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Conserved domains on  [gi|502942449|ref|WP_013177425|]
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NAD-dependent dihydropyrimidine dehydrogenase subunit PreA [Truepera radiovictrix]

Protein Classification

dihydropyrimidine dehydrogenase subunit B( domain architecture ID 11483255)

dihydropyrimidine dehydrogenase subunit B catalyzes the first step in pyrimidine degradation by conversion to their corresponding 5,6-dihydropyrimidines

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
1-433 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


:

Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 717.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   1 MADLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGTPVLNVS-SRYGGWEYGGNKLAAINNIELISD 79
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLGPPIVNVSsPRFGALVKEDRRFIGFNNIELITD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGMGSAVGQVPEYCSMIT 159
Cdd:PRK08318  81 RPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVEMYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 160 EWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSVIGVDLDAFTLKPNVGGKGGHGGYAGPAVKPIALS 239
Cdd:PRK08318 161 RWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPIALN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 240 MLSEVMQLPETRdfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASVRDVIGA 319
Cdd:PRK08318 241 MVAEIARDPETR--GLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 320 AAPRYSPFNQLDLSYKVVARIDPAKCIHCNLCFVACDEGAHQCIDLTVDGVKidpatyagpaktQPVVREDDCVGCNLCS 399
Cdd:PRK08318 319 AVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEDGTR------------TPEVIEEECVGCNLCA 386

                        410       420       430
                 ....*....|....*....|....*....|....
gi 502942449 400 LVCPVDGCITMLEVDSGRESVTWAEITERYPEVT 433
Cdd:PRK08318 387 HVCPVEGCITMGEVKFGKPYANWTTHPNNPARAA 420
 
Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
1-433 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 717.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   1 MADLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGTPVLNVS-SRYGGWEYGGNKLAAINNIELISD 79
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLGPPIVNVSsPRFGALVKEDRRFIGFNNIELITD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGMGSAVGQVPEYCSMIT 159
Cdd:PRK08318  81 RPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVEMYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 160 EWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSVIGVDLDAFTLKPNVGGKGGHGGYAGPAVKPIALS 239
Cdd:PRK08318 161 RWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPIALN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 240 MLSEVMQLPETRdfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASVRDVIGA 319
Cdd:PRK08318 241 MVAEIARDPETR--GLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 320 AAPRYSPFNQLDLSYKVVARIDPAKCIHCNLCFVACDEGAHQCIDLTVDGVKidpatyagpaktQPVVREDDCVGCNLCS 399
Cdd:PRK08318 319 AVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEDGTR------------TPEVIEEECVGCNLCA 386

                        410       420       430
                 ....*....|....*....|....*....|....
gi 502942449 400 LVCPVDGCITMLEVDSGRESVTWAEITERYPEVT 433
Cdd:PRK08318 387 HVCPVEGCITMGEVKFGKPYANWTTHPNNPARAA 420
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 3-301 3.75e-147

Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239244  Cd Length: 299  Bit Score: 421.31  E-value: 3.75e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIG---TPVLNVSSRYGGWEYGGNKLAAINNIELISD 79
Cdd:cd02940    1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGldkDIVTNVSPRIARLRTSGRGQIGFNNIELISE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGMGSAVGQVPEYCSMIT 159
Cdd:cd02940   81 KPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELVEEIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 160 EWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSVIGVDLDAFTLKPNVGGKGGHGGYAGPAVKPIALS 239
Cdd:cd02940  161 RWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVKPIALR 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502942449 240 MLSEVMQLPETrdfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGL 301
Cdd:cd02940  241 AVSQIARAPEP---GLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-313 2.49e-95

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 288.90  E-value: 2.49e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIG-TPVL-NVSSRYggWEYGGNklAAINNIELISDR 80
Cdd:COG0167    1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTpEPQPgNPRPRL--FRLPED--SGLINRMGLNNP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  81 PLEVNLREIAEVKRLfpDRAVIVSAMFeSDPQVWADAVRRIEDTGADAIELNYGCPHGmseRGMGSAVGQVPEYCSMITE 160
Cdd:COG0167   77 GVDAFLERLLPAKRY--DVPVIVNIGG-NTVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEALAELLA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 161 WVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSvIGVDLDafTLKPNVGGKGghggyagPAVKPIALSM 240
Cdd:COG0167  151 AVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLG-RAIDLE--TRRPVLANEAggl--sgPALKPIALRM 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502942449 241 LSEVMQLPETRdfrIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASV 313
Cdd:COG0167  226 VREVAQAVGGD---IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 4-320 8.59e-51

dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.


Pssm-ID: 130109 [Multi-domain]  Cd Length: 300  Bit Score: 174.15  E-value: 8.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449    4 LSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGtpvlnVSSRYGG-------WEYGgnklaAINNIEL 76
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIG-----LEPRPGYrnptiveTPCG-----MLNAIGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   77 iSDRPLEVNLREIAEVKRLFPdRAVIVSaMFESDPQVWADAVRRIEDTG--ADAIELNYGCPHGMserGMGSAVGQVPEY 154
Cdd:TIGR01037  71 -QNPGVEAFLEELKPVREEFP-TPLIAS-VYGSSVEEFAEVAEKLEKAPpyVDAYELNLSCPHVK---GGGIAIGQDPEL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  155 CSMITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTinsVIGVDLDAFTLKPNVggKGGHGGYAGPAVK 234
Cdd:TIGR01037 145 SADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDIKTGKPIL--ANKTGGLSGPAIK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  235 PIALSMLSEVmqlpeTRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFrIIEELTDGLSNWLDDKGAASVR 314
Cdd:TIGR01037 220 PIALRMVYDV-----YKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIE 293


                  ....*.
gi 502942449  315 DVIGAA 320
Cdd:TIGR01037 294 ELIGIA 299
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
4-301 3.28e-27

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 110.13  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449    4 LSTDFCGVKSPNPFWLASAPPTNTAyQVCKAFDYGWGGAVwkTIGTPVLNvsSRYGGWE--YGGNKLAAINNIELiSDRP 81
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASGFDKFGE-EALKWLALGKFGAI--EIKSVTPY--PQPGNPTprVFRLPEGVLNRMGL-NNPG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   82 LEVNLREIAEVKRLFPDRAVIVSA----MFESDpqvWADAVRRIEDTgADAIELNYGCPH--GmsergmGSAVGQVPEYC 155
Cdd:pfam01180  76 LDAVLAELLKRRKEYPRPDLGINLskagMTVDD---YVEVARKIGPF-ADYIELNVSCPNtpG------LRALQTDPELA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  156 SMITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINS-VIGVDLDAFTLKPnvGGKGGHGGYAGPAVK 234
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTtVRGMRIDLKTEKP--ILANGTGGLSGPPIK 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502942449  235 PIALSMLSEVMQLpetRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGL 301
Cdd:pfam01180 224 PIALKVIRELYQR---TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
 
Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
1-433 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 717.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   1 MADLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGTPVLNVS-SRYGGWEYGGNKLAAINNIELISD 79
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLGPPIVNVSsPRFGALVKEDRRFIGFNNIELITD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGMGSAVGQVPEYCSMIT 159
Cdd:PRK08318  81 RPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVEMYT 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 160 EWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSVIGVDLDAFTLKPNVGGKGGHGGYAGPAVKPIALS 239
Cdd:PRK08318 161 RWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPIALN 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 240 MLSEVMQLPETRdfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASVRDVIGA 319
Cdd:PRK08318 241 MVAEIARDPETR--GLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 320 AAPRYSPFNQLDLSYKVVARIDPAKCIHCNLCFVACDEGAHQCIDLTVDGVKidpatyagpaktQPVVREDDCVGCNLCS 399
Cdd:PRK08318 319 AVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDEDGTR------------TPEVIEEECVGCNLCA 386

                        410       420       430
                 ....*....|....*....|....*....|....
gi 502942449 400 LVCPVDGCITMLEVDSGRESVTWAEITERYPEVT 433
Cdd:PRK08318 387 HVCPVEGCITMGEVKFGKPYANWTTHPNNPARAA 420
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 3-301 3.75e-147

Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN, and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass the dimer interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239244  Cd Length: 299  Bit Score: 421.31  E-value: 3.75e-147
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIG---TPVLNVSSRYGGWEYGGNKLAAINNIELISD 79
Cdd:cd02940    1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGldkDIVTNVSPRIARLRTSGRGQIGFNNIELISE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGMGSAVGQVPEYCSMIT 159
Cdd:cd02940   81 KPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELVEEIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 160 EWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSVIGVDLDAFTLKPNVGGKGGHGGYAGPAVKPIALS 239
Cdd:cd02940  161 RWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVKPIALR 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502942449 240 MLSEVMQLPETrdfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGL 301
Cdd:cd02940  241 AVSQIARAPEP---GLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-313 2.49e-95

Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate dehydrogenase is part of the Pathway/BioSystem: Pyrimidine biosynthesis


Pssm-ID: 439937 [Multi-domain]  Cd Length: 296  Bit Score: 288.90  E-value: 2.49e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIG-TPVL-NVSSRYggWEYGGNklAAINNIELISDR 80
Cdd:COG0167    1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTpEPQPgNPRPRL--FRLPED--SGLINRMGLNNP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  81 PLEVNLREIAEVKRLfpDRAVIVSAMFeSDPQVWADAVRRIEDTGADAIELNYGCPHGmseRGMGSAVGQVPEYCSMITE 160
Cdd:COG0167   77 GVDAFLERLLPAKRY--DVPVIVNIGG-NTVEDYVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEALAELLA 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 161 WVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSvIGVDLDafTLKPNVGGKGghggyagPAVKPIALSM 240
Cdd:COG0167  151 AVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLG-RAIDLE--TRRPVLANEAggl--sgPALKPIALRM 225

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502942449 241 LSEVMQLPETRdfrIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASV 313
Cdd:COG0167  226 VREVAQAVGGD---IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSI 295
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 3-330 4.36e-95

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 291.74  E-value: 4.36e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPtNTAYQVCK-AFDYGWGGAVWKTI---GTPVLNVSSRY-----GGWEYGGNKLAAINN 73
Cdd:PLN02495  10 DLSVTVNGLKMPNPFVIGSGPP-GTNYTVMKrAFDEGWGGVIAKTVsldASKVINVTPRYarlraGANGSAKGRVIGWQN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  74 IELISDRPLEVNLREIAEVKRLFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGMGSAVGQVPE 153
Cdd:PLN02495  89 IELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVGQDCD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 154 YCSMITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSVIGVDLDAFTLKPNVGGKGGHGGYAGPAV 233
Cdd:PLN02495 169 LLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTLRPEPCVEGYSTPGGYSSKAV 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 234 KPIAlsmLSEVMQLPETRDFRIP----ISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKG 309
Cdd:PLN02495 249 RPIA---LAKVMAIAKMMKSEFPedrsLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHN 325

                        330       340
                 ....*....|....*....|.
gi 502942449 310 AASVRDVIGAAAPRYSPFNQL 330
Cdd:PLN02495 326 FSSIEDFRGASLPYFTTHTDL 346
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 5-320 2.21e-63

Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240091 [Multi-domain]  Cd Length: 296  Bit Score: 206.63  E-value: 2.21e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   5 STDFCGVKSPNPFWLASAppT-NTAYQVCKAFD-YGWGGAVWKTIGtpvlnVSSRYGG-----WEYGGnklAAINNIELI 77
Cdd:cd04740    1 SVELAGLRLKNPVILASG--TfGFGEELSRVADlGKLGAIVTKSIT-----LEPREGNppprvVETPG---GMLNAIGLQ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  78 SdrP-LEVNLREIAEVKRlFPDRAVIVSaMFESDPQVWADAVRRIEDTGADAIELNYGCPHgmsERGMGSAVGQVPEYCS 156
Cdd:cd04740   71 N--PgVEAFLEELLPWLR-EFGTPVIAS-IAGSTVEEFVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDPEAVA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 157 MITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTinsVIGVDLDAFTLKP---NVggkggHGGYAGPAV 233
Cdd:cd04740  144 EIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINT---LKGMAIDIETRKPilgNV-----TGGLSGPAI 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 234 KPIALSMLSEVmqlpeTRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMhYGFRIIEELTDGLSNWLDDKGAASV 313
Cdd:cd04740  216 KPIALRMVYQV-----YKAVEIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSI 289


                 ....*..
gi 502942449 314 RDVIGAA 320
Cdd:cd04740  290 EELVGLA 296
PRK07259 PRK07259
dihydroorotate dehydrogenase;
3-320 8.76e-60

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 197.68  E-value: 8.76e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASA-----PPTNTAYQVCKAfdygwGGAVWKTI------GTPVLNVSSRYGGWeyggnklaaI 71
Cdd:PRK07259   1 RLSVELPGLKLKNPVMPASGtfgfgGEYARFYDLNGL-----GAIVTKSTtlepreGNPTPRIAETPGGM---------L 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  72 NNIELiSDRPLEVNLREIAEVKRLFpDRAVIVSaMFESDPQVWADAVRRIEDTG-ADAIELNYGCPHGMserGMGSAVGQ 150
Cdd:PRK07259  67 NAIGL-QNPGVDAFIEEELPWLEEF-DTPIIAN-VAGSTEEEYAEVAEKLSKAPnVDAIELNISCPNVK---HGGMAFGT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 151 VPEYCSMITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTinsVIGVDLDAFTLKP---NVggkggHGG 227
Cdd:PRK07259 141 DPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDIKTRKPilaNV-----TGG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 228 YAGPAVKPIALSMLSEVMQlpetrDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMhYGFRIIEELTDGLSNWLDD 307
Cdd:PRK07259 213 LSGPAIKPIALRMVYQVYQ-----AVDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDK 286

                        330
                 ....*....|...
gi 502942449 308 KGAASVRDVIGAA 320
Cdd:PRK07259 287 YGIKSIEEIVGIA 299
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 4-320 8.59e-51

dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 dihydroorotate dehydrogenases while excluding the closely related subfamily 2 (TIGR01036). This family also includes a number of uncharacterized proteins and a domain of dihydropyrimidine dehydrogenase. The uncharacterized proteins might all be dihydroorotate dehydrogenase.


