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Conserved domains on  [gi|110625837|ref|NP_898988|]
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pyridine nucleotide-disulfide oxidoreductase domain-containing protein 1 isoform a [Mus musculus]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 1001407)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to nitrite reductase large subunit NirB

CATH:  3.30.390.30
EC:  1.-.-.-
Gene Ontology:  GO:0016491
PubMed:  2445993
SCOP:  4000121

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NirB super family cl34210
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
84-495 2.91e-38

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


The actual alignment was detected with superfamily member COG1251:

Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 144.13  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  84 VKQLKSEDHCIFTEDGREFVYKKLCLCAGAKP-KLIYEGN--PRVLGIRDTDSAQEFQKELAKARRIMIVGNGGIALELA 160
Cdd:COG1251   79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 161 YEI--EGCEVVWAIKDNAIGNTFFDAGAAEFLTSKLMSekseakiahkrtiytveeakketrtkskadyvgsalgpdwHG 238
Cdd:COG1251  159 AALrkRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEA----------------------------------------LG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 239 glalkgteefshsVHIETRCEVKKIYLEEefkimkkkslafpkdhhkSVTAdkemwpvyVELTNGTIYGCDFLVSATGVT 318
Cdd:COG1251  199 -------------VEVRLGTGVTEIEGDD------------------RVTG--------VRLADGEELPADLVVVAIGVR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 319 PNVhpflhrnnfALGE------DGGLRVDDQMRTSLPDIYAAGDIctACWqPSPVWQQ--MRLWTQARQMGYYAAKCMAa 390
Cdd:COG1251  240 PNT---------ELARaaglavDRGIVVDDYLRTSDPDIYAAGDC--AEH-PGPVYGRrvLELVAPAYEQARVAAANLA- 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 391 asmGHPIdmDFSFELFAHVTKFFNYKVVLLGKYNaqglGADHELMLRCTRGQEYVKVVMQNGRMMGAVLIGETDLEETFE 470
Cdd:COG1251  307 ---GGPA--AYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALR 377

                        410       420
                 ....*....|....*....|....*
gi 110625837 471 NLILNQMDLSsyGEDLLDPNIDIED 495
Cdd:COG1251  378 QLIKNGRPLP--PRALLDAALPLKE 400
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
84-495 2.91e-38

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 144.13  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  84 VKQLKSEDHCIFTEDGREFVYKKLCLCAGAKP-KLIYEGN--PRVLGIRDTDSAQEFQKELAKARRIMIVGNGGIALELA 160
Cdd:COG1251   79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 161 YEI--EGCEVVWAIKDNAIGNTFFDAGAAEFLTSKLMSekseakiahkrtiytveeakketrtkskadyvgsalgpdwHG 238
Cdd:COG1251  159 AALrkRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEA----------------------------------------LG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 239 glalkgteefshsVHIETRCEVKKIYLEEefkimkkkslafpkdhhkSVTAdkemwpvyVELTNGTIYGCDFLVSATGVT 318
Cdd:COG1251  199 -------------VEVRLGTGVTEIEGDD------------------RVTG--------VRLADGEELPADLVVVAIGVR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 319 PNVhpflhrnnfALGE------DGGLRVDDQMRTSLPDIYAAGDIctACWqPSPVWQQ--MRLWTQARQMGYYAAKCMAa 390
Cdd:COG1251  240 PNT---------ELARaaglavDRGIVVDDYLRTSDPDIYAAGDC--AEH-PGPVYGRrvLELVAPAYEQARVAAANLA- 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 391 asmGHPIdmDFSFELFAHVTKFFNYKVVLLGKYNaqglGADHELMLRCTRGQEYVKVVMQNGRMMGAVLIGETDLEETFE 470
Cdd:COG1251  307 ---GGPA--AYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALR 377

                        410       420
                 ....*....|....*....|....*
gi 110625837 471 NLILNQMDLSsyGEDLLDPNIDIED 495
Cdd:COG1251  378 QLIKNGRPLP--PRALLDAALPLKE 400
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 43-381 1.65e-19

