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Conserved domains on  [gi|1196905331|ref|WP_086344022|]
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MULTISPECIES: YpdA family putative bacillithiol disulfide reductase [Bacillus]

Protein Classification

YpdA family putative bacillithiol disulfide reductase( domain architecture ID 11499296)

YpdA family putative bacillithiol disulfide reductase may function as a thiol disulfide oxidoreductase and is present only in species with an active bacillithiol system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
 5-321 0e+00

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


:

Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 522.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQTFFSSSEKLEIGDVAFITENRKPVRIQALSYYREVV 84
Cdd:TIGR04018   1 DVIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYPTNMTFFSTSERLEIGGIPFISENPKPTRNEALEYYRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  85 KRKNIRVNAFEMVHKVTKTENNtFVIETSKETYKTPYCIIATGYYDHPNYMGVPGEDLPKVFHYFKEGHPYFDKDVVVIG 164
Cdd:TIGR04018  81 ERFKLNIRLYEEVLKVKKTDGG-FEVTTEKGTYQAKNVIVATGYYDIPNLLNVPGEDLPKVSHYYKEAHPYFGQKVVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 165 GKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFRSGEKELITIKND 244
Cdd:TIGR04018 160 GSNSAVDAALELYRKGAEVTMVHRGDEVSSSVKYWVRPDIENRIKEGSIKAYFNSRVKEITEDSVTLETPDGEVHTIPND 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905331 245 FVFAMTGYHPDHQFLEKIGVEIDKETGRPFFNEKTMETNVEGVFIAGVIAAGNNANEIFIENGRFHGGHIAAEIAKR 321
Cdd:TIGR04018 240 FVFALTGYRPDFEFLESLGVELDEDTGIPVYNPETMETNVPGLYLAGVIAAGMDTNKIFIENGRFHAPLIAEHIASK 316
 
Name Accession Description Interval E-value
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
 5-321 0e+00

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 522.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQTFFSSSEKLEIGDVAFITENRKPVRIQALSYYREVV 84
Cdd:TIGR04018   1 DVIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYPTNMTFFSTSERLEIGGIPFISENPKPTRNEALEYYRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  85 KRKNIRVNAFEMVHKVTKTENNtFVIETSKETYKTPYCIIATGYYDHPNYMGVPGEDLPKVFHYFKEGHPYFDKDVVVIG 164
Cdd:TIGR04018  81 ERFKLNIRLYEEVLKVKKTDGG-FEVTTEKGTYQAKNVIVATGYYDIPNLLNVPGEDLPKVSHYYKEAHPYFGQKVVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 165 GKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFRSGEKELITIKND 244
Cdd:TIGR04018 160 GSNSAVDAALELYRKGAEVTMVHRGDEVSSSVKYWVRPDIENRIKEGSIKAYFNSRVKEITEDSVTLETPDGEVHTIPND 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905331 245 FVFAMTGYHPDHQFLEKIGVEIDKETGRPFFNEKTMETNVEGVFIAGVIAAGNNANEIFIENGRFHGGHIAAEIAKR 321
Cdd:TIGR04018 240 FVFALTGYRPDFEFLESLGVELDEDTGIPVYNPETMETNVPGLYLAGVIAAGMDTNKIFIENGRFHAPLIAEHIASK 316
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
13-291 1.98e-133

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 381.19  E-value: 1.98e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  13 PCGLSAAIHLKQIGIDA-LVIEKGNVVNSIYNYPTHQTFFSSS---EKLEIGDVAFITENRKPV---------RIQALSY 79
Cdd:pfam13738   1 PAGIGCAIALKKAGLEDyLILEKGNIGNSFYRYPTHMTFFSPSftsNGFGIPDLNAISPGTSPAftfnrehpsGNEYAEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  80 YREVVKRKNIRVNAFEMVHKVTKtENNTFVIETSKETYKTPYCIIATGYYDHPNYMGVPgeDLPKVFHYFKEGHPYFDKD 159
Cdd:pfam13738  81 LRRVADHFELPINLFEEVTSVKK-EDDGFVVTTSKGTYQARYVIIATGEFDFPNKLGVP--ELPKHYSYVKDFHPYAGQK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 160 VVVIGGKNSSVDAALELVKSGARVTVLYRGNE-------YSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFR 232
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRKGARVTVLYRGSEwedrdsdPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVDVSYK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 233 SGEKELITI-KNDFVFAMTGYHPDHQFLEKIGVEIDkETGRPFFNEKTMETNVEGVFIAG 291
Cdd:pfam13738 238 VHTEDGRKVtSNDDPILATGYHPDLSFLKKGLFELD-EDGRPVLTEETESTNVPGLFLAG 296
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-291 4.69e-41

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 144.88  E-value: 4.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNV------VNSIYNYPthqtffsssekleigdvAFITENRKPVRIQALs 78
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPggqlatTKEIENYP-----------------GFPEGISGPELAERL- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  79 yyREVVKRKNIRVnAFEMVHKVTKtENNTFVIETSK-ETYKTPYCIIATGyyDHPNYMGVPGEDLPKVF--HYF--KEGH 153
Cdd:COG0492    64 --REQAERFGAEI-LLEEVTSVDK-DDGPFRVTTDDgTEYEAKAVIIATG--AGPRKLGLPGEEEFEGRgvSYCatCDGF 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 154 PYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYSPSiKPWIlpefEALVRNGTIRMEFGACVEKITENE----V 229
Cdd:COG0492   138 FFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS-KILV----ERLRANPKIEVLWNTEVTEIEGDGrvegV 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905331 230 VFRSGE-KELITIKNDFVFAMTGYHPDHQFLEKIGVEIDKE----TGRpffnekTMETNVEGVFIAG 291
Cdd:COG0492   213 TLKNVKtGEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyivVDE------DMETSVPGVFAAG 273
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-291 1.96e-20

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 91.39  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   1 MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNV------VNSIynyPThQTFFSSSEKLE-IGDVAFITENRKPVR 73
Cdd:PRK06292    1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLggtclnVGCI---PS-KALIAAAEAFHeAKHAEEFGIHADGPK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  74 IQalsyYREVVKRKNIRVNAF--EMVHKVTKTENNTF-----------VIETSKETYKTPYCIIATGYyDHPNymgVPGE 140
Cdd:PRK06292   77 ID----FKKVMARVRRERDRFvgGVVEGLEKKPKIDKikgtarfvdpnTVEVNGERIEAKNIVIATGS-RVPP---IPGV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 141 DLPkvfhyfkEGHPYFD-----------KDVVVIGGknsSVdAALEL--VKS--GARVTVLyrgnEYSPSIkpwiLPEFE 205
Cdd:PRK06292  149 WLI-------LGDRLLTsddafeldklpKSLAVIGG---GV-IGLELgqALSrlGVKVTVF----ERGDRI----LPLED 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 206 ALVRN-------GTIRMEFGACVEKITEN---EVVFRSGEKELITIKNDFVFAMTGYHP--DHQFLEKIGVEIDkETGRP 273
Cdd:PRK06292  210 PEVSKqaqkilsKEFKIKLGAKVTSVEKSgdeKVEELEKGGKTETIEADYVLVATGRRPntDGLGLENTGIELD-ERGRP 288

