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Conserved domains on  [gi|378976829|ref|YP_005224970|]
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4-hydroxybenzoate 3-monooxygenase [Klebsiella pneumoniae subsp. pneumoniae HS11286]

Protein Classification

4-hydroxybenzoate 3-monooxygenase( domain architecture ID 10013028)

4-hydroxybenzoate 3-monooxygenase catalyzes the formation of protocatechuate from 4-hydroxybenzoate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 1-392 0e+00

4-hydroxybenzoate 3-monooxygenase; Validated


:

Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 767.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:PRK08243   1 MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGLVHDGIELRFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVAIHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:PRK08243  81 GRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVTYEKDGEEHRLDCDFIAGCDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 161 FHGVSRQSIPAGILQTYESVWPFGWLGLLADTPPVNPELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEAWSDERFW 240
Cdd:PRK08243 161 FHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFALCSMRSPTRSRYYLQCPLDDKVEDWSDERFW 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 241 QELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRG 320
Cdd:PRK08243 241 DELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378976829 321 RSDLLAAYSQLALDRVWKGERFSWFMTRLLHDFPDQNAFDAKMQAADRRYYLGSRAGLTTIAENYVGLPMER 392
Cdd:PRK08243 321 DTALLDAYSATALRRVWKAERFSWWMTSMLHRFPDDDPFDQRIQLAELDYLTSSRAAATTLAENYVGLPFED 392
 
Name Accession Description Interval E-value
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 1-392 0e+00

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 767.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:PRK08243   1 MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGLVHDGIELRFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVAIHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:PRK08243  81 GRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVTYEKDGEEHRLDCDFIAGCDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 161 FHGVSRQSIPAGILQTYESVWPFGWLGLLADTPPVNPELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEAWSDERFW 240
Cdd:PRK08243 161 FHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFALCSMRSPTRSRYYLQCPLDDKVEDWSDERFW 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 241 QELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRG 320
Cdd:PRK08243 241 DELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378976829 321 RSDLLAAYSQLALDRVWKGERFSWFMTRLLHDFPDQNAFDAKMQAADRRYYLGSRAGLTTIAENYVGLPMER 392
Cdd:PRK08243 321 DTALLDAYSATALRRVWKAERFSWWMTSMLHRFPDDDPFDQRIQLAELDYLTSSRAAATTLAENYVGLPFED 392
pbenz_hydroxyl TIGR02360
4-hydroxybenzoate 3-monooxygenase; Members of this family are the enzyme 4-hydroxybenzoate ...
 1-389 0e+00

4-hydroxybenzoate 3-monooxygenase; Members of this family are the enzyme 4-hydroxybenzoate 3-monooxygenase, also called p-hydroxybenzoate hydroxylase. It converts 4-hydroxybenzoate + NADPH + molecular oxygen to protocatechuate + NADPH + water. It contains monooxygenase (pfam01360) and FAD binding (pfam01494) domains. Pathways that contain this enzyme include the protocatechuate 4,5-degradation pathway. [Energy metabolism, Other]


Pssm-ID: 131413 [Multi-domain]  Cd Length: 390  Bit Score: 659.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829    1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:TIGR02360   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQSRDYVLGRIRAGVLEQGTVDLLREAGVDERMDREGLVHEGTEIAFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   81 GQRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVAIHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:TIGR02360  81 GQRFRIDLKALTGGKTVMVYGQTEVTRDLMEAREAAGLTTVYDADDVRLHDLAGDRPYVTFERDGERHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  161 FHGVSRQSIPAGILQTYESVWPFGWLGLLADTPPVNPELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEAWSDERFW 240
Cdd:TIGR02360 161 FHGVSRASIPAEVLKEFERVYPFGWLGILSETPPVSHELIYSNHERGFALCSMRSATRSRYYVQVPLTDKVEDWSDDRFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  241 QELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRG 320
Cdd:TIGR02360 241 AELKRRLPSEAAERLVTGPSIEKSIAPLRSFVCEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVHYLYEALLEHYQEG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378976829  321 RSDLLAAYSQLALDRVWKGERFSWFMTRLLHDFPDQNAFDAKMQAADRRYYLGSRAGLTTIAENYVGLP 389
Cdd:TIGR02360 321 SSAGIEGYSARALARVWKAERFSWWMTSLLHRFPDTDAFDQRIQQAELEYLLGSEAAQATLAENYVGLP 389
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 2-343 6.43e-105

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: 313.49  E-value: 6.43e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829    2 KTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRirAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFDG 81
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPR--AHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   82 QRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVA-IHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:pfam01494  79 TRRRADLDFLTSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLSlEQDGDGVTAVVRDRRDGEEYTVRAKYLVGCDG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  161 FHGVSRQSIpaGILQTYESVWPFGWLGLLADTPPVNP--------ELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVE 232
Cdd:pfam01494 159 GRSPVRKTL--GIEFEGFEGVPFGSLDVLFDAPDLSDpverafvhYLIYAPHSRGFMVGPWRSAGRERYYVQVPWDEEVE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  233 AWSDERFWQELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYL-WR 311
Cdd:pfam01494 237 ERPEEFTDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLaWK 316

                         330       340       350
                  ....*....|....*....|....*....|..
gi 378976829  312 ILREYYHRGRSDLLAAYSQLALDRVWKGERFS 343
Cdd:pfam01494 317 LAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-372 5.29e-50

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: 171.27  E-value: 5.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPqyVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPP--PRPDGRGIALSPRSLELLRRLGLWDRLLARGAPIRGIRVRDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVALSELTDGKSVMVYG--QTEVTRDLMAARAASGAPIVYGVSEVAIHDAkSDRPTITyLSEGETcrLECDFIAGC 158
Cdd:COG0654   80 SDGRVLARFDAAETGLPAGLVvpRADLERALLEAARALGVELRFGTEVTGLEQD-ADGVTVT-LADGRT--LRADLVVGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 159 DGFHGVSRQSIPAGiLQTYESVWPFGWLGLLADtppvnpeliyahhqrgfvlcsqrsltrsryylqvpLSDKVEAWSDer 238
Cdd:COG0654  156 DGARSAVRRLLGIG-FTGRDYPQRALWAGVRTE-----------------------------------LRARLAAAGP-- 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 239 fwqelksRLPEELAsrlvtghALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYY- 317
Cdd:COG0654  198 -------RLGELLE-------LSPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALr 263

