIGAGTIGLELAASATQRRCKVTVIE 174
Cdd:pfam03486   3 VIVIGGGAAGLMAAISAAKRGRRVLLIE 30
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 148-280 3.42e-03

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 39.42  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 148 VIIGAGTIGLELAASATQRRCKVTVIELAATVMG--RNAPPPVQRYLlqrhQQAGVRIL---LNNAIEHVVDGEKVELTl 222
Cdd:PTZ00052  186 LIVGASYIGLETAGFLNELGFDVTVAVRSIPLRGfdRQCSEKVVEYM----KEQGTLFLegvVPINIEKMDDKIKVLFS- 260

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1560336878 223 qSGETLQADVVIYGIGISAN-EQLAREA---NLDTANGIVIDEACrTCDPAIFAGGDVAITR 280
Cdd:PTZ00052  261 -DGTTELFDTVLYATGRKPDiKGLNLNAigvHVNKSNKIIAPNDC-TNIPNIFAVGDVVEGR 320
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 141-234 4.50e-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: 38.97  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560336878 141 LQPERSVVIIGAGTIGLELAASATQRRCKvTVIelaatVMGRNAPPpvqrylLQRHQQAGVRILLNNAIEHVVDGEKvEL 220
Cdd:COG1063   159 VKPGDTVLVIGAGPIGLLAALAARLAGAA-RVI-----VVDRNPER------LELARELGADAVVNPREEDLVEAVR-EL 225

                          90
                  ....*....|....
gi 1560336878 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 6.94e-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: 38.12  E-value: 6.94e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1560336878 126 FTLRHAGDAARLREVLQPERSVVIIGAGTIGLELAASATQRRCKVTVIE 174
Cdd:COG0569    77 GLLEALRRRRMERGIKKLKMHVIIIGAGRVGRSLARELEEEGHDVVVID 125
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
190-234 8.36e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 37.64  E-value: 8.36e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1560336878 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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