                         330
                  ....*....|....*...
gi 1196905331 274 FFNEKTMeTNVEGVFIAG 291
Cdd:PRK06292  289 VVDEHTQ-TSVPGIYAAG 305
 
Name Accession Description Interval E-value
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
 5-321 0e+00

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 522.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQTFFSSSEKLEIGDVAFITENRKPVRIQALSYYREVV 84
Cdd:TIGR04018   1 DVIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYPTNMTFFSTSERLEIGGIPFISENPKPTRNEALEYYRRVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  85 KRKNIRVNAFEMVHKVTKTENNtFVIETSKETYKTPYCIIATGYYDHPNYMGVPGEDLPKVFHYFKEGHPYFDKDVVVIG 164
Cdd:TIGR04018  81 ERFKLNIRLYEEVLKVKKTDGG-FEVTTEKGTYQAKNVIVATGYYDIPNLLNVPGEDLPKVSHYYKEAHPYFGQKVVVVG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 165 GKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFRSGEKELITIKND 244
Cdd:TIGR04018 160 GSNSAVDAALELYRKGAEVTMVHRGDEVSSSVKYWVRPDIENRIKEGSIKAYFNSRVKEITEDSVTLETPDGEVHTIPND 239

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905331 245 FVFAMTGYHPDHQFLEKIGVEIDKETGRPFFNEKTMETNVEGVFIAGVIAAGNNANEIFIENGRFHGGHIAAEIAKR 321
Cdd:TIGR04018 240 FVFALTGYRPDFEFLESLGVELDEDTGIPVYNPETMETNVPGLYLAGVIAAGMDTNKIFIENGRFHAPLIAEHIASK 316
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
13-291 1.98e-133

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 381.19  E-value: 1.98e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  13 PCGLSAAIHLKQIGIDA-LVIEKGNVVNSIYNYPTHQTFFSSS---EKLEIGDVAFITENRKPV---------RIQALSY 79
Cdd:pfam13738   1 PAGIGCAIALKKAGLEDyLILEKGNIGNSFYRYPTHMTFFSPSftsNGFGIPDLNAISPGTSPAftfnrehpsGNEYAEY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  80 YREVVKRKNIRVNAFEMVHKVTKtENNTFVIETSKETYKTPYCIIATGYYDHPNYMGVPgeDLPKVFHYFKEGHPYFDKD 159
Cdd:pfam13738  81 LRRVADHFELPINLFEEVTSVKK-EDDGFVVTTSKGTYQARYVIIATGEFDFPNKLGVP--ELPKHYSYVKDFHPYAGQK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 160 VVVIGGKNSSVDAALELVKSGARVTVLYRGNE-------YSPSIKPWILPEFEALVRNGTIRMEFGACVEKITENEVVFR 232
Cdd:pfam13738 158 VVVIGGYNSAVDAALELVRKGARVTVLYRGSEwedrdsdPSYSLSPDTLNRLEELVKNGKIKAHFNAEVKEITEVDVSYK 237

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 233 SGEKELITI-KNDFVFAMTGYHPDHQFLEKIGVEIDkETGRPFFNEKTMETNVEGVFIAG 291
Cdd:pfam13738 238 VHTEDGRKVtSNDDPILATGYHPDLSFLKKGLFELD-EDGRPVLTEETESTNVPGLFLAG 296
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
5-291 4.69e-41

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 144.88  E-value: 4.69e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNV------VNSIYNYPthqtffsssekleigdvAFITENRKPVRIQALs 78
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGGEPggqlatTKEIENYP-----------------GFPEGISGPELAERL- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  79 yyREVVKRKNIRVnAFEMVHKVTKtENNTFVIETSK-ETYKTPYCIIATGyyDHPNYMGVPGEDLPKVF--HYF--KEGH 153
Cdd:COG0492    64 --REQAERFGAEI-LLEEVTSVDK-DDGPFRVTTDDgTEYEAKAVIIATG--AGPRKLGLPGEEEFEGRgvSYCatCDGF 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 154 PYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYSPSiKPWIlpefEALVRNGTIRMEFGACVEKITENE----V 229
Cdd:COG0492   138 FFRGKDVVVVGGGDSALEEALYLTKFASKVTLIHRRDELRAS-KILV----ERLRANPKIEVLWNTEVTEIEGDGrvegV 212

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905331 230 VFRSGE-KELITIKNDFVFAMTGYHPDHQFLEKIGVEIDKE----TGRpffnekTMETNVEGVFIAG 291
Cdd:COG0492   213 TLKNVKtGEEKELEVDGVFVAIGLKPNTELLKGLGLELDEDgyivVDE------DMETSVPGVFAAG 273
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 6-324 3.64e-31

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 121.12  E-value: 3.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   6 AIIIGGGPCGLSAAIHLKQIGIDALVIEKG-----------------NVVNSIYNYP-----THQTFFSSSEklEIgdva 63
Cdd:COG2072     9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKAddvggtwrdnrypglrlDTPSHLYSLPffpnwSDDPDFPTGD--EI---- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  64 fitenrkpvriqaLSYYREVVK----RKNIRVNafemvHKVTK----TENNTFVIETSK-ETYKTPYCIIATGYYDHPNY 134
Cdd:COG2072    83 -------------LAYLEAYADkfglRRPIRFG-----TEVTSarwdEADGRWTVTTDDgETLTARFVVVATGPLSRPKI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 135 MGVPGEDLPK--VFH--YFKEGHPYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRgneySPsikPWILP-------- 202
Cdd:COG2072   145 PDIPGLEDFAgeQLHsaDWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQR----TP---PWVLPrpnydper 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 203 -------------------------------------------------------EFEALVRNGTIRMEFGAcVEKITEN 227
Cdd:COG2072   218 grpanylgleappalnrrdarawlrrllraqvkdpelglltpdyppgckrpllstDYYEALRRGNVELVTGG-IERITED 296

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 228 EVVFRSGEKELI-TIkndfVFAmTGYHPDHQFLEKIGVEIDKETGRPFFNEKTMETNVEGVFIAGVIAAGNNANEIF-IE 305
Cdd:COG2072   297 GVVFADGTEHEVdVI----VWA-TGFRADLPWLAPLDVRGRDGRSGPRAYLGVVVPGFPNLFFLGPNSPSGHSSLTLgAE 371

                         410
                  ....*....|....*....
gi 1196905331 306 NgrfHGGHIAAEIAKRENH 324
Cdd:COG2072   372 R---QARYIARLIAHMRRR 387
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-291 4.37e-28