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 378976829 318 HRGRSDLLAAYSQLALDRVWKGERFSWFMTRLLH--DFPDQNAFDAKMQAADRRYYL 372
Cdd:COG0654  264 GRDDEAALARYERERRPRAARVQRAADALGRLFHpdSPPLRLLRNAGLRLLDRLPPL 320
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 5-101 5.54e-06

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: 47.91  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVIL-ERQTPQYVLGRiRAGIleSGTVDLLREAGVAQRMDAEglvhHGVEFLFDGQR 83
Cdd:cd08234  163 VLVFGAGPIGLLLAQLLKLNGASRVTVaEPNEEKLELAK-KLGA--TETVDPSREDPEAQKEDNP----YGFDVVIEATG 235

                         90       100
                 ....*....|....*....|..
gi 378976829  84 VPV----ALSELTDGKSVMVYG 101
Cdd:cd08234  236 VPKtleqAIEYARRGGTVLVFG 257
 
Name Accession Description Interval E-value
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 1-392 0e+00

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 767.04  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:PRK08243   1 MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGLVHDGIELRFD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVAIHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:PRK08243  81 GRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVTYEKDGEEHRLDCDFIAGCDG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 161 FHGVSRQSIPAGILQTYESVWPFGWLGLLADTPPVNPELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEAWSDERFW 240
Cdd:PRK08243 161 FHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFALCSMRSPTRSRYYLQCPLDDKVEDWSDERFW 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 241 QELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRG 320
Cdd:PRK08243 241 DELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 378976829 321 RSDLLAAYSQLALDRVWKGERFSWFMTRLLHDFPDQNAFDAKMQAADRRYYLGSRAGLTTIAENYVGLPMER 392
Cdd:PRK08243 321 DTALLDAYSATALRRVWKAERFSWWMTSMLHRFPDDDPFDQRIQLAELDYLTSSRAAATTLAENYVGLPFED 392
pbenz_hydroxyl TIGR02360
4-hydroxybenzoate 3-monooxygenase; Members of this family are the enzyme 4-hydroxybenzoate ...
 1-389 0e+00

4-hydroxybenzoate 3-monooxygenase; Members of this family are the enzyme 4-hydroxybenzoate 3-monooxygenase, also called p-hydroxybenzoate hydroxylase. It converts 4-hydroxybenzoate + NADPH + molecular oxygen to protocatechuate + NADPH + water. It contains monooxygenase (pfam01360) and FAD binding (pfam01494) domains. Pathways that contain this enzyme include the protocatechuate 4,5-degradation pathway. [Energy metabolism, Other]


Pssm-ID: 131413 [Multi-domain]  Cd Length: 390  Bit Score: 659.91  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829    1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:TIGR02360   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQSRDYVLGRIRAGVLEQGTVDLLREAGVDERMDREGLVHEGTEIAFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   81 GQRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVAIHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:TIGR02360  81 GQRFRIDLKALTGGKTVMVYGQTEVTRDLMEAREAAGLTTVYDADDVRLHDLAGDRPYVTFERDGERHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  161 FHGVSRQSIPAGILQTYESVWPFGWLGLLADTPPVNPELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEAWSDERFW 240
Cdd:TIGR02360 161 FHGVSRASIPAEVLKEFERVYPFGWLGILSETPPVSHELIYSNHERGFALCSMRSATRSRYYVQVPLTDKVEDWSDDRFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  241 QELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRG 320
Cdd:TIGR02360 241 AELKRRLPSEAAERLVTGPSIEKSIAPLRSFVCEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVHYLYEALLEHYQEG 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378976829  321 RSDLLAAYSQLALDRVWKGERFSWFMTRLLHDFPDQNAFDAKMQAADRRYYLGSRAGLTTIAENYVGLP 389
Cdd:TIGR02360 321 SSAGIEGYSARALARVWKAERFSWWMTSLLHRFPDTDAFDQRIQQAELEYLLGSEAAQATLAENYVGLP 389
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 2-343 6.43e-105

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: 313.49  E-value: 6.43e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829    2 KTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRirAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFDG 81
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPR--AHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   82 QRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVA-IHDAKSDRPTITYLSEGETCRLECDFIAGCDG 160
Cdd:pfam01494  79 TRRRADLDFLTSPPRVTVYPQTELEPILVEHAEARGAQVRFGTEVLSlEQDGDGVTAVVRDRRDGEEYTVRAKYLVGCDG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  161 FHGVSRQSIpaGILQTYESVWPFGWLGLLADTPPVNP--------ELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVE 232
Cdd:pfam01494 159 GRSPVRKTL--GIEFEGFEGVPFGSLDVLFDAPDLSDpverafvhYLIYAPHSRGFMVGPWRSAGRERYYVQVPWDEEVE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  233 AWSDERFWQELKSRLPEELASRLVTGHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYL-WR 311
Cdd:pfam01494 237 ERPEEFTDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLaWK 316

                         330       340       350
                  ....*....|....*....|....*....|..
gi 378976829  312 ILREYYHRGRSDLLAAYSQLALDRVWKGERFS 343
Cdd:pfam01494 317 LAAVLRGQAGESLLDTYSAERLPVAWAVVDFA 348
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-372 5.29e-50

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: 171.27  E-value: 5.29e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPqyVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:COG0654    2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPP--PRPDGRGIALSPRSLELLRRLGLWDRLLARGAPIRGIRVRDG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVALSELTDGKSVMVYG--QTEVTRDLMAARAASGAPIVYGVSEVAIHDAkSDRPTITyLSEGETcrLECDFIAGC 158
Cdd:COG0654   80 SDGRVLARFDAAETGLPAGLVvpRADLERALLEAARALGVELRFGTEVTGLEQD-ADGVTVT-LADGRT--LRADLVVGA 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 159 DGFHGVSRQSIPAGiLQTYESVWPFGWLGLLADtppvnpeliyahhqrgfvlcsqrsltrsryylqvpLSDKVEAWSDer 238
Cdd:COG0654  156 DGARSAVRRLLGIG-FTGRDYPQRALWAGVRTE-----------------------------------LRARLAAAGP-- 197

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 239 fwqelksRLPEELAsrlvtghALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYY- 317
Cdd:COG0654  198 -------RLGELLE-------LSPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALr 263

