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Conserved domains on  [gi|502833261|ref|WP_013068237|]
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NAD-dependent dihydropyrimidine dehydrogenase subunit PreA [Rhodobacter capsulatus]

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;
1-430 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


:

Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 826.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   1 MANLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGldgPPVVNVSGPRYGAIHGPDGTLLGLNNIEL 80
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG---PPIVNVSSPRFGALVKEDRRFIGFNNIEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  81 ITDRPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDSWKSILARVEETEADGVELNFGCPHGMAERGMGAAVGQVPDYVE 160
Cdd:PRK08318  78 ITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 161 MVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTIDGFGTHGGYCGPAVKPI 240
Cdd:PRK08318 158 MYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 241 ALNMVAEIARNPATRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTETREIVG 320
Cdd:PRK08318 238 ALNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 321 RAVPKVTDWQYLNLNYTTKASIAQDDCIKCGRCHIVCEDTSHQAIAM--AADRTVTVKEEECVACNLCVEVCPTK-CITM 397
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWdeDGTRTPEVIEEECVGCNLCAHVCPVEgCITM 397

                        410       420       430
                 ....*....|....*....|....*....|...
gi 502833261 398 RELSEGeldlrtakpvGDYLNWTGHPNNPMATT 430
Cdd:PRK08318 398 GEVKFG----------KPYANWTTHPNNPARAA 420
 
Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
1-430 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 826.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   1 MANLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGldgPPVVNVSGPRYGAIHGPDGTLLGLNNIEL 80
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG---PPIVNVSSPRFGALVKEDRRFIGFNNIEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  81 ITDRPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDSWKSILARVEETEADGVELNFGCPHGMAERGMGAAVGQVPDYVE 160
Cdd:PRK08318  78 ITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 161 MVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTIDGFGTHGGYCGPAVKPI 240
Cdd:PRK08318 158 MYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 241 ALNMVAEIARNPATRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTETREIVG 320
Cdd:PRK08318 238 ALNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 321 RAVPKVTDWQYLNLNYTTKASIAQDDCIKCGRCHIVCEDTSHQAIAM--AADRTVTVKEEECVACNLCVEVCPTK-CITM 397
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWdeDGTRTPEVIEEECVGCNLCAHVCPVEgCITM 397

                        410       420       430
                 ....*....|....*....|....*....|...
gi 502833261 398 RELSEGeldlrtakpvGDYLNWTGHPNNPMATT 430
Cdd:PRK08318 398 GEVKFG----------KPYANWTTHPNNPARAA 420
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 4-303 1.46e-178

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: 499.89  E-value: 1.46e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   4 LTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDGPPVVNVSgPRYGAIHGPDGTLLGLNNIELITD 83
Cdd:cd02940    2 LSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVS-PRIARLRTSGRGQIGFNNIELISE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  84 RPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDSWKSILARVEETEADGVELNFGCPHGMAERGMGAAVGQVPDYVEMVT 163
Cdd:cd02940   81 KPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELVEEIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 164 RWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTIDGFGTHGGYCGPAVKPIALN 243
Cdd:cd02940  161 RWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVKPIALR 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 244 MVAEIARNPAtRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGL 303
Cdd:cd02940  241 AVSQIARAPE-PGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-313 7.60e-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: 327.80  E-value: 7.60e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   3 NLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDgpPVVNVSGPRYGAIHGPDGtllgLNNIELIT 82
Cdd:COG0167    1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPE--PQPGNPRPRLFRLPEDSG----LINRMGLN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  83 DRPLEVNLREIKSVKRdyPDRALVVSLMVPCDEDsWKSILARVEETEADGVELNFGCPHGmaeRGMGAAVGQVPDYVEMV 162
Cdd:COG0167   75 NPGVDAFLERLLPAKR--YDVPVIVNIGGNTVED-YVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEALAEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 163 TRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSItsvDLDLFAPQPTIDgfGTHGGYCGPAVKPIAL 242
Cdd:COG0167  149 LAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR---AIDLETRRPVLA--NEAGGLSGPALKPIAL 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502833261 243 NMVAEIARNPATRgLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLT 313
Cdd:COG0167  224 RMVREVAQAVGGD-IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFS 293
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 10-322 1.55e-55

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: 186.09  E-value: 1.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   10 GIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGL------DGPPVVNVSGPRYGAIhgpdgtllGLNNielitd 83
Cdd:TIGR01037   7 GIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLeprpgyRNPTIVETPCGMLNAI--------GLQN------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   84 rP-LEVNLREIKSVKRDYPdRALVVSLMvPCDEDSWKSILARVEETE--ADGVELNFGCPHGMaerGMGAAVGQVPDYVE 160
Cdd:TIGR01037  73 -PgVEAFLEELKPVREEFP-TPLIASVY-GSSVEEFAEVAEKLEKAPpyVDAYELNLSCPHVK---GGGIAIGQDPELSA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  161 MVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITsvdLDLFAPQPTIDgfGTHGGYCGPAVKPI 240
Cdd:TIGR01037 147 DVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMK---IDIKTGKPILA--NKTGGLSGPAIKPI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  241 ALNMVAEIARNpatRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMtYGFKIVEEMISGLSDYMDRKGLTETREIVG 320
Cdd:TIGR01037 222 ALRMVYDVYKM---VDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVY-YRGFAFKKIIEGLIAFLKAEGFTSIEELIG 297


                  ..
gi 502833261  321 RA 322
Cdd:TIGR01037 298 IA 299
dihydoor_dh_Arch NF041011
dihydroorotate dehydrogenase PyrD;
10-323 9.73e-39

dihydroorotate dehydrogenase PyrD;


Pssm-ID: 468940  Cd Length: 289  Bit Score: 141.23  E-value: 9.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  10 GIKSPNPFWLASA-PPTDKEVNVRRAFEAGWGGVVWKTLGLDG-----PPVVnvsgprygaIHGPDGTLL---GLNNiel 80
Cdd:NF041011   5 GLELEDPLIIASGiLPDVPEYIERVCEKYGPSAITTKTLTLNPlephkPPTV---------VKLHDGCYLnaiGLGN--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  81 itdrPlevNLREIKSVKRDYpdRALVVSLMvPCDEDSWKSILARVEETeADGVELNFGCPHgmaERGMGAavgQVPDYVE 160
Cdd:NF041011  73 ----P---GIGLLEEIRVKL--CPLIVSIG-GSSLEEIVEVAEIAEEK-ADAIELNLSSPN---RKGYGA---SLASLVR 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 161 MVTRWVKQHSRMPCIVKLTP--NISDIrkpAEAAKRGGADAVSLINTINSItSVDLDLFAPqptIDGFGThGGYCGPAVK 238
Cdd:NF041011 136 EIVKAVKSVVKKPVFVKLGPwdNVLEI---AGKALEAGADGLTLINTVKGM-AIDVESFKP---VLSYGT-GGISGKCIH 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 239 PIALNMVAEIARNPATrglPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTeTREI 318
Cdd:NF041011 208 PLAVRIIYDVYREYEA---EIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDI 283


                 ....*
gi 502833261 319 VGRAV 323
Cdd:NF041011 284 IGIAV 288
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
4-307 4.21e-31

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 120.53  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261    4 LTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDGPPvvnvsG---PRYgaIHGPDGTL--LGLNNI 78
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQP-----GnptPRV--FRLPEGVLnrMGLNNP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   79 ELitdrplEVNLREIKSVKRDYPDRALVVSLMVP-CDEDSWKSILARVEETeADGVELNFGCPH--GmaergmGAAVGQV 155
Cdd:pfam01180  75 GL------DAVLAELLKRRKEYPRPDLGINLSKAgMTVDDYVEVARKIGPF-ADYIELNVSCPNtpG------LRALQTD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  156 PDYVEMVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVD-LDLFAPQPtIDGFGThGGYCG 234
Cdd:pfam01180 142 PELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMrIDLKTEKP-ILANGT-GGLSG 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502833261  235 PAVKPIALNMVAEIARNPATRgLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYM 307
Cdd:pfam01180 220 PPIKPIALKVIRELYQRTGPE-IPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 367-399 3.75e-04

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 41.77  E-value: 3.75e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 502833261 367 MAADRTVTVkEEECVACNLCVEVCPTKCITMRE 399
Cdd:NF038196 175 KVKDKKFHV-TDKCIGCGICAKVCPVNNIEMED 206
 
Name Accession Description Interval E-value
PRK08318 PRK08318
NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;
1-430 0e+00

NAD-dependent dihydropyrimidine dehydrogenase subunit PreA;


