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Conserved domains on  [gi|15595636|ref|NP_249130|]
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dihydropyrimidine dehydrogenase [Pseudomonas aeruginosa PAO1]

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;
2-424 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


:

Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 833.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    2 MADLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGedPAAVNVS-SRYSAHFGPNRQVQGINNIELI 80
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG--PPIVNVSsPRFGALVKEDRRFIGFNNIELI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   81 TDRSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEM 160
Cdd:PRK08318  79 TDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVEM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  161 VTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAVKPIA 240
Cdd:PRK08318 159 YTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  241 LNMVAEIARDPQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQRLSDFSGG 320
Cdd:PRK08318 239 LNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  321 AVGNTTDWKYLDINYQVIARIDQDACIGCGRCHIACEDTSHQAIASLPraDGTHRYEVIDAECVGCNLCQITCPVENCIE 400
Cdd:PRK08318 319 AVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDE--DGTRTPEVIEEECVGCNLCAHVCPVEGCIT 396

                        410       420
                 ....*....|....*....|....
gi 15595636  401 MVPQDTGKPYLNWTQDPRNPYREA 424
Cdd:PRK08318 397 MGEVKFGKPYANWTTHPNNPARAA 420
 
Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
2-424 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 833.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    2 MADLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGedPAAVNVS-SRYSAHFGPNRQVQGINNIELI 80
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG--PPIVNVSsPRFGALVKEDRRFIGFNNIELI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   81 TDRSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEM 160
Cdd:PRK08318  79 TDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVEM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  161 VTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAVKPIA 240
Cdd:PRK08318 159 YTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  241 LNMVAEIARDPQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQRLSDFSGG 320
Cdd:PRK08318 239 LNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  321 AVGNTTDWKYLDINYQVIARIDQDACIGCGRCHIACEDTSHQAIASLPraDGTHRYEVIDAECVGCNLCQITCPVENCIE 400
Cdd:PRK08318 319 AVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDE--DGTRTPEVIEEECVGCNLCAHVCPVEGCIT 396

                        410       420
                 ....*....|....*....|....
gi 15595636  401 MVPQDTGKPYLNWTQDPRNPYREA 424
Cdd:PRK08318 397 MGEVKFGKPYANWTTHPNNPARAA 420
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 4-302 0e+00

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: 510.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   4 DLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGED-PAAVNVSSRYSAHFGPNRQVQGINNIELITD 82
Cdd:cd02940   1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDkDIVTNVSPRIARLRTSGRGQIGFNNIELISE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  83 RSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEMVT 162
Cdd:cd02940  81 KPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELVEEIC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 163 RWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAVKPIALN 242
Cdd:cd02940 161 RWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVKPIALR 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 243 MVAEIARDPQtRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGL 302
Cdd:cd02940 241 AVSQIARAPE-PGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 4-315 2.09e-111

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: 328.96  E-value: 2.09e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   4 DLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGEDPAAVNVSSRYSAHFGPnrqvQGINNIELITDR 83
Cdd:COG0167   1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPED----SGLINRMGLNNP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  84 SLEINLREIAQVKKdwPDRALIVSLMVPCVEEsWKYILPLVEATGADGIELNFGCPHGmpeRGMGAAVGQVPEYVEMVTR 163
Cdd:COG0167  77 GVDAFLERLLPAKR--YDVPVIVNIGGNTVED-YVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEALAELLA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 164 WCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSItSVDLERMvaLPVVGTqsTHGGYCGSAVKPIALNM 243
Cdd:COG0167 151 AVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR-AIDLETR--RPVLAN--EAGGLSGPALKPIALRM 225

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595636 244 VAEIARDPQTRgLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQRLS 315
Cdd:COG0167 226 VREVAQAVGGD-IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 5-321 3.01e-50

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: 171.84  E-value: 3.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636     5 LSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLG-------EDPAAVNVSSRYsahfgpnrqvqgINNI 77
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGleprpgyRNPTIVETPCGM------------LNAI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    78 ELiTDRSLEINLREIAQVKKDWPdRALIVSLMVPCVEESWKYILPLVEAT-GADGIELNFGCPHGMperGMGAAVGQVPE 156
Cdd:TIGR01037  69 GL-QNPGVEAFLEELKPVREEFP-TPLIASVYGSSVEEFAEVAEKLEKAPpYVDAYELNLSCPHVK---GGGIAIGQDPE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   157 YVEMVTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSItSVDLerMVALPVVGTQSthGGYCGSAV 236
Cdd:TIGR01037 144 LSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGM-KIDI--KTGKPILANKT--GGLSGPAI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   237 KPIALNMVAEIArdpQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFrIVEDMQDGLARWMDSHGYQRLSD 316
Cdd:TIGR01037 219 KPIALRMVYDVY---KMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIEE 294


                  ....*
gi 15595636   317 FSGGA 321
Cdd:TIGR01037 295 LIGIA 299
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
5-306 2.56e-27

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 110.13  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636     5 LSIEFAGIKSPNPFWLASAppTDKAYNVVRAYQA--GWGGVVWKTLGEDPAAVNVSSRYSahfgpnRQVQGINNIELITD 82
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASG--FDKFGEEALKWLAlgKFGAIEIKSVTPYPQPGNPTPRVF------RLPEGVLNRMGLNN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    83 RSLEINLREIAQVKKDWPDRALIVSLMVP--CVE---ESWKYILPLveatgADGIELNFGCPH--GmpergmGAAVGQVP 155
Cdd:pfam01180  74 PGLDAVLAELLKRRKEYPRPDLGINLSKAgmTVDdyvEVARKIGPF-----ADYIELNVSCPNtpG------LRALQTDP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   156 EYVEMVTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSThGGYCGSA 235
Cdd:pfam01180 143 ELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILANGT-GGLSGPP 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595636   236 VKPIALNMVAEIARDPQTRgLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWM 306
Cdd:pfam01180 222 IKPIALKVIRELYQRTGPE-IPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
 
Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
2-424 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 833.05  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    2 MADLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGedPAAVNVS-SRYSAHFGPNRQVQGINNIELI 80
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG--PPIVNVSsPRFGALVKEDRRFIGFNNIELI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   81 TDRSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEM 160
Cdd:PRK08318  79 TDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVEM 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  161 VTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAVKPIA 240
Cdd:PRK08318 159 YTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPIA 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  241 LNMVAEIARDPQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQRLSDFSGG 320
Cdd:PRK08318 239 LNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVGL 318

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  321 AVGNTTDWKYLDINYQVIARIDQDACIGCGRCHIACEDTSHQAIASLPraDGTHRYEVIDAECVGCNLCQITCPVENCIE 400
Cdd:PRK08318 319 AVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWDE--DGTRTPEVIEEECVGCNLCAHVCPVEGCIT 396

                        410       420
                 ....*....|....*....|....
gi 15595636  401 MVPQDTGKPYLNWTQDPRNPYREA 424
Cdd:PRK08318 397 MGEVKFGKPYANWTTHPNNPARAA 420
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 4-302 0e+00

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: 510.29  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   4 DLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGED-PAAVNVSSRYSAHFGPNRQVQGINNIELITD 82
Cdd:cd02940   1 DLSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDkDIVTNVSPRIARLRTSGRGQIGFNNIELISE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  83 RSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPEYVEMVT 162
Cdd:cd02940  81 KPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELVEEIC 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 163 RWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAVKPIALN 242
Cdd:cd02940 161 RWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVKPIALR 240

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 243 MVAEIARDPQtRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGL 302
Cdd:cd02940 241 AVSQIARAPE-PGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 4-315 2.09e-111

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: 328.96  E-value: 2.09e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   4 DLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGEDPAAVNVSSRYSAHFGPnrqvQGINNIELITDR 83
Cdd:COG0167   1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPEPQPGNPRPRLFRLPED----SGLINRMGLNNP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  84 SLEINLREIAQVKKdwPDRALIVSLMVPCVEEsWKYILPLVEATGADGIELNFGCPHGmpeRGMGAAVGQVPEYVEMVTR 163
Cdd:COG0167  77 GVDAFLERLLPAKR--YDVPVIVNIGGNTVED-YVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEALAELLA 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 164 WCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSItSVDLERMvaLPVVGTqsTHGGYCGSAVKPIALNM 243
Cdd:COG0167 151 AVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR-AIDLETR--RPVLAN--EAGGLSGPALKPIALRM 225

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15595636 244 VAEIARDPQTRgLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQRLS 315
Cdd:COG0167 226 VREVAQAVGGD-IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFSSIS 296
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 4-326 2.83e-104

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 314.08  E-value: 2.83e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    4 DLSIEFAGIKSPNPFWLASAPPTDKaYNVV-RAYQAGWGGVVWKTLGEDPAAV-NVSSRY-----SAHFGPNRQVQGINN 76
Cdd:PLN02495  10 DLSVTVNGLKMPNPFVIGSGPPGTN-YTVMkRAFDEGWGGVIAKTVSLDASKViNVTPRYarlraGANGSAKGRVIGWQN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   77 IELITDRSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMPERGMGAAVGQVPE 156
Cdd:PLN02495  89 IELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVGQDCD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  157 YVEMVTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSTHGGYCGSAV 236
Cdd:PLN02495 169 LLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTLRPEPCVEGYSTPGGYSSKAV 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  237 KPIALNMVAEIARDPQT---RGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQR 313
Cdd:PLN02495 249 RPIALAKVMAIAKMMKSefpEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSS 328

                        330
                 ....*....|...
gi 15595636  314 LSDFSGGAVGNTT 326
Cdd:PLN02495 329 IEDFRGASLPYFT 341
PRK07259 PRK07259
dihydroorotate dehydrogenase;
4-321 1.03e-60

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 199.22  E-value: 1.03e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    4 DLSIEFAGIKSPNPFWLASA-----PPTDKAYNVVRAyqagwGGVVWKTLGEDPAAVNvssrysahfgPNRQV----QG- 73
Cdd:PRK07259   1 RLSVELPGLKLKNPVMPASGtfgfgGEYARFYDLNGL-----GAIVTKSTTLEPREGN----------PTPRIaetpGGm 65

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   74 INNIELiTDRSLEINLREIAQVKKDWpDRALIVSLMVPCVEESWKYILPLVEATGADGIELNFGCPHGMperGMGAAVGQ 153
Cdd:PRK07259  66 LNAIGL-QNPGVDAFIEEELPWLEEF-DTPIIANVAGSTEEEYAEVAEKLSKAPNVDAIELNISCPNVK---HGGMAFGT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  154 VPEYVEMVTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSItSVDLERMValPVVGTQSthGGYCG 233
Cdd:PRK07259 141 DPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINTLKGM-AIDIKTRK--PILANVT--GGLSG 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  234 SAVKPIALNMVAEIArdpQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMlHGFRIVEDMQDGLARWMDSHGYQR 313
Cdd:PRK07259 216 PAIKPIALRMVYQVY---QAVDIPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLDKYGIKS 291


                 ....*...
gi 15595636  314 LSDFSGGA 321
Cdd:PRK07259 292 IEEIVGIA 299
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 6-319 1.34e-58