Pssm-ID: 130109 [Multi-domain]  Cd Length: 300  Bit Score: 174.15  E-value: 8.59e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449    4 LSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGtpvlnVSSRYGG-------WEYGgnklaAINNIEL 76
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIG-----LEPRPGYrnptiveTPCG-----MLNAIGL 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   77 iSDRPLEVNLREIAEVKRLFPdRAVIVSaMFESDPQVWADAVRRIEDTG--ADAIELNYGCPHGMserGMGSAVGQVPEY 154
Cdd:TIGR01037  71 -QNPGVEAFLEELKPVREEFP-TPLIAS-VYGSSVEEFAEVAEKLEKAPpyVDAYELNLSCPHVK---GGGIAIGQDPEL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  155 CSMITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTinsVIGVDLDAFTLKPNVggKGGHGGYAGPAVK 234
Cdd:TIGR01037 145 SADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINT---LRGMKIDIKTGKPIL--ANKTGGLSGPAIK 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  235 PIALSMLSEVmqlpeTRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFrIIEELTDGLSNWLDDKGAASVR 314
Cdd:TIGR01037 220 PIALRMVYDV-----YKMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIE 293


                  ....*.
gi 502942449  315 DVIGAA 320
Cdd:TIGR01037 294 ELIGIA 299
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 6-297 1.70e-43

Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. DHPD catalyzes the first step in pyrimidine degradation: the NADPH-dependent reduction of uracil and thymine to the corresponding 5,6-dihydropyrimidines. DHPD contains two FAD, two FMN and eight [4Fe-4S] clusters, arranged in two electron transfer chains that pass its homodimeric interface twice. Two of the Fe-S clusters show a hitherto unobserved coordination involving a glutamine residue.


Pssm-ID: 239204 [Multi-domain]  Cd Length: 289  Bit Score: 154.43  E-value: 1.70e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   6 TDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTI------GTPVLNVSSRYGGWEYGGNKLAAINnIELISD 79
Cdd:cd02810    1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVtlhprpGNPLPRVARLPPEGESYPEQLGILN-SFGLPN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESdPQVWADAVRRIEDTGADAIELNYGCPHGMSERGmgsaVGQVPEYCSMIT 159
Cdd:cd02810   80 LGLDVWLQDIAKAKKEFPGQPLIASVGGSS-KEDYVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANLL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 160 EWVTSVASVPVIVKLTPNITDIKAP--ARAAIEGRAAALSLINTINSVIgVDLDAFTLKPnvggKGGHGGYAGPAVKPIA 237
Cdd:cd02810  155 KAVKAAVDIPLLVKLSPYFDLEDIVelAKAAERAGADGLTAINTISGRV-VDLKTVGPGP----KRGTGGLSGAPIRPLA 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 238 LSMLSEVMQLpetRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEEL 297
Cdd:cd02810  230 LRWVARLAAR---LQLDIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKI 286
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
4-301 3.28e-27

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 110.13  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449    4 LSTDFCGVKSPNPFWLASAPPTNTAyQVCKAFDYGWGGAVwkTIGTPVLNvsSRYGGWE--YGGNKLAAINNIELiSDRP 81
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASGFDKFGE-EALKWLALGKFGAI--EIKSVTPY--PQPGNPTprVFRLPEGVLNRMGL-NNPG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   82 LEVNLREIAEVKRLFPDRAVIVSA----MFESDpqvWADAVRRIEDTgADAIELNYGCPH--GmsergmGSAVGQVPEYC 155
Cdd:pfam01180  76 LDAVLAELLKRRKEYPRPDLGINLskagMTVDD---YVEVARKIGPF-ADYIELNVSCPNtpG------LRALQTDPELA 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  156 SMITEWVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINS-VIGVDLDAFTLKPnvGGKGGHGGYAGPAVK 234
Cdd:pfam01180 146 AILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTtVRGMRIDLKTEKP--ILANGTGGLSGPPIK 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502942449  235 PIALSMLSEVMQLpetRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGL 301
Cdd:pfam01180 224 PIALKVIRELYQR---TGPEIPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDEL 287
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 3-327 8.35e-25

Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively. This subgroup has the conserved FMN binding site, but lacks some catalytic residues and may therefore be inactive.


Pssm-ID: 240090  Cd Length: 325  Bit Score: 104.23  E-value: 8.35e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGTPVLnvssRYGGWEYGGNKLAAINNIELISDRP- 81
Cdd:cd04739    1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEEQI----EREAQELDRFLTYGSSFAEALSYFPe 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  82 -------LEVNLREIAEVKRLFpDRAVIVSAMFESDPQvWADAVRRIEDTGADAIELN-YGCPHGMSERgmGSAVGQVpe 153
Cdd:cd04739   77 ygrynlgPEEYLELIRRAKRAV-SIPVIASLNGVSAGG-WVDYARQIEEAGADALELNiYALPTDPDIS--GAEVEQR-- 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 154 YCSMITEwVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSViGVDLDAFTLKPNVGgkgghggyagpav 233
Cdd:cd04739  151 YLDILRA-VKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQP-DIDLETLEVVPNLL------------- 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 234 kpiaLSMLSEvMQLPET-------RDfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLD 306
Cdd:cd04739  216 ----LSSPAE-IRLPLRwiailsgRV-KASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWME 289

                        330       340
                 ....*....|....*....|.
gi 502942449 307 DKGAASVRDVIGAAAPRYSPF 327
Cdd:cd04739  290 EHGYESVQQLRGSMSQKNVPD 310
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
2-319 7.22e-22

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 96.09  E-value: 7.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   2 ADLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTIGTPVLNVSSRY--GGWEYG----GNKLAAINNIE 75
Cdd:PRK07565   1 MDLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLFEEQIRHEAAEldRHLTHGtesfAEALDYFPEPA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  76 LISDRPlEVNLREIAEVKRLFpDRAVIVSAMFESDPQvWADAVRRIEDTGADAIELN-YGCPHGMSERgmGSAVGQVpeY 154
Cdd:PRK07565  81 KFYVGP-EEYLELIRRAKEAV-DIPVIASLNGSSAGG-WVDYARQIEQAGADALELNiYYLPTDPDIS--GAEVEQR--Y 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 155 CSMITEwVTSVASVPVIVKLTPNITDIKAPARAAIEGRAAALSLINTINSViGVDLDAFTLKPNVGgkgghggyagpavk 234
Cdd:PRK07565 154 LDILRA-VKSAVSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQP-DIDLETLEVVPGLV-------------- 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 235 piaLSMLSEvMQLPET-------RDfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDD 307
Cdd:PRK07565 218 ---LSTPAE-LRLPLRwiailsgRV-GADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDYIGTILRGLEDWMER 292

                        330
                 ....*....|..
gi 502942449 308 KGAASVRDVIGA 319
Cdd:PRK07565 293 HGYESLQQFRGS 304
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 338-410 1.10e-20

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 434137 [Multi-domain]  Cd Length: 59  Bit Score: 85.03  E-value: 1.10e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502942449  338 ARIDPAKCIHCNLCFVACDEGAHQCIdltvdgvKIDPATYAgpaktqpVVREDDCVGCNLCSLVCPVDGCITM 410
Cdd:pfam14697   1 ARIDEDTCIGCGKCYIACPDTSHQAI-------VGDGKRHH-------TVIEDECTGCNLCVSVCPVDDCITM 59
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 68-301 1.08e-14

Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences and cellular location. Members of class 1 are cytosolic enzymes and multimers while class 2 enzymes are membrane associated and monomeric. The class 1 enzymes can be further divided into subtypes 1A and 1B which are homodimers and heterotetrameric proteins, respectively.


