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Conserved domains on  [gi|2418879974|gb|WBE26092|]
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tetracycline-inactivating monooxygenase Tet(X) [Denitrificimonas caeni]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 11428987)

FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 8-376 1.69e-48

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 166.65  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGGTLDlhrDSGQEAMKKAGLLQTYYDLALPM-GVNIAD-EK 85
Cdd:COG0654     5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALS---PRSLELLRRLGLWDRLLARGAPIrGIRVRDgSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  86 GNILTTKNVKPENRFDNPEINRNDLRTILLNSLQ--NNTVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGGMSK 163
Cdd:COG0654    82 GRVLARFDAAETGLPAGLVVPRADLERALLEAARalGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGARSA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 164 VRKYVtdtEVEATGTfniqaDIHQPAVNCpgffqlcngnrlmaahrgnllfanpnnngalhfgisfktpddwknktqvdf 243
Cdd:COG0654   162 VRRLL---GIGFTGR-----DYPQRALWA--------------------------------------------------- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 244 qdsnNIVDFLLKEFSDWDERYKELIRSTSSFVGLATRifPLAKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALI 323
Cdd:COG0654   183 ----GVRTELRARLAAAGPRLGELLELSPRSAFPLRR--RRAERWRRGR---VVLLGDAAHTMHPLGGQGANLALRDAAA 253

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2418879974 324 LSDNLIDGKFN-SMEEAIQNYEQHMFVYGREAQAESTINeTEMFSPDFSFQKLM 376
Cdd:COG0654   254 LAWKLAAALRGrDDEAALARYERERRPRAARVQRAADAL-GRLFHPDSPPLRLL 306
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 8-376 1.69e-48

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 166.65  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGGTLDlhrDSGQEAMKKAGLLQTYYDLALPM-GVNIAD-EK 85
Cdd:COG0654     5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALS---PRSLELLRRLGLWDRLLARGAPIrGIRVRDgSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  86 GNILTTKNVKPENRFDNPEINRNDLRTILLNSLQ--NNTVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGGMSK 163
Cdd:COG0654    82 GRVLARFDAAETGLPAGLVVPRADLERALLEAARalGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGARSA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 164 VRKYVtdtEVEATGTfniqaDIHQPAVNCpgffqlcngnrlmaahrgnllfanpnnngalhfgisfktpddwknktqvdf 243
Cdd:COG0654   162 VRRLL---GIGFTGR-----DYPQRALWA--------------------------------------------------- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 244 qdsnNIVDFLLKEFSDWDERYKELIRSTSSFVGLATRifPLAKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALI 323
Cdd:COG0654   183 ----GVRTELRARLAAAGPRLGELLELSPRSAFPLRR--RRAERWRRGR---VVLLGDAAHTMHPLGGQGANLALRDAAA 253

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2418879974 324 LSDNLIDGKFN-SMEEAIQNYEQHMFVYGREAQAESTINeTEMFSPDFSFQKLM 376
Cdd:COG0654   254 LAWKLAAALRGrDDEAALARYERERRPRAARVQRAADAL-GRLFHPDSPPLRLL 306
PRK06753 PRK06753
hypothetical protein; Provisional
 8-345 9.83e-23

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 98.22  E-value: 9.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYErdKDRDARIFGGTLDLhrdsGQEAMKKAGLlqtyYDLA---------LPmG 78
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE--KNESVKEVGAGIGI----GDNVIKKLGN----HDLAkgiknagqiLS-T 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  79 VNIADEKGNILTTknVKPENRFDNPEINRNDLRTILLNSLQNNTVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIAN 158
Cdd:PRK06753   71 MNLLDDKGTLLNK--VKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEAFDLCIGAD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 159 GGMSKVRKYVT-DTEVEATG--TFNIQADIHQpavncpgfFQLCNGNRLMAAHRGNL-LFANPNNNGALHFGISFKTPD- 233
Cdd:PRK06753  149 GIHSKVRQSVNaDSKVRYQGytCFRGLIDDID--------LKLPDCAKEYWGTKGRFgIVPLLNNQAYWFITINAKERDp 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 234 DWKNKTQVDFQdsnnivdfllKEFSDWDERYKELIRSTSSFVGLATRIFPLaKPWKSSRPLPITMVGDAAHLMPPFAGQG 313
Cdd:PRK06753  221 KYSSFGKPHLQ----------AYFNHYPNEVREILDKQSETGILHHDIYDL-KPLKSFVYGRIVLLGDAAHATTPNMGQG 289

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2418879974 314 VNSGLVDALILSDNLIDGKFnsmEEAIQNYEQ 345
Cdd:PRK06753  290 AGQAMEDAIVLANCLNAYDF---EKALQRYDK 318
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 8-321 1.14e-17

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


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 83.14  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDkdrdarifGGTLDLHRDSGQ-----EAMKKAGLLQTYYDLALP---MGV 79
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERH--------ATTSVLPRAHGLnqrtmELLRQAGLEDRILAEGVPhegMGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  80 NIADEKGNILTTKNVKPENRFDNPEinrNDLRTILLNSLQNN--TVIWDRKLVALE--PDKEKWVLSF-EDKPNET--AD 152
Cdd:pfam01494  75 AFYNTRRRADLDFLTSPPRVTVYPQ---TELEPILVEHAEARgaQVRFGTEVLSLEqdGDGVTAVVRDrRDGEEYTvrAK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 153 LVIIANGGMSKVRKYVtDTEVEATGT-----FNIQADIHQPAVNCPGFFQLCngnrlmaahrgnLLFANpnnngalHFGI 227
Cdd:pfam01494 152 YLVGCDGGRSPVRKTL-GIEFEGFEGvpfgsLDVLFDAPDLSDPVERAFVHY------------LIYAP-------HSRG 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 228 SFKTPddWKNKTQVDFQdsnnIVDFLLKEFSDW-----DERYKELIRSTSSFVGLATRIFP---------LAKPWKSSRp 293
Cdd:pfam01494 212 FMVGP--WRSAGRERYY----VQVPWDEEVEERpeeftDEELKQRLRSIVGIDLALVEILWksiwgvasrVATRYRKGR- 284

                         330       340
                  ....*....|....*....|....*...
gi 2418879974 294 lpITMVGDAAHLMPPFAGQGVNSGLVDA 321
Cdd:pfam01494 285 --VFLAGDAAHIHPPTGGQGLNTAIQDA 310
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 9-332 2.47e-13

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


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 70.70  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYER-------DKDRDARIFGgtldLHRDSgQEAMKKAGLLQTYYDL-ALPM-GV 79
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEAtplpapaDPGFDNRVSA----LSAAS-IRLLEKLGVWDKIEPArAQPIrDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  80 NIADEKGNILTtknvkpenRFDNPEINRNDL---------RTILLNSLQNN---TVIWDRKLVALEPDKEKWVLSFEDKP 147
Cdd:TIGR01988  77 HVSDGGSFGAL--------RFDADEIGLEALgyvvenrvlQQALWERLQELpnvTLLCPARVVELPRHSDHVELTLDDGQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 148 NETADLVIIANGGMSKVRKYvtdteveatgtFNIQADIH---QPAVNCpgffqlcngnrlmaahrgNLLFANPNNNGA-- 222
Cdd:TIGR01988 149 QLRARLLVGADGANSKVRQL-----------AGIPTTGWdygQSAVVA------------------NVKHERPHQGTAwe 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 223 --LHFG-------------ISFKTPDDWKNKTQVdfQDSNNIVDFLLKEFsdwDERYKELIRSTSSFvglatrIFPL--- 284
Cdd:TIGR01988 200 rfTPTGplallplpdnrssLVWTLPPEEAERLLA--LSDEEFLAELQRAF---GSRLGAITLVGERH------AFPLslt 268

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2418879974 285 -AKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALILSDNLIDGK 332
Cdd:TIGR01988 269 hAKRYVAPR---LALIGDAAHTIHPLAGQGLNLGLRDVAALAEVLEDAR 314
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 8-41 2.82e-04