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 378976829 318 HRGRSDLLAAYSQLALDRVWKGERFSWFMTRLLH--DFPDQNAFDAKMQAADRRYYL 372
Cdd:COG0654  264 GRDDEAALARYERERRPRAARVQRAADALGRLFHpdSPPLRLLRNAGLRLLDRLPPL 320
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 5-330 9.08e-15

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: 74.93  E-value: 9.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829    5 VAIIGAGPSGLLLGQLLHNAGIHTVILERQ------TPQYVlGRIRAgiLESGTVDLLREAGVAQR-MDAEGLVHHGVEF 77
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEATplpapaDPGFD-NRVSA--LSAASIRLLEKLGVWDKiEPARAQPIRDIHV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   78 LFDGQRVPVALSELTDGKSVMvyGQTEVTRDLMAA-----RAASGAPIVYGVSEVAIHDaKSDRPTITyLSEGEtcRLEC 152
Cdd:TIGR01988  79 SDGGSFGALRFDADEIGLEAL--GYVVENRVLQQAlwerlQELPNVTLLCPARVVELPR-HSDHVELT-LDDGQ--QLRA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  153 DFIAGCDGFHGVSRQSipAGILQTyesVWPFGWLGLLAdtppvNPELIYAHHQRGFvlcsQRSLT------------RSR 220
Cdd:TIGR01988 153 RLLVGADGANSKVRQL--AGIPTT---GWDYGQSAVVA-----NVKHERPHQGTAW----ERFTPtgplallplpdnRSS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  221 --YYLQVPLSDKVEAWSDERFWQELKSRLPEELASRLVTGhalEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKG 298
Cdd:TIGR01988 219 lvWTLPPEEAERLLALSDEEFLAELQRAFGSRLGAITLVG---ERHAFPLSLTHAKRYVAPRLALIGDAAHTIHPLAGQG 295

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 378976829  299 LNLAASDVNYLWRILREYYHRGR----SDLLAAYSQ 330
Cdd:TIGR01988 296 LNLGLRDVAALAEVLEDARRRGEdigsLRVLQRYER 331
PRK06126 PRK06126
hypothetical protein; Provisional
 1-328 1.61e-13

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 71.95  E-value: 1.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVlgRIRAGILESGTVDLLREAGVAQRMDAEGLvhhGVEFLFD 80
Cdd:PRK06126   6 SETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAF--NPKANTTSARSMEHFRRLGIADEVRSAGL---PVDYPTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 --------GQ-----RVPVALSELTDGKSVMVY----------GQTEVTRDLM-AARAASGAPIVYGVSEVAI-HDAKSD 135
Cdd:PRK06126  81 iayftrltGYelarfRLPSAREAITPVGGPDGSwpspelphriPQKYLEPILLeHAAAQPGVTLRYGHRLTDFeQDADGV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 136 RPTITYLSEGETCRLECDFIAGCDGFHGVSRQSIpaGIlqTYEsvwpfgwlGLLADTPPVN-----PELIYAH-HQRG-- 207
Cdd:PRK06126 161 TATVEDLDGGESLTIRADYLVGCDGARSAVRRSL--GI--SYE--------GTSGLQRDLSiyiraPGLAALVgHDPAwm 228

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 208 -FVLCSQRSLT------RSRYYLQVPLSDKVEAWSDER-----FWQELKSRLPEELASRLV-TGHALeksiaplrsfVVE 274
Cdd:PRK06126 229 yWLFNPDRRGVlvaidgRDEWLFHQLRGGEDEFTIDDVdarafVRRGVGEDIDYEVLSVVPwTGRRL----------VAD 298

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 378976829 275 PMQYGRLFLVGDAAHIVPPTGAKGLNLAASD-VNYLWRILREYYHRGRSDLLAAY 328
Cdd:PRK06126 299 SYRRGRVFLAGDAAHLFTPTGGYGMNTGIGDaVNLAWKLAAVLNGWAGPALLDSY 353
PRK06834 PRK06834
hypothetical protein; Provisional
 1-373 7.06e-13

hypothetical protein; Provisional


Pssm-ID: 235870 [Multi-domain]  Cd Length: 488  Bit Score: 69.66  E-value: 7.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRiRAGILESGTVDLLREAGVAQRmdaeglvhhgveFLFD 80
Cdd:PRK06834   2 TEHAVVIAGGGPTGLMLAGELALAGVDVAIVERRPNQELVGS-RAGGLHARTLEVLDQRGIADR------------FLAQ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVA-----LSELTDGKSVMVYG----QTEVTRDLMAARAASGAPIVYGvSEVAIHDAKSDRPTITyLSEGETCRle 151
Cdd:PRK06834  69 GQVAQVTgfaatRLDISDFPTRHNYGlalwQNHIERILAEWVGELGVPIYRG-REVTGFAQDDTGVDVE-LSDGRTLR-- 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 152 CDFIAGCDGFHGVSRQSipAGIlqtyesvwPF-GW----LGLLADTP-PVNPELIYAHHQRGFvlcsqRSLTRSRY--YL 223
Cdd:PRK06834 145 AQYLVGCDGGRSLVRKA--AGI--------DFpGWdpttSYLIAEVEmTEEPEWGVHRDALGI-----HAFGRLEDegPV 209

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 224 QVPLSDKVEAWSDERFWQELKsrlpEELASRLVTGHALeKSIAPLRSFVVEPMQ---Y--GRLFLVGDAAHIVPPTGAKG 298
Cdd:PRK06834 210 RVMVTEKQVGATGEPTLDDLR----EALIAVYGTDYGI-HSPTWISRFTDMARQaasYrdGRVLLAGDAAHVHSPVGGQG 284

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 299 LNLAASD-VNYLWRI-----------LREYYHRGRSDLLA-----AYSQLALDRVwkGER---FSWFMTRLLH-DFPDQN 357
Cdd:PRK06834 285 LNTGVQDaVNLGWKLaqvvkgtspesLLDTYHAERHPVAArvlrnTMAQVALLRP--DDRteaLRDIVAELLGmDEPRKR 362

                        410
                 ....*....|....*.
gi 378976829 358 aFDAKMQAADRRYYLG 373
Cdd:PRK06834 363 -IAAMMSGLDIHYDLG 377
PRK08244 PRK08244
monooxygenase;
1-344 9.03e-12