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: 88.91  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837   43 VIKAVTNFRQVSKVLEEFDVEEQPGTMLESRFPNIKVIEsGVKQLKSEDhcIFTEDGREFVYKKLCLCAGAKPKLI-YEG 121
Cdd:pfam07992  52 APEIASLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDP-GAKKVVLEE--LVDGDGETITYDRLVIATGARPRLPpIPG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  122 --NPRVLGIRDTDSAQEFQKELaKARRIMIVGNGGIALELAYEIE--GCEVVWaIKDNAIGNTFFDAGAAEFLtsklmse 197
Cdd:pfam07992 129 veLNVGFLVRTLDSAEALRLKL-LPKRVVVVGGGYIGVELAAALAklGKEVTL-IEALDRLLRAFDEEISAAL------- 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  198 kseakiahkrtiytvEEAKKEtrtkskadyvgsalgpdwhgglalkgteefsHSVHIETRCEVKKIyleeefkimkkksl 277
Cdd:pfam07992 200 ---------------EKALEK-------------------------------NGVEVRLGTSVKEI-------------- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  278 afpKDHHKSVTadkemwpvyVELTNGTIYGCDFLVSATGVTPNvHPFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDi 357
Cdd:pfam07992 220 ---IGDGDGVE---------VILKDGTEIDADLVVVAIGRRPN-TELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD- 285

                         330       340
                  ....*....|....*....|....
gi 110625837  358 ctaCWQPSPvwqqmRLWTQARQMG 381
Cdd:pfam07992 286 ---CRVGGP-----ELAQNAVAQG 301
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 98-357 4.42e-09

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 58.59  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837   98 DGREFVYKKLCLCA-GAKPKLiyegnPRVLGIRDTD--SAQEFQKELAKARRIMIVGNGGIALELA--YEIEGCEVVWAI 172
Cdd:TIGR02053 122 LGREVRGAKRFLIAtGARPAI-----PPIPGLKEAGylTSEEALALDRIPESLAVIGGGAIGVELAqaFARLGSEVTILQ 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  173 KDNAIgntffdagaaefltskLMSEKSEAKIAhkrtiytVEEAkketrtkskadyvgsalgpdwhggLALKGteefshsV 252
Cdd:TIGR02053 197 RSDRL----------------LPREEPEISAA-------VEEA------------------------LAEEG-------I 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  253 HIETRCEVKKIYLEEEFKImkkkslafpkdhhksVTADKEMWPVYVEltngtiygCDFLVSATGVTPNVHPF-LHRNNFA 331
Cdd:TIGR02053 223 EVVTSAQVKAVSVRGGGKI---------------ITVEKPGGQGEVE--------ADELLVATGRRPNTDGLgLEKAGVK 279

                         250       260
                  ....*....|....*....|....*.
gi 110625837  332 LGEDGGLRVDDQMRTSLPDIYAAGDI 357
Cdd:TIGR02053 280 LDERGGILVDETLRTSNPGIYAAGDV 305
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
58-356 9.49e-09

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 57.23  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  58 EEFDVEEQPGTMLESrfpnikvIESGVKQLKSedhcifteDGREFVYKKLCLCAGAK---PKLiyEGNPRVLGIrdtDSA 134
Cdd:PRK04965  69 EQFNLRLFPHTWVTD-------IDAEAQVVKS--------QGNQWQYDKLVLATGASafvPPI--PGRELMLTL---NSQ 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 135 QEF---QKELAKARRIMIVGNGGIALELAYEI--EGCEVVwaIKDNAigntffdagaaEFLTSKLMSEKSEAKIAHKRTi 209
Cdd:PRK04965 129 QEYraaETQLRDAQRVLVVGGGLIGTELAMDLcrAGKAVT--LVDNA-----------ASLLASLMPPEVSSRLQHRLT- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 210 ytveeakketrtkskadyvgsalgpdwhgglalkgteefSHSVHIETRCEVKKIyleeefkimkkkslafpkdhhkSVTA 289
Cdd:PRK04965 195 ---------------------------------------EMGVHLLLKSQLQGL----------------------EKTD 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625837 290 DKemwpVYVELTNGTIYGCDFLVSATGVTPNVhpflhrnnfALGEDGGLR------VDDQMRTSLPDIYAAGD 356
Cdd:PRK04965 214 SG----IRATLDSGRSIEVDAVIAAAGLRPNT---------ALARRAGLAvnrgivVDSYLQTSAPDIYALGD 273
 
Name Accession Description Interval E-value
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
84-495 2.91e-38