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 42.51  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVD-VTVYERDKDR 41
Cdd:cd08234   162 SVLVFGAGPIGLLLAQLLKLNGASrVTVAEPNEEK 196
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 8-376 1.69e-48

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 166.65  E-value: 1.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGGTLDlhrDSGQEAMKKAGLLQTYYDLALPM-GVNIAD-EK 85
Cdd:COG0654     5 DVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALS---PRSLELLRRLGLWDRLLARGAPIrGIRVRDgSD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  86 GNILTTKNVKPENRFDNPEINRNDLRTILLNSLQ--NNTVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGGMSK 163
Cdd:COG0654    82 GRVLARFDAAETGLPAGLVVPRADLERALLEAARalGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGARSA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 164 VRKYVtdtEVEATGTfniqaDIHQPAVNCpgffqlcngnrlmaahrgnllfanpnnngalhfgisfktpddwknktqvdf 243
Cdd:COG0654   162 VRRLL---GIGFTGR-----DYPQRALWA--------------------------------------------------- 182

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 244 qdsnNIVDFLLKEFSDWDERYKELIRSTSSFVGLATRifPLAKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALI 323
Cdd:COG0654   183 ----GVRTELRARLAAAGPRLGELLELSPRSAFPLRR--RRAERWRRGR---VVLLGDAAHTMHPLGGQGANLALRDAAA 253

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2418879974 324 LSDNLIDGKFN-SMEEAIQNYEQHMFVYGREAQAESTINeTEMFSPDFSFQKLM 376
Cdd:COG0654   254 LAWKLAAALRGrDDEAALARYERERRPRAARVQRAADAL-GRLFHPDSPPLRLL 306
PRK06753 PRK06753
hypothetical protein; Provisional
 8-345 9.83e-23

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 98.22  E-value: 9.83e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYErdKDRDARIFGGTLDLhrdsGQEAMKKAGLlqtyYDLA---------LPmG 78
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE--KNESVKEVGAGIGI----GDNVIKKLGN----HDLAkgiknagqiLS-T 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  79 VNIADEKGNILTTknVKPENRFDNPEINRNDLRTILLNSLQNNTVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIAN 158
Cdd:PRK06753   71 MNLLDDKGTLLNK--VKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEAFDLCIGAD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 159 GGMSKVRKYVT-DTEVEATG--TFNIQADIHQpavncpgfFQLCNGNRLMAAHRGNL-LFANPNNNGALHFGISFKTPD- 233
Cdd:PRK06753  149 GIHSKVRQSVNaDSKVRYQGytCFRGLIDDID--------LKLPDCAKEYWGTKGRFgIVPLLNNQAYWFITINAKERDp 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 234 DWKNKTQVDFQdsnnivdfllKEFSDWDERYKELIRSTSSFVGLATRIFPLaKPWKSSRPLPITMVGDAAHLMPPFAGQG 313
Cdd:PRK06753  221 KYSSFGKPHLQ----------AYFNHYPNEVREILDKQSETGILHHDIYDL-KPLKSFVYGRIVLLGDAAHATTPNMGQG 289

                         330       340       350
                  ....*....|....*....|....*....|..
gi 2418879974 314 VNSGLVDALILSDNLIDGKFnsmEEAIQNYEQ 345
Cdd:PRK06753  290 AGQAMEDAIVLANCLNAYDF---EKALQRYDK 318
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
9-360 4.60e-19

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 88.43  E-value: 4.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKDrdarifggTLDLHR----DSgqEAMKkagLLQTyydlalpmgVNIADE 84
Cdd:PRK06183   13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPT--------LYDLPRavgiDD--EALR---VLQA---------IGLADE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  85 ----------------KGNILTTKNVKPE--------NRFDNPEINRNdLRTiLLNSLQNNTVIWDRKLVALEPDKEKWV 140
Cdd:PRK06183   71 vlphttpnhgmrfldaKGRCLAEIARPSTgefgwprrNAFHQPLLEAV-LRA-GLARFPHVRVRFGHEVTALTQDDDGVT 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 141 LSFEDKPNE----TADLVIIANGGMSKVRKYVtDTEVEATGTFN----IQADIHQPAVNCPGFFQLCNGNRlmaahrgnl 212
Cdd:PRK06183  149 VTLTDADGQretvRARYVVGCDGANSFVRRTL-GVPFEDLTFPErwlvVDVLIANDPLGGPHTYQYCDPAR--------- 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 213 lfanPNNNGALHFGI---SFK-----TPDDWKnktqvdfQDSNniVDFLLKEFSDWDERYkELIRStssfvglATRIFP- 283
Cdd:PRK06183  219 ----PYTSVRLPHGRrrwEFMllpgeTEEQLA-------SPEN--VWRLLAPWGPTPDDA-ELIRH-------AVYTFHa 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 284 -LAKPWKSSRPLpitMVGDAAHLMPPFAGQGVNSGLVDALILS---DNLIDGKfnSMEEAIQNYEQHmfvygREAQAEST 359
Cdd:PRK06183  278 rVADRWRSGRVL---LAGDAAHLMPPFAGQGMNSGIRDAANLAwklAAVLRGR--AGDALLDTYEQE-----RRPHARAM 347


                  .
gi 2418879974 360 I 360
Cdd:PRK06183  348 I 348
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 8-321 1.14e-17

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


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 83.14  E-value: 1.14e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDkdrdarifGGTLDLHRDSGQ-----EAMKKAGLLQTYYDLALP---MGV 79
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGVRVVLVERH--------ATTSVLPRAHGLnqrtmELLRQAGLEDRILAEGVPhegMGL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  80 NIADEKGNILTTKNVKPENRFDNPEinrNDLRTILLNSLQNN--TVIWDRKLVALE--PDKEKWVLSF-EDKPNET--AD 152
Cdd:pfam01494  75 AFYNTRRRADLDFLTSPPRVTVYPQ---TELEPILVEHAEARgaQVRFGTEVLSLEqdGDGVTAVVRDrRDGEEYTvrAK 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 153 LVIIANGGMSKVRKYVtDTEVEATGT-----FNIQADIHQPAVNCPGFFQLCngnrlmaahrgnLLFANpnnngalHFGI 227
Cdd:pfam01494 152 YLVGCDGGRSPVRKTL-GIEFEGFEGvpfgsLDVLFDAPDLSDPVERAFVHY------------LIYAP-------HSRG 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 228 SFKTPddWKNKTQVDFQdsnnIVDFLLKEFSDW-----DERYKELIRSTSSFVGLATRIFP---------LAKPWKSSRp 293
Cdd:pfam01494 212 FMVGP--WRSAGRERYY----VQVPWDEEVEERpeeftDEELKQRLRSIVGIDLALVEILWksiwgvasrVATRYRKGR- 284

                         330       340
                  ....*....|....*....|....*...
gi 2418879974 294 lpITMVGDAAHLMPPFAGQGVNSGLVDA 321
Cdd:pfam01494 285 --VFLAGDAAHIHPPTGGQGLNTAIQDA 310
PRK06847 PRK06847
hypothetical protein; Provisional
 7-344 1.78e-15

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 76.84  E-value: 1.78e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDAR-----IFGGTLdlhrdsgqEAMKKAGLLQTYYDLALPM-GVN 80
Cdd:PRK06847    5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYgagitLQGNAL--------RALRELGVLDECLEAGFGFdGVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  81 IADEKGNILTTknvKPENRFDNPE------INRNDLRTILLNSLQ--NNTVIWDRKLVALEPDKEKWVLSFEDKPNETAD 152
Cdd:PRK06847   77 LFDPDGTLLAE---LPTPRLAGDDlpggggIMRPALARILADAARaaGADVRLGTTVTAIEQDDDGVTVTFSDGTTGRYD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 153 LVIIANGGMSKVRKYVTDTEVEA--TGTFNIQADIHQPA-VNCPGFFQlcnGNRLMAAhrgnllfANPNNNGALHFGISF 229
Cdd:PRK06847  154 LVVGADGLYSKVRSLVFPDEPEPeyTGQGVWRAVLPRPAeVDRSLMYL---GPTTKAG-------VVPLSEDLMYLFVTE 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 230 KTPDDwknkTQVDFQDSNNIVDFLLKEFSD--WDERyKELIRSTS--SFVGLATRIFPlaKPWKSSRplpITMVGDAAHL 305
Cdd:PRK06847  224 PRPDN----PRIEPDTLAALLRELLAPFGGpvLQEL-REQITDDAqvVYRPLETLLVP--APWHRGR---VVLIGDAAHA 293