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 66.31  E-value: 9.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILER--QTPQYVlgriRAGILESGTVDLLREAGVAQRMDAEG-LVHHGvef 77
Cdd:PRK08244   1 MKYEVIIIGGGPVGLMLASELALAGVKTCVIERlkETVPYS----KALTLHPRTLEILDMRGLLERFLEKGrKLPSG--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  78 LFDGQRVPVALSELtDGKS--VMVYGQTEvTRDLMAARAAS-GAPIVYGVSEVAIHDAKSDRPTITYLSEGETCrLECDF 154
Cdd:PRK08244  74 HFAGLDTRLDFSAL-DTSSnyTLFLPQAE-TEKVLEEHARSlGVEIFRGAEVLAVRQDGDGVEVVVRGPDGLRT-LTSSY 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 155 IAGCDGFHGVSRQSIPAGILQTYESVwpfgwLGLLADTPPVNPE----LIYAHHQRGFVLCS-----QRSLTRSRYYLQV 225
Cdd:PRK08244 151 VVGADGAGSIVRKQAGIAFPGTDATF-----TAMLGDVVLKDPPpssvLSLCTREGGVMIVPlsggiYRVLIIDPERPQV 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 226 PLSDKVEAwsderfwQELKSRLPEELASRLvtGHALEKSIAPLRSFVVEPMQY--GRLFLVGDAAHIVPPTGAKGLNLAA 303
Cdd:PRK08244 226 PKDEPVTL-------EELKTSLIRICGTDF--GLNDPVWMSRFGNATRQAERYrsGRIFLAGDAAHIHFPAGGQGLNVGL 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 378976829 304 SD-VNYLWRILREYYHRGRSDLLAAYSQlaldrvwkgERFSW 344
Cdd:PRK08244 297 QDaMNLGWKLAAAIKGWAPDWLLDSYHA---------ERHPV 329
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-328 5.61e-11

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 63.72  E-value: 5.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPqyVLGRIRAGILESGTVDLLREAGVAQRMDAegLVH---HGVEF 77
Cdd:PRK06185   5 ETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKHAD--FLRDFRGDTVHPSTLELMDELGLLERFLE--LPHqkvRTLRF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  78 LFDGQRVPVA-LSEL-TDGKSVMVYGQTEVTrDLMAARAAS--------GAPivygVSEVaIHDAksDRPT-ITYLSEGE 146
Cdd:PRK06185  81 EIGGRTVTLAdFSRLpTPYPYIAMMPQWDFL-DFLAEEASAypnftlrmGAE----VTGL-IEEG--GRVTgVRARTPDG 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 147 TCRLECDFIAGCDGFHGVSRQSipAGI-LQTYES---VWpfgWLGLlaDTPPVNPELIYAHHQRGFVLcsqrsLTRSRY- 221
Cdd:PRK06185 153 PGEIRADLVVGADGRHSRVRAL--AGLeVREFGApmdVL---WFRL--PREPDDPESLMGRFGPGQGL-----IMIDRGd 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 222 YLQVPLS------DKVEAWSDERFWQELKSRLPeELASRLvtgHALE--KSIAPLRSFVVEPMQYGR--LFLVGDAAHIV 291
Cdd:PRK06185 221 YWQCGYVipkggyAALRAAGLEAFRERVAELAP-ELADRV---AELKswDDVKLLDVRVDRLRRWHRpgLLCIGDAAHAM 296

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 378976829 292 PPTGAKGLNLAASDV----NYLWRILREyyHRGRSDLLAAY 328
Cdd:PRK06185 297 SPVGGVGINLAIQDAvaaaNILAEPLRR--GRVSDRDLAAV 335
PRK07190 PRK07190
FAD-binding protein;
1-330 3.47e-10

FAD-binding protein;


Pssm-ID: 235955 [Multi-domain]  Cd Length: 487  Bit Score: 61.37  E-value: 3.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVA---IIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRirAGILESGTVDLLREAGVAQRMDAEGLVHHGVEF 77
Cdd:PRK07190   1 MSTQVTdvvIIGAGPVGLMCAYLGQLCGLNTVIVDKSDGPLEVGR--ADALNARTLQLLELVDLFDELYPLGKPCNTSSV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  78 LFDGQRVPVALS--ELTDG---KSVMVYGQTEVTRDLMAARAASGAPIVYGVSEVAIHdaKSDRPTITYLSEGEtcRLEC 152
Cdd:PRK07190  79 WANGKFISRQSSwwEELEGclhKHFLMLGQSYVEKLLDDKLKEAGAAVKRNTSVVNIE--LNQAGCLTTLSNGE--RIQS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 153 DFIAGCDGFHGVSRQ--SIPAGILQTyESVWPFGWLGLLADTPPVnPELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDK 230
Cdd:PRK07190 155 RYVIGADGSRSFVRNhfNVPFEIIRP-QIIWAVIDGVIDTDFPKV-PEIIVFQAETSDVAWIPREGEIDRFYVRMDTKDF 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 231 VEAWSDERFWQELKsrlPEELASRLV---TGHALEKSIAplRSFVVEpmqyGRLFLVGDAAHIVPPTGAKGLNLAASDV- 306
Cdd:PRK07190 233 TLEQAIAKINHAMQ---PHRLGFKEIvwfSQFSVKESVA--EHFFIQ----DRIFLAGDACHIHSVNGGQGLNTGLADAf 303

                        330       340
                 ....*....|....*....|....
gi 378976829 307 NYLWRILREYYHRGRSDLLAAYSQ 330
Cdd:PRK07190 304 NLIWKLNMVIHHGASPELLQSYEA 327
PRK06847 PRK06847
hypothetical protein; Provisional
 4-305 6.01e-10

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 60.27  E-value: 6.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   4 QVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGrirAGILESG-TVDLLREAGVAQRMDAEGLVHHGVE-FLFDG 81
Cdd:PRK06847   6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYG---AGITLQGnALRALRELGVLDECLEAGFGFDGVDlFDPDG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  82 QRVPVALSELTDGKSV---MVYGQTEVTRDLMAARAASGAPIVYGVSEVAIhDAKSDRPTITyLSEGETCRLecDFIAGC 158
Cdd:PRK06847  83 TLLAELPTPRLAGDDLpggGGIMRPALARILADAARAAGADVRLGTTVTAI-EQDDDGVTVT-FSDGTTGRY--DLVVGA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 159 DGFHGVSRQSIPAGILQ---TYESVW------------PFGWLG--LLADTPPVNPELIYAhhqrgFVLcsqrSLTRSRY 221
Cdd:PRK06847 159 DGLYSKVRSLVFPDEPEpeyTGQGVWravlprpaevdrSLMYLGptTKAGVVPLSEDLMYL-----FVT----EPRPDNP 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 222 YLQvplsdkveawsDERFWQELKSRLPE-------ELASRLVTGHALekSIAPLRS-FVVEPMQYGRLFLVGDAAHIVPP 293
Cdd:PRK06847 230 RIE-----------PDTLAALLRELLAPfggpvlqELREQITDDAQV--VYRPLETlLVPAPWHRGRVVLIGDAAHATTP 296