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: 193.53  E-value: 1.34e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   6 SIEFAGIKSPNPFWLAS-APPTDKAY-NVVRAYQAGwgGVVWKTLGEDPAAVNVSSR---YSAHFgpnrqvqgINNIELi 80
Cdd:cd04740   1 SVELAGLRLKNPVILASgTFGFGEELsRVADLGKLG--AIVTKSITLEPREGNPPPRvveTPGGM--------LNAIGL- 69

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  81 TDRSLEINLREIAQVKKdWPDRALIVSLMVPCVEEsWKYILPLVEATGADGIELNFGCPHgmpERGMGAAVGQVPEYVEM 160
Cdd:cd04740  70 QNPGVEAFLEELLPWLR-EFGTPVIASIAGSTVEE-FVEVAEKLADAGADAIELNISCPN---VKGGGMAFGTDPEAVAE 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 161 VTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSItSVDLERmvALPVVGTqsTHGGYCGSAVKPIA 240
Cdd:cd04740 145 IVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGM-AIDIET--RKPILGN--VTGGLSGPAIKPIA 219

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595636 241 LNMVAEIArdpQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMlHGFRIVEDMQDGLARWMDSHGYQRLSDFSG 319
Cdd:cd04740 220 LRMVYQVY---KAVEIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKSIEELVG 294
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 7-297 5.71e-56

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: 186.41  E-value: 5.71e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   7 IEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGEDPAAVNVSSRYSA-HFGPNR--QVQGINNIELITDR 83
Cdd:cd02810   1 VNFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLHPRPGNPLPRVARlPPEGESypEQLGILNSFGLPNL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  84 SLEINLREIAQVKKDWPDRALIVSLMVPCVEEsWKYILPLVEATGADGIELNFGCPHGMPERGmgaaVGQVPEYVEMVTR 163
Cdd:cd02810  81 GLDVWLQDIAKAKKEFPGQPLIASVGGSSKED-YVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANLLK 155

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 164 WCKAHCSLPVIVKLTPNIT--DIRQSARAAHRGGADAVSLINTInSITSVDLERMVALPVvgtqSTHGGYCGSAVKPIAL 241
Cdd:cd02810 156 AVKAAVDIPLLVKLSPYFDleDIVELAKAAERAGADGLTAINTI-SGRVVDLKTVGPGPK----RGTGGLSGAPIRPLAL 230

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15595636 242 NMVAEIARDPQTRgLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVED 297
Cdd:cd02810 231 RWVARLAARLQLD-IPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRK 285
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 5-321 3.01e-50

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: 171.84  E-value: 3.01e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636     5 LSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLG-------EDPAAVNVSSRYsahfgpnrqvqgINNI 77
Cdd:TIGR01037   1 LEVELFGIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGleprpgyRNPTIVETPCGM------------LNAI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    78 ELiTDRSLEINLREIAQVKKDWPdRALIVSLMVPCVEESWKYILPLVEAT-GADGIELNFGCPHGMperGMGAAVGQVPE 156
Cdd:TIGR01037  69 GL-QNPGVEAFLEELKPVREEFP-TPLIASVYGSSVEEFAEVAEKLEKAPpYVDAYELNLSCPHVK---GGGIAIGQDPE 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   157 YVEMVTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSItSVDLerMVALPVVGTQSthGGYCGSAV 236
Cdd:TIGR01037 144 LSADVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGM-KIDI--KTGKPILANKT--GGLSGPAI 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   237 KPIALNMVAEIArdpQTRGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFrIVEDMQDGLARWMDSHGYQRLSD 316
Cdd:TIGR01037 219 KPIALRMVYDVY---KMVDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVYYRGF-AFKKIIEGLIAFLKAEGFTSIEE 294


                  ....*
gi 15595636   317 FSGGA 321
Cdd:TIGR01037 295 LIGIA 299
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
5-306 2.56e-27

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 110.13  E-value: 2.56e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636     5 LSIEFAGIKSPNPFWLASAppTDKAYNVVRAYQA--GWGGVVWKTLGEDPAAVNVSSRYSahfgpnRQVQGINNIELITD 82
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASG--FDKFGEEALKWLAlgKFGAIEIKSVTPYPQPGNPTPRVF------RLPEGVLNRMGLNN 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    83 RSLEINLREIAQVKKDWPDRALIVSLMVP--CVE---ESWKYILPLveatgADGIELNFGCPH--GmpergmGAAVGQVP 155
Cdd:pfam01180  74 PGLDAVLAELLKRRKEYPRPDLGINLSKAgmTVDdyvEVARKIGPF-----ADYIELNVSCPNtpG------LRALQTDP 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   156 EYVEMVTRWCKAHCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSITSVDLERMVALPVVGTQSThGGYCGSA 235
Cdd:pfam01180 143 ELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMRIDLKTEKPILANGT-GGLSGPP 221

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595636   236 VKPIALNMVAEIARDPQTRgLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWM 306
Cdd:pfam01180 222 IKPIALKVIRELYQRTGPE-IPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 339-401 6.96e-24

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: 93.88  E-value: 6.96e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595636   339 ARIDQDACIGCGRCHIACEDTSHQAIaslpRADGTHRYEVIDAECVGCNLCQITCPVENCIEM 401
Cdd:pfam14697   1 ARIDEDTCIGCGKCYIACPDTSHQAI----VGDGKRHHTVIEDECTGCNLCVSVCPVDDCITM 59
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 4-319 2.05e-22