Pssm-ID: 240092  Cd Length: 294  Bit Score: 74.28  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  68 LAAINNIELiSDRPLEVNLREIAEVKRLFPDRA----VIVSAMFESDpqvwADAVRRIEDT---GADAIELNYGCPH--G 138
Cdd:cd04741   60 LGSINSLGL-PNLGLDYYLEYIRTISDGLPGSAkpffISVTGSAEDI----AAMYKKIAAHqkqFPLAMELNLSCPNvpG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 139 MSERGMGSAvgQVPEYCsmitEWVTSVASVPVIVKLTPnITDIK--APARAAIEGRAAALSLINTINSV-IGVDLDAFTL 215
Cdd:cd04741  135 KPPPAYDFD--ATLEYL----TAVKAAYSIPVGVKTPP-YTDPAqfDTLAEALNAFACPISFITATNTLgNGLVLDPERE 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 216 KPNVGGKGGHGGYAGPAVKPIAlsmLSEVMQLPETRDFRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIE 295
Cdd:cd04741  208 TVVLKPKTGFGGLAGAYLHPLA---LGNVRTFRRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFA 284


                 ....*.
gi 502942449 296 ELTDGL 301
Cdd:cd04741  285 RIEKEL 290
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-318 3.35e-14

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 73.06  E-value: 3.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   3 DLSTDFCGVKSPNPFWLASAPPTNTAYQVCKAFDYGWGGAVWKTiGTPVL---NVSSRYGGWEYGgnklaAINNIELiSD 79
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVYCMTKEELEEVEASAAGAFVTKS-ATLEPrpgNPEPRYADTPLG-----SINSMGL-PN 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  80 RPLEVNLREIAEVKRLFPDRAVIVSAMFESdPQVWADAVRRIEDTG-ADAIELNYGCPH--GMSErgmgsaVGQVPEYCS 156
Cdd:PRK02506  74 LGFDYYLDYVLELQKKGPNKPHFLSVVGLS-PEETHTILKKIQASDfNGLVELNLSCPNvpGKPQ------IAYDFETTE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 157 MITEWVTSVASVPVIVKLTPNItDIKAPARAAIEGRAAALSLINTINS-----VIGVDLDAFTLKPNvggkGGHGGYAGP 231
Cdd:PRK02506 147 QILEEVFTYFTKPLGVKLPPYF-DIVHFDQAAAIFNKFPLAFVNCINSignglVIDPEDETVVIKPK----NGFGGIGGD 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 232 AVKPIALSMLSEVMQL--PEtrdfrIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKG 309
Cdd:PRK02506 222 YIKPTALANVRAFYQRlnPS-----IQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKG 296


                 ....*....
gi 502942449 310 AASVRDVIG 318
Cdd:PRK02506 297 YQSLEDFRG 305
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 337-417 4.69e-12

MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function prediction only];


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 60.90  E-value: 4.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 337 VARIDPAKCIHCNLCFVACDEGAhqcidLTVDGVKidpatyagpaktQPVVREDDCVGCNLCSLVCPVdGCITMLEVDSG 416
Cdd:COG1149    5 IPVIDEEKCIGCGLCVEVCPEGA-----IKLDDGG------------APVVDPDLCTGCGACVGVCPT-GAITLEEREAG 66


                 .
gi 502942449 417 R 417
Cdd:COG1149   67 K 67
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 340-410 1.90e-11

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 59.68  E-value: 1.90e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502942449 340 IDPAKCIHCNLCFVACdegAHQCIDLTVDGVkidpatyagpaktqPVVREDDCVGCNLCSLVCPVDgCITM 410
Cdd:COG1144   27 VDEDKCIGCGLCWIVC---PDGAIRVDDGKY--------------YGIDYDYCKGCGICAEVCPVK-AIEM 79
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 338-410 2.44e-11

NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and metabolism];


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 58.95  E-value: 2.44e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502942449 338 ARIDPAKCIHCNLCFVACdegAHQCIDLTVDGVKIdpatyagpaktqPVVREDDCVGCNLCSLVCPVdGCITM 410
Cdd:COG1146    3 PVIDTDKCIGCGACVEVC---PVDVLELDEEGKKA------------LVINPEECIGCGACELVCPV-GAITV 59
PRK06991 PRK06991
electron transport complex subunit RsxB;
337-427 1.77e-10

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 61.35  E-value: 1.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 337 VARIDPAKCIHCNLCFVACdegahqcidlTVDGVkidpatyAGPAKTQPVVREDDCVGCNLCSLVCPVDgCITMLEVdsG 416
Cdd:PRK06991  79 VAVIDEQLCIGCTLCMQAC----------PVDAI-------VGAPKQMHTVLADLCTGCDLCVPPCPVD-CIDMVPV--T 138

                         90
                 ....*....|.
gi 502942449 417 RESVTWAEITE 427
Cdd:PRK06991 139 GERTGWDAWSQ 149
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 337-413 1.78e-09

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 56.73  E-value: 1.78e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502942449  337 VARIDPAKCIHCNLCFVACdegahqcidlTVDGVkidpatyAGPAKTQPVVREDDCVGCNLCSLVCPVDgCITMLEV 413
Cdd:TIGR01944 107 VALIDEDNCIGCTKCIQAC----------PVDAI-------VGAAKAMHTVIADECTGCDLCVEPCPTD-CIEMIPV 165
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 335-422 2.16e-09

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 56.88  E-value: 2.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 335 KVVARIDPAKCIHCNLCFVACdegahqcidlTVDGVkidpatyAGPAKTQPVVREDDCVGCNLCSLVCPVDgCITMLEVD 414
Cdd:PRK05113 106 RKVAFIDEDNCIGCTKCIQAC----------PVDAI-------VGATKAMHTVISDLCTGCDLCVAPCPTD-CIEMIPVA 167


                 ....*...
gi 502942449 415 SGRESVTW 422
Cdd:PRK05113 168 ETPDNWKW 175
PLN02826 PLN02826
dihydroorotate dehydrogenase
 168-320 2.39e-08

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 55.90  E-value: 2.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 168 VPVIVKLTPNIT--DIKAPARAAIEGRAAALSLINTINSvigvdldaftlKPN-VGGKGGHGGYAGPAVKPI-ALS--ML 241
Cdd:PLN02826 263 PPLLVKIAPDLSkeDLEDIAAVALALGIDGLIISNTTIS-----------RPDsVLGHPHADEAGGLSGKPLfDLSteVL 331

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502942449 242 SEVMQLpeTRDfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASVRDVIGAA 320
Cdd:PLN02826 332 REMYRL--TRG-KIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVGAD 407
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 342-414 2.50e-08

Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy production and conversion]; Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) is part of the Pathway/BioSystem: NADH dehydrogenase