                        330
                 ....*....|..
gi 378976829 294 TGAKGLNLAASD 305
Cdd:PRK06847 297 HLAQGAGMAIED 308
PRK06753 PRK06753
hypothetical protein; Provisional
 1-344 6.44e-10

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 60.09  E-value: 6.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKtqVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGrirAGILESGTV-DLLREAGVAQRMDAEGLVHHGVEFLF 79
Cdd:PRK06753   1 MK--IAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVKEVG---AGIGIGDNViKKLGNHDLAKGIKNAGQILSTMNLLD 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  80 DGQRVpvaLSELTDGKSVMVYgqTEVTRDLMAAraasgapIVYGVSEVAIHDAK--------SDRPTITYlSEGETCRLe 151
Cdd:PRK06753  76 DKGTL---LNKVKLKSNTLNV--TLHRQTLIDI-------IKSYVKEDAIFTGKevtkieneTDKVTIHF-ADGESEAF- 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 152 cDFIAGCDGFHGVSRQSIPAGILQTYEsvwpfG---WLGLLADtppvnpelIYAHHQRGFvlcSQRSLTRSRYYLqVPLS 228
Cdd:PRK06753 142 -DLCIGADGIHSKVRQSVNADSKVRYQ-----GytcFRGLIDD--------IDLKLPDCA---KEYWGTKGRFGI-VPLL 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 229 DKVEAW--------SDERFwqelKSRLPEELASRLVTGH-----ALEKS------------IAPLRSFVvepmqYGRLFL 283
Cdd:PRK06753 204 NNQAYWfitinakeRDPKY----SSFGKPHLQAYFNHYPnevreILDKQsetgilhhdiydLKPLKSFV-----YGRIVL 274

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378976829 284 VGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRgrsDLLAAYSQLALDRVWKGERFSW 344
Cdd:PRK06753 275 LGDAAHATTPNMGQGAGQAMEDAIVLANCLNAYDFE---KALQRYDKIRVKHTAKVIKRSR 332
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
1-330 1.16e-09

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 59.92  E-value: 1.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQtPQyVLGRIRAGILESGTVDLLREAGVAQRMDAEGLVHHGVEFLFD 80
Cdd:PRK06183   9 HDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERW-PT-LYDLPRAVGIDDEALRVLQAIGLADEVLPHTTPNHGMRFLDA 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVpvaLSELtDGKSVMVYG--------QTEVTRdLMAARAA--SGAPIVYGVSEVAIHDAkSDRPTITYLS-EGETCR 149
Cdd:PRK06183  87 KGRC---LAEI-ARPSTGEFGwprrnafhQPLLEA-VLRAGLArfPHVRVRFGHEVTALTQD-DDGVTVTLTDaDGQRET 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 150 LECDFIAGCDGFHGVSRQSIPAGIL-QTYESVWpfgwlgLLADTPPVNPELIYAHHqrgFVLCSQRsltrsRYYLQVPLS 228
Cdd:PRK06183 161 VRARYVVGCDGANSFVRRTLGVPFEdLTFPERW------LVVDVLIANDPLGGPHT---YQYCDPA-----RPYTSVRLP 226

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 229 DKVEAWsderfwqELKsRLPEELASRLVTGHALEKSIAPL-----------------RSFVVEPMQYGRLFLVGDAAHIV 291
Cdd:PRK06183 227 HGRRRW-------EFM-LLPGETEEQLASPENVWRLLAPWgptpddaelirhavytfHARVADRWRSGRVLLAGDAAHLM 298

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 378976829 292 PPTGAKGLNLAASDV-NYLWRILReyYHRGRSD--LLAAYSQ 330
Cdd:PRK06183 299 PPFAGQGMNSGIRDAaNLAWKLAA--VLRGRAGdaLLDTYEQ 338
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
3-328 2.83e-09

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 58.38  E-value: 2.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   3 TQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPqYVLGRIRAgiLESGTVDLLREAGVAQRM--DAEGLVhhGVEFLFD 80
Cdd:PRK07494   8 TDIAVIGGGPAGLAAAIALARAGASVALVAPEPP-YADLRTTA--LLGPSIRFLERLGLWARLapHAAPLQ--SMRIVDA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  81 GQRVPVA------LSELTDgksvMVYG---QTEVTRDLMAARAASGAPIVYGVSEVAIHDAKSDRPTITyLSEGETcrLE 151
Cdd:PRK07494  83 TGRLIRApevrfrAAEIGE----DAFGyniPNWLLNRALEARVAELPNITRFGDEAESVRPREDEVTVT-LADGTT--LS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 152 CDFIAGCDGFHGVSRQSipAGIlqtyeSV--WPFGWLGLLadtppvnpeLIYAH---HQrgFVlcSQRSLTRSRYYLQVP 226
Cdd:PRK07494 156 ARLVVGADGRNSPVREA--AGI-----GVrtWSYPQKALV---------LNFTHsrpHQ--NV--STEFHTEGGPFTQVP 215

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 227 LSDK------VEAWSDErfwQELKSRLPEELASRL------VTGH-ALEKSIA--PLRSFVVEPMQYGRLFLVGDAAHIV 291
Cdd:PRK07494 216 LPGRrsslvwVVRPAEA---ERLLALSDAALSAAIeermqsMLGKlTLEPGRQawPLSGQVAHRFAAGRTALVGEAAHVF 292

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 378976829 292 PPTGAKGLNLAASDVNYLWRILREY-YHRGRSDLLAAY 328
Cdd:PRK07494 293 PPIGAQGLNLGLRDVATLVEIVEDRpEDPGSAAVLAAY 330
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
10-338 7.84e-08