Pssm-ID: 236237 [Multi-domain]  Cd Length: 420  Bit Score: 826.51  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   1 MANLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGldgPPVVNVSGPRYGAIHGPDGTLLGLNNIEL 80
Cdd:PRK08318   1 MADLSITFCGIKSPNPFWLASAPPTNKYYNVARAFEAGWGGVVWKTLG---PPIVNVSSPRFGALVKEDRRFIGFNNIEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  81 ITDRPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDSWKSILARVEETEADGVELNFGCPHGMAERGMGAAVGQVPDYVE 160
Cdd:PRK08318  78 ITDRPLEVNLREIRRVKRDYPDRALIASIMVECNEEEWKEIAPLVEETGADGIELNFGCPHGMSERGMGSAVGQVPELVE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 161 MVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTIDGFGTHGGYCGPAVKPI 240
Cdd:PRK08318 158 MYTRWVKRGSRLPVIVKLTPNITDIREPARAAKRGGADAVSLINTINSITGVDLDRMIPMPIVNGKSSHGGYCGPAVKPI 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 241 ALNMVAEIARNPATRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTETREIVG 320
Cdd:PRK08318 238 ALNMVAEIARDPETRGLPISGIGGIETWRDAAEFILLGAGTVQVCTAAMQYGFRIVEDMISGLSHYMDEKGFASLEDMVG 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 321 RAVPKVTDWQYLNLNYTTKASIAQDDCIKCGRCHIVCEDTSHQAIAM--AADRTVTVKEEECVACNLCVEVCPTK-CITM 397
Cdd:PRK08318 318 LAVPNVTDWEDLDLNYIVYARIDQDKCIGCGRCYIACEDTSHQAIEWdeDGTRTPEVIEEECVGCNLCAHVCPVEgCITM 397

                        410       420       430
                 ....*....|....*....|....*....|...
gi 502833261 398 RELSEGeldlrtakpvGDYLNWTGHPNNPMATT 430
Cdd:PRK08318 398 GEVKFG----------KPYANWTTHPNNPARAA 420
DHPD_FMN cd02940
Dihydropyrimidine dehydrogenase (DHPD) FMN-binding domain. DHPD catalyzes the first step in ...
 4-303 1.46e-178

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: 499.89  E-value: 1.46e-178
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   4 LTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDGPPVVNVSgPRYGAIHGPDGTLLGLNNIELITD 83
Cdd:cd02940    2 LSVTFCGIKFPNPFGLASAPPTTSYPMIRRAFEAGWGGAVTKTLGLDKDIVTNVS-PRIARLRTSGRGQIGFNNIELISE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  84 RPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDSWKSILARVEETEADGVELNFGCPHGMAERGMGAAVGQVPDYVEMVT 163
Cdd:cd02940   81 KPLEYWLKEIRELKKDFPDKILIASIMCEYNKEDWTELAKLVEEAGADALELNFSCPHGMPERGMGAAVGQDPELVEEIC 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 164 RWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTIDGFGTHGGYCGPAVKPIALN 243
Cdd:cd02940  161 RWVREAVKIPVIAKLTPNITDIREIARAAKEGGADGVSAINTVNSLMGVDLDGTPPAPGVEGKTTYGGYSGPAVKPIALR 240

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 244 MVAEIARNPAtRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGL 303
Cdd:cd02940  241 AVSQIARAPE-PGLPISGIGGIESWEDAAEFLLLGASVVQVCTAVMNQGFTIVDDMCTGL 299
PLN02495 PLN02495
oxidoreductase, acting on the CH-CH group of donors
 3-327 2.90e-111

oxidoreductase, acting on the CH-CH group of donors


Pssm-ID: 215273 [Multi-domain]  Cd Length: 385  Bit Score: 332.19  E-value: 2.90e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   3 NLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDGPPVVNVSgPRY-----GAIHGPDGTLLGLNN 77
Cdd:PLN02495  10 DLSVTVNGLKMPNPFVIGSGPPGTNYTVMKRAFDEGWGGVIAKTVSLDASKVINVT-PRYarlraGANGSAKGRVIGWQN 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  78 IELITDRPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDSWKSILARVEETEADGVELNFGCPHGMAERGMGAAVGQVPD 157
Cdd:PLN02495  89 IELISDRPFETMLAEFKQLKEEYPDRILIASIMEEYNKDAWEEIIERVEETGVDALEINFSCPHGMPERKMGAAVGQDCD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 158 YVEMVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTIDGFGTHGGYCGPAV 237
Cdd:PLN02495 169 LLEEVCGWINAKATVPVWAKMTPNITDITQPARVALKSGCEGVAAINTIMSVMGINLDTLRPEPCVEGYSTPGGYSSKAV 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 238 KPIALNMVAEIARNPAT---RGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTE 314
Cdd:PLN02495 249 RPIALAKVMAIAKMMKSefpEDRSLSGIGGVETGGDAAEFILLGADTVQVCTGVMMHGYPLVKNLCAELQDFMKKHNFSS 328

                        330
                 ....*....|...
gi 502833261 315 TREIVGRAVPKVT 327
Cdd:PLN02495 329 IEDFRGASLPYFT 341
PyrD COG0167
Dihydroorotate dehydrogenase [Nucleotide transport and metabolism]; Dihydroorotate ...
 3-313 7.60e-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: 327.80  E-value: 7.60e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   3 NLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDgpPVVNVSGPRYGAIHGPDGtllgLNNIELIT 82
Cdd:COG0167    1 DLSVELAGLKFPNPVGLASGFFDKNAEYIDALDLLGFGAVEVKTVTPE--PQPGNPRPRLFRLPEDSG----LINRMGLN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  83 DRPLEVNLREIKSVKRdyPDRALVVSLMVPCDEDsWKSILARVEETEADGVELNFGCPHGmaeRGMGAAVGQVPDYVEMV 162
Cdd:COG0167   75 NPGVDAFLERLLPAKR--YDVPVIVNIGGNTVED-YVELARRLADAGADYLELNISCPNT---PGGGRALGQDPEALAEL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 163 TRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSItsvDLDLFAPQPTIDgfGTHGGYCGPAVKPIAL 242
Cdd:COG0167  149 LAAVKAATDKPVLVKLAPDLTDIVEIARAAEEAGADGVIAINTTLGR---AIDLETRRPVLA--NEAGGLSGPALKPIAL 223

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502833261 243 NMVAEIARNPATRgLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLT 313
Cdd:COG0167  224 RMVREVAQAVGGD-IPIIGVGGISTAEDALEFILAGASAVQVGTALFYEGPGLVRRIIRGLEAYLEEKGFS 293
PRK07259 PRK07259
dihydroorotate dehydrogenase;
3-322 6.27e-61

dihydroorotate dehydrogenase;


Pssm-ID: 235982  Cd Length: 301  Bit Score: 199.99  E-value: 6.27e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   3 NLTSTFLGIKSPNPFWLASA-----PPTDKEVNVRRAfeagwGGVVWKTLGLDgppvvnvsgPRYG-----AIHGPDGTL 72
Cdd:PRK07259   1 RLSVELPGLKLKNPVMPASGtfgfgGEYARFYDLNGL-----GAIVTKSTTLE---------PREGnptprIAETPGGML 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  73 --LGLNNielitdrP-LEVNLREIKSVKRDYpDRALVVSLMVPCDEDsWKSILARVEET-EADGVELNFGCPHGMaerGM 148
Cdd:PRK07259  67 naIGLQN-------PgVDAFIEEELPWLEEF-DTPIIANVAGSTEEE-YAEVAEKLSKApNVDAIELNISCPNVK---HG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 149 GAAVGQVPDYVEMVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTinsITSVDLDLFAPQPtIDGFGT 228
Cdd:PRK07259 135 GMAFGTDPELAYEVVKAVKEVVKVPVIVKLTPNVTDIVEIAKAAEEAGADGLSLINT---LKGMAIDIKTRKP-ILANVT 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 229 hGGYCGPAVKPIALNMVAEIARnpATRgLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMtYGFKIVEEMISGLSDYMD 308
Cdd:PRK07259 211 -GGLSGPAIKPIALRMVYQVYQ--AVD-IPIIGMGGISSAEDAIEFIMAGASAVQVGTANF-YDPYAFPKIIEGLEAYLD 285

                        330
                 ....*....|....
gi 502833261 309 RKGLTETREIVGRA 322
Cdd:PRK07259 286 KYGIKSIEEIVGIA 299
DHOD_1B_like cd04740
Dihydroorotate dehydrogenase (DHOD) class 1B FMN-binding domain. DHOD catalyzes the oxidation ...
 7-322 6.23e-59