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: 110.49  E-value: 4.37e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKGNvvnsiyNYPTHQTFFSSseklEIGDVAFITENRKpVRIQALSYYREVVKR 86
Cdd:pfam07992   4 VVIGGGPAGLAAALTLAQLGGKVTLIEDEG------TCPYGGCVLSK----ALLGAAEAPEIAS-LWADLYKRKEEVVKK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  87 KNIRVnafEMVHKVTKTE----NNTFVIETSK----ETYKTPYCIIATGyyDHPNYMGVPGEDLPKVFHYF----KEG-- 152
Cdd:pfam07992  73 LNNGI---EVLLGTEVVSidpgAKKVVLEELVdgdgETITYDRLVIATG--ARPRLPPIPGVELNVGFLVRtldsAEAlr 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 153 HPYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNE----YSPSIKPWILpefEALVRNGtIRMEFGACVEKITENE 228
Cdd:pfam07992 148 LKLLPKRVVVVGGGYIGVELAAALAKLGKEVTLIEALDRllraFDEEISAALE---KALEKNG-VEVRLGTSVKEIIGDG 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1196905331 229 VVFRSGEKELITIKNDFVFAMTGYHPDHQFLEKIGVEIDkETGRPFFNEkTMETNVEGVFIAG 291
Cdd:pfam07992 224 DGVEVILKDGTEIDADLVVVAIGRRPNTELLEAAGLELD-ERGGIVVDE-YLRTSVPGIYAAG 284
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 1-291 1.96e-20

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 91.39  E-value: 1.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   1 MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNV------VNSIynyPThQTFFSSSEKLE-IGDVAFITENRKPVR 73
Cdd:PRK06292    1 MEKYDVIVIGAGPAGYVAARRAAKLGKKVALIEKGPLggtclnVGCI---PS-KALIAAAEAFHeAKHAEEFGIHADGPK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  74 IQalsyYREVVKRKNIRVNAF--EMVHKVTKTENNTF-----------VIETSKETYKTPYCIIATGYyDHPNymgVPGE 140
Cdd:PRK06292   77 ID----FKKVMARVRRERDRFvgGVVEGLEKKPKIDKikgtarfvdpnTVEVNGERIEAKNIVIATGS-RVPP---IPGV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 141 DLPkvfhyfkEGHPYFD-----------KDVVVIGGknsSVdAALEL--VKS--GARVTVLyrgnEYSPSIkpwiLPEFE 205
Cdd:PRK06292  149 WLI-------LGDRLLTsddafeldklpKSLAVIGG---GV-IGLELgqALSrlGVKVTVF----ERGDRI----LPLED 209

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 206 ALVRN-------GTIRMEFGACVEKITEN---EVVFRSGEKELITIKNDFVFAMTGYHP--DHQFLEKIGVEIDkETGRP 273
Cdd:PRK06292  210 PEVSKqaqkilsKEFKIKLGAKVTSVEKSgdeKVEELEKGGKTETIEADYVLVATGRRPntDGLGLENTGIELD-ERGRP 288

                         330
                  ....*....|....*...
gi 1196905331 274 FFNEKTMeTNVEGVFIAG 291
Cdd:PRK06292  289 VVDEHTQ-TSVPGIYAAG 305
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 8-291 1.55e-17

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: 82.49  E-value: 1.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGIDALVIEK----GNVVnsIYNYPTHqtffssseKLEigdvafitenrkpvriqalsyyREV 83
Cdd:COG0493   126 VVGSGPAGLAAAYQLARAGHEVTVFEAldkpGGLL--RYGIPEF--------RLP----------------------KDV 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  84 VKRkniRVNAFEM--VHKVTKTE-NNTFVIETSKETYKtpYCIIATGYYDhPNYMGVPGEDLPKVF-----------HYF 149
Cdd:COG0493   174 LDR---EIELIEAlgVEFRTNVEvGKDITLDELLEEFD--AVFLATGAGK-PRDLGIPGEDLKGVHsamdfltavnlGEA 247

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 150 KEGHPYFDKDVVVIGGKNSSVDAALELVKSGAR-VTVLYR-GNEYSPS--------------IKPWILP-EFEAlVRNG- 211
Cdd:COG0493   248 PDTILAVGKRVVVIGGGNTAMDCARTALRLGAEsVTIVYRrTREEMPAskeeveealeegveFLFLVAPvEIIG-DENGr 326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 212 -----TIRMEFGACVEkitENEVVFRSGEKELITIKNDFVFAMTGYHPDHQFLEK-IGVEIDKeTGRPFFNEKTMETNVE 285
Cdd:COG0493   327 vtgleCVRMELGEPDE---SGRRRPVPIEGSEFTLPADLVILAIGQTPDPSGLEEeLGLELDK-RGTIVVDEETYQTSLP 402


                  ....*.
gi 1196905331 286 GVFIAG 291
Cdd:COG0493   403 GVFAGG 408
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 81-291 4.08e-17

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: 80.63  E-value: 4.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  81 REVVKRKNIRVNafeMVHKVTK--TENNTFVIET-SKETYKtpYCIIATGyyDHPNYMGVPGEDLPKVFH---------- 147
Cdd:COG0446    43 PESFERKGIDVR---TGTEVTAidPEAKTVTLRDgETLSYD--KLVLATG--ARPRPPPIPGLDLPGVFTlrtlddadal 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 148 --YFKEGHPyfdKDVVVIGGKNSSVDAALELVKSGARVTVLYRgneySPSIKPWILPEF-----EALVRNGtIRMEFGAC 220
Cdd:COG0446   116 reALKEFKG---KRAVVIGGGPIGLELAEALRKRGLKVTLVER----APRLLGVLDPEMaalleEELREHG-VELRLGET 187

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196905331 221 VEKITENE---VVFRSGEkeliTIKNDFVFAMTGYHPDHQFLEKIGVEIDKETGRPFfNEkTMETNVEGVFIAG 291
Cdd:COG0446   188 VVAIDGDDkvaVTLTDGE----EIPADLVVVAPGVRPNTELAKDAGLALGERGWIKV-DE-TLQTSDPDVYAAG 255
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-291 7.16e-15

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: 74.74  E-value: 7.16e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKGNV----VNS--IynyPThQTFFSSSEKLEIGDVAfiteNRKPVRIQALSY- 79
Cdd:COG1249     7 VVIGAGPGGYVAAIRAAQLGLKVALVEKGRLggtcLNVgcI---PS-KALLHAAEVAHEARHA----AEFGISAGAPSVd 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  80 YREVVKRKNIRVNAF-EMVHKVTKTENNTFV-----------IE-TSKETYKTPYCIIATGYydHPNYMGVPGEDLPKVF 146
Cdd:COG1249    79 WAALMARKDKVVDRLrGGVEELLKKNGVDVIrgrarfvdphtVEvTGGETLTADHIVIATGS--RPRVPPIPGLDEVRVL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 147 HY-----FKEgHPyfdKDVVVIGGknsSVdAALELV----KSGARVTVLYRGNEyspsikpwILPEF---------EALV 208
Cdd:COG1249   157 TSdealeLEE-LP---KSLVVIGG---GY-IGLEFAqifaRLGSEVTLVERGDR--------LLPGEdpeisealeKALE 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 209 RNGtIRMEFGACVEKITENE----VVFRSGEKElITIKNDFVFAMTGYHP--DHQFLEKIGVEIDkETGRPFFNEkTMET 282
Cdd:COG1249   221 KEG-IDILTGAKVTSVEKTGdgvtVTLEDGGGE-EAVEADKVLVATGRRPntDGLGLEAAGVELD-ERGGIKVDE-YLRT 296