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 53.05  E-value: 7.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  10 AGPSGLLLGQLLHNAGIHTVILERQTpqYVLGRIRAGILESGTVDLLREAGVAQRMDAEglvhhgveflFDGQRVpvals 89
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGS--FPGDKICGGGLLPRALEELEPLGLDEPLERP----------VRGARF----- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  90 ELTDGKSVMVYGQTE----VTR----DLMAARA-ASGAPIVYG--VSEVAIHDaksDRPTITYLSEGEtcrLECDFIAGC 158
Cdd:COG0644   64 YSPGGKSVELPPGRGggyvVDRarfdRWLAEQAeEAGAEVRTGtrVTDVLRDD---GRVVVRTGDGEE---IRADYVVDA 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 159 DGFHGV--------SRQSIPAGILQTYESVWPFGWLglladtppvnpeliyAHHQRGFVLCSQRSLTRSRYYLQVPLSDk 230
Cdd:COG0644  138 DGARSLlarklglkRRSDEPQDYALAIKEHWELPPL---------------EGVDPGAVEFFFGEGAPGGYGWVFPLGD- 201

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 231 veawsderfwqelksrlpeelasrlvtGHAlekSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYLW 310
Cdd:COG0644  202 ---------------------------GRV---SVGIPLGGPRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAA 251

                        330       340       350
                 ....*....|....*....|....*....|
gi 378976829 311 RILREYYHRG--RSDLLAAYSQlALDRVWK 338
Cdd:COG0644  252 EAIAEALEGGdfSAEALAEYER-RLRELLK 280
PRK07364 PRK07364
FAD-dependent hydroxylase;
5-320 6.27e-07

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 51.17  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRIRAGILESGTVDLLREAGVAQRMdAEGLVHHGVEFLFDG--- 81
Cdd:PRK07364  21 VAIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAAKGQAYALSLLSARIFEGIGVWEKI-LPQIGKFRQIRLSDAdyp 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  82 QRVPVALSELtdGKSVMVY-GQTEVTRDLMAARAASGAPIVYGVS-EVAIHDAKSDRPTITYLSEGETCRLECDFIAGCD 159
Cdd:PRK07364 100 GVVKFQPTDL--GTEALGYvGEHQVLLEALQEFLQSCPNITWLCPaEVVSVEYQQDAATVTLEIEGKQQTLQSKLVVAAD 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 160 GFHGVSRQSipAGIlQT------------------------YESVWPFGWLGLLAdtppvnpeliyahhqrgfvlcsqrs 215
Cdd:PRK07364 178 GARSPIRQA--AGI-KTkgwkywqscvtatvkheaphndiaYERFWPSGPFAILP------------------------- 229

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 216 LTRSRYylQV------PLSDKVEAWSDERFWQELKSRLPEELAS-RLVtghaleksiAPLRSFVVEPMQ---Y--GRLFL 283
Cdd:PRK07364 230 LPGNRC--QIvwtaphAQAKALLALPEAEFLAELQQRYGDQLGKlELL---------GDRFLFPVQLMQsdrYvqHRLAL 298

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 378976829 284 VGDAAHIVPPTGAKGLNLAASDVNYLWRILREYYHRG 320
Cdd:PRK07364 299 VGDAAHCCHPVGGQGLNLGIRDAAALAQVLQTAHQRG 335
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 5-305 9.03e-07

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 50.54  E-value: 9.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGR---IRAGILESGTVDLLRE----AGVAQR------------- 64
Cdd:PRK08850   7 VAIIGGGMVGLALAAALKESDLRIAVIEGQLPEEALNElpdVRVSALSRSSEHILRNlgawQGIEARraapyiamevweq 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  65 -------MDAEGLVHHGVEFLFDGQRVPVALSE-LTDGKSVMVygqtevtrdLMAARAASgapIVYGVSEVAIHdaksdr 136
Cdd:PRK08850  87 dsfarieFDAESMAQPDLGHIVENRVIQLALLEqVQKQDNVTL---------LMPARCQS---IAVGESEAWLT------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 137 ptityLSEGETcrLECDFIAGCDGFHG-VSRQ-SIPAgilqtyeSVWPFGWLGLLADTPPVNP------ELIYAHHQRGF 208
Cdd:PRK08850 149 -----LDNGQA--LTAKLVVGADGANSwLRRQmDIPL-------THWDYGHSALVANVRTVDPhnsvarQIFTPQGPLAF 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 209 VLCSQRSLTRSRYYLQVPLSDKVEAWSDERFWQELKSRLPEELASRLVTGhalEKSIAPL-----RSFVVEpmqygRLFL 283
Cdd:PRK08850 215 LPMSEPNMSSIVWSTEPLRAEALLAMSDEQFNKALTAEFDNRLGLCEVVG---ERQAFPLkmryaRDFVRE-----RVAL 286

                        330       340
                 ....*....|....*....|..
gi 378976829 284 VGDAAHIVPPTGAKGLNLAASD 305
Cdd:PRK08850 287 VGDAAHTIHPLAGQGVNLGLLD 308
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
1-326 1.26e-06

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 49.95  E-value: 1.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLG-----RIRAgiLESGTVDLLREAGVAQRMDAEglvhhgv 75
Cdd:PRK07608   4 MKFDVVVVGGGLVGASLALALAQSGLRVALLAPRAPPRPADdawdsRVYA--ISPSSQAFLERLGVWQALDAA------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  76 eflfdgqRV-PVAlseltdgkSVMVYGQTEVTRDLMAAraASGAP----IV-YGVSEVAIHDAKSDRPTITY-------- 141
Cdd:PRK07608  75 -------RLaPVY--------DMRVFGDAHARLHFSAY--QAGVPqlawIVeSSLIERALWAALRFQPNLTWfparaqgl 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 142 ----------LSEGEtcRLECDFIAGCDGFHGVSRQSipAGIlqtYESVWPFGWLGLLAdtppvNPELIYAHH------- 204
Cdd:PRK07608 138 evdpdaatltLADGQ--VLRADLVVGADGAHSWVRSQ--AGI---KAERRPYRQTGVVA-----NFKAERPHRgtayqwf 205

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 205 QRGFVLCsqrsltrsryYLqvPLSDKVEA--WS-DERFWQELKSRLPEELASRL--VTGHALEK----SIA---PLRSFV 272
Cdd:PRK07608 206 RDDGILA----------LL--PLPDGHVSmvWSaRTAHADELLALSPEALAARVerASGGRLGRlecvTPAagfPLRLQR 273