Pssm-ID: 440758 [Multi-domain]  Cd Length: 66  Bit Score: 50.51  E-value: 2.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502942449 342 PAKCIHCNLCFVACdegAHQCIDLTVDgvkidpatyagPAKTQPVVREDDCVGCNLCSLVCPVDgCITMLEVD 414
Cdd:COG1143    1 EDKCIGCGLCVRVC---PVDAITIEDG-----------EPGKVYVIDPDKCIGCGLCVEVCPTG-AISMTPFE 58
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 337-422 2.62e-08

Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and conversion]; Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit is part of the Pathway/BioSystem: Na+-translocating Fd:NADH oxidoreductase


Pssm-ID: 442125 [Multi-domain]  Cd Length: 254  Bit Score: 54.62  E-value: 2.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 337 VARIDPAK-----CIHCNLCFVACDEGAhqcIDLTVDGVkidpatyagpaktqPVVREDDCVGCNLCSLVCPVDgCITML 411
Cdd:COG2878  126 AAVIGGPKgceygCIGCGDCIKACPFDA---IVGAAKGM--------------HTVDEDKCTGCGLCVEACPVD-CIEMV 187

                         90
                 ....*....|.
gi 502942449 412 EVDSGRESVTW 422
Cdd:COG2878  188 PVSPTVVVSSW 198
NapF COG1145
Ferredoxin [Energy production and conversion];
305-410 7.24e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 53.19  E-value: 7.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 305 LDDKGAASVRDVIGAAAPRYSPFNQLDLSYKVVARIDPAKCIHCNLCFVACDEGAhqcIDLtvdgvkidpatyaGPAKTQ 384
Cdd:COG1145  144 LAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPTGA---IRL-------------KDGKPQ 207

                         90       100
                 ....*....|....*....|....*.
gi 502942449 385 PVVREDDCVGCNLCSLVCPVdGCITM 410
Cdd:COG1145  208 IVVDPDKCIGCGACVKVCPV-GAISL 232
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 340-410 9.72e-08

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 50.47  E-value: 9.72e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502942449 340 IDPAKCIHCNLCFVACDEGAhqcIDLTVDGVKIDPAtyagpaKTQPVVREDDCVGCNLCSLVCPVDgCITM 410
Cdd:cd10549   37 IDEDKCVFCGACVEVCPTGA---IELTPEGKEYVPK------EKEAEIDEEKCIGCGLCVKVCPVD-AITL 97
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 75-198 9.89e-08

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 52.50  E-value: 9.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  75 ELISDRPLevnLREIAEVKRLFP----DRAVIVSaMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSER-GMGSAVG 149
Cdd:cd02801   30 EMISAKAL---LRGNRKRLRLLTrnpeERPLIVQ-LGGSDPETLAEAAKIVEELGADGIDLNMGCPSPKVTKgGAGAALL 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502942449 150 QVPEY-CSMITEwVTSVASVPVIVK------LTPNITDIkapARAAIEGRAAALSL 198
Cdd:cd02801  106 KDPELvAEIVRA-VREAVPIPVTVKirlgwdDEEETLEL---AKALEDAGASALTV 157
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 75-173 1.01e-07

Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archae. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD. Some family members may be targeted to the mitochondria and even have a role in mitochondria.


Pssm-ID: 426126  Cd Length: 309  Bit Score: 53.48  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449   75 ELISDRPLevnLREIAEVKRLFP----DRAVIVSaMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSERGM-GSAVG 149
Cdd:pfam01207  29 EMVTAKAQ---LRPEKVRIRMLSeleePTPLAVQ-LGGSDPALLAEAAKLVEDRGADGIDINMGCPSKKVTRGGgGAALL 104

                          90       100
                  ....*....|....*....|....*
gi 502942449  150 QVPE-YCSMITEWVTSVaSVPVIVK 173
Cdd:pfam01207 105 RNPDlVAQIVKAVVKAV-GIPVTVK 128
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 109-198 2.20e-07

tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; tRNA-dihydrouridine synthase is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 439812 [Multi-domain]  Cd Length: 310  Bit Score: 52.40  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 109 SDPQVWADAVRRIEDTGADAIELNYGCPhgmSER----GMGSAVGQVPEYCSMITEWVTSVASVPVIVKL-------TPN 177
Cdd:COG0042   71 SDPEELAEAARIAEELGADEIDINMGCP---VKKvtkgGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIrlgwdddDEN 147

                         90       100
                 ....*....|....*....|.
gi 502942449 178 ITDIkapARAAIEGRAAALSL 198
Cdd:COG0042  148 ALEF---ARIAEDAGAAALTV 165
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 336-419 2.92e-07

HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a membrane-associated formate hydrogenlyase system (FHL-1) in Escherichia coli that breaks down formate, produced during anaerobic fermentation, to H2 and CO2. FHL-1 consists of formate dehydrogenase H (FDH-H) and the hydrogenase 3 complex (Hyd-3). HycB is thought to code for the [4Fe-4S] ferredoxin subunit of hydrogenase 3, which functions as an intermediate electron carrier protein between hydrogenase 3 and formate dehydrogenase. HydN codes for the [4Fe-4S] ferredoxin subunit of FDH-H; a hydN in-frame deletion mutation causes only weak reduction in hydrogenase activity, but loss of more than 60% of FDH-H activity. This pathway is only active at low pH and high formate concentrations, and is thought to provide a detoxification/de-acidification system countering the buildup of formate during fermentation.


Pssm-ID: 319876 [Multi-domain]  Cd Length: 149  Bit Score: 49.57  E-value: 2.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 336 VVAriDPAKCIHCNLCFVACDEGAHQCIDLTVDGVKIDPA-------TYAGPAKTQ-------------PV--------- 386
Cdd:cd10554    2 VIA--DPDKCIGCRTCEVACAAAHSGKGIFEAGTDGLPFLprlrvvkTGEVTAPVQcrqcedapcanvcPVgaisqedgv 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 502942449 387 --VREDDCVGCNLCSLVCPVdGCITMLEVDSGRES 419
Cdd:cd10554   80 vqVDEERCIGCKLCVLACPF-GAIEMAPTTVPGVD 113
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 339-409 3.24e-07

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 47.35  E-value: 3.24e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502942449 339 RIDPAKCIHCNLCFVACDEGAhqcIDLTVDGVKIDpatyagpaktqpvvrEDDCVGCNLCSLVCPvDGCIT 409
Cdd:COG2221   11 KIDEEKCIGCGLCVAVCPTGA---ISLDDGKLVID---------------EEKCIGCGACIRVCP-TGAIK 62
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 345-405 8.61e-07

4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich. Domain contains two 4Fe4S clusters.