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 2418879974 306 MPPFAGQGVNSGLVDALILSDNLIDGkfNSMEEAIQNYE 344
Cdd:PRK06847  294 TTPHLAQGAGMAIEDAIVLAEELARH--DSLEAALQAYY 330
PRK05868 PRK05868
FAD-binding protein;
7-355 8.55e-15

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 75.02  E-value: 8.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDkdRDARIFGGTLDLhRDSGQEAMKKAGLLQTYYDLALPM-GVNIADEK 85
Cdd:PRK05868    2 KTVVVSGASVAGTAAAYWLGRHGYSVTMVERH--PGLRPGGQAIDV-RGPALDVLERMGLLAAAQEHKTRIrGASFVDRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  86 GNILT--TKNVKPENRFDNPEIN--RNDLRTILLNSLQNNT-VIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGG 160
Cdd:PRK05868   79 GNELFrdTESTPTGGPVNSPDIEllRDDLVELLYGATQPSVeYLFDDSISTLQDDGDSVRVTFERAAAREFDLVIGADGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 161 MSKVRKYVTDTE---VEATGTfniqadiHQPAVNCPGFFQLcngNRLMAAHRGNLLFA---NPNNNGALHFGISFKtpdd 234
Cdd:PRK05868  159 HSNVRRLVFGPEeqfVKRLGT-------HAAIFTVPNFLEL---DYWQTWHYGDSTMAgvySARNNTEARAALAFM---- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 235 wKNKTQVDFQDSNnivdfllKEFSDWDERYKE----------LIRSTSSF-VGLATRIfpLAKPWKSSRplpITMVGDAA 303
Cdd:PRK05868  225 -DTELRIDYRDTE-------AQFAELQRRMAEdgwvraqllhYMRSAPDFyFDEMSQI--LMDRWSRGR---VALVGDAG 291

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2418879974 304 HLMPPFAGQGVNSGLVDALILSDNLiDGKFNSMEEAIQNYEQHMFVYGREAQ 355
Cdd:PRK05868  292 YCCSPLSGQGTSVALLGAYILAGEL-KAAGDDYQLGFANYHAEFHGFVERNQ 342
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 9-332 2.47e-13

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


Pssm-ID: 273913 [Multi-domain]  Cd Length: 385  Bit Score: 70.70  E-value: 2.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYER-------DKDRDARIFGgtldLHRDSgQEAMKKAGLLQTYYDL-ALPM-GV 79
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEAtplpapaDPGFDNRVSA----LSAAS-IRLLEKLGVWDKIEPArAQPIrDI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  80 NIADEKGNILTtknvkpenRFDNPEINRNDL---------RTILLNSLQNN---TVIWDRKLVALEPDKEKWVLSFEDKP 147
Cdd:TIGR01988  77 HVSDGGSFGAL--------RFDADEIGLEALgyvvenrvlQQALWERLQELpnvTLLCPARVVELPRHSDHVELTLDDGQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 148 NETADLVIIANGGMSKVRKYvtdteveatgtFNIQADIH---QPAVNCpgffqlcngnrlmaahrgNLLFANPNNNGA-- 222
Cdd:TIGR01988 149 QLRARLLVGADGANSKVRQL-----------AGIPTTGWdygQSAVVA------------------NVKHERPHQGTAwe 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 223 --LHFG-------------ISFKTPDDWKNKTQVdfQDSNNIVDFLLKEFsdwDERYKELIRSTSSFvglatrIFPL--- 284
Cdd:TIGR01988 200 rfTPTGplallplpdnrssLVWTLPPEEAERLLA--LSDEEFLAELQRAF---GSRLGAITLVGERH------AFPLslt 268

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 2418879974 285 -AKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALILSDNLIDGK 332
Cdd:TIGR01988 269 hAKRYVAPR---LALIGDAAHTIHPLAGQGLNLGLRDVAALAEVLEDAR 314
PRK06126 PRK06126
hypothetical protein; Provisional
 8-325 3.43e-11

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 64.63  E-value: 3.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERdkdRDARIFGGTLDLHRDSGQEAMKKAGLLQTYYDLALPmgVNIADEkgN 87
Cdd:PRK06126    9 PVLIVGGGPVGLALALDLGRRGVDSILVER---KDGTAFNPKANTTSARSMEHFRRLGIADEVRSAGLP--VDYPTD--I 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  88 ILTTKNVKPE-NRFDNP-----------------------EINRNDLRTILLNSLQ---NNTVIWDRKLVALEPDKEKWV 140
Cdd:PRK06126   82 AYFTRLTGYElARFRLPsareaitpvggpdgswpspelphRIPQKYLEPILLEHAAaqpGVTLRYGHRLTDFEQDADGVT 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 141 LSFED-KPNET----ADLVIIANGGMSKVRK-----YVTDTEVEATGTFNIQAdihqpavncPGFFQLCNGNRlmaAHRG 210
Cdd:PRK06126  162 ATVEDlDGGESltirADYLVGCDGARSAVRRslgisYEGTSGLQRDLSIYIRA---------PGLAALVGHDP---AWMY 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 211 NLLfaNPNNNGALhfgISFKTPDDWKNKTQVDFQDSNNIVDFllkefsDWDERYKELIRSTSSFVGLATrifplaKPWKS 290
Cdd:PRK06126  230 WLF--NPDRRGVL---VAIDGRDEWLFHQLRGGEDEFTIDDV------DARAFVRRGVGEDIDYEVLSV------VPWTG 292

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2418879974 291 SRPLPITM-------VGDAAHLMPPFAGQGVNSGLVDALILS 325
Cdd:PRK06126  293 RRLVADSYrrgrvflAGDAAHLFTPTGGYGMNTGIGDAVNLA 334
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
7-157 9.69e-10

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 59.12  E-value: 9.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYErdKDRDA-------RIFGGTLDlH-------RDSG-QEAMKK---AGLLQ 68
Cdd:COG3380     4 PDIAIIGAGIAGLAAARALQDAGHEVTVFE--KSRGVggrmatrRLDGGRFD-HgaqyftaRDPRfQALVEEwlaAGLVA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  69 TYYDlalpmgvNIADEKGNILTTKNVKPENRFdnpeINRNDLRTILLNSLQNNTVIWDRKLVALEPDKEKWVLSFED-KP 147
Cdd:COG3380    81 PWTF-------DFVVLDADGLVSPRDDGEPRY----VGVPGMNALAKHLAAGLDVRLGTRVTALERDGDGWRLTDEDgEE 149

                         170
                  ....*....|
gi 2418879974 148 NETADLVIIA 157
Cdd:COG3380   150 YGPFDAVVLA 159
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 5-50 6.06e-09

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 57.45  E-value: 6.06e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKdrdarIFGGTL 50
Cdd:COG0493   120 TGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALD-----KPGGLL 160
PRK07236 PRK07236
hypothetical protein; Provisional
 1-165 7.91e-09

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 56.85  E-value: 7.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   1 MNLLNNKKIAIIGAGPVGLTMARLLQQNGVDVTVYER-DKDRDARifGGTLDLHRDsgqeaMKKAgLLQTYYDLALPMGV 79
Cdd:PRK07236    1 MTHMSGPRAVVIGGSLGGLFAALLLRRAGWDVDVFERsPTELDGR--GAGIVLQPE-----LLRA-LAEAGVALPADIGV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  80 NIA-----DEKGNILTtknvkpenRFDNPEI--NRNDLRTILLNSLQNNTVIWDRKLVALEPDKEKWVLSFEDKPNETAD 152
Cdd:PRK07236   73 PSReriylDRDGRVVQ--------RRPMPQTqtSWNVLYRALRAAFPAERYHLGETLVGFEQDGDRVTARFADGRRETAD 144