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378976829 273 VEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYL---------------WRILREYYHRGRSDLLA 326
Cdd:PRK07608 274 VDRLVAPRVALVGDAAHLIHPLAGQGMNLGLRDVAALadvlagrepfrdlgdLRLLRRYERARREDILA 342
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 5-101 5.54e-06

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: 47.91  E-value: 5.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVIL-ERQTPQYVLGRiRAGIleSGTVDLLREAGVAQRMDAEglvhHGVEFLFDGQR 83
Cdd:cd08234  163 VLVFGAGPIGLLLAQLLKLNGASRVTVaEPNEEKLELAK-KLGA--TETVDPSREDPEAQKEDNP----YGFDVVIEATG 235

                         90       100
                 ....*....|....*....|..
gi 378976829  84 VPV----ALSELTDGKSVMVYG 101
Cdd:cd08234  236 VPKtleqAIEYARRGGTVLVFG 257
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
228-348 1.06e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 47.16  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 228 SDKVEAWSDERFWQELKsrlpEELASRLVTGHALEKSIA-PLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDV 306
Cdd:PRK08773 234 AERVLALDEAAFSRELT----QAFAARLGEVRVASPRTAfPLRRQLVQQYVSGRVLTLGDAAHVVHPLAGQGVNLGLRDV 309

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 378976829 307 NYLWRILREYYHRG----------------RSD-LLAAYSQLALDRVWKGERFSWFMTR 348
Cdd:PRK08773 310 AALQQLVRQAHARRadwaaphrlqrwartrRSDnTVAAYGFDAINRVFSNDEMHLTLLR 368
PRK06184 PRK06184
hypothetical protein; Provisional
 279-300 2.09e-05

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 46.52  E-value: 2.09e-05
                         10        20
                 ....*....|....*....|..
gi 378976829 279 GRLFLVGDAAHIVPPTGAKGLN 300
Cdd:PRK06184 281 GRVFLAGDAAHVHPPAGGQGLN 302
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 131-320 4.58e-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: 45.13  E-value: 4.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  131 DAKSDRPTITyLSEGETcrLECDFIAGCDGFHGVSRQSipAGILQTyesVWPFGWLGLLA----DTPPVNpeliyahhQR 206
Cdd:TIGR01989 154 NDNSNWVHIT-LSDGQV--LYTKLLIGADGSNSNVRKA--ANIDTT---GWNYNQHAVVAtlklEEATEN--------DV 217

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  207 GFvlcsQRSLTRSRYYLqVPLSDKVEA--WS-DERFWQELKSrLPEE-----LASRLVTGHA-------LEKSIAPLRSF 271
Cdd:TIGR01989 218 AW----QRFLPTGPIAL-LPLPDNNSTlvWStSPEEALRLLS-LPPEdfvdaLNAAFDLGYSdhpysylLDYAMEKLNED 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  272 V-------VEPMQY---------------------------GRLFLVGDAAHIVPPTGAKGLNLAASDVNYLWRILREYY 317
Cdd:TIGR01989 292 IgfrtegsKSCFQVpprvigvvdksraafplglghadeyvtKRVALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAV 371


                  ...
gi 378976829  318 HRG 320
Cdd:TIGR01989 372 SVG 374
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
111-306 6.70e-05

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 44.59  E-value: 6.70e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 111 AARAAsGAPIVYGVSeVAIHDAKSDRPTITyLSEGETcrLECDFIAGCDGFHGVSRQSipAGIlQTYEsvWPFGWLGLLA 190
Cdd:PRK07333 120 RAEAL-GIDLREATS-VTDFETRDEGVTVT-LSDGSV--LEARLLVAADGARSKLREL--AGI-KTVG--WDYGQSGIVC 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 191 DTPPVNPeliyaHH--------------------QRGFVLCSQRSLTRSRYYlqvplsdkveAWSDERFWQELKSRLPEE 250
Cdd:PRK07333 190 TVEHERP-----HGgraeehflpagpfailplkgNRSSLVWTERTADAERLV----------ALDDLVFEAELEQRFGHR 254

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 378976829 251 LASRLVTGhalEKSIAPL-----RSFVVEpmqygRLFLVGDAAHIVPPTGAKGLNLAASDV 306
Cdd:PRK07333 255 LGELKVLG---KRRAFPLgltlaRSFVAP-----RFALVGDAAHGIHPIAGQGLNLGLKDV 307
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 229-335 7.15e-05

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 44.46  E-value: 7.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 229 DKVEAWSDERFWQELKS----RLpeelaSRLVtgHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAAS 304
Cdd:PRK05732 235 EEVLSWSDAQFLAELQQafgwRL-----GRIT--HAGKRSAYPLALVTAAQQISHRLALVGNAAQTLHPIAGQGFNLGLR 307

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 378976829 305 DVNYLWRILREYYHR----GRSDLLAAYSQL-ALDR 335
Cdd:PRK05732 308 DVMSLAETLTQALARgediGDYAVLQRYQQRrQQDR 343
PRK07045 PRK07045
putative monooxygenase; Reviewed
 5-309 1.81e-04

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 43.36  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVILERQTPQYVLGRirAGILESGTVDLLREAGV-AQRMDAEGLVHHGVEFLFDGQR 83
Cdd:PRK07045   8 VLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNG--ADLLKPSGIGVVRAMGLlDDVFAAGGLRRDAMRLYHDKEL 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  84 VPVALSELTDGKSVMVYGQTEVTRDLMAARAaSGAPIVYGVSEVAIHDAKSD-RPTIT--YLSEGETCRLECdfIAGCDG 160
Cdd:PRK07045  86 IASLDYRSASALGYFILIPCEQLRRLLLAKL-DGLPNVRLRFETSIERIERDaDGTVTsvTLSDGERVAPTV--LVGADG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 161 FHGVSRQS---IPAGiLQTYESVWPFGWLGLladTPPVNP-ELIYAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEAWSD 236
Cdd:PRK07045 163 ARSMIRDDvlrMPAE-RVPYATPMAFGTIAL---TDSVREcNRLYVDSNQGLAYFYPIGDQATRLVVSFPADEMQGYLAD 238

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378976829 237 ERfWQELKSRLPE----ELASRLVT-GHALEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVNYL 309
Cdd:PRK07045 239 TT-RTKLLARLNEfvgdESADAMAAiGAGTAFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQGMNLAIEDAGEL 315
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-67 2.12e-04