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: 96.92  E-value: 2.05e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   4 DLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGEDpaAVNVSSRYSAHFGpnrqVQGINNIELITDR 83
Cdd:cd04739   1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEE--QIEREAQELDRFL----TYGSSFAEALSYF 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  84 --------SLEINLREIAQVKK--DWPdraLIVSLmvPCVEES-WKYILPLVEATGADGIELNFgcpHGMP--ERGMGAA 150
Cdd:cd04739  75 peygrynlGPEEYLELIRRAKRavSIP---VIASL--NGVSAGgWVDYARQIEEAGADALELNI---YALPtdPDISGAE 146

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 151 VGQVpeYVEMVTRWCKAhCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSiTSVDLERMVALPVVGTQSThgg 230
Cdd:cd04739 147 VEQR--YLDILRAVKSA-VTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNRFYQ-PDIDLETLEVVPNLLLSSP--- 219

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 231 ycGSAVKPIALNMVAEiARDpqtrGLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHG 310
Cdd:cd04739 220 --AEIRLPLRWIAILS-GRV----KASLAASGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDYIGTLLAGLEAWMEEHG 292


                ....*....
gi 15595636 311 YQRLSDFSG 319
Cdd:cd04739 293 YESVQQLRG 301
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
3-319 4.52e-20

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 90.70  E-value: 4.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    3 ADLSIEFAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTL------GEDPAAVNVSSRYSAHFG------PNRQ 70
Cdd:PRK07565   1 MDLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLfeeqirHEAAELDRHLTHGTESFAealdyfPEPA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   71 VQGInnielitdrSLEINLREIAQVKK--DWPdraLIVSLmvPCVEES-WKYILPLVEATGADGIELNFgcpHGMP--ER 145
Cdd:PRK07565  81 KFYV---------GPEEYLELIRRAKEavDIP---VIASL--NGSSAGgWVDYARQIEQAGADALELNI---YYLPtdPD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  146 GMGAAVGQVpeYVEMVTRWCKAhCSLPVIVKLTPNITDIRQSARAAHRGGADAVSLINTINSiTSVDLERMvalpvvgtq 225
Cdd:PRK07565 144 ISGAEVEQR--YLDILRAVKSA-VSIPVAVKLSPYFSNLANMAKRLDAAGADGLVLFNRFYQ-PDIDLETL--------- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  226 sthggycgsAVKPialNMV---AEIARDPQT-------R-GLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRI 294
Cdd:PRK07565 211 ---------EVVP---GLVlstPAELRLPLRwiailsgRvGADLAATTGVHDAEDVIKMLLAGADVVMIASALLRHGPDY 278

                        330       340
                 ....*....|....*....|....*
gi 15595636  295 VEDMQDGLARWMDSHGYQRLSDFSG 319
Cdd:PRK07565 279 IGTILRGLEDWMERHGYESLQQFRG 303
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 4-319 1.32e-17

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 83.08  E-value: 1.32e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636    4 DLSIEFAGIKSPNPFWLASAP--PTDKAYNVVRAYQAGwgGVVWKTLGEDPAAVNVSSRY-SAHFGpnrqvqGINNIELi 80
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVycMTKEELEEVEASAAG--AFVTKSATLEPRPGNPEPRYaDTPLG------SINSMGL- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   81 TDRSLEINLREIAQVKKDWPDRALIVSLMVPCVEESWkYILPLVEATGADG-IELNFGCPH--GMPErgmgaaVGQVPEY 157
Cdd:PRK02506  72 PNLGFDYYLDYVLELQKKGPNKPHFLSVVGLSPEETH-TILKKIQASDFNGlVELNLSCPNvpGKPQ------IAYDFET 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  158 VEMVTRWCKAHCSLPVIVKLTPNItDIRQSARAAHRGGADAVSLINTINSI-----TSVDLERMVALPVVGtqstHGGYC 232
Cdd:PRK02506 145 TEQILEEVFTYFTKPLGVKLPPYF-DIVHFDQAAAIFNKFPLAFVNCINSIgnglvIDPEDETVVIKPKNG----FGGIG 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  233 GSAVKPIAL-NMVAEIAR-DPQtrgLPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHG 310
Cdd:PRK02506 220 GDYIKPTALaNVRAFYQRlNPS---IQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKAIMAEKG 296


                 ....*....
gi 15595636  311 YQRLSDFSG 319
Cdd:PRK02506 297 YQSLEDFRG 305
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 9-306 1.53e-16

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: 79.68  E-value: 1.53e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   9 FAGIKSPNPFWLASAPPTDKAYNVVRAYQAGWGGVVWKTLGEDPAAVNVSSRYsaHFGPNrqvQGINNIELiTDRSLEIN 88
Cdd:cd04741   3 PPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRPGNPEPRY--YAFPL---GSINSLGL-PNLGLDYY 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  89 LREIAQVKKDWPDRA--LIVSL--MVPCVEESWKYILPLvEATGADGIELNFGCPH--GMPERGmgAAVGQVPEYVEMVt 162
Cdd:cd04741  77 LEYIRTISDGLPGSAkpFFISVtgSAEDIAAMYKKIAAH-QKQFPLAMELNLSCPNvpGKPPPA--YDFDATLEYLTAV- 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 163 rwcKAHCSLPVIVKLTPnITDIRQSARAAHRGGADA--VSLINTINSITS---VDLERMValPVVGTQSTHGGYCGSAVK 237
Cdd:cd04741 153 ---KAAYSIPVGVKTPP-YTDPAQFDTLAEALNAFAcpISFITATNTLGNglvLDPERET--VVLKPKTGFGGLAGAYLH 226

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595636 238 PIALNMVAEIAR--DPQTRglpICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWM 306
Cdd:cd04741 227 PLALGNVRTFRRllPSEIQ---IIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 341-405 4.50e-13