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 144.13  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  84 VKQLKSEDHCIFTEDGREFVYKKLCLCAGAKP-KLIYEGN--PRVLGIRDTDSAQEFQKELAKARRIMIVGNGGIALELA 160
Cdd:COG1251   79 VTAIDRAARTVTLADGETLPYDKLVLATGSRPrVPPIPGAdlPGVFTLRTLDDADALRAALAPGKRVVVIGGGLIGLEAA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 161 YEI--EGCEVVWAIKDNAIGNTFFDAGAAEFLTSKLMSekseakiahkrtiytveeakketrtkskadyvgsalgpdwHG 238
Cdd:COG1251  159 AALrkRGLEVTVVERAPRLLPRQLDEEAGALLQRLLEA----------------------------------------LG 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 239 glalkgteefshsVHIETRCEVKKIYLEEefkimkkkslafpkdhhkSVTAdkemwpvyVELTNGTIYGCDFLVSATGVT 318
Cdd:COG1251  199 -------------VEVRLGTGVTEIEGDD------------------RVTG--------VRLADGEELPADLVVVAIGVR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 319 PNVhpflhrnnfALGE------DGGLRVDDQMRTSLPDIYAAGDIctACWqPSPVWQQ--MRLWTQARQMGYYAAKCMAa 390
Cdd:COG1251  240 PNT---------ELARaaglavDRGIVVDDYLRTSDPDIYAAGDC--AEH-PGPVYGRrvLELVAPAYEQARVAAANLA- 306

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 391 asmGHPIdmDFSFELFAHVTKFFNYKVVLLGKYNaqglGADHELMLRCTRGQEYVKVVMQNGRMMGAVLIGETDLEETFE 470
Cdd:COG1251  307 ---GGPA--AYEGSVPSTKLKVFGVDVASAGDAE----GDEEVVVRGDPARGVYKKLVLRDGRLVGAVLVGDTSDAGALR 377

                        410       420
                 ....*....|....*....|....*
gi 110625837 471 NLILNQMDLSsyGEDLLDPNIDIED 495
Cdd:COG1251  378 QLIKNGRPLP--PRALLDAALPLKE 400
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 75-430 1.98e-25

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: 106.43  E-value: 1.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  75 PNIKVI-ESGVKQLKSEDHCIFTEDGREFVYKKLCLCAGAKPKLI-YEG--NPRVLGIRDTDSAQEFQKELA--KARRIM 148
Cdd:COG0446   49 KGIDVRtGTEVTAIDPEAKTVTLRDGETLSYDKLVLATGARPRPPpIPGldLPGVFTLRTLDDADALREALKefKGKRAV 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 149 IVGNGGIALELAYeiegcevvwaikdnaignTFFDAGAaefltsklmsekseaKIahkrtiyTVEEAkketrtkskADYV 228
Cdd:COG0446  129 VIGGGPIGLELAE------------------ALRKRGL---------------KV-------TLVER---------APRL 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 229 GSALGPDwhggLALKGTEEF-SHSVHIETRCEVKKIyleeefkimkkkslafpKDHHKsvtadkemwpVYVELTNGTIYG 307
Cdd:COG0446  160 LGVLDPE----MAALLEEELrEHGVELRLGETVVAI-----------------DGDDK----------VAVTLTDGEEIP 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 308 CDFLVSATGVTPNVHpFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDICTACWQPSPVWQQMRLWTQARQMGYYAAKC 387
Cdd:COG0446  209 ADLVVVAPGVRPNTE-LAKDAGLALGERGWIKVDETLQTSDPDVYAAGDCAEVPHPVTGKTVYIPLASAANKQGRVAAEN 287

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|...
gi 110625837 388 MAaasmGHPIDMDFsfeLFAHVTKFFNYKVVLLGKYnaQGLGA 430
Cdd:COG0446  288 IL----GGPAPFPG---LGTFISKVFDLCIASTGTG--RLLGA 321
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 43-381 1.65e-19

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: 88.91  E-value: 1.65e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837   43 VIKAVTNFRQVSKVLEEFDVEEQPGTMLESRFPNIKVIEsGVKQLKSEDhcIFTEDGREFVYKKLCLCAGAKPKLI-YEG 121
Cdd:pfam07992  52 APEIASLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDP-GAKKVVLEE--LVDGDGETITYDRLVIATGARPRLPpIPG 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  122 --NPRVLGIRDTDSAQEFQKELaKARRIMIVGNGGIALELAYEIE--GCEVVWaIKDNAIGNTFFDAGAAEFLtsklmse 197
Cdd:pfam07992 129 veLNVGFLVRTLDSAEALRLKL-LPKRVVVVGGGYIGVELAAALAklGKEVTL-IEALDRLLRAFDEEISAAL------- 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  198 kseakiahkrtiytvEEAKKEtrtkskadyvgsalgpdwhgglalkgteefsHSVHIETRCEVKKIyleeefkimkkksl 277
Cdd:pfam07992 200 ---------------EKALEK-------------------------------NGVEVRLGTSVKEI-------------- 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  278 afpKDHHKSVTadkemwpvyVELTNGTIYGCDFLVSATGVTPNvHPFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDi 357
Cdd:pfam07992 220 ---IGDGDGVE---------VILKDGTEIDADLVVVAIGRRPN-TELLEAAGLELDERGGIVVDEYLRTSVPGIYAAGD- 285