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: 194.69  E-value: 6.23e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   7 TFLGIKSPNPFWLAS----APPTDKEV-NVRRAfeagwGGVVWKTLGLD------GPPVVNVSGPRYGAIhgpdgtllGL 75
Cdd:cd04740    3 ELAGLRLKNPVILASgtfgFGEELSRVaDLGKL-----GAIVTKSITLEpregnpPPRVVETPGGMLNAI--------GL 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  76 NNielitdrP-LEVNLREIKSVKRDYpDRALVVSLMVPCDEDsWKSILARVEETEADGVELNFGCPHgmAERGmGAAVGQ 154
Cdd:cd04740   70 QN-------PgVEAFLEELLPWLREF-GTPVIASIAGSTVEE-FVEVAEKLADAGADAIELNISCPN--VKGG-GMAFGT 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 155 VPDYVEMVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSItSVDLDLFAPqptIDGFGThGGYCG 234
Cdd:cd04740  138 DPEAVAEIVKAVKKATDVPVIVKLTPNVTDIVEIARAAEEAGADGLTLINTLKGM-AIDIETRKP---ILGNVT-GGLSG 212

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 235 PAVKPIALNMVAEIARnpATrGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMtYGFKIVEEMISGLSDYMDRKGLTE 314
Cdd:cd04740  213 PAIKPIALRMVYQVYK--AV-EIPIIGVGGIASGEDALEFLMAGASAVQVGTANF-VDPEAFKEIIEGLEAYLDEEGIKS 288


                 ....*...
gi 502833261 315 TREIVGRA 322
Cdd:cd04740  289 IEELVGLA 296
pyrD_sub1_fam TIGR01037
dihydroorotate dehydrogenase (subfamily 1) family protein; This family includes subfamily 1 ...
 10-322 1.55e-55

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: 186.09  E-value: 1.55e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   10 GIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGL------DGPPVVNVSGPRYGAIhgpdgtllGLNNielitd 83
Cdd:TIGR01037   7 GIRFKNPLILASGIMGSGVESLRRIDRSGAGAVVTKSIGLeprpgyRNPTIVETPCGMLNAI--------GLQN------ 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   84 rP-LEVNLREIKSVKRDYPdRALVVSLMvPCDEDSWKSILARVEETE--ADGVELNFGCPHGMaerGMGAAVGQVPDYVE 160
Cdd:TIGR01037  73 -PgVEAFLEELKPVREEFP-TPLIASVY-GSSVEEFAEVAEKLEKAPpyVDAYELNLSCPHVK---GGGIAIGQDPELSA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  161 MVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITsvdLDLFAPQPTIDgfGTHGGYCGPAVKPI 240
Cdd:TIGR01037 147 DVVKAVKDKTDVPVFAKLSPNVTDITEIAKAAEEAGADGLTLINTLRGMK---IDIKTGKPILA--NKTGGLSGPAIKPI 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  241 ALNMVAEIARNpatRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMtYGFKIVEEMISGLSDYMDRKGLTETREIVG 320
Cdd:TIGR01037 222 ALRMVYDVYKM---VDIPIIGVGGITSFEDALEFLMAGASAVQVGTAVY-YRGFAFKKIIEGLIAFLKAEGFTSIEELIG 297


                  ..
gi 502833261  321 RA 322
Cdd:TIGR01037 298 IA 299
DHOD_DHPD_FMN cd02810
Dihydroorotate dehydrogenase (DHOD) and Dihydropyrimidine dehydrogenase (DHPD) FMN-binding ...
 7-300 8.98e-50

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: 170.61  E-value: 8.98e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   7 TFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDgpPVVNVSGPRYGAIHGPDGTL---LGLNNIELITD 83
Cdd:cd02810    2 NFLGLKLKNPFGVAAGPLLKTGELIARAAAAGFGAVVYKTVTLH--PRPGNPLPRVARLPPEGESYpeqLGILNSFGLPN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  84 RPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDsWKSILARVEETEADGVELNFGCPHGMAERGmgaaVGQVPDYVEMVT 163
Cdd:cd02810   80 LGLDVWLQDIAKAKKEFPGQPLIASVGGSSKED-YVELARKIERAGAKALELNLSCPNVGGGRQ----LGQDPEAVANLL 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 164 RWVKQHSRMPCIVKLTPNISDIRKP--AEAAKRGGADAVSLINTInsitsVDLDLFAPQPTIDGFGTHGGYCGPAVKPIA 241
Cdd:cd02810  155 KAVKAAVDIPLLVKLSPYFDLEDIVelAKAAERAGADGLTAINTI-----SGRVVDLKTVGPGPKRGTGGLSGAPIRPLA 229

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 242 LNMVAEI-ARNPAtrGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMI 300
Cdd:cd02810  230 LRWVARLaARLQL--DIPIIGVGGIDSGEDVLEMLMAGASAVQVATALMWDGPDVIRKIK 287
dihydoor_dh_Arch NF041011
dihydroorotate dehydrogenase PyrD;
10-323 9.73e-39

dihydroorotate dehydrogenase PyrD;


Pssm-ID: 468940  Cd Length: 289  Bit Score: 141.23  E-value: 9.73e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  10 GIKSPNPFWLASA-PPTDKEVNVRRAFEAGWGGVVWKTLGLDG-----PPVVnvsgprygaIHGPDGTLL---GLNNiel 80
Cdd:NF041011   5 GLELEDPLIIASGiLPDVPEYIERVCEKYGPSAITTKTLTLNPlephkPPTV---------VKLHDGCYLnaiGLGN--- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  81 itdrPlevNLREIKSVKRDYpdRALVVSLMvPCDEDSWKSILARVEETeADGVELNFGCPHgmaERGMGAavgQVPDYVE 160
Cdd:NF041011  73 ----P---GIGLLEEIRVKL--CPLIVSIG-GSSLEEIVEVAEIAEEK-ADAIELNLSSPN---RKGYGA---SLASLVR 135

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 161 MVTRWVKQHSRMPCIVKLTP--NISDIrkpAEAAKRGGADAVSLINTINSItSVDLDLFAPqptIDGFGThGGYCGPAVK 238
Cdd:NF041011 136 EIVKAVKSVVKKPVFVKLGPwdNVLEI---AGKALEAGADGLTLINTVKGM-AIDVESFKP---VLSYGT-GGISGKCIH 207

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 239 PIALNMVAEIARNPATrglPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTeTREI 318
Cdd:NF041011 208 PLAVRIIYDVYREYEA---EIIGVGGVFSWRDAIELMSVGAKAVGVGTAIIDKGLSVISEIRKGLEEYLEEKGLK-LEDI 283


                 ....*
gi 502833261 319 VGRAV 323
Cdd:NF041011 284 IGIAV 288
DHO_dh pfam01180
Dihydroorotate dehydrogenase;
4-307 4.21e-31

Dihydroorotate dehydrogenase;


Pssm-ID: 426103  Cd Length: 291  Bit Score: 120.53  E-value: 4.21e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261    4 LTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDGPPvvnvsG---PRYgaIHGPDGTL--LGLNNI 78
Cdd:pfam01180   2 LATKIPGLDFKNPIGLASGFDKFGEEALKWLALGKFGAIEIKSVTPYPQP-----GnptPRV--FRLPEGVLnrMGLNNP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   79 ELitdrplEVNLREIKSVKRDYPDRALVVSLMVP-CDEDSWKSILARVEETeADGVELNFGCPH--GmaergmGAAVGQV 155
Cdd:pfam01180  75 GL------DAVLAELLKRRKEYPRPDLGINLSKAgMTVDDYVEVARKIGPF-ADYIELNVSCPNtpG------LRALQTD 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  156 PDYVEMVTRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTINSITSVD-LDLFAPQPtIDGFGThGGYCG 234
Cdd:pfam01180 142 PELAAILLKVVKEVSKVPVLVKLAPDLTDIVIIDIADVALGEDGLDGINATNTTVRGMrIDLKTEKP-ILANGT-GGLSG 219

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502833261  235 PAVKPIALNMVAEIARNPATRgLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYM 307
Cdd:pfam01180 220 PPIKPIALKVIRELYQRTGPE-IPIIGVGGIESGEDALEKILAGASAVQIGTALIFGGPFIFPKIIDELPELL 291
Fer4_21 pfam14697
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 340-397 1.51e-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: 95.81  E-value: 1.51e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 502833261  340 ASIAQDDCIKCGRCHIVCEDTSHQAIAMAADRTVTVKEEECVACNLCVEVCPT-KCITM 397
Cdd:pfam14697   1 ARIDEDTCIGCGKCYIACPDTSHQAIVGDGKRHHTVIEDECTGCNLCVSVCPVdDCITM 59
DHOD_1A_like cd04741
Dihydroorotate dehydrogenase (DHOD) class 1A FMN-binding domain. DHOD catalyzes the oxidation ...
 7-307 5.49e-18