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: 64.30  E-value: 4.50e-13
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595636 341 IDQDACIGCGRCHIACEDtshQAIaslpRADGTHRYEVIDAECVGCNLCQITCPVeNCIEMVPQD 405
Cdd:COG1144  27 VDEDKCIGCGLCWIVCPD---GAI----RVDDGKYYGIDYDYCKGCGICAEVCPV-KAIEMVPEE 83
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 338-408 1.65e-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: 62.44  E-value: 1.65e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595636 338 IARIDQDACIGCGRCHIACEdtsHQAIaslpRADGTHRYEVIDAECVGCNLCQITCPvENCIEMVPQDTGK 408
Cdd:COG1149   5 IPVIDEEKCIGCGLCVEVCP---EGAI----KLDDGGAPVVDPDLCTGCGACVGVCP-TGAITLEEREAGK 67
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 337-409 8.78e-12

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 60.11  E-value: 8.78e-12
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595636 337 VIARIDQDACIGCGRCHIACEdtsHQAIAslPRADGTHRYEVIDAECVGCNLCQITCPVEnCIEMVPQDTGKP 409
Cdd:COG1146   1 MMPVIDTDKCIGCGACVEVCP---VDVLE--LDEEGKKALVINPEECIGCGACELVCPVG-AITVEDDEPEEQ 67
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
166-310 5.37e-11

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 63.64  E-value: 5.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  166 KAHCSLPVIVKLTPNITD--IRQSARAAHRGGADAVSLINTinsitSVDLERMVALPVVGTQsthGGYCGSAVKPIALNM 243
Cdd:PRK05286 207 ELHGYVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNT-----TLSRDGLKGLPNADEA---GGLSGRPLFERSTEV 278

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15595636  244 VAEIARdpQTRG-LPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHG 310
Cdd:PRK05286 279 IRRLYK--ELGGrLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 333-403 3.23e-10

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: 58.66  E-value: 3.23e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15595636   333 INYQVIARIDQDACIGCGRCHIACedtSHQAIASLPRADGThryeVIDAECVGCNLCQITCPVeNCIEMVP 403
Cdd:TIGR01944 102 IQPPMVALIDEDNCIGCTKCIQAC---PVDAIVGAAKAMHT----VIADECTGCDLCVEPCPT-DCIEMIP 164
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 172-302 3.67e-10

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: 60.98  E-value: 3.67e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 172 PVIVKLTPNITD--IRQSARAAHRGGADAVSLINTinsiTsvdLERMValpvvGTQSTH----GGYCGSAVKPIALNMVA 245
Cdd:cd04738 204 PLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNT----T---ISRPG-----LLRSPLanetGGLSGAPLKERSTEVLR 271

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15595636 246 EIARdpQTRG-LPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGL 302
Cdd:cd04738 272 ELYK--LTGGkIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 338-417 4.37e-10

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 58.80  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  338 IARIDQDACIGCGRCHIACE-DtshqAIASLPRADGThryeVIDAECVGCNLCQITCPVeNCIEMVPQDTGKPYLNWTQD 416
Cdd:PRK05113 108 VAFIDEDNCIGCTKCIQACPvD----AIVGATKAMHT----VISDLCTGCDLCVAPCPT-DCIEMIPVAETPDNWKWDLN 178


                 .
gi 15595636  417 P 417
Cdd:PRK05113 179 T 179
PRK06991 PRK06991
electron transport complex subunit RsxB;
338-415 5.27e-10

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 59.81  E-value: 5.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  338 IARIDQDACIGCGRCHIACedtSHQAIASLPRADGThryeVIDAECVGCNLCQITCPVEnCIEMVP---QDTGKPylNWT 414
Cdd:PRK06991  79 VAVIDEQLCIGCTLCMQAC---PVDAIVGAPKQMHT----VLADLCTGCDLCVPPCPVD-CIDMVPvtgERTGWD--AWS 148


                 .
gi 15595636  415 Q 415
Cdd:PRK06991 149 Q 149
PLN02826 PLN02826
dihydroorotate dehydrogenase
 171-323 2.05e-09

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 58.98  E-value: 2.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  171 LPVIVKLTPNIT--DIRQSARAAHRGGADAVSLINTINSITSvdlerMVALPVVGTQSthGGYCGSAVKPIALNMVAEIA 248
Cdd:PLN02826 263 PPLLVKIAPDLSkeDLEDIAAVALALGIDGLIISNTTISRPD-----SVLGHPHADEA--GGLSGKPLFDLSTEVLREMY 335

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595636  249 RdpQTRG-LPICGIGGIGSWRDAAEFVALGCGAVQVCTAAMLHGFRIVEDMQDGLARWMDSHGYQRLSDfsggAVG 323
Cdd:PLN02826 336 R--LTRGkIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQE----AVG 405
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 330-413 2.25e-09

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: 57.70  E-value: 2.25e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 330 YLDINYQVIARI-----DQDACIGCGRCHIACE-DtshqAIasLPRADGTHRyeVIDAECVGCNLCQITCPVeNCIEMVP 403
Cdd:COG2878 118 YDGIKDCRAAVIggpkgCEYGCIGCGDCIKACPfD----AI--VGAAKGMHT--VDEDKCTGCGLCVEACPV-DCIEMVP 188

                        90
                ....*....|
gi 15595636 404 QDTGKPYLNW 413
Cdd:COG2878 189 VSPTVVVSSW 198
NapF COG1145
Ferredoxin [Energy production and conversion];
337-405 1.25e-08