Pssm-ID: 463724 [Multi-domain]  Cd Length: 51  Bit Score: 45.60  E-value: 8.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502942449  345 CIHCNLCFVACDEGAhqcidLTVDGVKIDPAtyagpaKTQPVVREDDCVGCNLCSLVCPVD 405
Cdd:pfam12838   1 CIGCGACVAACPVGA-----ITLDEVGEKKG------TKTVVIDPERCVGCGACVAVCPTG 50
PRK10415 PRK10415
tRNA-dihydrouridine synthase B; Provisional
 77-174 1.19e-06

tRNA-dihydrouridine synthase B; Provisional


Pssm-ID: 182440  Cd Length: 321  Bit Score: 50.35  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  77 ISDRPLEVNLREIAEvkrlfpdrAVIVSAMFESDPQVW------------------------------ADAVRRIEDTGA 126
Cdd:PRK10415  20 ITDRPFRTLCYEMGA--------GLTVSEMMSSNPQVWesdksrlrmvhidepgirtvqiagsdpkemADAARINVESGA 91

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 502942449 127 DAIELNYGCPHGMSERGM-GSAVGQVPEYCSMITEWVTSVASVPVIVKL 174
Cdd:PRK10415  92 QIIDINMGCPAKKVNRKLaGSALLQYPDLVKSILTEVVNAVDVPVTLKI 140
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
335-417 1.25e-06

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 45.88  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 335 KVVARIDPAKCIHCNLCFVACdegAHQCIDLTVDGVKIDPatyagpaktqpvvreDDCVGCNLCSLVCPVdGCITMLEVD 414
Cdd:COG2768    3 LGKPYVDEEKCIGCGACVKVC---PVGAISIEDGKAVIDP---------------EKCIGCGACIEVCPV-GAIKIEWEE 63


                 ...
gi 502942449 415 SGR 417
Cdd:COG2768   64 DEE 66
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 168-301 1.92e-06

Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S)-dihydroorotate to orotate. This is the fourth step and the only redox reaction in the de novo biosynthesis of UMP, the precursor of all pyrimidine nucleotides. DHOD requires FMN as co-factor. DHOD divides into class 1 and class 2 based on their amino acid sequences, their cellular location and their natural electron acceptor used to reoxidize the flavin group. Members of class 1 are cytosolic enzymes and multimers, while class 2 enzymes are membrane associated, monomeric and use respiratory quinones as their physiological electron acceptors.


Pssm-ID: 240089  Cd Length: 327  Bit Score: 49.42  E-value: 1.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 168 VPVIVKLTPNITD--IKAPARAAIEGRAAALSLINTinsvigvdldafTLKPNVGGKGGHGGYAG----PAVKPIALSML 241
Cdd:cd04738  203 VPLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNT------------TISRPGLLRSPLANETGglsgAPLKERSTEVL 270

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 242 SEVMQLpeTRDfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGL 301
Cdd:cd04738  271 RELYKL--TGG-KIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 338-410 2.81e-06

TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and conversion];


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 45.03  E-value: 2.81e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502942449 338 ARIDPAKCIHCNLCFVACDEGahqCIDLTVDGVKIDPatyagpaktqpvvreDDCVGCNLCSLVCPVDgCITM 410
Cdd:COG4231   17 YVIDEDKCTGCGACVKVCPAD---AIEEGDGKAVIDP---------------DLCIGCGSCVQVCPVD-AIKL 70
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 68-284 3.50e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 47.58  E-value: 3.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449  68 LAAINNIELISDRPLEVNLREIAEVKRlFPDRAVIVSAMFESDPQVWADAVRRIEDTGADAIELNYGCPHGMSErgmgsa 147
Cdd:cd04722   28 AIIVGTRSSDPEEAETDDKEVLKEVAA-ETDLPLGVQLAINDAAAAVDIAAAAARAAGADGVEIHGAVGYLARE------ 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 148 vgqVPEYCSMITEwvtSVASVPVIVKLTPNITDikaparAAIEGRAAALSLINTINSVIGvdldaftlkpnvggkgghgg 227
Cdd:cd04722  101 ---DLELIRELRE---AVPDVKVVVKLSPTGEL------AAAAAEEAGVDEVGLGNGGGG-------------------- 148

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502942449 228 YAGPAVKPIALSMLSEVMQLPetrdfRIPISGMGGIQTWRDAAEFLLLGATSLQVCT 284
Cdd:cd04722  149 GGGRDAVPIADLLLILAKRGS-----KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 337-406 7.22e-06

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319895 [Multi-domain]  Cd Length: 154  Bit Score: 45.71  E-value: 7.22e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502942449 337 VARIDPAKCI------HCNLCFVACDEGAhqcidltvdgvkidPATYAGPAKTQPVVREDDCVGCNLCSLVCPVDG 406
Cdd:cd16373   85 VAVIDKDRCLawqggtDCGVCVEACPTEA--------------IAIVLEDDVLRPVVDEDKCVGCGLCEYVCPVEP 146
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 340-410 1.42e-05

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 44.31  E-value: 1.42e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502942449 340 IDPAKCIHCNLCFVACDEGAhqcIDLTVDGVKIDPatyagpaktqPVVREDDCVGCNLCSLVCPVdGCITM 410
Cdd:cd10549    3 YDPEKCIGCGICVKACPTDA---IELGPNGAIARG----------PEIDEDKCVFCGACVEVCPT-GAIEL 59
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
167-309 3.59e-05

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 45.54  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 167 SVPVIVKLTPNITD--IKAPARAAIEGRAAALSLINTinsvigvdldafTL-KPNVGGKGGHGGYA----GPaVKPIALS 239
Cdd:PRK05286 211 YVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNT------------TLsRDGLKGLPNADEAGglsgRP-LFERSTE 277

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 240 MLSEVMQlpETRDfRIPISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKG 309
Cdd:PRK05286 278 VIRRLYK--ELGG-RLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 385-412 7.05e-05

Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit [Energy production and conversion]; Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta subunit is part of the Pathway/BioSystem: Pyruvate oxidation


Pssm-ID: 440759 [Multi-domain]  Cd Length: 84  Bit Score: 41.19  E-value: 7.05e-05
                         10        20
                 ....*....|....*....|....*...
gi 502942449 385 PVVREDDCVGCNLCSLVCPvDGCITMLE 412
Cdd:COG1144   25 PVVDEDKCIGCGLCWIVCP-DGAIRVDD 51
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
339-405 9.34e-05

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 43.90  E-value: 9.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502942449 339 RIDPAKCIHCNLCFVACDEGahqcidltvdgvkIDPAtyagpaktQPVVREDDCVGCNLCSLVCPVD 405
Cdd:COG0348  206 RYDRGDCIDCGLCVKVCPMG-------------IDIR--------KGEINQSECINCGRCIDACPKD 251
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 337-423 1.10e-04

bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily of SIMIBI superfamily. Proteins in this superfamily contain an ATP-binding domain and use energy from hydrolysis of ATP to transfer electron or ion. The specific function of this family is unknown.


Pssm-ID: 349764 [Multi-domain]  Cd Length: 246  Bit Score: 43.53  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 337 VARIDPAKCIHCNLCFVACDEGAhqcidLTVDGVKidpatyagpaktqPVVREDDCVGCNLCSLVCPvDGCITMLEVDSG 416
Cdd:cd03110   58 KAFIDQEKCIRCGNCERVCKFGA-----ILEFFQK-------------LIVDESLCEGCGACVIICP-RGAIYLKDRDTG 118


                 ....*..
gi 502942449 417 RESVTWA 423
Cdd:cd03110  119 KIFISSS 125
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 389-432 1.11e-04

NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of the NADH-quinone oxidoreductase complex I which generally couples NADH and ubiquinone oxidation/reduction in bacteria and mammalian mitochondria, but may act on NADPH and/or plastoquinone in cyanobacteria and plant chloroplasts. This model excludes "I" subunits from the closely related F420H2 dehydrogenase and formate hydrogenlyase complexes. [Energy metabolism, Electron transport]


Pssm-ID: 273902 [Multi-domain]  Cd Length: 122  Bit Score: 41.63  E-value: 1.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 502942449  389 EDDCVGCNLCSLVCPVDgCITMlevdsgresVTWA-EITERYPEV 432
Cdd:TIGR01971  42 EEKCIGCTLCAAVCPAD-AIRV---------VPAEgEDGKRRLKF 76
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 335-405 1.12e-04

Uncharacterized polyferredoxin-like protein; This family contains uncharacterized polyferredoxin protein similar to Methanobacterium thermoautotrophicum MvhB. The mvhB is a gene of the methylviologen-reducing hydrogenase operon. It is predicted to contain 12 [4Fe-4S] clusters, and was therefore suggested to be a polyferredoxin. As a subfamily of the beta subunit of the DMSO Reductase (DMSOR) family, it is predicted to function as electron carrier in the reducing reaction.