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: 83.91  E-value: 5.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   7 TFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDGPPvvNVSGPRYGAihGPDGTL--LGLNNielitdR 84
Cdd:cd04741    2 TPPGLTISPPLMNAAGPWCTTLEDLLELAASSTGAVTTRSSTLAGRP--GNPEPRYYA--FPLGSInsLGLPN------L 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  85 PLEVNLREIKSVKRDYPDRA--LVVSL--MVpcdEDSWKSiLARVEETE---ADGVELNFGCPH--GMAERGMGAavgqv 155
Cdd:cd04741   72 GLDYYLEYIRTISDGLPGSAkpFFISVtgSA---EDIAAM-YKKIAAHQkqfPLAMELNLSCPNvpGKPPPAYDF----- 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 156 pDYVEMVTRWVKQHSRMPCIVKLTPnISDIRKPAEAAKRGGADA--VSLINTINSITS-VDLDLFAPQPTIDGFGTHGGY 232
Cdd:cd04741  143 -DATLEYLTAVKAAYSIPVGVKTPP-YTDPAQFDTLAEALNAFAcpISFITATNTLGNgLVLDPERETVVLKPKTGFGGL 220

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502833261 233 CGPAVKPIALNMVAEIaRNPATRGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYM 307
Cdd:cd04741  221 AGAYLHPLALGNVRTF-RRLLPSEIQIIGVGGVLDGRGAFRMRLAGASAVQVGTALGKEGPKVFARIEKELEDIW 294
DHOD_like cd04739
Dihydroorotate dehydrogenase (DHOD) like proteins. DHOD catalyzes the oxidation of (S) ...
 3-332 1.22e-16

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: 80.35  E-value: 1.22e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   3 NLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTLGLDgpPVVNVSgprygAIHGPDGTLlGLNNIELIT 82
Cdd:cd04739    1 DLSTTYLGLSLKNPLVASASPLSRNLDNIRRLEDAGAGAIVLPSLFEE--QIEREA-----QELDRFLTY-GSSFAEALS 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  83 DRP--------LEVNLREIKSVKR--DYPdraLVVSLMVPCDeDSWKSILARVEETEADGVELN-FGCPHGMAERGmgAA 151
Cdd:cd04739   73 YFPeygrynlgPEEYLELIRRAKRavSIP---VIASLNGVSA-GGWVDYARQIEEAGADALELNiYALPTDPDISG--AE 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 152 VGQVpdYVEMVtRWVKQHSRMPCIVKLTPNISDIRKPAEAAKRGGADAVSLINTinsitsvdldlfAPQPTIDgfgthgg 231
Cdd:cd04739  147 VEQR--YLDIL-RAVKSAVTIPVAVKLSPFFSALAHMAKQLDAAGADGLVLFNR------------FYQPDID------- 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 232 ycgpavkpI-ALNMVAE-IARNPATRGLPISGI--------------GGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKI 295
Cdd:cd04739  205 --------LeTLEVVPNlLLSSPAEIRLPLRWIailsgrvkaslaasGGVHDAEDVVKYLLAGADVVMTTSALLRHGPDY 276

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 502833261 296 VEEMISGLSDYMDRKGLTETREIVG----RAVPKVTDW---QYL 332
Cdd:cd04739  277 IGTLLAGLEAWMEEHGYESVQQLRGsmsqKNVPDPAAFeraQYM 320
PRK07565 PRK07565
dihydroorotate dehydrogenase-like protein;
2-321 2.04e-16

dihydroorotate dehydrogenase-like protein;


Pssm-ID: 236051  Cd Length: 334  Bit Score: 79.91  E-value: 2.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   2 ANLTSTFLGIKSPNPFWLASAPPTDKEVNVRRAFEAGWGGVVWKTL----------GLDGPpvvnvsgprygAIHGPDGT 71
Cdd:PRK07565   1 MDLSTTYLGLTLRNPLVASASPLSESVDNVKRLEDAGAGAVVLKSLfeeqirheaaELDRH-----------LTHGTESF 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  72 LLGLNNIELITDRPLEVN--LREIKSVKR--DYPdraLVVSLmvPCDEDS-WKSILARVEETEADGVELN-FGCPHGMAE 145
Cdd:PRK07565  70 AEALDYFPEPAKFYVGPEeyLELIRRAKEavDIP---VIASL--NGSSAGgWVDYARQIEQAGADALELNiYYLPTDPDI 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 146 RGmgAAVGQVpdYVEMVTRwVKQHSRMPCIVKLTPNISDirkPAEAAKR---GGADAVSLINTinsitsvdldlfAPQPT 222
Cdd:PRK07565 145 SG--AEVEQR--YLDILRA-VKSAVSIPVAVKLSPYFSN---LANMAKRldaAGADGLVLFNR------------FYQPD 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 223 IDgfgthggycgpavkpiaLNMVAEIAR----NPATRGLPISGI--------------GGVTTWRDAAEFMALGAHNVQV 284
Cdd:PRK07565 205 ID-----------------LETLEVVPGlvlsTPAELRLPLRWIailsgrvgadlaatTGVHDAEDVIKMLLAGADVVMI 267

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 502833261 285 CTAVMTYGFKIVEEMISGLSDYMDRKGLTETREIVGR 321
Cdd:PRK07565 268 ASALLRHGPDYIGTILRGLEDWMERHGYESLQQFRGS 304
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 339-405 2.18e-15

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 70.53  E-value: 2.18e-15
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502833261 339 KASIAQDDCIKCGRCHIVCEdtsHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMRELSEGEL 405
Cdd:COG1149    5 IPVIDEEKCIGCGLCVEVCP---EGAIKLDDGGAPVVDPDLCTGCGACVGVCPTGAITLEEREAGKI 68
PRK02506 PRK02506
dihydroorotate dehydrogenase 1A; Reviewed
 3-321 1.39e-14

dihydroorotate dehydrogenase 1A; Reviewed


Pssm-ID: 235045  Cd Length: 310  Bit Score: 74.22  E-value: 1.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   3 NLTSTFLGIKSPNPFWLASAP--PTDKEVNVRRAFEAGwgGVVWKTLGLDgPPVVNVSgPRYGAIhgPDGTL--LGLNNI 78
Cdd:PRK02506   1 STSTQIAGFKFDNCLMNAAGVycMTKEELEEVEASAAG--AFVTKSATLE-PRPGNPE-PRYADT--PLGSInsMGLPNL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  79 ELitDRPLEVNLReiksVKRDYPDRALVVSLMVPCDEDSWkSILARVEETEADG-VELNFGCPH--GMAErgmgaaVGQV 155
Cdd:PRK02506  75 GF--DYYLDYVLE----LQKKGPNKPHFLSVVGLSPEETH-TILKKIQASDFNGlVELNLSCPNvpGKPQ------IAYD 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 156 PDYVEMVTRWVKQHSRMPCIVKLTP--NISDIRKPAEAAKRGGadaVSLINTINSITS---VDLDlfAPQPTI---DGFG 227
Cdd:PRK02506 142 FETTEQILEEVFTYFTKPLGVKLPPyfDIVHFDQAAAIFNKFP---LAFVNCINSIGNglvIDPE--DETVVIkpkNGFG 216

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 228 thgGYCGPAVKPIAL-NMVAEIAR-NPatrGLPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSD 305
Cdd:PRK02506 217 ---GIGGDYIKPTALaNVRAFYQRlNP---SIQIIGTGGVKTGRDAFEHILCGASMVQVGTALHKEGPAVFERLTKELKA 290

                        330
                 ....*....|....*.
gi 502833261 306 YMDRKGLTETREIVGR 321
Cdd:PRK02506 291 IMAEKGYQSLEDFRGK 306
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 342-399 2.83e-14

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: 67.77  E-value: 2.83e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 342 IAQDDCIKCGRCHIVCEDtshQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG1144   27 VDEDKCIGCGLCWIVCPD---GAIRVDDGKYYGIDYDYCKGCGICAEVCPVKAIEMVP 81
PreA COG1146
NAD-dependent dihydropyrimidine dehydrogenase, PreA subunit [Nucleotide transport and ...
 338-404 3.42e-13

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


Pssm-ID: 440761 [Multi-domain]  Cd Length: 67  Bit Score: 64.35  E-value: 3.42e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502833261 338 TKASIAQDDCIKCGRCHIVCEdtsHQAIAMAAD--RTVTVKEEECVACNLCVEVCPTKCITMRELSEGE 404
Cdd:COG1146    1 MMPVIDTDKCIGCGACVEVCP---VDVLELDEEgkKALVINPEECIGCGACELVCPVGAITVEDDEPEE 66
RnfB COG2878
Na+-translocating ferredoxin:NAD+ oxidoreductase RNF, RnfB subunit [Energy production and ...
 345-402 1.03e-12