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 55.50  E-value: 1.25e-08
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595636 337 VIARIDQDACIGCGRCHIACEdtsHQAIAslpRADGTHRYEVIDAECVGCNLCQITCPVeNCIEMVPQD 405
Cdd:COG1145 175 AKAVIDAEKCIGCGLCVKVCP---TGAIR---LKDGKPQIVVDPDKCIGCGACVKVCPV-GAISLEPKE 236
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 346-395 1.49e-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: 47.91  E-value: 1.49e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 15595636   346 CIGCGRCHIACEdtsHQAIASLPR--ADGTHRYEVIDAECVGCNLCQITCPV 395
Cdd:pfam12838   1 CIGCGACVAACP---VGAITLDEVgeKKGTKTVVIDPERCVGCGACVAVCPT 49
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 343-405 2.52e-07

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: 47.43  E-value: 2.52e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595636 343 QDACIGCGRCHIACEdtsHQAIaSLPRADGTHRYEVIDAECVGCNLCQITCPVeNCIEMVPQD 405
Cdd:COG1143   1 EDKCIGCGLCVRVCP---VDAI-TIEDGEPGKVYVIDPDKCIGCGLCVEVCPT-GAISMTPFE 58
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 338-416 3.04e-07

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: 51.23  E-value: 3.04e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595636 338 IARIDQDACIGCGRCHIACEdtsHQAIASLPRADgthryEVIDAECVGCNLCQITCPvENCIEMVPQDTGKPYLNWTQD 416
Cdd:cd03110  58 KAFIDQEKCIRCGNCERVCK---FGAILEFFQKL-----IVDESLCEGCGACVIICP-RGAIYLKDRDTGKIFISSSDG 127
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
337-401 1.01e-06

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 51.01  E-value: 1.01e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595636 337 VIARIDQDACIGCGRCHIACedtSHQAIaslpRADGTHRYEVIDAECVGCNLCQITCPvENCIEM 401
Cdd:COG1148 489 SVAEVDPEKCTGCGRCVEVC---PYGAI----SIDEKGVAEVNPALCKGCGTCAAACP-SGAISL 545
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 123-288 1.07e-06

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: 49.42  E-value: 1.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 123 LVEATGADGIELNFGCPhgMP---ERGMGAAVGQVPEYVEMVTRWCKAHCSLPVIVK------LTPNITDIrqsARAAHR 193
Cdd:cd02801  75 IVEELGADGIDLNMGCP--SPkvtKGGAGAALLKDPELVAEIVRAVREAVPIPVTVKirlgwdDEEETLEL---AKALED 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 194 GGADAVSLintinsitsvdlermvalpvvgtqstHG-----GYCGSAVkpiaLNMVAEIARDPQtrgLPICGIGGIGSWR 268
Cdd:cd02801 150 AGASALTV--------------------------HGrtreqRYSGPAD----WDYIAEIKEAVS---IPVIANGDIFSLE 196

                       170       180
                ....*....|....*....|.
gi 15595636 269 DAAEFVAL-GCGAVQVCTAAM 288
Cdd:cd02801 197 DALRCLEQtGVDGVMIGRGAL 217
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 341-402 2.37e-06

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: 46.62  E-value: 2.37e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15595636 341 IDQDACIGCGRCHIACedtSHQAI----ASLPRADGTHRYEVIDAECVGCNLCQITCPVeNCIEMV 402
Cdd:cd10549  37 IDEDKCVFCGACVEVC---PTGAIeltpEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPV-DAITLE 98
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 341-403 3.17e-06

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: 46.24  E-value: 3.17e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595636 341 IDQDACIGCGRCHIACedtSHQAIaSLPRADGTHRYEVIDAE-CVGCNLCQITCPVeNCIEMVP 403
Cdd:cd10549   3 YDPEKCIGCGICVKAC---PTDAI-ELGPNGAIARGPEIDEDkCVFCGACVEVCPT-GAIELTP 61
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 123-281 3.18e-06

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: 48.55  E-value: 3.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 123 LVEATGADGIELNFGCPhgMP---ERGMGAAVGQVPEYVEMVTRWCKAHCSLPVIVKL-------TPNITDIrqsARAAH 192
Cdd:COG0042  82 IAEELGADEIDINMGCP--VKkvtKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIrlgwdddDENALEF---ARIAE 156

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 193 RGGADAVSLintinsitsvdlermvalpvvgtqstHG-----GYcgsavKPIA-LNMVAEIARDpqtRGLPICGIGGIGS 266
Cdd:COG0042 157 DAGAAALTV--------------------------HGrtreqRY-----KGPAdWDAIARVKEA---VSIPVIGNGDIFS 202

                       170
                ....*....|....*.
gi 15595636 267 WRDAAEFVAL-GCGAV 281
Cdd:COG0042 203 PEDAKRMLEEtGCDGV 218
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 333-396 5.99e-06

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 43.89  E-value: 5.99e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595636 333 INYQVIARIDQDACIGCGRCHIACEdtsHQAIaslpRADGtHRYEVIDAECVGCNLCQITCPVE 396
Cdd:COG2221   4 IIGTWPPKIDEEKCIGCGLCVAVCP---TGAI----SLDD-GKLVIDEEKCIGCGACIRVCPTG 59
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
339-406 1.73e-05

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 42.41  E-value: 1.73e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595636 339 ARIDQDACIGCGRCHIACedtSHQAIaslpraDGTHRYEVIDAE-CVGCNLCQITCPVeNCIEMVPQDT 406
Cdd:COG2768   6 PYVDEEKCIGCGACVKVC---PVGAI------SIEDGKAVIDPEkCIGCGACIEVCPV-GAIKIEWEED 64
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 80-285 1.78e-05