Pssm-ID: 319871 [Multi-domain]  Cd Length: 128  Bit Score: 42.00  E-value: 1.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502942449 335 KVVARIDPAKCIHCNLCFVACDEGAhqcIDLTVDGvkidpatyagpaktQPVVREDDCVGCNLCSLVCPVD 405
Cdd:cd10549   70 EKEAEIDEEKCIGCGLCVKVCPVDA---ITLEDEL--------------EIVIDKEKCIGCGICAEVCPVN 123
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
340-420 1.25e-04

Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 41.95  E-value: 1.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 340 IDPAKCIHCNLCFVACDEgAHQCIDLT-----VDGVKIDPATYAG--------------PA------KTQPVVREDDCVG 394
Cdd:COG1142    7 ADPEKCIGCRTCEAACAV-AHEGEEGEpflprIRVVRKAGVSAPVqcrhcedapcaevcPVgaitrdDGAVVVDEEKCIG 85

                         90       100
                 ....*....|....*....|....*.
gi 502942449 395 CNLCSLVCPVdGCITMLEVDSGRESV 420
Cdd:COG1142   86 CGLCVLACPF-GAITMVGEKSRAVAV 110
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 344-413 1.30e-04

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 41.17  E-value: 1.30e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 344 KCIHCNLCFVACDEGAhqcidltvdgVKIDPATYagpaktqPVVREDDCVGCNLCSLVCPVDGCITMLEV 413
Cdd:PRK09624  52 KCVRCYLCYIYCPEPA----------IYLDEEGY-------PVFDYDYCKGCGICANECPTKAIEMVRET 104
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
335-404 2.37e-04

Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 43.48  E-value: 2.37e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 335 KVVARIDPAKCIHCNLCFVACDEGAhqcIDLTVDGVKIDpatyagpaktqpvvrEDDCVGCNLCSLVCPV 404
Cdd:COG4624   83 GPSIIRDKEKCKNCYPCVRACPVKA---IKVDDGKAEID---------------EEKCISCGQCVAVCPF 134
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 340-427 2.61e-04

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 40.09  E-value: 2.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 340 IDPAKCIHCNLCFVACDEGahqcidltVDGVKIDPATYAGpaKTQPVVREDDCVGCNLCSLVCPvDGCITMLEvdsgRES 419
Cdd:PRK09626  13 VDESRCKACDICVSVCPAG--------VLAMRIDPHAVLG--KMIKVVHPESCIGCRECELHCP-DFAIYVAD----RKE 77


                 ....*...
gi 502942449 420 VTWAEITE 427
Cdd:PRK09626  78 FKFAKLSK 85
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
389-410 2.71e-04

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 41.41  E-value: 2.71e-04
                         10        20
                 ....*....|....*....|..
gi 502942449 389 EDDCVGCNLCSLVCPVDgCITM 410
Cdd:PRK05888  57 EERCIACKLCAAICPAD-AITI 77
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 339-403 2.77e-04

4Fe-4S dicluster domain; This family includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. The structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 404174 [Multi-domain]  Cd Length: 56  Bit Score: 38.77  E-value: 2.77e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502942449  339 RIDPAKCIHCNLCFVACDEGAhqcidltvdgvKIDPATYAGPAKTQPVVREDDCVGCNLCSLVCP 403
Cdd:pfam13237   3 VIDPDKCIGCGRCTAACPAGL-----------TRVGAIVERLEGEAVRIGVWKCIGCGACVEACP 56
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
307-410 3.64e-04

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 40.67  E-value: 3.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 307 DKGAASVRDVIGAAAprySPFNQLDLSYKV--VARIDPAKCIHCNLCFVACdegahqcidlTVDGVkidpatyAGPAKTQ 384
Cdd:PRK08764  50 DAGARALAQVLGVPA---RPYDRSRGTHKLpqVAWIVEADCIGCTKCIQAC----------PVDAI-------VGGAKHM 109

                         90       100
                 ....*....|....*....|....*.
gi 502942449 385 PVVREDDCVGCNLCSLVCPVDgCITM 410
Cdd:PRK08764 110 HTVIAPLCTGCELCVPACPVD-CIEL 134
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 336-410 4.07e-04

NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, the iron-sulfur subunit of periplasmic nitrate reductase. The periplasmic nitrate reductase NapABC of Escherichia coli likely functions during anaerobic growth in low-nitrate environments; napF operon expression is activated by cyclic AMP receptor protein (Crp). NapF is a subfamily of the beta subunit of DMSO reductase (DMSOR) family. DMSOR family members have a large, periplasmic molybdenum-containing alpha subunit as well as a small beta FeS subunit, and may also have a small gamma subunit. The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319886 [Multi-domain]  Cd Length: 139  Bit Score: 40.30  E-value: 4.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 336 VVARIDPAkC-----IHCNLCFVACDEGAhqcidltvdgVKIDPATyAGPAktQPVVREDDCVGCNLCSLVCPVDGcITM 410
Cdd:cd10564   72 LRAEIGDS-ClalqgVECRSCQDACPTQA----------IRFRPRL-GGIA--LPELDADACTGCGACVSVCPVGA-ITL 136
PsaC COG5703
Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and ...
 345-418 4.31e-04

Photosystem I reaction center iron-sulfur center subunit VII, PsaC [Energy production and conversion]; Photosystem I reaction center iron-sulfur center subunit VII, PsaC is part of the Pathway/BioSystem: Photosystem I


Pssm-ID: 444413 [Multi-domain]  Cd Length: 82  Bit Score: 39.04  E-value: 4.31e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502942449 345 CIHCNLCFVACDEGAHQCIdltvdgvkidPATYAGPAKTQPVVREDDCVGCNLCSLVCPVDGCITMLEVDSGRE 418
Cdd:COG5703   11 CIGCTQCVRACPTDVLEMV----------PWDGCKAGQIAASPRTEDCVGCKRCETACPTDFLSIRVYLSNAET 74
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 337-359 1.38e-03

4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 432822 [Multi-domain]  Cd Length: 24  Bit Score: 36.05  E-value: 1.38e-03
                          10        20
                  ....*....|....*....|...
gi 502942449  337 VARIDPAKCIHCNLCFVACDEGA 359
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVCPYGA 23
PRK13795 PRK13795
hypothetical protein; Provisional
 299-404 1.70e-03