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: 67.71  E-value: 1.03e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502833261 345 DDCIKCGRCHIVCE-DtshqAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMRELSE 402
Cdd:COG2878  137 YGCIGCGDCIKACPfD----AIVGAAKGMHTVDEDKCTGCGLCVEACPVDCIEMVPVSP 191
PRK05286 PRK05286
quinone-dependent dihydroorotate dehydrogenase;
167-311 2.28e-12

quinone-dependent dihydroorotate dehydrogenase;


Pssm-ID: 235388  Cd Length: 344  Bit Score: 67.88  E-value: 2.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 167 KQHSRMPCIVKLTPNISD--IRKPAEAAKRGGADAVSLINTinsitSVDLDLFAPQPTIDGFGthgGYCGPAVKPIALNM 244
Cdd:PRK05286 207 ELHGYVPLLVKIAPDLSDeeLDDIADLALEHGIDGVIATNT-----TLSRDGLKGLPNADEAG---GLSGRPLFERSTEV 278

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 245 VAEIARnpATRG-LPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKG 311
Cdd:PRK05286 279 IRRLYK--ELGGrLPIIGVGGIDSAEDAYEKIRAGASLVQIYSGLIYEGPGLVKEIVRGLARLLRRDG 344
NuoI COG1143
Formate hydrogenlyase subunit 6/NADH:ubiquinone oxidoreductase 23 kD subunit (chain I) [Energy ...
 344-399 8.03e-12

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: 60.14  E-value: 8.03e-12
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502833261 344 QDDCIKCGRCHIVCEdtsHQAIAMAAD---RTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG1143    1 EDKCIGCGLCVRVCP---VDAITIEDGepgKVYVIDPDKCIGCGLCVEVCPTGAISMTP 56
PLN02826 PLN02826
dihydroorotate dehydrogenase
 171-320 3.35e-11

dihydroorotate dehydrogenase


Pssm-ID: 178421  Cd Length: 409  Bit Score: 64.76  E-value: 3.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 171 RMPCIVKLTPNIS--DIRKPAEAAKRGGADAVSLINTINSITSVDLDLFAPQPTidgfgthGGYCGPAVKPIALNMVAEI 248
Cdd:PLN02826 262 PPPLLVKIAPDLSkeDLEDIAAVALALGIDGLIISNTTISRPDSVLGHPHADEA-------GGLSGKPLFDLSTEVLREM 334

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502833261 249 ARnpATRG-LPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTETREIVG 320
Cdd:PLN02826 335 YR--LTRGkIPLVGCGGVSSGEDAYKKIRAGASLVQLYTAFAYEGPALIPRIKAELAACLERDGFKSIQEAVG 405
DHOD_2_like cd04738
Dihydroorotate dehydrogenase (DHOD) class 2. DHOD catalyzes the oxidation of (S) ...
 173-303 9.47e-11

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: 62.52  E-value: 9.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 173 PCIVKLTPNISD--IRKPAEAAKRGGADAVSLINTinsitSVDLDLFAPQPTIDGfgtHGGYCGPAVKPIALNMVAEIAR 250
Cdd:cd04738  204 PLLVKIAPDLSDeeLEDIADVALEHGVDGIIATNT-----TISRPGLLRSPLANE---TGGLSGAPLKERSTEVLRELYK 275

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502833261 251 npATRG-LPISGIGGVTTWRDAAEFMALGAHNVQVCTAVMTYGFKIVEEMISGL 303
Cdd:cd04738  276 --LTGGkIPIIGVGGISSGEDAYEKIRAGASLVQLYTGLVYEGPGLVKRIKREL 327
NapF COG1145
Ferredoxin [Energy production and conversion];
276-399 1.32e-10

Ferredoxin [Energy production and conversion];


Pssm-ID: 440760 [Multi-domain]  Cd Length: 238  Bit Score: 61.28  E-value: 1.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 276 ALGAHNVQVCTAVMTYGFKIVEEMISGLSDYMDRKGLTETREIVGRAVPKVTDWQYLNLNYTT-KASIAQDDCIKCGRCH 354
Cdd:COG1145  112 RLIISAVKLVAGLVVAAGEVLLVIAAALAEAGLAILGAAAPVDALAISGGKKIEEELKIAIKKaKAVIDAEKCIGCGLCV 191

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 502833261 355 IVCEdtsHQAIAMAADR-TVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG1145  192 KVCP---TGAIRLKDGKpQIVVDPDKCIGCGACVKVCPVGAISLEP 234
rnfB TIGR01944
electron transport complex, RnfABCDGE type, B subunit; The six subunit complex RnfABCDGE in ...
 340-399 4.63e-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: 58.27  E-value: 4.63e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  340 ASIAQDDCIKCGRCHIVCedtSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:TIGR01944 108 ALIDEDNCIGCTKCIQAC---PVDAIVGAAKAMHTVIADECTGCDLCVEPCPTDCIEMIP 164
IorA COG4231
TPP-dependent indolepyruvate ferredoxin oxidoreductase, alpha subunit [Energy production and ...
 335-399 8.07e-10

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


Pssm-ID: 443375 [Multi-domain]  Cd Length: 76  Bit Score: 55.05  E-value: 8.07e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 335 NYTT--KASIAQDDCIKCGRCHIVCEdtshqAIAMAA-DRTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG4231   10 NRTTamRYVIDEDKCTGCGACVKVCP-----ADAIEEgDGKAVIDPDLCIGCGSCVQVCPVDAIKLEK 72
COG2768 COG2768
Uncharacterized Fe-S cluster protein [Function unknown];
339-405 3.04e-09

Uncharacterized Fe-S cluster protein [Function unknown];


Pssm-ID: 442050 [Multi-domain]  Cd Length: 74  Bit Score: 53.20  E-value: 3.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502833261 339 KASIAQDDCIKCGRCHIVCedtSHQAIAMAaDRTVTVKEEECVACNLCVEVCPTKCITMRELSEGEL 405
Cdd:COG2768    5 KPYVDEEKCIGCGACVKVC---PVGAISIE-DGKAVIDPEKCIGCGACIEVCPVGAIKIEWEEDEEF 67
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 337-396 3.47e-09

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 52.75  E-value: 3.47e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 337 TTKASIAQDDCIKCGRCHIVCEdtsHQAIAMAaDRTVTVKEEECVACNLCVEVCPTKCIT 396
Cdd:COG2221    7 TWPPKIDEEKCIGCGLCVAVCP---TGAISLD-DGKLVIDEEKCIGCGACIRVCPTGAIK 62
PRK05113 PRK05113
electron transport complex protein RnfB; Provisional
 340-402 9.15e-09

electron transport complex protein RnfB; Provisional


Pssm-ID: 235347 [Multi-domain]  Cd Length: 191  Bit Score: 54.95  E-value: 9.15e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502833261 340 ASIAQDDCIKCGRCHIVCE-DtshqAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMRELSE 402
Cdd:PRK05113 109 AFIDEDNCIGCTKCIQACPvD----AIVGATKAMHTVISDLCTGCDLCVAPCPTDCIEMIPVAE 168
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 333-399 9.63e-09

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: 53.55  E-value: 9.63e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502833261 333 NLNYTTKASIAQDDCIKCGRCHIVC-----EDTSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:cd10549   28 NGAIARGPEIDEDKCVFCGACVEVCptgaiELTPEGKEYVPKEKEAEIDEEKCIGCGLCVKVCPVDAITLED 99
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 339-397 1.04e-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: 53.17  E-value: 1.04e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502833261 339 KASIAQDDCIKCGRCHIVCEdtsHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITM 397
Cdd:cd10549   72 EAEIDEEKCIGCGLCVKVCP---VDAITLEDELEIVIDKEKCIGCGICAEVCPVNAIKL 127
MtMvhB_like cd10549
Uncharacterized polyferredoxin-like protein; This family contains uncharacterized ...
 344-402 1.82e-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: 52.78  E-value: 1.82e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502833261 344 QDDCIKCGRCHIVCedtSHQAIAMAAD----RTVTVKEEECVACNLCVEVCPTKCITMRELSE 402
Cdd:cd10549    5 PEKCIGCGICVKAC---PTDAIELGPNgaiaRGPEIDEDKCVFCGACVEVCPTGAIELTPEGK 64
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 347-394 4.62e-08

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: 49.06  E-value: 4.62e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 502833261  347 CIKCGRCHIVCEdtsHQAIAMAAD------RTVTVKEEECVACNLCVEVCPTKC 394
Cdd:pfam12838   1 CIGCGACVAACP---VGAITLDEVgekkgtKTVVIDPERCVGCGACVAVCPTGA 51
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
347-399 2.07e-07