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: 45.27  E-value: 1.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  80 ITDRSLEINLREIAQVKKDWPDRALIVSLMV-PCVEEsWKYILPLVEATGADGIELNFGCPHGMPErgmgaavgqVPEYV 158
Cdd:cd04722  36 SDPEEAETDDKEVLKEVAAETDLPLGVQLAInDAAAA-VDIAAAAARAAGADGVEIHGAVGYLARE---------DLELI 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 159 EMVtrwCKAHCSLPVIVKLTPNITDIRqsaRAAHRGGADAVSLINTInsitsvdlermvalpvvgtqsthGGYCGSAVKP 238
Cdd:cd04722 106 REL---REAVPDVKVVVKLSPTGELAA---AAAEEAGVDEVGLGNGG-----------------------GGGGGRDAVP 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*..
gi 15595636 239 IALNMVAEIARDPqtrGLPICGIGGIGSWRDAAEFVALGCGAVQVCT 285
Cdd:cd04722 157 IADLLLILAKRGS---KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 339-402 2.10e-05

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 42.34  E-value: 2.10e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595636 339 ARIDQDACIGCGRCHIACEdtshqAIAsLPRADGTHryeVID-AECVGCNLCQITCPVeNCIEMV 402
Cdd:COG4231  17 YVIDEDKCTGCGACVKVCP-----ADA-IEEGDGKA---VIDpDLCIGCGSCVQVCPV-DAIKLE 71
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 340-394 3.72e-05

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: 41.08  E-value: 3.72e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 15595636   340 RIDQDACIGCGRCHIACEDTSHQAIASLPRADGTHRyEVIDAECVGCNLCQITCP 394
Cdd:pfam13237   3 VIDPDKCIGCGRCTAACPAGLTRVGAIVERLEGEAV-RIGVWKCIGCGACVEACP 56
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 341-402 4.58e-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: 42.77  E-value: 4.58e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595636 341 IDQDACIGCGRCHIACEdtsHQAIASlpRADGTHryeVIDAE-CVGCNLCQITCPVeNCIEMV 402
Cdd:cd10549  75 IDEEKCIGCGLCVKVCP---VDAITL--EDELEI---VIDKEkCIGCGICAEVCPV-NAIKLV 128
fdxN_nitrog TIGR02936
ferredoxin III, nif-specific; Members of this family are homodimeric ferredoxins from nitrogen ...
 336-403 7.16e-05

ferredoxin III, nif-specific; Members of this family are homodimeric ferredoxins from nitrogen fixation regions of many nitrogen-fixing bacteria. As characterized in Rhodobacter capsulatus, these proteins are homodimeric, with two 4Fe-4S clusters bound per monomer. Although nif-specific, this protein family is not usiveral, as other nitrogenase systems may substitute flavodoxins, or different types of ferredoxin. [Central intermediary metabolism, Nitrogen fixation]


Pssm-ID: 274356 [Multi-domain]  Cd Length: 91  Bit Score: 41.24  E-value: 7.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   336 QVIARIDQDACIGCGRCHIAC--------EDTSHQAIASLPRADG--THRYEVID--AECVGCNLCQITCPvENCIEMVP 403
Cdd:TIGR02936  13 QFVTSIDQEKCIGCGRCYKVCgrdvltlkGINEEGELVASDDDDDeiERKVMVVAnpGNCIGCGACARVCP-KKCQTHAP 91
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 338-403 1.02e-04

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: 42.24  E-value: 1.02e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595636 338 IARIDQDACI------GCGRCHIACEdtsHQAIASLPRADGTHRYeVIDAECVGCNLCQITCPVEN--CIEMVP 403
Cdd:cd16373  85 VAVIDKDRCLawqggtDCGVCVEACP---TEAIAIVLEDDVLRPV-VDEDKCVGCGLCEYVCPVEPpkAIVVEP 154
NapF_like cd10564
NapF, iron-sulfur subunit of periplasmic nitrate reductase; This family contains NapF protein, ...
 336-404 1.54e-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: 41.46  E-value: 1.54e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595636 336 QVIARIdQDAC-----IGCGRCHIACEDtshQAIASLPRADGTHRYEVIDAECVGCNLCQITCPVeNCIEMVPQ 404
Cdd:cd10564  71 PLRAEI-GDSClalqgVECRSCQDACPT---QAIRFRPRLGGIALPELDADACTGCGACVSVCPV-GAITLTPL 139
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 123-201 2.09e-04

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: 43.08  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636   123 LVEATGADGIELNFGCP-HGMPERGMGAAVGQVPEYVEMVTRWCKAHCSLPVIVKLTPNITDIRQS----ARAAHRGGAD 197
Cdd:pfam01207  74 LVEDRGADGIDINMGCPsKKVTRGGGGAALLRNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENaveiAKIVEDAGAQ 153


                  ....
gi 15595636   198 AVSL 201
Cdd:pfam01207 154 ALTV 157
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
338-402 4.56e-04

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 40.29  E-value: 4.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15595636  338 IARIDQDACIGCGRCHIACedtSHQAIAslprADGTHRYEVIDAECVGCNLCQITCPVEnCIEMV 402
Cdd:PRK08764  79 VAWIVEADCIGCTKCIQAC---PVDAIV----GGAKHMHTVIAPLCTGCELCVPACPVD-CIELH 135
PRK14028 PRK14028
pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional
 310-402 5.25e-04

pyruvate ferredoxin oxidoreductase subunit gamma/delta; Provisional


Pssm-ID: 172522 [Multi-domain]  Cd Length: 312  Bit Score: 41.91  E-value: 5.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636  310 GYQRLSdfSGGAVGNTTDWKYLDINYQVIAR-IDQDACIGCGRCHIACEDTShqAIASLPRADGTH----RYEVID---A 381
Cdd:PRK14028 214 GWQEVN--KAGAVFPGSSFPYLTGGWRIDKPvIDHSKCIMCRKCWLYCPDDA--IIEAWREAEGPRgrkfRMKMIDfdyQ 289