                         170
                  ....*....|...
gi 2418879974 153 LVIIANGGMSKVR 165
Cdd:PRK07236  145 LLVGADGGRSTVR 157
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 7-50 9.63e-09

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 56.71  E-value: 9.63e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDkDRdariFGGTL 50
Cdd:PRK12810  144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERA-DR----IGGLL 182
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 5-37 2.13e-08

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 55.57  E-value: 2.13e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK11749  139 TGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEA 171
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 7-57 4.75e-08

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


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 54.45  E-value: 4.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDkDRdariFGGTLDLHRDSG 57
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS-DR----VGGLIRTVEVDG 47
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 6-95 5.67e-08

Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms];


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 53.53  E-value: 5.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   6 NKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFG-GTLDLHRD-SGQEAMKKAGLLQTyyDLALpmgVNIAD 83
Cdd:COG0569    95 KMHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEeDVLVIVGDaTDEEVLEEAGIEDA--DAVI---AATGD 169

                          90
                  ....*....|..
gi 2418879974  84 EKGNILTTKNVK 95
Cdd:COG0569   170 DEANILACLLAK 181
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 8-74 6.14e-08

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 54.03  E-value: 6.14e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERdKDRDA---RIFGGTL-----DLHRDSGQEA-MKKAGLLQTYYDLA 74
Cdd:PRK08243    4 QVAIIGAGPAGLLLGQLLHLAGIDSVVLER-RSREYvegRIRAGVLeqgtvDLLREAGVGErMDREGLVHDGIELR 78
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 8-329 9.04e-08

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 53.72  E-value: 9.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDK-------------------DR---------------DARIFGG----- 48
Cdd:PRK08132   25 PVVVVGAGPVGLALAIDLAQQGVPVVLLDDDDtlstgsraicfakrsleifDRlgcgermvdkgvswnVGKVFLRdeevy 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  49 TLDLHRDSGQE--AMKKaglLQTYY------DLALpmgvniadekgnilttknvkpenrfDNPEInrnDLRtillnslqn 120
Cdd:PRK08132  105 RFDLLPEPGHRrpAFIN---LQQYYvegylvERAQ-------------------------ALPNI---DLR--------- 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 121 ntviWDRKLVALEPDKEKWVLSFEDkPNET----ADLVIIANGGMSKVRKYVtdtEVEATGT-----FNIqADIHQPAvn 191
Cdd:PRK08132  145 ----WKNKVTGLEQHDDGVTLTVET-PDGPytleADWVIACDGARSPLREML---GLEFEGRtfedrFLI-ADVKMKA-- 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 192 cpGFfqlcngnrlmAAHRgnlLF-----ANPNNNGALHfgisfKTPDD-WKnktqVDFQ---DSN--------NI---VD 251
Cdd:PRK08132  214 --DF----------PTER---WFwfdppFHPGQSVLLH-----RQPDNvWR----IDFQlgwDADpeaekkpeNViprVR 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 252 FLLKE---FS-DWDERYKELIRSTSSFV-GlatRIFplakpwkssrplpitMVGDAAHLMPPFAGQGVNSGLVDAlilsD 326
Cdd:PRK08132  270 ALLGEdvpFElEWVSVYTFQCRRMDRFRhG---RVL---------------FAGDAAHQVSPFGARGANSGIQDA----D 327


                  ...
gi 2418879974 327 NLI 329
Cdd:PRK08132  328 NLA 330
PRK07208 PRK07208
hypothetical protein; Provisional
 5-38 1.86e-07

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 52.58  E-value: 1.86e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERD 38
Cdd:PRK07208    3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEAD 36
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 9-54 3.20e-07

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


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 51.79  E-value: 3.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKDrdariFGGTLDLHR 54
Cdd:COG2072     9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADD-----VGGTWRDNR 49
PRK07045 PRK07045
putative monooxygenase; Reviewed
 5-348 3.44e-07

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 51.83  E-value: 3.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKdRDARIFGGtlDLHRDSGQEAMKKAGLL--------------QTY 70
Cdd:PRK07045    4 NPVDVLINGSGIAGVALAHLLGARGHSVTVVERAA-RNRAQNGA--DLLKPSGIGVVRAMGLLddvfaagglrrdamRLY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  71 YDLALPMGVNI--ADEKGNILTtknvkpenrfdnpeINRNDLRTILLNSLQ---NNTVIWDRKLVALEPDKEKWVLSFED 145
Cdd:PRK07045   81 HDKELIASLDYrsASALGYFIL--------------IPCEQLRRLLLAKLDglpNVRLRFETSIERIERDADGTVTSVTL 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 146 KPNETA--DLVIIANGGMSKVRKYVTDTEVE--------ATGTFNIQADIHQpavncpgffqlCNgnRLMAAHRGNLLFA 215
Cdd:PRK07045  147 SDGERVapTVLVGADGARSMIRDDVLRMPAErvpyatpmAFGTIALTDSVRE-----------CN--RLYVDSNQGLAYF 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 216 NPNNNGALHFGISFktPDDWKNKTQVDFQDSNnivdfLLKEFSDW--DERYKEL--IRSTSSFVGLATRIFPLAKPWKSS 291
Cdd:PRK07045  214 YPIGDQATRLVVSF--PADEMQGYLADTTRTK-----LLARLNEFvgDESADAMaaIGAGTAFPLIPLGRMNLDRYHKRN 286

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 292 rplpITMVGDAAHLMPPFAGQGVNSGLVDALILSDNL---IDGKFnSMEEAIQNYEQHMF 348
Cdd:PRK07045  287 ----VVLLGDAAHSIHPITGQGMNLAIEDAGELGACLdlhLSGQI-ALADALERFERIRR 341
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 6-160 8.64e-07

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 51.00  E-value: 8.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   6 NKKIAIIGAGPVGLTMARLLQQNGVDVTVYER----------------------DKDRDARIFG---------------- 47
Cdd:PRK01747  260 ARDAAIIGGGIAGAALALALARRGWQVTLYEAdeapaqgasgnrqgalypllskDDNALSRFFRaaflfarrfydalpaa 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  48 ---------GTLDLHRDSG-QEAMKKAGLLQTYYDLALPMGVNIADEKGNILTTKN---------VKPenrfdnPEINRN 108
Cdd:PRK01747  340 gvafdhdwcGVLQLAWDEKsAEKIAKMLALGLPAELARALDAEEAEELAGLPVPCGgifypqggwLCP------AELCRA 413

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2418879974 109 dlrtiLLNSLQNN-TVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGG 160
Cdd:PRK01747  414 -----LLALAGQQlTIHFGHEVARLEREDDGWQLDFAGGTLASAPVVVLANGH 461
PRK07233 PRK07233
hypothetical protein; Provisional
 8-59 1.68e-06

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 49.50  E-value: 1.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDrdariFGGTLDLHRDSGQE 59
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQ-----LGGLAASFEFGGLP 47
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
7-48 2.33e-06

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 49.15  E-value: 2.33e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYE-RDkdrdaRIfGG 48
Cdd:COG1231     8 KDVVIVGAGLAGLAAARELRKAGLDVTVLEaRD-----RV-GG 44
PRK06617 PRK06617
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 9-325 2.79e-06

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 168629 [Multi-domain]  Cd Length: 374  Bit Score: 48.77  E-value: 2.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGG----TLDLHR-------DSGQEAMKKAGLLQTYYdlalpm 77
Cdd:PRK06617    4 TVILGCGLSGMLTALSFAQKGIKTTIFESKSVKSPEFFKDirttALTPHSknflfsiDIWEELEKFVAEMQDIY------ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  78 gvnIADEKGN-ILTTKNvkPENRFDNPEINRNDLRTILLNSLQNN---TVIWDRKLVALEPDKEKWVLSFEDKpNETADL 153
Cdd:PRK06617   78 ---VVDNKASeILDLRN--DADAVLGYVVKNSDFKKILLSKITNNpliTLIDNNQYQEVISHNDYSIIKFDDK-QIKCNL 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 154 VIIANGGMSKVRKYVTDTEVE----ATGTFNIQADihQPAVNCP-------GFFQLCNgnrLMAAHRGNLLFANPNNNGA 222
Cdd:PRK06617  152 LIICDGANSKVRSHYFANEIEkpyqTALTFNIKHE--KPHENCAmehflplGPFALLP---LKDQYASSVIWSTSSDQAA 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 223 LHFGISFKtpddwknktQVDFQDSNNIVDFLlkefsdwderYKELIRSTSSFVGLATRIfplAKPWKSSRplpITMVGDA 302
Cdd:PRK06617  227 LIVNLPVE---------EVRFLTQRNAGNSL----------GKITIDSEISSFPLKARI---ANRYFHNR---IVLIADT 281