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 52.24  E-value: 2.07e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502833261 347 CIKCGRCHIVCEDtshQAIAMAADRTVtVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:PRK07118 215 CIGCGKCVKACPA---GAITMENNLAV-IDQEKCTSCGKCVEKCPTKAIRILN 263
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 123-289 6.76e-07

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: 50.19  E-value: 6.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 123 ARVEETEADGVELNFGCPHGMAER-GMGAAVGQVPDYVEMVTRWVKQHSRMPCIVK------LTPNISDIrkpAEAAKRG 195
Cdd:cd02801   74 KIVEELGADGIDLNMGCPSPKVTKgGAGAALLKDPELVAEIVRAVREAVPIPVTVKirlgwdDEEETLEL---AKALEDA 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 196 GADAVSLintinsitsvdldlfapqptidgfgtHG-----GYCGPAVkpiaLNMVAEIARNPatrGLPISGIGGVTTWRD 270
Cdd:cd02801  151 GASALTV--------------------------HGrtreqRYSGPAD----WDYIAEIKEAV---SIPVIANGDIFSLED 197

                        170
                 ....*....|....*....
gi 502833261 271 AAEFMALGAhnvqvCTAVM 289
Cdd:cd02801  198 ALRCLEQTG-----VDGVM 211
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
345-398 1.33e-06

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 49.68  E-value: 1.33e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502833261 345 DDCIKCGRCHIVCEdtSHQAIamaadRTVTVKEEECVACNLCVEVCPTKCITMR 398
Cdd:COG0348  210 GDCIDCGLCVKVCP--MGIDI-----RKGEINQSECINCGRCIDACPKDAIRFS 256
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
342-398 2.15e-06

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 49.64  E-value: 2.15e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502833261 342 IAQDDCIKCGRCHIVCedtSHQAIAMAaDRTVTVKEEECVACNLCVEVCPTKCITMR 398
Cdd:COG4624   88 RDKEKCKNCYPCVRAC---PVKAIKVD-DGKAEIDEEKCISCGQCVAVCPFGAITEK 140
PRK06991 PRK06991
electron transport complex subunit RsxB;
340-397 2.48e-06

electron transport complex subunit RsxB;


Pssm-ID: 235903 [Multi-domain]  Cd Length: 270  Bit Score: 48.64  E-value: 2.48e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 340 ASIAQDDCIKCGRCHIVCedtSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITM 397
Cdd:PRK06991  80 AVIDEQLCIGCTLCMQAC---PVDAIVGAPKQMHTVLADLCTGCDLCVPPCPVDCIDM 134
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
338-398 4.38e-06

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


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 48.70  E-value: 4.38e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502833261 338 TKASIAQDDCIKCGRCHIVCedtSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMR 398
Cdd:COG1148  489 SVAEVDPEKCTGCGRCVEVC---PYGAISIDEKGVAEVNPALCKGCGTCAAACPSGAISLK 546
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
377-397 1.22e-05

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 45.26  E-value: 1.22e-05
                         10        20
                 ....*....|....*....|.
gi 502833261 377 EEECVACNLCVEVCPTKCITM 397
Cdd:PRK05888  57 EERCIACKLCAAICPADAITI 77
vorD PRK09623
3-methyl-2-oxobutanoate dehydrogenase subunit delta;
328-397 1.62e-05

3-methyl-2-oxobutanoate dehydrogenase subunit delta;


Pssm-ID: 170016 [Multi-domain]  Cd Length: 105  Bit Score: 43.78  E-value: 1.62e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 328 DWQylnlnyTTKASIAQDDCIKCGRCHIVCEDTshqAIAMAADRTVTVKEEECVACNLCVEVCPTKCITM 397
Cdd:PRK09623  40 DWR------TFMPVVDESKCVKCYICWKFCPEP---AIYIKEDGYVAIDYDYCKGCGICANECPTKAITM 100
DsrA COG2221
Dissimilatory sulfite reductase (desulfoviridin), alpha and beta subunits [Inorganic ion ...
 371-399 3.24e-05

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


Pssm-ID: 441823 [Multi-domain]  Cd Length: 69  Bit Score: 41.58  E-value: 3.24e-05
                         10        20
                 ....*....|....*....|....*....
gi 502833261 371 RTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG2221    8 WPPKIDEEKCIGCGLCVAVCPTGAISLDD 36
PRK08348 PRK08348
NADH-plastoquinone oxidoreductase subunit; Provisional
 345-397 3.70e-05

NADH-plastoquinone oxidoreductase subunit; Provisional


Pssm-ID: 181399 [Multi-domain]  Cd Length: 120  Bit Score: 42.90  E-value: 3.70e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502833261 345 DDCIKCGRCHIVCedTSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITM 397
Cdd:PRK08348  42 DKCVGCRMCVTVC--PAGVFVYLPEIRKVALWTGRCVFCGQCVDVCPTGALQM 92
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 340-397 4.99e-05

Beta subunit of the DMSO Reductase (DMSOR) 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: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 42.76  E-value: 4.99e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502833261 340 ASIAQDDCIKCGRCHIVCEdtsHQAIAMAADRTVTVKeeeCVACN---------LCVEVCPTKCITM 397
Cdd:cd04410   75 VLIDEDKCIGCGSCVEACP---YGAIVFDPEPGKAVK---CDLCGdrldeglepACVKACPTGALTF 135
porD PRK09625
pyruvate flavodoxin oxidoreductase subunit delta; Reviewed
 345-392 5.33e-05

pyruvate flavodoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 236596 [Multi-domain]  Cd Length: 133  Bit Score: 42.81  E-value: 5.33e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502833261 345 DDCIKCGRCHIVCEDTShqaIAMAADRTVTVKEEECVACNLCVEVCPT 392
Cdd:PRK09625  59 EICINCFNCWVYCPDAA---ILSRDKKLKGVDYSHCKGCGVCVEVCPT 103
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 70-286 6.06e-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: 43.73  E-value: 6.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261  70 GTLLGLNNIELITDRPLEVNLREIKSVKRDYPDRALVVSLMVPCDEDsWKSILARVEETEADGVELNFGCPHGMAErgmg 149
Cdd:cd04722   26 ADAIIVGTRSSDPEEAETDDKEVLKEVAAETDLPLGVQLAINDAAAA-VDIAAAAARAAGADGVEIHGAVGYLARE---- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 150 aavgqvpdYVEMVtRWVKQH-SRMPCIVKLTPNISDIRKPAEAAkrgGADAVSLINTInsitsvdldlfapqptidgfgt 228
Cdd:cd04722  101 --------DLELI-RELREAvPDVKVVVKLSPTGELAAAAAEEA---GVDEVGLGNGG---------------------- 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 229 hGGYCGPAVKPIAlnMVAEIARNPATrGLPISGIGGVTTWRDAAEFMALGAHNVQVCT 286
Cdd:cd04722  147 -GGGGGRDAVPIA--DLLLILAKRGS-KVPVIAGGGINDPEDAAEALALGADGVIVGS 200
PRK05888 PRK05888
NADH-quinone oxidoreductase subunit NuoI;
347-397 9.36e-05

NADH-quinone oxidoreductase subunit NuoI;


Pssm-ID: 235637 [Multi-domain]  Cd Length: 164  Bit Score: 42.56  E-value: 9.36e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 347 CIKCGRCHIVCedtSHQAIAM-AADRTVTVKEEE--------CVACNLCVEVCPTKCITM 397
Cdd:PRK05888  60 CIACKLCAAIC---PADAITIeAAEREDGRRRTTrydinfgrCIFCGFCEEACPTDAIVE 116
PRK08764 PRK08764
Rnf electron transport complex subunit RnfB;
340-398 9.50e-05

Rnf electron transport complex subunit RnfB;


Pssm-ID: 181550 [Multi-domain]  Cd Length: 135  Bit Score: 42.22  E-value: 9.50e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 502833261 340 ASIAQDDCIKCGRCHIVCedtSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCITMR 398
Cdd:PRK08764  80 AWIVEADCIGCTKCIQAC---PVDAIVGGAKHMHTVIAPLCTGCELCVPACPVDCIELH 135
Fer4 pfam00037
4Fe-4S binding domain; Superfamily includes proteins containing domains which bind to ...
 373-396 1.27e-04