                         330       340
                  ....*....|....*....|....
gi 110625837  358 ctaCWQPSPvwqqmRLWTQARQMG 381
Cdd:pfam07992 286 ---CRVGGP-----ELAQNAVAQG 301
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
73-396 3.02e-17

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 83.26  E-value: 3.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  73 RFPNIKVIESGVKQLKSEDHCIFTEDGREFVYKKLCLCAGAKPKliYEGNPRV----LGIRDTDSAQEFQKEL------- 141
Cdd:COG1252   67 RRAGVRFIQGEVTGIDPEARTVTLADGRTLSYDYLVIATGSVTN--FFGIPGLaehaLPLKTLEDALALRERLlaafera 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 142 --AKARRIMIVGNGGIALELAYEIegcevvwaikdnaigntffdagaAEFLTSKLmsekSEAKIAHKRT-IYTVEeakke 218
Cdd:COG1252  145 erRRLLTIVVVGGGPTGVELAGEL-----------------------AELLRKLL----RYPGIDPDKVrITLVE----- 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 219 trtksKADYVGSALGPDwhggLALKGTEEF-SHSVHIETRCEVKkiyleeefkimkkkslafpkdhhkSVTADKemwpvy 297
Cdd:COG1252  193 -----AGPRILPGLGEK----LSEAAEKELeKRGVEVHTGTRVT------------------------EVDADG------ 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 298 VELTNGTIYGCDFLVSATGVTPNvhPFLHRNNFALGEDGGLRVDDQMRT-SLPDIYAAGDiCTACWQPSPVWQ----QMr 372
Cdd:COG1252  234 VTLEDGEEIPADTVIWAAGVKAP--PLLADLGLPTDRRGRVLVDPTLQVpGHPNVFAIGD-CAAVPDPDGKPVpktaQA- 309

                        330       340
                 ....*....|....*....|....
gi 110625837 373 lwtqARQMGYYAAKCMAAASMGHP 396
Cdd:COG1252  310 ----AVQQAKVLAKNIAALLRGKP 329
MerA TIGR02053
mercury(II) reductase; This model represents the mercuric reductase found in the mer operon ...
 98-357 4.42e-09

mercury(II) reductase; This model represents the mercuric reductase found in the mer operon for the detoxification of mercury compounds. MerA is a FAD-containing flavoprotein which reduces Hg(II) to Hg(0) utilizing NADPH. [Cellular processes, Detoxification]


Pssm-ID: 273944 [Multi-domain]  Cd Length: 463  Bit Score: 58.59  E-value: 4.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837   98 DGREFVYKKLCLCA-GAKPKLiyegnPRVLGIRDTD--SAQEFQKELAKARRIMIVGNGGIALELA--YEIEGCEVVWAI 172
Cdd:TIGR02053 122 LGREVRGAKRFLIAtGARPAI-----PPIPGLKEAGylTSEEALALDRIPESLAVIGGGAIGVELAqaFARLGSEVTILQ 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  173 KDNAIgntffdagaaefltskLMSEKSEAKIAhkrtiytVEEAkketrtkskadyvgsalgpdwhggLALKGteefshsV 252
Cdd:TIGR02053 197 RSDRL----------------LPREEPEISAA-------VEEA------------------------LAEEG-------I 222

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  253 HIETRCEVKKIYLEEEFKImkkkslafpkdhhksVTADKEMWPVYVEltngtiygCDFLVSATGVTPNVHPF-LHRNNFA 331
Cdd:TIGR02053 223 EVVTSAQVKAVSVRGGGKI---------------ITVEKPGGQGEVE--------ADELLVATGRRPNTDGLgLEKAGVK 279

                         250       260
                  ....*....|....*....|....*.
gi 110625837  332 LGEDGGLRVDDQMRTSLPDIYAAGDI 357
Cdd:TIGR02053 280 LDERGGILVDETLRTSNPGIYAAGDV 305
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
58-356 9.49e-09

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 57.23  E-value: 9.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  58 EEFDVEEQPGTMLESrfpnikvIESGVKQLKSedhcifteDGREFVYKKLCLCAGAK---PKLiyEGNPRVLGIrdtDSA 134
Cdd:PRK04965  69 EQFNLRLFPHTWVTD-------IDAEAQVVKS--------QGNQWQYDKLVLATGASafvPPI--PGRELMLTL---NSQ 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 135 QEF---QKELAKARRIMIVGNGGIALELAYEI--EGCEVVwaIKDNAigntffdagaaEFLTSKLMSEKSEAKIAHKRTi 209
Cdd:PRK04965 129 QEYraaETQLRDAQRVLVVGGGLIGTELAMDLcrAGKAVT--LVDNA-----------ASLLASLMPPEVSSRLQHRLT- 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 210 ytveeakketrtkskadyvgsalgpdwhgglalkgteefSHSVHIETRCEVKKIyleeefkimkkkslafpkdhhkSVTA 289
Cdd:PRK04965 195 ---------------------------------------EMGVHLLLKSQLQGL----------------------EKTD 213