                         90       100
                 ....*....|....*....|.
gi 15595636  382 ECVGCNLCQITCPVeNCIEMV 402
Cdd:PRK14028 290 YCKGCGVCAEVCPT-GAIQMV 309
DMSOR_beta_like cd16367
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 341-402 7.67e-04

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: 319889 [Multi-domain]  Cd Length: 138  Bit Score: 39.60  E-value: 7.67e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 341 IDQDACIGCGRCHIACEDTsHQAIASLPR---------------------------ADGTHRYE----VIDAECVGCNLC 389
Cdd:cd16367  16 IDLDRCIRCDNCEKACADT-HDGHSRLDRnglrfgnllvptacrhcvdpvcmigcpTGAIHRDDggevVISDACCGCGNC 94

                        90
                ....*....|...
gi 15595636 390 QITCPVENcIEMV 402
Cdd:cd16367  95 ASACPYGA-IQMV 106
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 146-286 1.05e-03

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 40.54  E-value: 1.05e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 146 GMG--AAVGQVPEYVEMVTRWCKAHCSLPVIVKLT--PNITDIRQSARAAHRGGADAVSL----------------INTI 205
Cdd:cd04730  27 GLGfiGAGYLTPEALRAEIRKIRALTDKPFGVNLLvpSSNPDFEALLEVALEEGVPVVSFsfgppaevverlkaagIKVI 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15595636 206 NSITSVDLERMV------ALPVVGTQSthGGYCGS-AVKPIALnmVAEIARdpqTRGLPICGIGGIGSWRDAAEFVALGC 278
Cdd:cd04730 107 PTVTSVEEARKAeaagadALVAQGAEA--GGHRGTfDIGTFAL--VPEVRD---AVDIPVIAAGGIADGRGIAAALALGA 179


                ....*...
gi 15595636 279 GAVQVCTA 286
Cdd:cd04730 180 DGVQMGTR 187
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
346-403 1.16e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 39.48  E-value: 1.16e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15595636  346 CIGCGRCHIACedtSHQAIA--SLPRADG---THRYEvID-AECVGCNLCQITCPVeNCIEMVP 403
Cdd:PRK05888  60 CIACKLCAAIC---PADAITieAAEREDGrrrTTRYD-INfGRCIFCGFCEEACPT-DAIVETP 118
NuoI TIGR01971
NADH-quinone oxidoreductase, chain I; This model represents the I subunit (one of 14: A->N) of ...
 368-411 1.55e-03

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: 38.17  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15595636   368 PRADGTH---RYEVIDAECVGCNLCQITCPVeNCIEMVPQ--DTGKPYL 411
Cdd:TIGR01971  27 PRFRGRIvltRDPNGEEKCIGCTLCAAVCPA-DAIRVVPAegEDGKRRL 74
GlpC COG0247
Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy ...
 344-395 2.88e-03

Fe-S cluster-containing oxidoreductase, includes glycolate oxidase subunit GlcF [Energy production and conversion];


Pssm-ID: 440017 [Multi-domain]  Cd Length: 420  Bit Score: 39.68  E-value: 2.88e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15595636 344 DACIGCGRCHIAC--------EDTSHQAIASLPRA--------DGTHR-YEVIDAeCVGCNLCQITCPV 395
Cdd:COG0247  78 DACVGCGFCRAMCpsykatgdEKDSPRGRINLLREvlegelplDLSEEvYEVLDL-CLTCKACETACPS 145
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
368-401 3.29e-03

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 37.94  E-value: 3.29e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 15595636  368 PRADGTH---RYEVIDAECVGCNLCQITCPVeNCIEM 401
Cdd:PRK05888  42 PRFRGRHalrRDPNGEERCIACKLCAAICPA-DAITI 77
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
340-394 3.55e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 38.89  E-value: 3.55e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15595636 340 RIDQDACIGCGRCHIACEdtSHQAIaslpradgtHRYEVIDAECVGCNLCQITCP 394
Cdd:COG0348 206 RYDRGDCIDCGLCVKVCP--MGIDI---------RKGEINQSECINCGRCIDACP 249
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 338-356 3.63e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 37.54  E-value: 3.63e-03
                        10
                ....*....|....*....
gi 15595636 338 IARIDQDACIGCGRCHIAC 356
Cdd:cd16371  78 IVVVDQDKCIGCGYCVWAC 96
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
338-356 4.51e-03

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 35.86  E-value: 4.51e-03
                        10
                ....*....|....*....
gi 15595636 338 IARIDQDACIGCGRCHIAC 356
Cdd:COG2768  34 KAVIDPEKCIGCGACIEVC 52
Fer4_6 pfam12837
4Fe-4S binding domain; This superfamily includes proteins containing domains which bind to ...
 338-356 5.47e-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: 34.13  E-value: 5.47e-03
                          10
                  ....*....|....*....
gi 15595636   338 IARIDQDACIGCGRCHIAC 356
Cdd:pfam12837   1 VVEVDPDKCIGCGRCVVVC 19
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
333-395 8.86e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 38.08  E-value: 8.86e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15595636 333 INYQVIARIDQDACIGCGRCHIACedtSHQAIASlprADGTHryEVIDAECVGCNLCQITCPV 395
Cdd:COG4624  80 DKRGPSIIRDKEKCKNCYPCVRAC---PVKAIKV---DDGKA--EIDEEKCISCGQCVAVCPF 134
 
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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