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: 38.77  E-value: 1.27e-04
                          10        20
                  ....*....|....*....|....
gi 502833261  373 VTVKEEECVACNLCVEVCPTKCIT 396
Cdd:pfam00037   1 VVIDEEKCIGCGACVEVCPVGAIT 24
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 342-399 1.45e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 41.17  E-value: 1.45e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 342 IAQDDCIKCGRCHIVCedtSHQAIAMAADRTVTVKeeeCVACNLCVEVCPTKCITMRE 399
Cdd:cd16372   74 INKKLCVGCLMCVGFC---PEGAMFKHEDYPEPFK---CIACGICVKACPTGALELVE 125
PRK06273 PRK06273
ferredoxin; Provisional
 374-418 1.53e-04

ferredoxin; Provisional


Pssm-ID: 235764 [Multi-domain]  Cd Length: 165  Bit Score: 42.00  E-value: 1.53e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 502833261 374 TVKEEECVACNLCVEVCPTKCITMRELSEGELD---LRTAKPVGDYLN 418
Cdd:PRK06273  45 KVFEELCIGCGGCANVCPTKAIEMIPVEPVKITegyVKTKIPKIDYEK 92
Fer4_10 pfam13237
4Fe-4S dicluster domain; This family includes proteins containing domains which bind to ...
 345-391 1.71e-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: 39.16  E-value: 1.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 502833261  345 DDCIKCGRCHIVC--EDTSHQAIAMAADRTVTVKE-EECVACNLCVEVCP 391
Cdd:pfam13237   7 DKCIGCGRCTAACpaGLTRVGAIVERLEGEAVRIGvWKCIGCGACVEACP 56
Fer4_9 pfam13187
4Fe-4S dicluster domain;
346-395 1.71e-04

4Fe-4S dicluster domain;


Pssm-ID: 463801 [Multi-domain]  Cd Length: 50  Bit Score: 39.07  E-value: 1.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 502833261  346 DCIKCGRCHIVCEDTSHQAIAMAADRTVTVKEEECVACNLCVEVCPTKCI 395
Cdd:pfam13187   1 KCTGCGACVAACPAGAIVPDLVGQTIRGDIAGLACIGCGACVDACPRGAI 50
SIMIBI_bact_arch cd03110
bacterial and archaeal subfamily of SIMIBI; Uncharacterized bacterial and archaeal subfamily ...
 339-405 2.03e-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: 42.76  E-value: 2.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502833261 339 KASIAQDDCIKCGRCHIVCEdtsHQAIAMAADRTVtVKEEECVACNLCVEVCPTKCITMRELSEGEL 405
Cdd:cd03110   58 KAFIDQEKCIRCGNCERVCK---FGAILEFFQKLI-VDESLCEGCGACVIICPRGAIYLKDRDTGKI 120
porD PRK09624
pyruvate ferredoxin oxidoreductase subunit delta; Reviewed
 344-399 2.65e-04

pyruvate ferredoxin oxidoreductase subunit delta; Reviewed


Pssm-ID: 170017 [Multi-domain]  Cd Length: 105  Bit Score: 40.01  E-value: 2.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 502833261 344 QDDCIKCGRCHIVCEDTshqAIAMAADRTVTVKEEECVACNLCVEVCPTKCITM-RE 399
Cdd:PRK09624  50 RDKCVRCYLCYIYCPEP---AIYLDEEGYPVFDYDYCKGCGICANECPTKAIEMvRE 103
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 339-392 2.79e-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: 41.09  E-value: 2.79e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502833261 339 KASIAQDDCI------KCGRCHIVCEdtsHQAIAMAADRTV---TVKEEECVACNLCVEVCPT 392
Cdd:cd16373   85 VAVIDKDRCLawqggtDCGVCVEACP---TEAIAIVLEDDVlrpVVDEDKCVGCGLCEYVCPV 144
DMSOR_beta_like cd16371
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 344-399 2.81e-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: 319893 [Multi-domain]  Cd Length: 140  Bit Score: 41.01  E-value: 2.81e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502833261 344 QDDCIKCGRCHIVCEDTsHQAIAMAADRTVTVKEEE----------CVACN-----LCVEVCPTKCITMRE 399
Cdd:cd16371    6 QERCIGCKACEIACKDK-NDLPPGVNWRRVYEYEGGefpevfayflSMSCNhcenpACVKVCPTGAITKRE 75
COG1149 COG1149
MinD superfamily P-loop ATPase, contains an inserted ferredoxin domain [General function ...
 371-399 2.95e-04

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


Pssm-ID: 440763 [Multi-domain]  Cd Length: 68  Bit Score: 38.94  E-value: 2.95e-04
                         10        20
                 ....*....|....*....|....*....
gi 502833261 371 RTVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG1149    4 KIPVIDEEKCIGCGLCVEVCPEGAIKLDD 32
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
342-396 3.38e-04

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 40.41  E-value: 3.38e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502833261 342 IAQDDCIKCGRCHIVCedtSHQAIAMAA--DRTVTVKeeeCVACN------LCVEVCPTKCIT 396
Cdd:COG1142   78 VDEEKCIGCGLCVLAC---PFGAITMVGekSRAVAVK---CDLCGgreggpACVEACPTGALR 134
DMSOR_beta_like cd16373
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 380-409 3.43e-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: 40.70  E-value: 3.43e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 502833261 380 CVACNLCVEVCPTKCITMRELSEGELDLRT 409
Cdd:cd16373   16 CIRCGLCVEACPTGVIQPAGLEDGLEGGRT 45
ferrodoxin_EFR1 NF038196
EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight ...
 367-399 3.75e-04

EFR1 family ferrodoxin; Members of the family have a C-terminal ferrodoxin domain, with eight conserved Cys residues in two CxxCxxCxxxCP motifs, each of which binds a 4Fe-4S cluster. The N-terminal region resembles flavodoxin domains, with some members of the family recognized by Pfam models PF12724 (Flavodoxin_5) or PF00258 (Flavodoxin_1).


Pssm-ID: 468407 [Multi-domain]  Cd Length: 243  Bit Score: 41.77  E-value: 3.75e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 502833261 367 MAADRTVTVkEEECVACNLCVEVCPTKCITMRE 399
Cdd:NF038196 175 KVKDKKFHV-TDKCIGCGICAKVCPVNNIEMED 206
DusA COG0042
tRNA-dihydrouridine synthase [Translation, ribosomal structure and biogenesis]; ...
 123-289 4.98e-04

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: 42.00  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 123 ARVEETEADGVELNFGCPHGM-AERGMGAAVGQVPDYVEMVTRWVKQHSRMPCIVKL-------TPNISDIrkpAEAAKR 194
Cdd:COG0042   81 RIAEELGADEIDINMGCPVKKvTKGGAGAALLRDPELVAEIVKAVVEAVDVPVTVKIrlgwdddDENALEF---ARIAED 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 195 GGADAVSLintinsitsvdldlfapqptidgfgtHG-----GYCGPAvkpiALNMVAEIARNpatRGLPISGIGGVTTWR 269
Cdd:COG0042  158 AGAAALTV--------------------------HGrtreqRYKGPA----DWDAIARVKEA---VSIPVIGNGDIFSPE 204

                        170       180
                 ....*....|....*....|
gi 502833261 270 DAAEFMALGAhnvqvCTAVM 289
Cdd:COG0042  205 DAKRMLEETG-----CDGVM 219
PRK13795 PRK13795
hypothetical protein; Provisional
 347-391 6.59e-04

hypothetical protein; Provisional


Pssm-ID: 237510 [Multi-domain]  Cd Length: 636  Bit Score: 41.90  E-value: 6.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 502833261 347 CIKCGRCHIVCedtSHQAIAM-AADRTVTVKEEECVACNLCVEVCP 391
Cdd:PRK13795 583 CVGCGVCVGAC---PTGAIRIeEGKRKISVDEEKCIHCGKCTEVCP 625
PRK12387 PRK12387
formate hydrogenlyase complex iron-sulfur subunit; Provisional
 345-395 6.62e-04

formate hydrogenlyase complex iron-sulfur subunit; Provisional


Pssm-ID: 183492 [Multi-domain]  Cd Length: 180  Bit Score: 40.40  E-value: 6.62e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502833261 345 DDCIKCGRCHIVCEDtshQAIAMAADRTVTVKEEE-----CVACNLCVEVCPTKCI 395
Cdd:PRK12387  38 QQCIGCAACVNACPS---NALTVETDLATGELAWEfnlgrCIFCGRCEEVCPTAAI 90
PorD COG1144
Pyruvate:ferredoxin oxidoreductase or related 2-oxoacid:ferredoxin oxidoreductase, delta ...
 374-399 6.67e-04

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: 38.49  E-value: 6.67e-04
                         10        20
                 ....*....|....*....|....*.
gi 502833261 374 TVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG1144   26 VVDEDKCIGCGLCWIVCPDGAIRVDD 51
DMSOR_beta_like cd16372
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 347-392 1.01e-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: 319894 [Multi-domain]  Cd Length: 125  Bit Score: 38.86  E-value: 1.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 502833261 347 CIKCGRCHIVCEDtshQAIAMAADRTVTVKEEECVACNLCVEVCPT 392
Cdd:cd16372   49 CNQCGECIDVCPT---GAITRDANGVVMINKKLCVGCLMCVGFCPE 91
Dus pfam01207
Dihydrouridine synthase (Dus); Members of this family catalyze the reduction of the 5,6-double ...
 79-202 1.35e-03