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 110625837 290 DKemwpVYVELTNGTIYGCDFLVSATGVTPNVhpflhrnnfALGEDGGLR------VDDQMRTSLPDIYAAGD 356
Cdd:PRK04965 214 SG----IRATLDSGRSIEVDAVIAAAGLRPNT---------ALARRAGLAvnrgivVDSYLQTSAPDIYALGD 273
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 296-462 1.30e-08

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: 57.02  E-value: 1.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 296 VYVELTNG---TIYGCDFLVSATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDiCTACWQPSPVwqqm 371
Cdd:COG1249  242 VTVTLEDGggeEAVEADKVLVATGRRPNTDGLgLEAAGVELDERGGIKVDEYLRTSVPGIYAIGD-VTGGPQLAHV---- 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 372 rlwtqARQMGYYAAKcMAAASMGHPIDMD------FSF-ELfAHV--------TKFFNYKVvllGKYNAQGLG-AdheLM 435
Cdd:COG1249  317 -----ASAEGRVAAE-NILGKKPRPVDYRaipsvvFTDpEI-ASVglteeearEAGIDVKV---GKFPFAANGrA---LA 383

                        170       180
                 ....*....|....*....|....*....
gi 110625837 436 LRCTRGqeYVKVV--MQNGRMMGAVLIGE 462
Cdd:COG1249  384 LGETEG--FVKLIadAETGRILGAHIVGP 410
PRK13748 PRK13748
putative mercuric reductase; Provisional
 308-368 2.76e-08

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 56.31  E-value: 2.76e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110625837 308 CDFLVSATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDiCTAcwQPSPVW 368
Cdd:PRK13748 354 ADKLLVATGRAPNTRSLaLDAAGVTVNAQGAIVIDQGMRTSVPHIYAAGD-CTD--QPQFVY 412
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 63-259 3.91e-08

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 55.32  E-value: 3.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  63 EEQPGTMLESRFPNIKVIE--SG--VKQLKSEDHCIFTEDGREFVYKKLCLCAGAKPK---LIYEGNPRVLGIRDTDSAQ 135
Cdd:PRK09754  56 SPQLQQVLPANWWQENNVHlhSGvtIKTLGRDTRELVLTNGESWHWDQLFIATGAAARplpLLDALGERCFTLRHAGDAA 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 136 EFQKELAKARRIMIVGNGGIALELAYEI--EGCEV-VWAIKDNAIG------------NTFFDAGAAEFLTSKLMSEKSE 200
Cdd:PRK09754 136 RLREVLQPERSVVIVGAGTIGLELAASAtqRRCKVtVIELAATVMGrnapppvqryllQRHQQAGVRILLNNAIEHVVDG 215

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 110625837 201 AKIahkrtiytveEAKKETRTKSKADYVGSALGPDWHGGLALKGTEEFSHSVHIETRCE 259
Cdd:PRK09754 216 EKV----------ELTLQSGETLQADVVIYGIGISANDQLAREANLDTANGIVIDEACR 264
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
308-359 3.37e-07

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 52.04  E-value: 3.37e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110625837 308 CDFLVSATGVTPNVHPFLHrNNFALGEDGGLRVDDQMRTSLPDIYAAGDICT 359
Cdd:COG0492  227 VDGVFVAIGLKPNTELLKG-LGLELDEDGYIVVDEDMETSVPGVFAAGDVRD 277
PRK06370 PRK06370
FAD-containing oxidoreductase;
308-358 6.44e-07

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 51.74  E-value: 6.44e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 110625837 308 CDFLVSATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDIC 358
Cdd:PRK06370 260 GSHILVAVGRVPNTDDLgLEAAGVETDARGYIKVDDQLRTTNPGIYAAGDCN 311
PRK14989 PRK14989
nitrite reductase subunit NirD; Provisional
 302-489 2.79e-06

nitrite reductase subunit NirD; Provisional


Pssm-ID: 184951 [Multi-domain]  Cd Length: 847  Bit Score: 50.12  E-value: 2.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 302 NGTIYGCDFLVSATGVTPNvHPFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDiCTAcwqpspvWQQMRLWTQARqmG 381
Cdd:PRK14989 228 DGSELEVDFIVFSTGIRPQ-DKLATQCGLAVAPRGGIVINDSCQTSDPDIYAIGE-CAS-------WNNRVFGLVAP--G 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 382 YYaakcMAAASMGHPIDMDFSFE---LFAHVtKFFNYKVVLLGKYNAQGLGADHELMLrcTRGQEYVK---VVMQNGRMM 455
Cdd:PRK14989 297 YK----MAQVAVDHLLGSENAFEgadLSAKL-KLLGVDVGGIGDAHGRTPGARSYVYL--DESKEIYKrliVSEDNKTLL 369