                  ....*....
gi 1196905331 283 NVEGVFIAG 291
Cdd:COG1249   297 SVPGIYAIG 305
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 8-296 7.61e-14

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 71.75  E-value: 7.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGidalviekgnvvnsiynyptHQ-TFFSSSEK----LEIGDVAFitenRKPVRIQAlsyyRE 82
Cdd:PRK11749  145 VIGAGPAGLTAAHRLARKG--------------------YDvTIFEARDKagglLRYGIPEF----RLPKDIVD----RE 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  83 VVKRKNIRVNaFEMVHKVTKTenntFVIETSKETYKTpyCIIATGYYDhPNYMGVPGEDLPKVFH---YFKE---GHPYF 156
Cdd:PRK11749  197 VERLLKLGVE-IRTNTEVGRD----ITLDELRAGYDA--VFIGTGAGL-PRFLGIPGENLGGVYSavdFLTRvnqAVADY 268

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 157 D----KDVVVIGGKNSSVDAALELVKSGAR-VTVLYRGNEY--SPSIKpwilpEFEALVRNGtIRMEFGACVEKITENEV 229
Cdd:PRK11749  269 DlpvgKRVVVIGGGNTAMDAARTAKRLGAEsVTIVYRRGREemPASEE-----EVEHAKEEG-VEFEWLAAPVEILGDEG 342

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 230 VFR--------------SG------EKELITIKNDFVFAMTGYHPDHQFLEKI-GVEIDKEtGRPFFNEKTMETNVEGVF 288
Cdd:PRK11749  343 RVTgvefvrmelgepdaSGrrrvpiEGSEFTLPADLVIKAIGQTPNPLILSTTpGLELNRW-GTIIADDETGRTSLPGVF 421


                  ....*...
gi 1196905331 289 IAGVIAAG 296
Cdd:PRK11749  422 AGGDIVTG 429
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 5-296 4.07e-12

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 66.17  E-value: 4.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEK-----GNVVNSIynyPTH----QTFFSSSEKLEIGDVAFIT-----ENRK 70
Cdd:PRK12770   20 KVAIIGAGPAGLAAAGYLACLGYEVHVYDKlpepgGLMLFGI---PEFripiERVREGVKELEEAGVVFHTrtkvcCGEP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  71 PVRIQALSYYREVVKRKNIrVNAFEMVhkvtktenntfvietsketyktpycIIATGYYdHPNYMGVPGEDLPKV----- 145
Cdd:PRK12770   97 LHEEEGDEFVERIVSLEEL-VKKYDAV-------------------------LIATGTW-KSRKLGIPGEDLPGVysale 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 146 ----FHYFKEGH-------PYFDKDVVVIGGKNSSVDAALELVKSGA-RVTVLY-RGNEYSPSIKpwilPEFEALVRNGT 212
Cdd:PRK12770  150 ylfrIRAAKLGYlpwekvpPVEGKKVVVVGAGLTAVDAALEAVLLGAeKVYLAYrRTINEAPAGK----YEIERLIARGV 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 213 IRMEFGACVEKITENEV---------------------VFRSGEKELITIknDFVFAMTGYHPDHQF-LEKIGVEIDKEt 270
Cdd:PRK12770  226 EFLELVTPVRIIGEGRVegvelakmrlgepdesgrprpVPIPGSEFVLEA--DTVVFAIGEIPTPPFaKECLGIELNRK- 302

                         330       340
                  ....*....|....*....|....*.
gi 1196905331 271 GRPFFNEKTMeTNVEGVFIAGVIAAG 296
Cdd:PRK12770  303 GEIVVDEKHM-TSREGVFAAGDVVTG 327
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-299 5.10e-10

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 60.16  E-value: 5.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDA--LVIEKGNVVNsiYNYP------THQTffsSSEKLEIGDVAFITENRkpVRIqals 78
Cdd:COG1251     5 VIIGAGMAGVRAAEELRKLDPDGeiTVIGAEPHPP--YNRPplskvlAGET---DEEDLLLRPADFYEENG--IDL---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  79 yyrevvkRKNIRVNAFEMVHKVTKTENNtfvietskETYktPY--CIIATGyyDHPNYMGVPGEDLPKVFHY-------- 148
Cdd:COG1251    74 -------RLGTRVTAIDRAARTVTLADG--------ETL--PYdkLVLATG--SRPRVPPIPGADLPGVFTLrtlddada 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 149 ----FKEGhpyfdKDVVVIGGKNSSVDAALELVKSGARVTVLYRGneyspsikPWILP--------EF--EALVRNGtIR 214
Cdd:COG1251   135 lraaLAPG-----KRVVVIGGGLIGLEAAAALRKRGLEVTVVERA--------PRLLPrqldeeagALlqRLLEALG-VE 200

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 215 MEFGACVEKITENE----VVFRSGEkeliTIKNDFVFAMTGYHPDHQFLEKIGVEIDK-----EtgrpffnekTMETNVE 285
Cdd:COG1251   201 VRLGTGVTEIEGDDrvtgVRLADGE----ELPADLVVVAIGVRPNTELARAAGLAVDRgivvdD---------YLRTSDP 267

                         330
                  ....*....|....
gi 1196905331 286 GVFIAGVIAAGNNA 299
Cdd:COG1251   268 DIYAAGDCAEHPGP 281
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
7-295 1.22e-09

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


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 58.61  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQI---GIDALVIEKGNVvnsiYNYPT--HQTFFSSsekLEIGDVAFitenrkPvriqalsyYR 81
Cdd:COG1252     5 VIVGGGFAGLEAARRLRKKlggDAEVTLIDPNPY----HLFQPllPEVAAGT---LSPDDIAI------P--------LR 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  82 EVVKRKNIRVnafemVH-KVTK--TENNTfVIETSKETYKTPYCIIATGYydHPNYMGVPG-----------EDL----P 143
Cdd:COG1252    64 ELLRRAGVRF-----IQgEVTGidPEART-VTLADGRTLSYDYLVIATGS--VTNFFGIPGlaehalplktlEDAlalrE 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 144 KVFHYFKEGHPYFDKDVVVIGGKNSSVDAALELV-------------KSGARVTVLYRGneyspsikPWILPEF------ 204
Cdd:COG1252   136 RLLAAFERAERRRLLTIVVVGGGPTGVELAGELAellrkllrypgidPDKVRITLVEAG--------PRILPGLgeklse 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 205 ---EALVRNGtIRMEFGACVEKITENEVVFRSGEkeliTIKNDFVFAMTGYHPdHQFLEKIGVEIDkETGRPFFNEkTME 281
Cdd:COG1252   208 aaeKELEKRG-VEVHTGTRVTEVDADGVTLEDGE----EIPADTVIWAAGVKA-PPLLADLGLPTD-RRGRVLVDP-TLQ 279

                         330
                  ....*....|....*
gi 1196905331 282 T-NVEGVFIAGVIAA 295
Cdd:COG1252   280 VpGHPNVFAIGDCAA 294
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 135-291 1.58e-09