                         330       340
                  ....*....|....*....|...
gi 2418879974 303 AHLMPPFAGQGVNSGLVDALILS 325
Cdd:PRK06617  282 AHTVHPLAGQGLNQGIKDIEILS 304
PRK07588 PRK07588
FAD-binding domain;
7-375 4.73e-06

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 48.19  E-value: 4.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYER-DKDRDarifGGTLDLHRDSGQEAMKKAGLLQTYYDLALPM-GVNIADE 84
Cdd:PRK07588    1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERaPELRT----GGYMVDFWGVGYEVAKRMGITDQLREAGYQIeHVRSVDP 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  85 KGNI---LTTKNVKPENRFDNPEINRNDLRTILLNSLQNNT-VIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGG 160
Cdd:PRK07588   77 TGRRkadLNVDSFRRMVGDDFTSLPRGDLAAAIYTAIDGQVeTIFDDSIATIDEHRDGVRVTFERGTPRDFDLVIGADGL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 161 MSKVRKYVTDTEveatGTFNIQADIHQPAVNCPGF-------FQLCNGNRLMAAH---RGN-----LLFANPNNNGALhf 225
Cdd:PRK07588  157 HSHVRRLVFGPE----RDFEHYLGCKVAACVVDGYrprdertYVLYNEVGRQVARvalRGDrtlflFIFRAEHDNPPL-- 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 226 gisfkTPDDWKNKTQVDFQD----SNNIVDFLlkefSDWDERYKEL---IRSTSsfvglatrifplakpWKSSRplpITM 298
Cdd:PRK07588  231 -----TPAEEKQLLRDQFGDvgweTPDILAAL----DDVEDLYFDVvsqIRMDR---------------WSRGR---VAL 283

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418879974 299 VGDAAHLMPPFAGQGVNSGLVDALILSDNLIDGKfNSMEEAIQNYEQHM--FVYGREAQAESTINeteMFSPDFSFQKL 375
Cdd:PRK07588  284 VGDAAACPSLLGGEGSGLAITEAYVLAGELARAG-GDHRRAFDAYEKRLrpFIAGKQAAAAKFLS---VFAPKTRFGLY 358
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
14-347 4.99e-06

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 47.65  E-value: 4.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  14 AGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGG-----TLDLHRDSGQEAMKKAGLLQTYYDLALPMGVNIADEKGNI 88
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGgllprALEELEPLGLDEPLERPVRGARFYSPGGKSVELPPGRGGG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  89 LTtknvkpenrfdnpeINRNDLRTILLNSLQNN--TVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANGGMSKVRK 166
Cdd:COG0644    81 YV--------------VDRARFDRWLAEQAEEAgaEVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGARSLLAR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 167 YvtdteveatgtFNIQADIHQPAVNCPGFFQLCNGNRLMAAHRgnllfanpnnnGALHFGISFKTPDDWknktqvdfqds 246
Cdd:COG0644   147 K-----------LGLKRRSDEPQDYALAIKEHWELPPLEGVDP-----------GAVEFFFGEGAPGGY----------- 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 247 nnivdfllkefsdwderykelirstsSFvglatrIFPLAK-------PWKSSRPLPIT----MVGDAAHLMPPFAGQGVN 315
Cdd:COG0644   194 --------------------------GW------VFPLGDgrvsvgiPLGGPRPRLVGdgvlLVGDAAGFVDPLTGEGIH 241

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2418879974 316 SGLVDALILSDNLID--GKFNSMEEAIQNYEQHM 347
Cdd:COG0644   242 LAMKSGRLAAEAIAEalEGGDFSAEALAEYERRL 275
PLN02976 PLN02976
amine oxidase
 7-36 6.53e-06

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 48.33  E-value: 6.53e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 2418879974    7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PLN02976   694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLE 723
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
11-37 7.31e-06

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 43.29  E-value: 7.31e-06
                          10        20
                  ....*....|....*....|....*..
gi 2418879974  11 IIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
PRK12831 PRK12831
putative oxidoreductase; Provisional
 5-36 7.83e-06

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 47.71  E-value: 7.83e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PRK12831  139 KGKKVAVIGSGPAGLTCAGDLAKMGYDVTIFE 170
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 8-40 7.83e-06

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 47.39  E-value: 7.83e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKD 40
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGDD 33
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 282-371 8.89e-06

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 47.46  E-value: 8.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 282 FPL----AKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALILSDNLI----DGKFNSMEEAIQNYEQHmfvygRE 353
Cdd:PRK08850  269 FPLkmryARDFVRER---VALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILalwqQGRDIGLKRNLRGYERW-----RK 340

                          90
                  ....*....|....*...
gi 2418879974 354 AQAESTINETEMFSPDFS 371
Cdd:PRK08850  341 AEAAKMIAAMQGFRDLFS 358
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
8-38 9.32e-06

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 47.21  E-value: 9.32e-06
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERD 38
Cdd:COG0665     4 DVVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 5-37 9.93e-06

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 46.91  E-value: 9.93e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK12770   17 TGKKVAIIGAGPAGLAAAGYLACLGYEVHVYDK 49
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 7-37 1.07e-05

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 47.43  E-value: 1.07e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK12769  328 KRVAIIGAGPAGLACADVLARNGVAVTVYDR 358
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
296-330 1.27e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 46.87  E-value: 1.27e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2418879974 296 ITMVGDAAHLMPPFAGQGVNSGLVDALILSDNLID 330
Cdd:PRK07608  282 VALVGDAAHLIHPLAGQGMNLGLRDVAALADVLAG 316
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 7-36 1.83e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 46.65  E-value: 1.83e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PRK12814  194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFD 223
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 5-48 2.15e-05

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 46.38  E-value: 2.15e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERdkdrdARIFGG 48
Cdd:COG1233     2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEK-----NDTPGG 40
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 296-329 2.36e-05

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 45.98  E-value: 2.36e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2418879974 296 ITMVGDAAHLMPPFAGQGVNSGLVDALILSDNLI 329
Cdd:PRK05714  287 LALIGDAAHTIHPLAGQGVNLGFLDAAVLAEVLL 320
PRK13984 PRK13984
putative oxidoreductase; Provisional
 6-36 2.68e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 46.30  E-value: 2.68e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   6 NKKIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PRK13984  283 NKKVAIVGSGPAGLSAAYFLATMGYEVTVYE 313
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
7-58 3.08e-05

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 45.49  E-value: 3.08e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNgVDVTVYERDkDRdariFGG---TLDLHRDSGQ 58
Cdd:COG2907     4 MRIAVIGSGISGLTAAWLLSRR-HDVTLFEAN-DR----LGGhthTVDVDLDGRT 52
trkA PRK09496
Trk system potassium transporter TrkA;
1-41 3.25e-05

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 45.50  E-value: 3.25e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2418879974   1 MNLLNN-----KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDR 41
Cdd:PRK09496  221 MSEFGRlekpvKRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDPER 266
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 296-334 3.39e-05

ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase responsible for the 4-hydroxylateion of the phenol ring in the aerobic biosynthesis of ubiquinone


Pssm-ID: 273914 [Multi-domain]  Cd Length: 437  Bit Score: 45.52  E-value: 3.39e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2418879974 296 ITMVGDAAHLMPPFAGQGVNSGLVDALILSDNLIDGKFN 334
Cdd:TIGR01989 335 VALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSV 373
PRK06185 PRK06185
FAD-dependent oxidoreductase;
10-76 4.09e-05