                        170       180       190
                 ....*....|....*....|....*....|....
gi 110625837 456 GAVLIGETDLEETFENLILNQMDLSSYGEDLLDP 489
Cdd:PRK14989 370 GAVLVGDTSDYGNLLQLVLNAIELPENPDSLILP 403
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 296-363 5.29e-06

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 48.88  E-value: 5.29e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 110625837 296 VYVELTNGTIYGCDFLVSATGVTPNVHpFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDiCTACWQ 363
Cdd:PRK09564 223 VEGVVTDKGEYEADVVIVATGVKPNTE-FLEDTGLKTLKNGAIIVDEYGETSIENIYAAGD-CATIYN 288
lipoamide_DH TIGR01350
dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a ...
 309-400 7.76e-06

dihydrolipoamide dehydrogenase; This model describes dihydrolipoamide dehydrogenase, a flavoprotein that acts in a number of ways. It is the E3 component of dehydrogenase complexes for pyruvate, 2-oxoglutarate, 2-oxoisovalerate, and acetoin. It can also serve as the L protein of the glycine cleavage system. This family includes a few members known to have distinct functions (ferric leghemoglobin reductase and NADH:ferredoxin oxidoreductase) but that may be predicted by homology to act as dihydrolipoamide dehydrogenase as well. The motif GGXCXXXGCXP near the N-terminus contains a redox-active disulfide.


Pssm-ID: 273568 [Multi-domain]  Cd Length: 460  Bit Score: 48.41  E-value: 7.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  309 DFLVSATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDIcTACWQpspvwqqmrLWTQARQMGYYAAKC 387
Cdd:TIGR01350 259 EKVLVAVGRKPNTEGLgLEKLGVELDERGRIVVDEYMRTNVPGIYAIGDV-IGGPM---------LAHVASHEGIVAAEN 328

                          90
                  ....*....|...
gi 110625837  388 MAAASmGHPIDMD 400
Cdd:TIGR01350 329 IAGKE-PAHIDYD 340
PRK07251 PRK07251
FAD-containing oxidoreductase;
259-357 9.13e-06

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 47.82  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 259 EVKKIYLEEEfkimkkkSLAFPKDHHKSVTADKEMWPVYVelTNGTIYGCDFLVSATGVTPNVHPF-LHRNNFALGEDGG 337
Cdd:PRK07251 202 ALAKQYMEED-------GITFLLNAHTTEVKNDGDQVLVV--TEDETYRFDALLYATGRKPNTEPLgLENTDIELTERGA 272

                         90       100
                 ....*....|....*....|
gi 110625837 338 LRVDDQMRTSLPDIYAAGDI 357
Cdd:PRK07251 273 IKVDDYCQTSVPGVFAVGDV 292
PRK06116 PRK06116
glutathione reductase; Validated
 298-357 1.32e-05

glutathione reductase; Validated


Pssm-ID: 235701 [Multi-domain]  Cd Length: 450  Bit Score: 47.46  E-value: 1.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110625837 298 VELTNGTIYGCDFLVSATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDI 357
Cdd:PRK06116 244 LTLEDGETLTVDCLIWAIGREPNTDGLgLENAGVKLNEKGYIIVDEYQNTNVPGIYAVGDV 304
nitri_red_nirB TIGR02374
nitrite reductase [NAD(P)H], large subunit; [Central intermediary metabolism, Nitrogen ...
 298-480 2.47e-05

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


Pssm-ID: 162827 [Multi-domain]  Cd Length: 785  Bit Score: 47.13  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  298 VELTNGTIYGCDFLVSATGVTPNVHpfLHRNNfALGEDGGLRVDDQMRTSLPDIYAAGDIctACWQPSPVWQQMRLWTQA 377
Cdd:TIGR02374 217 IRFKDGSSLEADLIVMAAGIRPNDE--LAVSA-GIKVNRGIIVNDSMQTSDPDIYAVGEC--AEHNGRVYGLVAPLYEQA 291