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: 40.39  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261   79 ELITDRPLevnLREIKSVKRDYP----DRALVVSLMVpCDEDSWKSILARVEETEADGVELNFGCPHGMAERGM-GAAVG 153
Cdd:pfam01207  29 EMVTAKAQ---LRPEKVRIRMLSeleePTPLAVQLGG-SDPALLAEAAKLVEDRGADGIDINMGCPSKKVTRGGgGAALL 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 502833261  154 QVPDYVEMVTRWVKQHSRMPCIVKLTPNISDIRKP----AEAAKRGGADAVSL 202
Cdd:pfam01207 105 RNPDLVAQIVKAVVKAVGIPVTVKIRIGWDDSHENaveiAKIVEDAGAQALTV 157
Nar1 COG4624
Iron only hydrogenase large subunit, C-terminal domain [Energy production and conversion];
308-399 1.41e-03

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


Pssm-ID: 443663 [Multi-domain]  Cd Length: 450  Bit Score: 40.78  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502833261 308 DRKGLTETREIVGRAVPKVTDWQYLNLNYTTKASIAQDDCIKCGRC-----HIVCEDTSHQAIAMAADRTVTVKEEECVA 382
Cdd:COG4624   16 GDELLLLEEAERVLRIIILEALLPEHVDDDSACSCCPRCCLCCCCCcrccvAISCIQVRGIIIIDKRGPSIIRDKEKCKN 95

                         90
                 ....*....|....*..
gi 502833261 383 CNLCVEVCPTKCITMRE 399
Cdd:COG4624   96 CYPCVRACPVKAIKVDD 112
PRK07118 PRK07118
Fe-S cluster domain-containing protein;
347-402 1.47e-03

Fe-S cluster domain-containing protein;


Pssm-ID: 235941 [Multi-domain]  Cd Length: 280  Bit Score: 40.30  E-value: 1.47e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502833261 347 CIKCGRCHIVCEdtsHQAIAMAaDRTVTVKEEECVACNLCVEVCPTKCITMRELSE 402
Cdd:PRK07118 141 CLGLGSCVAACP---FDAIHIE-NGLPVVDEDKCTGCGACVKACPRNVIELIPKSA 192
DMSOR_beta-like cd04410
Beta subunit of the DMSO Reductase (DMSOR) family; This family consists of the small beta ...
 347-399 1.54e-03

Beta subunit of the DMSO Reductase (DMSOR) 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: 319870 [Multi-domain]  Cd Length: 136  Bit Score: 38.52  E-value: 1.54e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502833261 347 CIKCGRCHIVCEDTSHQAIAMAADRTVTVKEEE---------CVACN--LCVEVCPTKCITMRE 399
Cdd:cd04410    8 CIGCGTCEVACKQEHGLRPGPDWSRIKVIEGGGleraflpvsCMHCEdpPCVKACPTGAIYKDE 71
DMSOR_beta_like cd10550
uncharacterized subfamily of DMSO Reductase beta subunit family; This family consists of the ...
 344-396 2.18e-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: 319872 [Multi-domain]  Cd Length: 130  Bit Score: 37.94  E-value: 2.18e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 502833261 344 QDDCIKCGRCHIVCedtSHQAIAMAADRTVTVKeeeCVACN---LCVEVCPTKCIT 396
Cdd:cd10550   79 EDKCIGCGMCVEAC---PFGAIRVDPETGKAIK---CDLCGgdpACVKVCPTGALE 128
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
353-399 2.33e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 38.10  E-value: 2.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 502833261 353 CHIvCEDTS------HQAIAMAADRtVTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:COG1142   52 CRH-CEDAPcaevcpVGAITRDDGA-VVVDEEKCIGCGLCVLACPFGAITMVG 102
napF TIGR00402
ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of ...
 347-392 2.91e-03

ferredoxin-type protein NapF; The gene codes for a ferredoxin-type cytosolic protein, NapF, of the periplasmic nitrate reductase system, as in Escherichia coli. NapF interacts with the catalytic subunit, NapA, and may be an accessory protein for NapA maturation. [Energy metabolism, Electron transport]


Pssm-ID: 273060 [Multi-domain]  Cd Length: 101  Bit Score: 37.23  E-value: 2.91e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 502833261  347 CIKCGRCHIVCEDTSHQaIAMAADRTVTVKEEECVACNLCVEVCPT 392
Cdd:TIGR00402  36 CTRCGECASACENNILQ-LGQQGQPTVEFDNAECDFCGKCAEACPT 80
PRK08222 PRK08222
hydrogenase 4 subunit H; Validated
 347-402 2.98e-03

hydrogenase 4 subunit H; Validated


Pssm-ID: 181301 [Multi-domain]  Cd Length: 181  Bit Score: 38.58  E-value: 2.98e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502833261 347 CIKCGRCHIVCedtSHQAIAMAAD-----RTVTVKEEECVACNLCVEVCPTKCITMRELSE 402
Cdd:PRK08222  40 CIACGACTCAC---PANALTIQTDdqqnsRTWQLYLGRCIYCGRCEEVCPTRAIQLTNNFE 97
oorD PRK09626
2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed
 373-399 3.21e-03

2-oxoglutarate-acceptor oxidoreductase subunit OorD; Reviewed


Pssm-ID: 236597 [Multi-domain]  Cd Length: 103  Bit Score: 37.01  E-value: 3.21e-03
                         10        20
                 ....*....|....*....|....*..
gi 502833261 373 VTVKEEECVACNLCVEVCPTKCITMRE 399
Cdd:PRK09626  11 VWVDESRCKACDICVSVCPAGVLAMRI 37
thiE PRK00043
thiamine phosphate synthase;
236-289 3.30e-03

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 38.63  E-value: 3.30e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 502833261 236 AVKPIALNMVAEIARnpATRGLPISGIGGVTTwRDAAEFMALGAHNVQVCTAVM 289
Cdd:PRK00043 142 AKAPQGLEGLREIRA--AVGDIPIVAIGGITP-ENAPEVLEAGADGVAVVSAIT 192
Fer4_7 pfam12838
4Fe-4S dicluster domain; Superfamily includes proteins containing domains which bind to ...
 380-402 3.85e-03

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: 35.19  E-value: 3.85e-03
                          10        20
                  ....*....|....*....|...
gi 502833261  380 CVACNLCVEVCPTKCITMRELSE 402
Cdd:pfam12838   1 CIGCGACVAACPVGAITLDEVGE 23
HycB COG1142
Fe-S-cluster-containing hydrogenase component 2 [Energy production and conversion];
342-399 5.05e-03

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


Pssm-ID: 440757 [Multi-domain]  Cd Length: 138  Bit Score: 37.33  E-value: 5.05e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 342 IAQDDCIKCGRCHIVCEdTSHQAIAMAADR---TVTVKEE-----ECVACNL--CVEVCPTKCITMRE 399
Cdd:COG1142    7 ADPEKCIGCRTCEAACA-VAHEGEEGEPFLpriRVVRKAGvsapvQCRHCEDapCAEVCPVGAITRDD 73
Fer4_16 pfam13484
4Fe-4S double cluster binding domain;
380-401 5.16e-03

4Fe-4S double cluster binding domain;


Pssm-ID: 463893 [Multi-domain]  Cd Length: 65  Bit Score: 35.54  E-value: 5.16e-03
                          10        20
                  ....*....|....*....|..
gi 502833261  380 CVACNLCVEVCPTKCITMRELS 401
Cdd:pfam13484   1 CGSCGKCIDACPTGAIVGPEGV 22
NapH COG0348
Polyferredoxin NapH [Energy production and conversion];
372-395 8.08e-03

Polyferredoxin NapH [Energy production and conversion];


Pssm-ID: 440117 [Multi-domain]  Cd Length: 263  Bit Score: 37.73  E-value: 8.08e-03
                         10        20
                 ....*....|....*....|....
gi 502833261 372 TVTVKEEECVACNLCVEVCPTKCI 395
Cdd:COG0348  204 RVRYDRGDCIDCGLCVKVCPMGID 227
HycB_like cd10554
HycB, HydN and similar proteins; This family includes HycB, the FeS subunit of a ...
 344-397 8.99e-03

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: 36.47  E-value: 8.99e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502833261 344 QDDCIKCGRCHIVCedtSHQAIAMA---ADRTVTVKEEECVA--CNLC---------VEVCPTKCITM 397
Cdd:cd10554   84 EERCIGCKLCVLAC---PFGAIEMApttVPGVDWERGPRAVAvkCDLCagreggpacVEACPTKALTL 148
 
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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