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 58.97  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 135 MGVPGEDLPKV------FHYFKEG---HPyfDKDVVVIGGKNSSVDAALELVKSGAR-VTVLY-RGNEYSP--------- 194
Cdd:PRK12814  294 MGIPGEELPGVisgidfLRNVALGtalHP--GKKVVVIGGGNTAIDAARTALRLGAEsVTILYrRTREEMPanraeieea 371

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 195 -----SIKPWILPEFEALVRNGT----IRMEFGACVEKITENEVVFRSGEkelITIKNDFVFAMTGYHPDHQFLEKIGVE 265
Cdd:PRK12814  372 laegvSLRELAAPVSIERSEGGLeltaIKMQQGEPDESGRRRPVPVEGSE---FTLQADTVISAIGQQVDPPIAEAAGIG 448

                         170       180
                  ....*....|....*....|....*.
gi 1196905331 266 IDKEtGRPFFNEKTMETNVEGVFIAG 291
Cdd:PRK12814  449 TSRN-GTVKVDPETLQTSVAGVFAGG 473
PRK15317 PRK15317
alkyl hydroperoxide reductase subunit F; Provisional
 7-300 2.12e-09

alkyl hydroperoxide reductase subunit F; Provisional


Pssm-ID: 237942 [Multi-domain]  Cd Length: 517  Bit Score: 58.25  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGID-ALVIEK-GNVVN---SIYNypthqtFFSSSEkleigdvafiTENRKPVriQALsyyR 81
Cdd:PRK15317  215 LVVGGGPAGAAAAIYAARKGIRtGIVAERfGGQVLdtmGIEN------FISVPE----------TEGPKLA--AAL---E 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  82 EVVKRKNIRVNAFEMVHKVTKTENNTFVIETSKETYKTPYCIIATGyyDHPNYMGVPGEDlpkvfHYFKEG-----H--- 153
Cdd:PRK15317  274 EHVKEYDVDIMNLQRASKLEPAAGLIEVELANGAVLKAKTVILATG--ARWRNMNVPGED-----EYRNKGvaycpHcdg 346

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 154 PYF-DKDVVVIGGKNSSVDAALELVKSGARVTVLyrgnEYSPSIKPwilpeFEALVR------NGTIRM-----EFGACV 221
Cdd:PRK15317  347 PLFkGKRVAVIGGGNSGVEAAIDLAGIVKHVTVL----EFAPELKA-----DQVLQDklrslpNVTIITnaqttEVTGDG 417

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 222 EKITENEVVFRSGEkELITIKNDFVFAMTGYHPDHQFLE------KIG-VEIDkETGrpffnektmETNVEGVFIAG--- 291
Cdd:PRK15317  418 DKVTGLTYKDRTTG-EEHHLELEGVFVQIGLVPNTEWLKgtvelnRRGeIIVD-ARG---------ATSVPGVFAAGdct 486

                         330
                  ....*....|....*.
gi 1196905331 292 -------VIAAGNNAN 300
Cdd:PRK15317  487 tvpykqiIIAMGEGAK 502
TIGR00275 TIGR00275
flavoprotein, HI0933 family; The model when searched with a partial length search brings in ...
 7-127 1.61e-08

flavoprotein, HI0933 family; The model when searched with a partial length search brings in proteins with a dinucleotide-binding motif (Rossman fold) over the initial 40 residues of the model, including oxidoreductases and dehydrogenases. Partially characterized members include an FAD-binding protein from Bacillus cereus and flavoprotein HI0933 from Haemophilus influenzae. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 272992 [Multi-domain]  Cd Length: 400  Bit Score: 55.29  E-value: 1.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKG---------------NVVNS------IYNYPTHQTFFSSS----------- 54
Cdd:TIGR00275   1 IIIGGGAAGLMAAITAARAGLSVLLLEKNkkigkkllisgggrcNLTNScptpefVAYYPRNGKFLRSAlsrfsnkdlid 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  55 --EKLEI-------GDVAFITENRKPVrIQALsyyREVVKRKNIRVNAFEMVHKVTKTENNtFVIETSKETYKTPYCIIA 125
Cdd:TIGR00275  81 ffESLGLelkveedGRVFPCSDSAADV-LDAL---LNELKELGVEILTNSKVKSIEKEDGG-FGVETSGGEYEADKVIIA 155


                  ..
gi 1196905331 126 TG 127
Cdd:TIGR00275 156 TG 157
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 7-296 5.50e-08

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 54.00  E-value: 5.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKGNV----VN-------------SIYNYPTHqtffssSEKLEIgDVAFITENR 69
Cdd:PRK06416    8 IVIGAGPGGYVAAIRAAQLGLKVAIVEKEKLggtcLNrgcipskallhaaERADEARH------SEDFGI-KAENVGIDF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  70 KPVRiqalSYYREVVKRKN------IRVNAFEMVHKVTK-TENNTFVIETSK--ETYKTPYCIIATGYYdhpnymgvpge 140
Cdd:PRK06416   81 KKVQ----EWKNGVVNRLTggveglLKKNKVDIIRGEAKlVDPNTVRVMTEDgeQTYTAKNIILATGSR----------- 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 141 dlPKVFHYFKEGH------------PYFDKDVVVIGG-----KNSSVDAALelvksGARVTVLyrgnEYSPSikpwILPE 203
Cdd:PRK06416  146 --PRELPGIEIDGrviwtsdealnlDEVPKSLVVIGGgyigvEFASAYASL-----GAEVTIV----EALPR----ILPG 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 204 FE---------ALVRNGtIRMEFGACVEKITENE----VVFRSGEKELiTIKNDFVFAMTGYHP--DHQFLEKIGVEIDk 268
Cdd:PRK06416  211 EDkeisklaerALKKRG-IKIKTGAKAKKVEQTDdgvtVTLEDGGKEE-TLEADYVLVAVGRRPntENLGLEELGVKTD- 287

                         330       340       350
                  ....*....|....*....|....*....|
gi 1196905331 269 etgRPFF--NEKtMETNVEGVFIAGVIAAG 296
Cdd:PRK06416  288 ---RGFIevDEQ-LRTNVPNIYAIGDIVGG 313
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 123-291 2.50e-07

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 51.70  E-value: 2.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 123 IIATGYYDhPNYMGVPGEDLPKVfHY------------FKEGHPYF----DKDVVVIGGKNSSVDAALELVKSGAR-VTV 185
Cdd:PRK12810  233 FLGTGAYK-PRDLGIPGRDLDGV-HFamdfliqntrrvLGDETEPFisakGKHVVVIGGGDTGMDCVGTAIRQGAKsVTQ 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 186 LYRGNEySPS--IKPWILPEFEALVR------NGTIRM----------EFGAcVEKITENEVVFRSGEKELI-----TIK 242
Cdd:PRK12810  311 RDIMPM-PPSrrNKNNPWPYWPMKLEvsnaheEGVEREfnvqtkefegENGK-VTGVKVVRTELGEGDFEPVegsefVLP 388

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1196905331 243 NDFVF-AMTGYHPDHQFLEKIGVEIDkETGRPFFNEKTMETNVEGVFIAG 291
Cdd:PRK12810  389 ADLVLlAMGFTGPEAGLLAQFGVELD-ERGRVAAPDNAYQTSNPKVFAAG 437
HI0933_like pfam03486
HI0933-like protein;
5-127 2.63e-07