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  378 RqmgyYAAKCMAAASMGHPIDMDFSFELfahvtKFFNYKVVLLGKYNAqglgADHELMLRCTRGQE--YVKVVMQNGRMM 455
Cdd:TIGR02374 292 K----VLADHICGVECEEYEGSDLSAKL-----KLLGVDVWSAGDAQE----TERTTSIKIYDEQKgiYKKLVLSDDKLL 358

                         170       180
                  ....*....|....*....|....*
gi 110625837  456 GAVLIGETDLEETFENLILNQMDLS 480
Cdd:TIGR02374 359 GAVLFGDTSDYGRLLDMVLKQADIS 383
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 289-357 3.72e-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: 45.90  E-value: 3.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 110625837 289 ADKEMWPVYVEltnGT--IYGCDFLVSATGVTPNVHPFLHRNNFALGEDGGLRVDDQ-MRTSLPDIYAAGDI 357
Cdd:COG0493  342 ESGRRRPVPIE---GSefTLPADLVILAIGQTPDPSGLEEELGLELDKRGTIVVDEEtYQTSLPGVFAGGDA 410
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 309-357 5.03e-05

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 45.52  E-value: 5.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 110625837 309 DFLVSATGVTPNVhpflhrNNFALGE-----DGGL-RVDDQMRTSLPDIYAAGDI 357
Cdd:PRK06416 262 DYVLVAVGRRPNT------ENLGLEElgvktDRGFiEVDEQLRTNVPNIYAIGDI 310
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 298-421 5.07e-05

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 45.54  E-value: 5.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 298 VELTNGTIYGCDFLVSATGVTPNVHpFLHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDICTACWQPSPVWQQMRL-Wtq 376
Cdd:PRK13512 220 VTFKSGKVEHYDMIIEGVGTHPNSK-FIESSNIKLDDKGFIPVNDKFETNVPNIYAIGDIITSHYRHVDLPASVPLaW-- 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 110625837 377 arqmGYYAAKCMAAASMGHPIDMDFSFELFAHVTKFFNYKVVLLG 421
Cdd:PRK13512 297 ----GAHRAASIVAEQIAGNDTIEFKGFLGNNIVKFFDYTFASVG 337
PRK07846 PRK07846
mycothione reductase; Reviewed
 296-359 5.21e-05

mycothione reductase; Reviewed


Pssm-ID: 181142 [Multi-domain]  Cd Length: 451  Bit Score: 45.72  E-value: 5.21e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110625837 296 VYVELTNGTIYGCDFLVSATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDICT 359
Cdd:PRK07846 239 VTLRLDDGSTVEADVLLVATGRVPNGDLLdAAAAGVDVDEDGRVVVDEYQRTSAEGVFALGDVSS 303
PRK07845 PRK07845
flavoprotein disulfide reductase; Reviewed
 296-359 5.28e-05

flavoprotein disulfide reductase; Reviewed


Pssm-ID: 236112 [Multi-domain]  Cd Length: 466  Bit Score: 45.62  E-value: 5.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110625837 296 VYVELTNG-TIYGCDFLVsATGVTPNVHPF-LHRNNFALGEDGGLRVDDQMRTSLPDIYAAGDiCT 359
Cdd:PRK07845 251 VVVTLTDGrTVEGSHALM-AVGSVPNTAGLgLEEAGVELTPSGHITVDRVSRTSVPGIYAAGD-CT 314
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 308-359 1.23e-04

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 44.40  E-value: 1.23e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 110625837 308 CDFLVSATGVTPNVHPFLHRNNFALGEDGGLRVDDQ-MRTSLPDIYAAGDICT 359
Cdd:PRK11749 376 ADLVIKAIGQTPNPLILSTTPGLELNRWGTIIADDEtGRTSLPGVFAGGDIVT 428
PTZ00318 PTZ00318
NADH dehydrogenase-like protein; Provisional
 259-430 2.55e-04

NADH dehydrogenase-like protein; Provisional


Pssm-ID: 185553 [Multi-domain]  Cd Length: 424  Bit Score: 43.22  E-value: 2.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 259 EVKKIYLEEEFKI-------MKKKSLAFPKDHHKSV---TADKEMWPVYVELTNGTIYGCDFLVSATGVTPnvHPFLHRN 328
Cdd:PTZ00318 210 ECKVTVLEAGSEVlgsfdqaLRKYGQRRLRRLGVDIrtkTAVKEVLDKEVVLKDGEVIPTGLVVWSTGVGP--GPLTKQL 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 329 NFALGEDGGLRVDDQMRTS-LPDIYAAGDICTACWQPSPVWQQMrlwtqARQMGYYAAKCMAAASMGHPIDMDFSFELFA 407
Cdd:PTZ00318 288 KVDKTSRGRISVDDHLRVKpIPNVFALGDCAANEERPLPTLAQV-----ASQQGVYLAKEFNNELKGKPMSKPFVYRSLG 362