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 45.24  E-value: 4.09e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2418879974  10 AIIGAGPVGLTMARLLQQNGVDVTVYERDKD--RDARifGGTldLHRDSgQEAMKKAGLLQTYydLALP 76
Cdd:PRK06185   10 CIVGGGPAGMMLGLLLARAGVDVTVLEKHADflRDFR--GDT--VHPST-LELMDELGLLERF--LELP 71
PRK09126 PRK09126
FAD-dependent hydroxylase;
9-37 4.19e-05

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 45.32  E-value: 4.19e-05
                          10        20
                  ....*....|....*....|....*....
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK09126    6 IVVVGAGPAGLSFARSLAGSGLKVTLIER 34
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 5-36 4.80e-05

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 45.50  E-value: 4.80e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PRK12778  430 NGKKVAVIGSGPAGLSFAGDLAKRGYDVTVFE 461
PRK08244 PRK08244
monooxygenase;
9-324 5.00e-05

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 45.12  E-value: 5.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKD--RDARifggTLDLHRDSgQEAMKKAGLLQTYydlaLPMGVNIADEKG 86
Cdd:PRK08244    5 VIIIGGGPVGLMLASELALAGVKTCVIERLKEtvPYSK----ALTLHPRT-LEILDMRGLLERF----LEKGRKLPSGHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  87 NILTTknvkpenRFDNPEINRNDLRTILLNSLQNNTVI--WDRKL----------VALEPDKEKWVLSFEDKPNE---TA 151
Cdd:PRK08244   76 AGLDT-------RLDFSALDTSSNYTLFLPQAETEKVLeeHARSLgveifrgaevLAVRQDGDGVEVVVRGPDGLrtlTS 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 152 DLVIIANGGMSKVRKYV------TDTEVEAtgtfnIQADIhqpAVNCP---GFFQLCNgnrlmaahRGNLLFANPNNNGA 222
Cdd:PRK08244  149 SYVVGADGAGSIVRKQAgiafpgTDATFTA-----MLGDV---VLKDPppsSVLSLCT--------REGGVMIVPLSGGI 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 223 LHFGISfkTPDdwknKTQVdfqdsnnivdfLLKEFSDWDERYKELIRSTSSFVGL-----------ATRifpLAKPWKSS 291
Cdd:PRK08244  213 YRVLII--DPE----RPQV-----------PKDEPVTLEELKTSLIRICGTDFGLndpvwmsrfgnATR---QAERYRSG 272

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2418879974 292 RplpITMVGDAAHLMPPFAGQGVNSGLVDALIL 324
Cdd:PRK08244  273 R---IFLAGDAAHIHFPAGGQGLNVGLQDAMNL 302
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 277-323 5.39e-05

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 44.97  E-value: 5.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2418879974 277 LATRIFPLAKPWKSSRPLP-ITMVGDAAHLMPPFAGQGVNSGL--VDALI 323
Cdd:PRK08020  263 VAAGAFPLTRRHALQYVQPgLALVGDAAHTINPLAGQGVNLGYrdVDALL 312
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
 7-44 5.57e-05

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 44.34  E-value: 5.57e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDAR 44
Cdd:COG2084     2 MKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEA 39
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 8-59 5.60e-05

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 44.46  E-value: 5.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDkDRDARIFGGTLDLHRDSGQE 59
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVARG-AHAEALRENGLRLESPDGDR 52
PRK07538 PRK07538
hypothetical protein; Provisional
 8-36 5.88e-05

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 44.89  E-value: 5.88e-05
                          10        20
                  ....*....|....*....|....*....
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PRK07538    2 KVLIAGGGIGGLTLALTLHQRGIEVVVFE 30
trkA PRK09496
Trk system potassium transporter TrkA;
8-52 7.24e-05

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 44.73  E-value: 7.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRdARIFGGTLDL 52
Cdd:PRK09496    2 KIIIVGAGQVGYTLAENLSGENNDVTVIDTDEER-LRRLQDRLDV 45
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 7-39 9.20e-05

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 44.48  E-value: 9.20e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDK 39
Cdd:PRK12771  138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGP 170
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 7-58 9.31e-05

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 44.07  E-value: 9.31e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERdkdrdARIFGG--------TLDLHRDSGQ 58
Cdd:COG3349     4 PRVVVVGGGLAGLAAAVELAEAGFRVTLLEA-----RPRLGGrarsfpdpDTGLPIDNGQ 58
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 2-39 1.13e-04

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 44.08  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2418879974   2 NLLNNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDK 39
Cdd:PLN02172    6 NPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREK 43
PRK08013 PRK08013
oxidoreductase; Provisional
 281-328 1.22e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 43.88  E-value: 1.22e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2418879974 281 IFPL----AKPWKSSRplpITMVGDAAHLMPPFAGQGVNSGLVDALILSDNL 328
Cdd:PRK08013  268 VFPLtgryARQFAAHR---LALVGDAAHTIHPLAGQGVNLGFMDAAELIAEL 316
ApbA pfam02558
Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also ...
 9-59 1.40e-04

Ketopantoate reductase PanE/ApbA; This is a family of 2-dehydropantoate 2-reductases also known as ketopantoate reductases, EC:1.1.1.169. The reaction catalyzed by this enzyme is: (R)-pantoate + NADP(+) <=> 2-dehydropantoate + NADPH. AbpA catalyzes the NADPH reduction of ketopantoic acid to pantoic acid in the alternative pyrimidine biosynthetic (APB) pathway. ApbA and PanE are allelic. ApbA, the ketopantoate reductase enzyme is required for the synthesis of thiamine via the APB biosynthetic pathway.


Pssm-ID: 426831 [Multi-domain]  Cd Length: 147  Bit Score: 41.83  E-value: 1.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGGtLDLHRDSGQE 59
Cdd:pfam02558   1 IAILGAGAIGSLLGARLAKAGHDVTLILRGAELAAIKKNG-LRLTSPGGER 50
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 4-44 1.60e-04

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 43.53  E-value: 1.60e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2418879974   4 LNNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDAR 44
Cdd:COG0771     2 LKGKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPAPELA 42
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-164 2.44e-04

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 42.69  E-value: 2.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYErdkDRDARIFGG-----TLDLHRDSGQEAMKKAGLLQTYYDLALPMGVNI 81
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIE---DEGTCPYGGcvlskALLGAAEAPEIASLWADLYKRKEEVVKKLNNGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  82 AdekgnILTTKNVKpenrfdnpeinrndlrtillnslqnnTVIWDRKLVALEPDKEKWVLSFedkpneTADLVIIANGGM 161
Cdd:pfam07992  78 E-----VLLGTEVV--------------------------SIDPGAKKVVLEELVDGDGETI------TYDRLVIATGAR 120


                  ...
gi 2418879974 162 SKV 164
Cdd:pfam07992 121 PRL 123
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 8-41 2.82e-04

L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine, via NAD(H)-dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176196 [Multi-domain]  Cd Length: 334  Bit Score: 42.51  E-value: 2.82e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVD-VTVYERDKDR 41
Cdd:cd08234   162 SVLVFGAGPIGLLLAQLLKLNGASrVTVAEPNEEK 196
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
1-324 4.12e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 42.16  E-value: 4.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   1 MNLLNNKKIAIIGAGPVGLTMARLLQQNGVDVTVYE-RDKDR------DARIFGGTLD---LHRDSGQEAMKKAGLLQTY 70
Cdd:PRK08773    1 MSRRSRRDAVIVGGGVVGAACALALADAGLSVALVEgREPPRwqadqpDLRVYAFAADnaaLLDRLGVWPAVRAARAQPY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  71 YDLalpmgvNIADEKGNilttknvkPENRFDNPEINRNDLRTILLNSLQNNTViWDR------------KLVALEPDKEK 138
Cdd:PRK08773   81 RRM------RVWDAGGG--------GELGFDADTLGREQLGWIVENDLLVDRL-WAAlhaagvqlhcpaRVVALEQDADR 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 139 WVLSFEDKPNETADLVIIANGGMSKVRKyVTDTEVEAtgtfniqADIHQPAVncPGFFQLCNGNRLMAAHR----GNLLF 214
Cdd:PRK08773  146 VRLRLDDGRRLEAALAIAADGAASTLRE-LAGLPVSR-------HDYAQRGV--VAFVDTEHPHQATAWQRflptGPLAL 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974 215 AnPNNNGalHFGISFKTPDDwknktqvdfqDSNNIVDFLLKEFSdwderyKELIRSTSSFVGlATRI------FPL---- 284
Cdd:PRK08773  216 L-PFADG--RSSIVWTLPDA----------EAERVLALDEAAFS------RELTQAFAARLG-EVRVasprtaFPLrrql 275