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 40.75  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 299 DGLSNWLDDKGAASVR---DVIGAAAPRYSPFNQLDLSYKVVARIdpAKCIHCNLCFVACDEGAhqcIDLTVDGVKIdpa 375
Cdd:PRK13795 536 EELGMVLTKKGTVKVFasgNIWARSEDKEAAASLFKDAARLLRRA--AECVGCGVCVGACPTGA---IRIEEGKRKI--- 607

                         90       100
                 ....*....|....*....|....*....
gi 502942449 376 tyagpaktqpVVREDDCVGCNLCSLVCPV 404
Cdd:PRK13795 608 ----------SVDEEKCIHCGKCTEVCPV 626
PRK06273 PRK06273
ferredoxin; Provisional
 379-429 3.46e-03

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 38.15  E-value: 3.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 502942449 379 GPAKTQPVVREDDCVGCNLCSLVCPVdGCITMLEVdsgrESVtwaEITERY 429
Cdd:PRK06273  38 GTVELPKKVFEELCIGCGGCANVCPT-KAIEMIPV----EPV---KITEGY 80
DMSOR_beta_like cd16369
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 340-405 3.48e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319891 [Multi-domain]  Cd Length: 172  Bit Score: 38.14  E-value: 3.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 340 IDPAKCIHCNLCFVACDE-GAHQCIDL-TVDgvKIDPATyagPAKTQPVVreddCVGCNL--CSLVCPVD 405
Cdd:cd16369    6 IDPSRCIGCRACVAACREcGTHRGKSMiHVD--YIDRGE---STQTAPTV----CMHCEDptCAEVCPAD 66
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 349-408 4.57e-03

electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in Rhodobacter capsulatus encodes an apparent NADH oxidoreductase responsible for electron transport to nitrogenase, necessary for nitrogen fixation. A closely related complex in E. coli, RsxABCDGE (Reducer of SoxR), reduces the 2Fe-2S-containing superoxide sensor SoxR, active as a transcription factor when oxidized. This family of putative NADH oxidoreductase complexes exists in many of the same species as the related NQR, a Na(+)-translocating NADH-quinone reductase, but is distinct. This model describes the B subunit. [Energy metabolism, Electron transport]


Pssm-ID: 273887 [Multi-domain]  Cd Length: 165  Bit Score: 37.85  E-value: 4.57e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502942449  349 NLCFVACDEGAHQCIDLTvdGVKIDPATYAGPAKTQPV-----VREDDCVGCNLCSLVCPVDGCI 408
Cdd:TIGR01944  69 NKCPPGGEAVILALAELL--GVEPIPQPLDADAGTIQPpmvalIDEDNCIGCTKCIQACPVDAIV 131
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 385-417 5.44e-03

Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion transport and metabolism];


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 35.41  E-value: 5.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 502942449 385 PVVREDDCVGCNLCSLVCPVdGCITM----LEVDSGR 417
Cdd:COG2221   10 PKIDEEKCIGCGLCVAVCPT-GAISLddgkLVIDEEK 45
FDH-N cd10558
The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS ...
 340-408 5.62e-03

The beta FeS subunit of formate dehydrogenase-N (FDH-N); This subfamily contains beta FeS subunit of formate dehydrogenase-N (FDH-N), a member of the DMSO reductase family. FDH-N is involved in the major anaerobic respiratory pathway in the presence of nitrate, catalyzing the oxidation of formate to carbon dioxide at the expense of nitrate reduction to nitrite. Thus, FDH-N is a major component of nitrate respiration of Escherichia coli. This integral membrane enzyme forms a heterotrimer; the alpha-subunit (FDH-G) is the catalytic site of formate oxidation and membrane-associated, incorporating a selenocysteine (SeCys) residue and a [4Fe/4S] cluster in addition to two bis-MGD cofactors, the beta subunit (FDH-H) contains four [4Fe/4S] clusters which transfer the electrons from the alpha subunit to the gamma-subunit (FDH-I), a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups.


Pssm-ID: 319880 [Multi-domain]  Cd Length: 208  Bit Score: 38.14  E-value: 5.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 340 IDPAKCIHCNLCFVACDEGAhqciDLTvDGVKIDPATYAGPAKTQP-------------------VVREDDCVGCN--LC 398
Cdd:cd10558    4 IDVSKCIGCKACQVACKEWN----DLR-AEVGHNVGTYQNPADLSPetwtlmkfrevedngklewLIRKDGCMHCAdpGC 78

                         90
                 ....*....|
gi 502942449 399 SLVCPVDGCI 408
Cdd:cd10558   79 LKACPSPGAI 88
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 385-405 6.13e-03

4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to iron-sulfur clusters. Members include bacterial ferredoxins, various dehydrogenases, and various reductases. Structure of the domain is an alpha-antiparallel beta sandwich.


Pssm-ID: 459642 [Multi-domain]  Cd Length: 24  Bit Score: 34.15  E-value: 6.13e-03
                          10        20
                  ....*....|....*....|.
gi 502942449  385 PVVREDDCVGCNLCSLVCPVD 405
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVG 21
NapF COG1145
Ferredoxin [Energy production and conversion];
257-412 7.37e-03

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 38.17  E-value: 7.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502942449 257 ISGMGGIQTWRDAAEFLLLGATSLQVCTAVMHYGFRIIEELTDGLSNWLDDKGAASVRDVIGAAAPRYSPFNQLDLSYKV 336
Cdd:COG1145   49 PIIGILAKEAFDALKDVLGILGAIVIGIGAGEIVRVGIAAADLNLKAVALVLLLALAVAGAAKRLIISAVKLVAGLVVAA 128

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502942449 337 VARIDPAKCIHCNLCFVACDEGAHQCIDLTVDGVKIDPATYAGPAKTQPVVREDDCVGCNLCSLVCPVdGCITMLE 412
Cdd:COG1145  129 GEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKAKAVIDAEKCIGCGLCVKVCPT-GAIRLKD 203
DMSOR_beta_like cd16374
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 342-403 7.98e-03

uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the small beta iron-sulfur (FeS) subunit of the DMSO Reductase (DMSOR) family. Members of this family also contain a large, periplasmic molybdenum-containing alpha subunit and may have a small gamma subunit as well. Examples of heterodimeric members with alpha and beta subunits include arsenite oxidase, and tungsten-containing formate dehydrogenase (FDH-T) while heterotrimeric members containing alpha, beta, and gamma subunits include formate dehydrogenase-N (FDH-N), and nitrate reductase (NarGHI). The beta subunit contains four Fe4/S4 and/or Fe3/S4 clusters which transfer the electrons from the alpha subunit to a hydrophobic integral membrane protein, presumably a cytochrome containing two b-type heme groups. The reducing equivalents are then transferred to menaquinone, which finally reduces the electron-accepting enzyme system.


Pssm-ID: 319896 [Multi-domain]  Cd Length: 139  Bit Score: 36.48  E-value: 7.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502942449 342 PAKCIHCN--LCFVACDEGAhqcIDLTVDG-VKIDPatyagpaktqpvvreDDCVGCNLCSLVCP 403
Cdd:cd16374   40 PVRCRHCEdaPCMEVCPTGA---IYRDEDGaVLVDP---------------DKCIGCGMCAMACP 86
 
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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