HI0933-like protein;


Pssm-ID: 427330 [Multi-domain]  Cd Length: 406  Bit Score: 51.81  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKG---------------NVVNS-------IYNYPTHQTFFSSS-------- 54
Cdd:pfam03486   2 DVIVIGGGAAGLMAAISAAKRGRRVLLIEKGkklgrkilisgggrcNVTNLseepdnfLSRYPGNPKFLKSAlsrftpwd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  55 -----EKLEIgdvAFITENRK---PVRIQAlsyyREVV-------KRKNIRVNAFEMVHKVTKTENNTFVIETSKETYKT 119
Cdd:pfam03486  82 fiaffESLGV---PLKEEDHGrlfPDSDKA----SDIVdallnelKELGVKIRLRTRVLSVEKDDDGRFRVKTGGEELEA 154


                  ....*...
gi 1196905331 120 PYCIIATG 127
Cdd:pfam03486 155 DSLVLATG 162
PRK12831 PRK12831
putative oxidoreductase; Provisional
 4-296 7.60e-07

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 50.40  E-value: 7.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   4 EKAIIIGGGPCGLSAAIHLKQIGIDALVIEK----GNVVnsIYNYPthqtffsssekleigdvafitENRKPvriqalsy 79
Cdd:PRK12831  141 KKVAVIGSGPAGLTCAGDLAKMGYDVTIFEAlhepGGVL--VYGIP---------------------EFRLP-------- 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  80 yREVVKRKNIrvnafEMVHKV-TKTENNTFVIET-------SKETYKTPYciIATGYyDHPNYMGVPGEDLPKVF----- 146
Cdd:PRK12831  190 -KETVVKKEI-----ENIKKLgVKIETNVVVGKTvtidellEEEGFDAVF--IGSGA-GLPKFMGIPGENLNGVFsanef 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 147 ----HYFKEGHPYFD------KDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEyspSIKPWILPEFEALVRNGTIRME 216
Cdd:PRK12831  261 ltrvNLMKAYKPEYDtpikvgKKVAVVGGGNVAMDAARTALRLGAEVHIVYRRSE---EELPARVEEVHHAKEEGVIFDL 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 217 FGACVEKIT-ENEVVF-------------RSGEKELITIKN-------DFVFAMTGYHPDHQFLEKI-GVEIDKEtGRPF 274
Cdd:PRK12831  338 LTNPVEILGdENGWVKgmkcikmelgepdASGRRRPVEIEGsefvlevDTVIMSLGTSPNPLISSTTkGLKINKR-GCIV 416

                         330       340
                  ....*....|....*....|..
gi 1196905331 275 FNEKTMETNVEGVFIAGVIAAG 296
Cdd:PRK12831  417 ADEETGLTSKEGVFAGGDAVTG 438
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 5-38 1.60e-06

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 49.45  E-value: 1.60e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVV 38
Cdd:COG1232     3 RVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRV 36
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-34 2.75e-06

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: 48.40  E-value: 2.75e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1196905331   1 MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEK 34
Cdd:COG0654     1 MMRTDVLIVGGGPAGLALALALARAGIRVTVVER 34
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 5-294 6.74e-06

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 47.47  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIekgnvvnsIYNYPTHQTFFSSSEKLEIGDvafITENRKpvriQALSYYREVV 84
Cdd:PRK13512    3 KIIVVGAVAGGATCASQIRRLDKESDII--------IFEKDRDMSFANCALPYYIGE---VVEDRK----YALAYTPEKF 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  85 K-RKNIRVNAFemvHKVTK--TENNTFVI------ETSKETYKtpYCIIATGY------YDHPNYMGVPG-EDLPKVFHY 148
Cdd:PRK13512   68 YdRKQITVKTY---HEVIAinDERQTVTVlnrktnEQFEESYD--KLILSPGAsanslgFESDITFTLRNlEDTDAIDQF 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 149 FKEGHPyfdKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYSPSIKPWI-LPEFEALVRNGtIRMEFGACVEKITEN 227
Cdd:PRK13512  143 IKANQV---DKALVVGAGYISLEVLENLYERGLHPTLIHRSDKINKLMDADMnQPILDELDKRE-IPYRLNEEIDAINGN 218

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1196905331 228 EVVFRSGEKElitiKNDFVFAMTGYHPDHQFLEKIGVEIDKETGRPfFNEKtMETNVEGVFIAGVIA 294
Cdd:PRK13512  219 EVTFKSGKVE----HYDMIIEGVGTHPNSKFIESSNIKLDDKGFIP-VNDK-FETNVPNIYAIGDII 279
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 5-191 7.45e-06

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 47.43  E-value: 7.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKgnvvnsiynypTHqtffssseklEIGDVAF--ITENRKPVRIqalsYYRE 82
Cdd:PRK12778  433 KVAVIGSGPAGLSFAGDLAKRGYDVTVFEA-----------LH----------EIGGVLKygIPEFRLPKKI----VDVE 487

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  83 VVKRKNIRVNaFEMVHKVTKTENntfVIETSKETYKTpyCIIATGYyDHPNYMGVPGEDLPKVF---------HYFKEGH 153
Cdd:PRK12778  488 IENLKKLGVK-FETDVIVGKTIT---IEELEEEGFKG--IFIASGA-GLPNFMNIPGENSNGVMssneyltrvNLMDAAS 560

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1196905331 154 PYFD------KDVVVIGGKNSSVDAALELVKSGA-RVTVLYRGNE 191
Cdd:PRK12778  561 PDSDtpikfgKKVAVVGGGNTAMDSARTAKRLGAeRVTIVYRRSE 605
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
8-55 1.37e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 42.13  E-value: 1.37e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGIDALVIEKGNVV----------NSIYNYPTHqTFFSSSE 55
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLggnaysyrvpGYVFDYGAH-IFHGSDE 57
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 5-191 2.18e-05

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 46.09  E-value: 2.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331    5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPthqtffsssekleigdvafITENRKPVRIqalsYYREVV 84
Cdd:PRK12775   432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQYG-------------------IPSFRLPRDI----IDREVQ 488

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   85 KRKNIRVNaFEmvhkVTKTENNTFVIET--SKETYKTPYCIIATGyydHPNYMGVPGEDLPKVFHYFK----------EG 152
Cdd:PRK12775   489 RLVDIGVK-IE----TNKVIGKTFTVPQlmNDKGFDAVFLGVGAG---APTFLGIPGEFAGQVYSANEfltrvnlmggDK 560

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1196905331  153 HPYFD------KDVVVIGGKNSSVDaALELVK--SGARVTVLYRGNE 191
Cdd:PRK12775   561 FPFLDtpislgKSVVVIGAGNTAMD-CLRVAKrlGAPTVRCVYRRSE 606
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 8-291 2.65e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 45.64  E-value: 2.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNY--PTHQTffsSSEKL--EIGdvafitenrkpvRIQALSyyreV 83
Cdd:PRK12771  142 VIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGGMMRYgiPAYRL---PREVLdaEIQ------------RILDLG----V 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  84 VKRKNIRVNAFEMVHKVTKTENNTFVietsketyktpyciiATGyyDH-PNYMGVPGEDLPKVF------HYFKEGH-PY 155
Cdd:PRK12771  203 EVRLGVRVGEDITLEQLEGEFDAVFV---------------AIG--AQlGKRLPIPGEDAAGVLdavdflRAVGEGEpPF 265