                        170       180
                 ....*....|....*....|....
gi 110625837 408 HVTKFFNYK-VVLLGKYNAQGLGA 430
Cdd:PTZ00318 363 SLAYLGNYSaIVQLGAFDLSGFKA 386
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 264-357 3.73e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 42.86  E-value: 3.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 264 YLEEEFKImkkkslaFPKDHHKSVTADKEMWPVYVELTNGTIY-GCDFLVSATGVTPNV-HPFLHRNNFALGEDGGLRVD 341
Cdd:PRK06292 219 ILSKEFKI-------KLGAKVTSVEKSGDEKVEELEKGGKTETiEADYVLVATGRRPNTdGLGLENTGIELDERGRPVVD 291

                         90
                 ....*....|....*.
gi 110625837 342 DQMRTSLPDIYAAGDI 357
Cdd:PRK06292 292 EHTQTSVPGIYAAGDV 307
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 308-358 5.63e-04

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 41.84  E-value: 5.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 110625837  308 CDFLVSATGVTPNVHPFLHRnnFALGEDGGLRVDDQMRTSLPDIYAAGDIC 358
Cdd:TIGR01292 226 VDGVFIAIGHEPNTELLKGL--LELDENGYIVTDEGMRTSVPGVFAAGDVR 274
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 295-359 9.08e-04

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.04  E-value: 9.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 110625837 295 PVYVELTNGTIyGCDFLVSATGVTPNvhPFLHRN--NFALGEDGGLRVDDQMRTSLPDIYAAGDICT 359
Cdd:PRK12778 663 PVAIPGSTFTV-DVDLVIVSVGVSPN--PLVPSSipGLELNRKGTIVVDEEMQSSIPGIYAGGDIVR 726
PRK05249 PRK05249
Si-specific NAD(P)(+) transhydrogenase;
296-357 1.56e-03

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


Pssm-ID: 235373 [Multi-domain]  Cd Length: 461  Bit Score: 40.91  E-value: 1.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 110625837 296 VYVELTNGTIYGCDFLVSATGVTPNVHPfLHRNNFALGED--GGLRVDDQMRTSLPDIYAAGDI 357
Cdd:PRK05249 249 VIVHLKSGKKIKADCLLYANGRTGNTDG-LNLENAGLEADsrGQLKVNENYQTAVPHIYAVGDV 311
PTZ00058 PTZ00058
glutathione reductase; Provisional
 97-358 1.89e-03

glutathione reductase; Provisional


Pssm-ID: 185420 [Multi-domain]  Cd Length: 561  Bit Score: 40.75  E-value: 1.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837  97 EDGREFVYKKLCLCAGAKPKLiyegnPRVLGIRDTDSAQEFQKeLAKARRIMIVGNGGIALELAyeiegcevvwaikdna 176
Cdd:PTZ00058 196 DDGQVIEGKNILIAVGNKPIF-----PDVKGKEFTISSDDFFK-IKEAKRIGIAGSGYIAVELI---------------- 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 177 igNTFFDAGAAEFLTSKlmsekseakiAHKRTIYTVEEAKKETRTKSKADyvgsalgpdwhgglalkgteefshSVHIET 256
Cdd:PTZ00058 254 --NVVNRLGAESYIFAR----------GNRLLRKFDETIINELENDMKKN------------------------NINIIT 297

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110625837 257 RCEVKKIYLEEEfkimkKKSLAFPKDHHKSVTADkemwpvyveltngtiygcdFLVSATGVTPNVHPFLHRNNFALGEDG 336
Cdd:PTZ00058 298 HANVEEIEKVKE-----KNLTIYLSDGRKYEHFD-------------------YVIYCVGRSPNTEDLNLKALNIKTPKG 353

                        250       260
                 ....*....|....*....|..
gi 110625837 337 GLRVDDQMRTSLPDIYAAGDIC 358
Cdd:PTZ00058 354 YIKVDDNQRTSVKHIYAVGDCC 375
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 308-357 5.42e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 39.14  E-value: 5.42e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 110625837 308 CDFLVSATGVTPNVHPFLHRN-NFALGEDGGLRVDDQMRTSLPDIYAAGDI 357
Cdd:PRK06327 273 VDKLIVSIGRVPNTDGLGLEAvGLKLDERGFIPVDDHCRTNVPNVYAIGDV 323
 
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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