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 2418879974 285 AKPWKSSRPLpitMVGDAAHLMPPFAGQGVNSGLVDALIL 324
Cdd:PRK08773  276 VQQYVSGRVL---TLGDAAHVVHPLAGQGVNLGLRDVAAL 312
PRK06522 PRK06522
2-dehydropantoate 2-reductase; Reviewed
 8-37 4.30e-04

2-dehydropantoate 2-reductase; Reviewed


Pssm-ID: 235821 [Multi-domain]  Cd Length: 304  Bit Score: 41.76  E-value: 4.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK06522    2 KIAILGAGAIGGLFGAALAQAGHDVTLVAR 31
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
298-330 4.34e-04

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 41.89  E-value: 4.34e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974 298 MVGDAAHLMPPFAGQGVNSGLVDALILSDNLID 330
Cdd:PRK07333  284 LVGDAAHGIHPIAGQGLNLGLKDVAALAEVVVE 316
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 7-37 4.41e-04

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 41.72  E-value: 4.41e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:COG0446   125 KRAVVIGGGPIGLELAEALRKRGLKVTLVER 155
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 7-65 4.85e-04

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 42.09  E-value: 4.85e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYER--------DKD-RDA--RIFGGTLDLHRDSGQEAMKKAG 65
Cdd:PRK06292  170 KSLAVIGGGVIGLELGQALSRLGVKVTVFERgdrilpleDPEvSKQaqKILSKEFKIKLGAKVTSVEKSG 239
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 9-95 5.31e-04

TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD.


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 39.43  E-value: 5.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGvDVTVYERDKDRdarifggtLDLHRDSG----------QEAMKKAGLLQtyYDLALpmg 78
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKDEER--------VEELREEGvpvvvgdatdEEVLEEAGIEE--ADAVI--- 66

                          90
                  ....*....|....*..
gi 2418879974  79 VNIADEKGNILTTKNVK 95
Cdd:pfam02254  67 AATGDDEANILIVLLAR 83
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
9-37 5.58e-04

L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 41.67  E-value: 5.58e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2418879974   9 IAIIGAGPVGLTMARLLQQ-NGVDVTVYER 37
Cdd:COG0579     7 VVIIGAGIVGLALARELSRyEDLKVLVLEK 36
COG2085 COG2085
Predicted dinucleotide-binding enzyme [General function prediction only];
9-41 5.80e-04

Predicted dinucleotide-binding enzyme [General function prediction only];


Pssm-ID: 441688 [Multi-domain]  Cd Length: 205  Bit Score: 40.54  E-value: 5.80e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKDR 41
Cdd:COG2085     1 IGIIGTGNIGSALARRLAAAGHEVVIGSRDPEK 33
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
 7-37 6.21e-04

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 41.55  E-value: 6.21e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK12409    2 SHIAVIGAGITGVTTAYALAQRGYQVTVFDR 32
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 5-51 8.32e-04

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 41.18  E-value: 8.32e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKdrdaRIFGGTLD 51
Cdd:PRK09564  148 EIKNIVIIGAGFIGLEAVEAAKHLGKNVRIIQLED----RILPDSFD 190
GpsA COG0240
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
 7-40 1.09e-03

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440010 [Multi-domain]  Cd Length: 327  Bit Score: 40.40  E-value: 1.09e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKD 40
Cdd:COG0240     1 MKIAVLGAGSWGTALAKVLARNGHEVTLWGRDPE 34
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
7-159 1.21e-03

Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 40.71  E-value: 1.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVG-LTMARLLQQ--NGVDVTVYERDKDRDARI-FGGTLDLHRdsgqeamkkagllqtyydLALP---MGV 79
Cdd:COG4529     6 KRIAIIGGGASGtALAIHLLRRapEPLRITLFEPRPELGRGVaYSTDSPEHL------------------LNVPagrMSA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974  80 nIADEKGNILTTknVKPENRFDNPEINRND----------LRTILLNSLQN-----NTVIWDRKLVALEPDKEKWVLSFE 144
Cdd:COG4529    68 -FPDDPDHFLRW--LRENGARAAPAIDPDAfvprrlfgeyLRERLAEALARapagvRLRHIRAEVVDLERDDGGYRVTLA 144

                         170
                  ....*....|....*
gi 2418879974 145 DKPNETADLVIIANG 159
Cdd:COG4529   145 DGETLRADAVVLATG 159
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 7-65 1.25e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 40.38  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERdKDRDARIFGGTLdlhRDSGQEAMKKAG 65
Cdd:pfam07992 153 KRVVVVGGGYIGVELAAALAKLGKEVTLIEA-LDRLLRAFDEEI---SAALEKALEKNG 207
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
11-47 1.50e-03

Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 40.10  E-value: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2418879974  11 IIGAGPVGLTMARLLQQNGVDVTVYERDKDR--DARIFG 47
Cdd:COG1226   129 IAGFGRVGQIVARLLRAEGIPFVVIDLDPERveELRRFG 167
PRK12921 PRK12921
oxidoreductase;
8-58 1.62e-03

oxidoreductase;


Pssm-ID: 183829 [Multi-domain]  Cd Length: 305  Bit Score: 39.84  E-value: 1.62e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKdRDARIFGGTLDLHRDSGQ 58
Cdd:PRK12921    2 RIAVVGAGAVGGTFGGRLLEAGRDVTFLVRPK-RAKALRERGLVIRSDHGD 51
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 4-55 1.71e-03

Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 37.46  E-value: 1.71e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2418879974   4 LNNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARifgGTLDLHRD 55
Cdd:pfam13241   5 LRGKRVLVVGGGEVAARKARKLLEAGAKVTVVSPEITPFLE---GLLDLIRR 53
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
5-45 1.76e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 40.10  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARI 45
Cdd:COG2509    29 LKYDVVIVGAGPAGLFAALELAEAGLKPLVLERGKDVEERT 69
NDP-sugDHase TIGR03026
nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent ...
 7-64 1.87e-03

nucleotide sugar dehydrogenase; Enzymes in this family catalyze the NAD-dependent alcohol-to-acid oxidation of nucleotide-linked sugars. Examples include UDP-glucose 6-dehydrogenase (1.1.1.22), GDP-mannose 6-dehydrogenase (1.1.1.132), UDP-N-acetylglucosamine 6-dehydrogenase (1.1.1.136), UDP-N-acetyl-D-galactosaminuronic acid dehydrogenase, and UDP-N-acetyl-D-mannosaminuronic acid dehydrogenase. These enzymes are most often involved in the biosynthesis of polysaccharides and are often found in operons devoted to that purpose. All of these enzymes contain three Pfam domains, pfam03721, pfam00984, and pfam03720 for the N-terminal, central, and C-terminal regions respectively.