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 156 FDKDVVVIGGKNSSVDAALELVKSGA-RVTVLYRgneySPSIKPWILP-EFEALVRNGT--------------------- 212
Cdd:PRK12771  266 LGKRVVVIGGGNTAMDAARTARRLGAeEVTIVYR----RTREDMPAHDeEIEEALREGVeinwlrtpveiegdengatgl 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 213 --IRMEFGACVEKITENEVvfrsgEKELITIKNDFVFAMTGYHPDHQFLEKI-GVeidkETGRPFF--NEKTMETNVEGV 287
Cdd:PRK12771  342 rvITVEKMELDEDGRPSPV-----TGEEETLEADLVVLAIGQDIDSAGLESVpGV----EVGRGVVqvDPNFMMTGRPGV 412


                  ....
gi 1196905331 288 FIAG 291
Cdd:PRK12771  413 FAGG 416
PRK07208 PRK07208
hypothetical protein; Provisional
 5-81 7.02e-05

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 44.11  E-value: 7.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNYPTHQ---------TFFSSSEKL-----EI--GDVaFITEN 68
Cdd:PRK07208    6 SVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGGISRTVTYKgnrfdigghRFFSKSPEVmdlwnEIlpDDD-FLLRP 84

                          90
                  ....*....|...
gi 1196905331  69 RKPvRIqalsYYR 81
Cdd:PRK07208   85 RLS-RI----YYR 92
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 1-38 7.17e-05

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 44.07  E-value: 7.17e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1196905331   1 MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVV 38
Cdd:COG1233     1 MMMYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTP 38
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
1-38 1.09e-04

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 43.56  E-value: 1.09e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1196905331   1 MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVV 38
Cdd:COG2509    28 SLKYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKDV 65
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
5-37 2.81e-04

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 42.20  E-value: 2.81e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNV 37
Cdd:COG0665     4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERGRP 36
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 6-53 2.86e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 42.27  E-value: 2.86e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1196905331   6 AIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSiynypthQTFFSS 53
Cdd:pfam00890   2 VLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPFGG-------ATAWSS 42
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 8-275 3.25e-04

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 42.16  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNSIYNY------------PT----HQTFFSS------SEKLEIGDVAFI 65
Cdd:PLN02172   15 VIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYtpksesdplsldPTrsivHSSVYESlrtnlpRECMGYRDFPFV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  66 ----TENRKPVRI----QALSYYREVVKRKNIRvnafEMVH---KVTKTE--NNTFVIETSK-------ETYKTpyCIIA 125
Cdd:PLN02172   95 prfdDESRDSRRYpshrEVLAYLQDFAREFKIE----EMVRfetEVVRVEpvDGKWRVQSKNsggfskdEIFDA--VVVC 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 126 TGYYDHPNYMGVPG-EDLPKV---FHYFKEGHPYFDKDVVVIGGKNSSVDAALELVKSGARVTVLYRGNEYS-------P 194
Cdd:PLN02172  169 NGHYTEPNVAHIPGiKSWPGKqihSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRASESDtyeklpvP 248

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 195 SIKPWILPEFEALVRNGTIrmefgacvekitenevVFRSGEkeliTIKNDFVFAMTGYHPDHQFLEKIG-VEIDKETGRP 273
Cdd:PLN02172  249 QNNLWMHSEIDTAHEDGSI----------------VFKNGK----VVYADTIVHCTGYKYHFPFLETNGyMRIDENRVEP 308


                  ..
gi 1196905331 274 FF 275
Cdd:PLN02172  309 LY 310
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 7-34 3.70e-04

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 41.93  E-value: 3.70e-04
                          10        20
                  ....*....|....*....|....*...
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEK 34
Cdd:pfam01494   5 LIVGGGPAGLMLALLLARAGVRVVLVER 32
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 132-188 4.10e-04

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 42.13  E-value: 4.10e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196905331 132 PNYMGVPGEDLPKVF---------HYFKEGHPYFD--------KDVVVIGGKNSSVDAALELVKSGARVTVLYR 188
Cdd:PRK12779  405 PTFMNVPGEHLLGVMsanefltrvNLMRGLDDDYEtplpevkgKEVFVIGGGNTAMDAARTAKRLGGNVTIVYR 478
PRK13748 PRK13748
putative mercuric reductase; Provisional
 161-291 4.63e-04

putative mercuric reductase; Provisional


Pssm-ID: 184298 [Multi-domain]  Cd Length: 561  Bit Score: 41.68  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 161 VVIGgknSSVdAALELVKS----GARVTVLYRGNEYS---PSIKpwilpefEALvrNGTIRMEFGACVEKITENEVVFRS 233
Cdd:PRK13748  274 AVIG---SSV-VALELAQAfarlGSKVTILARSTLFFredPAIG-------EAV--TAAFRAEGIEVLEHTQASQVAHVD 340

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1196905331 234 GEKELIT----IKNDFVFAMTGYHPDHQF--LEKIGVEIDKEtGRPFFNeKTMETNVEGVFIAG 291
Cdd:PRK13748  341 GEFVLTTghgeLRADKLLVATGRAPNTRSlaLDAAGVTVNAQ-GAIVID-QGMRTSVPHIYAAG 402
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 160-234 5.03e-04

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: 38.34  E-value: 5.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 160 VVVIGGKNSSVDAALELVKSGARVTVLyrgnEYSPSIKPWILPEFEALVR-----NGtIRMEFGACVEKITENE----VV 230
Cdd:pfam00070   2 VVVVGGGYIGLELAGALARLGSKVTVV----ERRDRLLPGFDPEIAKILQeklekNG-IEFLLNTTVEAIEGNGdgvvVV 76


                  ....
gi 1196905331 231 FRSG 234
Cdd:pfam00070  77 LTDG 80
PRK06126 PRK06126
hypothetical protein; Provisional
 1-35 5.11e-04

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 41.52  E-value: 5.11e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1196905331   1 MIQEKAIIIGGGPCGLSAAIHLKQIGIDALVIEKG 35
Cdd:PRK06126    5 TSETPVLIVGGGPVGLALALDLGRRGVDSILVERK 39
PTZ00052 PTZ00052
thioredoxin reductase; Provisional
 7-296 5.36e-04

thioredoxin reductase; Provisional


Pssm-ID: 185416 [Multi-domain]  Cd Length: 499  Bit Score: 41.35  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIE-------------KGNVVN----------------SIYNYPTHQTFFSSSEKL 57
Cdd:PTZ00052    9 VVIGGGSGGMAAAKEAAAHGKKVALFDyvkpstqgtkwglGGTCVNvgcvpkklmhyaanigSIFHHDSQMYGWKTSSSF 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331  58 EIGDVafITENRKPVRIQALSYyrevvkRKNIRVNAFEMVHKVTKTENNTFVI---ETSKETYKTPYCIIATGYYDHpny 134
Cdd:PTZ00052   89 NWGKL--VTTVQNHIRSLNFSY------RTGLRSSKVEYINGLAKLKDEHTVSygdNSQEETITAKYILIATGGRPS--- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 135 mgVPgEDLPKVFHYFKEGHPYF--DKD---VVVIGGKNSSVDAALELVKSGARVTV-----LYRGNEYSPSIKPWI-LPE 203
Cdd:PTZ00052  158 --IP-EDVPGAKEYSITSDDIFslSKDpgkTLIVGASYIGLETAGFLNELGFDVTVavrsiPLRGFDRQCSEKVVEyMKE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331 204 FEALVRNGTIRMEfgacVEKITEN-EVVFRSGEKELItiknDFVFAMTGYHPDHQF--LEKIGVEIDKETGRPFFNEKtm 280
Cdd:PTZ00052  235 QGTLFLEGVVPIN----IEKMDDKiKVLFSDGTTELF----DTVLYATGRKPDIKGlnLNAIGVHVNKSNKIIAPNDC-- 304

                         330
                  ....*....|....*.
gi 1196905331 281 eTNVEGVFIAGVIAAG 296
Cdd:PTZ00052  305 -TNIPNIFAVGDVVEG 319
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 7-42 7.83e-04

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


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 40.97  E-value: 7.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKGNVV--NSIY 42
Cdd:COG1053     7 VVVGSGGAGLRAALEAAEAGLKVLVLEKVPPRggHTAA 44
PRK06753 PRK06753
hypothetical protein; Provisional
 5-129 7.85e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 40.83  E-value: 7.85e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEK--------------GNVVNSIYNYPTHQ----------TFFSSSEKLEIG 60
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFEKnesvkevgagigigDNVIKKLGNHDLAKgiknagqilsTMNLLDDKGTLL 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1196905331  61 DVAFITENRKPVRIQ-------ALSYYREvvkrknirvNAFEMVHKVTKTENN---TFVIETSKETYKTPYCIIATGYY 129
Cdd:PRK06753   82 NKVKLKSNTLNVTLHrqtlidiIKSYVKE---------DAIFTGKEVTKIENEtdkVTIHFADGESEAFDLCIGADGIH 151
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
11-35 1.05e-03

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 39.95  E-value: 1.05e-03
                          10        20
                  ....*....|....*....|....*
gi 1196905331  11 GGPCGLSAAIHLKQIGIDALVIEKG 35
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKG 25
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
8-45 1.12e-03

bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 40.66  E-value: 1.12e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGIDALVIEKgnvVNSIYNYP 45
Cdd:PRK06183   15 IVGAGPVGLTLANLLGQYGVRVLVLER---WPTLYDLP 49
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 5-40 1.17e-03

FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: Glycerol-3-phosphate dehydrogenase EC:1.1.99.5, Sarcosine oxidase beta subunit EC:1.5.3.1, D-alanine oxidase EC:1.4.99.1, D-aspartate oxidase EC:1.4.3.1.


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 40.07  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEKGNVVNS 40
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 7-36 1.97e-03

geranylgeranyl reductase family; This model represents a subfamily which includes geranylgeranyl reductases involved in chlorophyll and bacteriochlorophyll biosynthesis as well as other related enzymes which may also act on geranylgeranyl groups or related substrates. [Biosynthesis of cofactors, prosthetic groups, and carriers, Chlorophyll and bacteriochlorphyll]


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 39.22  E-value: 1.97e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKGN 36
Cdd:TIGR02032   4 VVVGAGPAGASAAYRLADKGLRVLLLEKKS 33
PRK06847 PRK06847
hypothetical protein; Provisional
 4-34 1.99e-03

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 39.47  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1196905331   4 EKAIIIGGGPCGLSAAIHLKQIGIDALVIEK 34
Cdd:PRK06847    5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEI 35
PRK07538 PRK07538
hypothetical protein; Provisional
 5-33 2.57e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 39.11  E-value: 2.57e-03
                          10        20
                  ....*....|....*....|....*....
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIE 33
Cdd:PRK07538    2 KVLIAGGGIGGLTLALTLHQRGIEVVVFE 30
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
7-33 4.04e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 38.75  E-value: 4.04e-03
                          10        20
                  ....*....|....*....|....*..
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIE 33
Cdd:COG1231    11 VIVGAGLAGLAAARELRKAGLDVTVLE 37
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 5-34 4.41e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 38.70  E-value: 4.41e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1196905331   5 KAIIIGGGPCGLSAAIHLKQIGIDALVIEK 34
Cdd:PRK08132   25 PVVVVGAGPVGLALAIDLAQQGVPVVLLDD 54
PLN02976 PLN02976
amine oxidase
 5-33 5.22e-03

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 38.70  E-value: 5.22e-03
                           10        20
                   ....*....|....*....|....*....
gi 1196905331    5 KAIIIGGGPCGLSAAIHLKQIGIDALVIE 33
Cdd:PLN02976   695 KIIVVGAGPAGLTAARHLQRQGFSVTVLE 723
PRK07233 PRK07233
hypothetical protein; Provisional
 8-38 7.63e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 37.94  E-value: 7.63e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1196905331   8 IIGGGPCGLSAAIHLKQIGIDALVIEKGNVV 38
Cdd:PRK07233    4 IVGGGIAGLAAAYRLAKRGHEVTVFEADDQL 34
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 157-214 8.05e-03

Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and metabolism]; Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 37.05  E-value: 8.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1196905331 157 DKDVVVIGGKNssvdAALE----LVKSGARVTVlyrgneYSPSIKpwilPEFEALVRNGTIR 214
Cdd:COG1648    12 GRRVLVVGGGE----VAARkarlLLKAGARVTV------VAPEFS----PELAALAEEGRIE 59
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 7-35 9.29e-03

Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a family of FAD-dependent hydroxylases (monooxygenases) which are all believed to act in the aerobic ubiquinone biosynthesis pathway. A separate set of hydroxylases, as yet undiscovered, are believed to be active under anaerobic conditions. In E. coli three enzyme activities have been described, UbiB (which acts first at position 6, see TIGR01982), UbiH (which acts at position 4) and UbiF (which acts at position 5). UbiH and UbiF are similar to one another and form the basis of this subfamily. Interestingly, E. coli contains another hydroxylase gene, called visC, that is highly similar to UbiF, adjacent to UbiH and, when mutated, results in a phenotype similar to that of UbiH (which has also been named visB). Several other species appear to have three homologs in this family, although they assort themselves differently on phylogenetic trees (e.g. Xylella and Mesorhizobium) making it difficult to ascribe a specific activity to each one. Eukaryotes appear to have only a single homolog in this subfamily (COQ6) which complements UbiH, but also possess a non-orthologous gene, COQ7 which complements UbiF. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 37.57  E-value: 9.29e-03
                          10        20
                  ....*....|....*....|....*....
gi 1196905331   7 IIIGGGPCGLSAAIHLKQIGIDALVIEKG 35
Cdd:TIGR01988   3 VIVGGGMVGLALALALARSGLKVALIEAT 31
 
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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