Pssm-ID: 274399 [Multi-domain]  Cd Length: 409  Bit Score: 39.90  E-value: 1.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGGTLDLHRDSGQEAMKKA 64
Cdd:TIGR03026   1 MKIAVIGLGYVGLPLAALLADLGHDVTGVDIDQEKVDKLNKGKSPIYEPGLDELLAKA 58
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 6-64 1.91e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 39.74  E-value: 1.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2418879974   6 NKKIAIIGAGPVGLTMARLLQQNGV-DVTVYERDKDR-D-ARIFG--GTLDLHRDSGQEAMKKA 64
Cdd:COG1063   162 GDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERlElARELGadAVVNPREEDLVEAVREL 225
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
7-57 2.02e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 39.74  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYErdkdRDARIFGGTLD---------LHRDSG 57
Cdd:COG1251   143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVE----RAPRLLPRQLDeeagallqrLLEALG 198
PRK14619 PRK14619
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional
 5-37 2.13e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237771 [Multi-domain]  Cd Length: 308  Bit Score: 39.59  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974   5 NNKKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK14619    3 QPKTIAILGAGAWGSTLAGLASANGHRVRVWSR 35
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 8-65 2.83e-03

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 36.41  E-value: 2.83e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERdKDRDARIFGGTLdlhRDSGQEAMKKAG 65
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKVTVVER-RDRLLPGFDPEI---AKILQEKLEKNG 54
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 8-64 3.00e-03

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 39.31  E-value: 3.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDRDARIFGGTLDLHRDSGQEAMKKA 64
Cdd:cd01620   164 KVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRYSQKEELEKE 220
PRK07364 PRK07364
FAD-dependent hydroxylase;
298-330 3.16e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 39.23  E-value: 3.16e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2418879974 298 MVGDAAHLMPPFAGQGVNSGLVDALILSDNLID 330
Cdd:PRK07364  298 LVGDAAHCCHPVGGQGLNLGIRDAAALAQVLQT 330
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 8-36 3.39e-03

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


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 39.54  E-value: 3.39e-03
                           10        20
                   ....*....|....*....|....*....
gi 2418879974    8 KIAIIGAGPVGLTMARLLQQNGVDVTVYE 36
Cdd:PRK12775   432 KVAICGSGPAGLAAAADLVKYGVDVTVYE 460
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
 109-159 3.73e-03

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 39.17  E-value: 3.73e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2418879974 109 DLRTILLNSLQNN-TVIWDRKLVALEPDKEKWVLSFEDKPNETADLVIIANG 159
Cdd:TIGR03197 136 QLCRALLAHAGIRlTLHFNTEITSLERDGEGWQLLDANGEVIAASVVVLANG 187
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 7-44 4.60e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 38.91  E-value: 4.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDK------DRDAR 44
Cdd:COG1249   169 KSLVVIGGGYIGLEFAQIFARLGSEVTLVERGDrllpgeDPEIS 212
PRK06184 PRK06184
hypothetical protein; Provisional
 298-321 5.06e-03

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 38.81  E-value: 5.06e-03
                          10        20
                  ....*....|....*....|....
gi 2418879974 298 MVGDAAHLMPPFAGQGVNSGLVDA 321
Cdd:PRK06184  285 LAGDAAHVHPPAGGQGLNTSVQDA 308
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 298-324 5.16e-03

2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 38.60  E-value: 5.16e-03
                          10        20
                  ....*....|....*....|....*..
gi 2418879974 298 MVGDAAHLMPPFAGQGVNSGLVDALIL 324
Cdd:PRK08849  283 LLGDAAHTINPLAGQGVNLGFKDVDVL 309
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
 7-37 5.41e-03

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 38.85  E-value: 5.41e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:PRK12809  311 EKVAVIGAGPAGLGCADILARAGVQVDVFDR 341
gpsA PRK00094
NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;
7-40 6.36e-03

NAD(P)H-dependent glycerol-3-phosphate dehydrogenase;


Pssm-ID: 234629 [Multi-domain]  Cd Length: 325  Bit Score: 38.13  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDKD 40
Cdd:PRK00094    2 MKIAVLGAGSWGTALAIVLARNGHDVTLWARDPE 35
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 9-49 6.89e-03

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 38.14  E-value: 6.89e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2418879974   9 IAIIGAGPVGLTMARLLQQNGVDVTVYERDKdrdariFGGT 49
Cdd:COG1249     6 LVVIGAGPGGYVAAIRAAQLGLKVALVEKGR------LGGT 40
PRK06834 PRK06834
hypothetical protein; Provisional
 298-324 7.44e-03

hypothetical protein; Provisional


Pssm-ID: 235870 [Multi-domain]  Cd Length: 488  Bit Score: 38.08  E-value: 7.44e-03
                          10        20
                  ....*....|....*....|....*..
gi 2418879974 298 MVGDAAHLMPPFAGQGVNSGLVDALIL 324
Cdd:PRK06834  269 LAGDAAHVHSPVGGQGLNTGVQDAVNL 295
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
 8-41 7.52e-03

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 36.68  E-value: 7.52e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERDKDR 41
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEK 34
CysG2 COG1648
Siroheme synthase (precorrin-2 oxidase/ferrochelatase domain) [Coenzyme transport and ...
 4-35 7.83e-03

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


Pssm-ID: 441254 [Multi-domain]  Cd Length: 211  Bit Score: 37.44  E-value: 7.83e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2418879974   4 LNNKKIAIIGAGPVGLTMARLLQQNGVDVTVY 35
Cdd:COG1648    10 LEGRRVLVVGGGEVAARKARLLLKAGARVTVV 41
BVR-B_like_SDR_a cd05244
biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; ...
 8-48 7.86e-03

biliverdin IX beta reductase (BVR-B, aka flavin reductase)-like proteins; atypical (a) SDRs; Human BVR-B catalyzes pyridine nucleotide-dependent production of bilirubin-IX beta during fetal development; in the adult BVR-B has flavin and ferric reductase activities. Human BVR-B catalyzes the reduction of FMN, FAD, and riboflavin. Recognition of flavin occurs mostly by hydrophobic interactions, accounting for the broad substrate specificity. Atypical SDRs are distinct from classical SDRs. BVR-B does not share the key catalytic triad, or conserved tyrosine typical of SDRs. The glycine-rich NADP-binding motif of BVR-B is GXXGXXG, which is similar but not identical to the pattern seen in extended SDRs. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif.


Pssm-ID: 187555 [Multi-domain]  Cd Length: 207  Bit Score: 37.22  E-value: 7.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2418879974   8 KIAIIGA-GPVGLTMARLLQQNGVDVTVYERDKDRDARIFGG 48
Cdd:cd05244     1 KIAIIGAtGRTGSAIVREALARGHEVTALVRDPAKLPAEHEK 42
glucose_DH cd08230
Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain ...
 4-37 8.54e-03

Glucose dehydrogenase; Glucose dehydrogenase (GlcDH), a member of the medium chain dehydrogenase/zinc-dependent alcohol dehydrogenase-like family, catalyzes the NADP(+)-dependent oxidation of glucose to gluconate, the first step in the Entner-Doudoroff pathway, an alternative to or substitute for glycolysis or the pentose phosphate pathway. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossman fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.


Pssm-ID: 176192 [Multi-domain]  Cd Length: 355  Bit Score: 37.97  E-value: 8.54e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2418879974   4 LNNKKIAIIGAGPVGLTMARLLQQNGVDVTVYER 37
Cdd:cd08230   171 WNPRRALVLGAGPIGLLAALLLRLRGFEVYVLNR 204
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
296-326 8.56e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 37.96  E-value: 8.56e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974 296 ITMVGDAAHLMPPFAGQGVNSGLVDALILSD 326
Cdd:PRK07494  282 TALVGEAAHVFPPIGAQGLNLGLRDVATLVE 312
PRK06370 PRK06370
FAD-containing oxidoreductase;
7-43 8.84e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 37.87  E-value: 8.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2418879974   7 KKIAIIGAGPVGLTMARLLQQNGVDVTVYERDK------DRDA 43
Cdd:PRK06370  172 EHLVIIGGGYIGLEFAQMFRRFGSEVTVIERGPrllpreDEDV 214
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
8-38 9.48e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 37.41  E-value: 9.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2418879974   8 KIAIIGAGPVGLTMARLLQQNGVDVTVYERD 38
Cdd:COG0492     2 DVVIIGAGPAGLTAAIYAARAGLKTLVIEGG 32
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
8-47 9.71e-03

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 38.00  E-value: 9.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2418879974   8 KIAIIGAGPVGLTMARL--LQQNGVDVTVYERDKDRDAriFG 47
Cdd:PRK08255    2 RIVCIGGGPAGLYFALLmkLLDPAHEVTVVERNRPYDT--FG 41
 
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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