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 43.01  E-value: 2.12e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQ------TPQYVlGRIRAgiLESGTVDLLREAGVAQRMDA 67
Cdd:PRK09126   2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQplaalaDPAFD-GREIA--LTHASREILQRLGAWDRIPE 71
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 5-101 2.60e-04

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: 42.81  E-value: 2.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVILERQ---------------TPQYVLGRIRAGILESG-------------TVDLL 56
Cdd:COG0493  124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALdkpggllrygipefrLPKDVLDREIELIEALGvefrtnvevgkdiTLDEL 203

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 378976829  57 RE----------AGVAQRMDAEG--L--VHHGVEFLFDGQRVPVALSELTDGKSVMVYG 101
Cdd:COG0493  204 LEefdavflatgAGKPRDLGIPGedLkgVHSAMDFLTAVNLGEAPDTILAVGKRVVVIG 262
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-170 2.97e-04

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


Pssm-ID: 273936 [Multi-domain]  Cd Length: 295  Bit Score: 42.31  E-value: 2.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829    5 VAIIGAGPSGLLLGQLLHNAGIHTVILER-QTPQYVlgrIRAGILESGTVDLLREAGVAqrmdAEGLVHHGVEFLFDGQr 83
Cdd:TIGR02032   3 VVVVGAGPAGASAAYRLADKGLRVLLLEKkSFPRYK---PCGGALSPRALEELDLPGEL----IVNLVRGARFFSPNGD- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   84 vPVALSELTDGKSV---MVYGQtevtrdLMAARAA-SGAPIVYG--VSEVAIHDaksDRPTITYLSEGETcrLECDFIAG 157
Cdd:TIGR02032  75 -SVEIPIETELAYVidrDAFDE------QLAERAQeAGAELRLGtrVLDVEIHD---DRVVVIVRGSEGT--VTAKIVIG 142

                         170
                  ....*....|...
gi 378976829  158 CDGFHGVSRQSIP 170
Cdd:TIGR02032 143 ADGSRSIVAKKLG 155
PRK06617 PRK06617
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 3-316 3.15e-04

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 168629 [Multi-domain]  Cd Length: 374  Bit Score: 42.60  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   3 TQVAIIGAGPSGLLLGQLLHNAGIHTVILERQ---TPQYvLGRIRAGILESGTVDLLREAGVAQRMdaEGLVHHGVEFLF 79
Cdd:PRK06617   2 SNTVILGCGLSGMLTALSFAQKGIKTTIFESKsvkSPEF-FKDIRTTALTPHSKNFLFSIDIWEEL--EKFVAEMQDIYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  80 DGQRVPVALSELTDGKSVMVYGQTEVTRDLMAARAASGAPIV-----YGVSEVAIHDAKSdrpTITYLSEgetcRLECDF 154
Cdd:PRK06617  79 VDNKASEILDLRNDADAVLGYVVKNSDFKKILLSKITNNPLItlidnNQYQEVISHNDYS---IIKFDDK----QIKCNL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 155 IAGCDGFHGVSRQSIPAG-ILQTYESVWPFGwlglladtppvnpeliyAHHQRGFVLCSQRSLTRSRYYLQVPLSDKVEA 233
Cdd:PRK06617 152 LIICDGANSKVRSHYFANeIEKPYQTALTFN-----------------IKHEKPHENCAMEHFLPLGPFALLPLKDQYAS 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829 234 ---WSDERFWQELKSRLPEELASRLV---TGHAL-------EKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLN 300
Cdd:PRK06617 215 sviWSTSSDQAALIVNLPVEEVRFLTqrnAGNSLgkitidsEISSFPLKARIANRYFHNRIVLIADTAHTVHPLAGQGLN 294

                        330       340
                 ....*....|....*....|..
gi 378976829 301 LAASDVNYLWRI------LREY 316
Cdd:PRK06617 295 QGIKDIEILSMIvsnngtLQEY 316
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 2-65 7.10e-04

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: 41.36  E-value: 7.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 378976829   2 KTQVAIIGAGPSGLLLGQLLHNAGIHTVILERQTpqYVLGRIR----AG-ILESG----------TVDLLREAGVAQRM 65
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASD--RVGGLIRtvevDGfRIDRGphsfltrdpeVLELLRELGLGDEL 77
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-33 9.94e-04

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 40.63  E-value: 9.94e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILER 33
Cdd:COG3380    2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEK 34
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 278-300 2.21e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 40.24  E-value: 2.21e-03
                         10        20
                 ....*....|....*....|...
gi 378976829 278 YGRLFLVGDAAHIVPPTGAKGLN 300
Cdd:PRK08132 298 HGRVLFAGDAAHQVSPFGARGAN 320
PRK07208 PRK07208
hypothetical protein; Provisional
 1-33 3.02e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 39.49  E-value: 3.02e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 378976829   1 MKTQVAIIGAGPSGLLLGQLLHNAGIHTVILER 33
Cdd:PRK07208   3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 3-33 3.65e-03

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: 39.08  E-value: 3.65e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 378976829   3 TQVAIIGAGPSGLLLGQLLHNAGIHTVILER 33
Cdd:COG2072    7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
7-34 4.11e-03

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 35.58  E-value: 4.11e-03
                          10        20
                  ....*....|....*....|....*...
gi 378976829    7 IIGAGPSGLLLGQLLHNAGIHTVILERQ 34
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKR 28
sugar_DH cd08236
NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol ...
 5-31 4.65e-03

NAD(P)-dependent sugar dehydrogenases; This group contains proteins identified as sorbitol dehydrogenases and other sugar dehydrogenases of the medium-chain dehydrogenase/reductase family (MDR), which includes zinc-dependent alcohol dehydrogenase and related proteins. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose. Sorbitol dehydrogenase is tetrameric and has a single catalytic zinc per subunit. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Related proteins include threonine dehydrogenase, formaldehyde dehydrogenase, and butanediol dehydrogenase. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. 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. Horse liver alcohol dehydrogenase is a dimeric enzyme and each subunit has two domains. The NAD binding domain is in a Rossmann fold and the catalytic domain contains a zinc ion to which substrates bind. There is a cleft between the domains that closes upon formation of the ternary complex.


Pssm-ID: 176198 [Multi-domain]  Cd Length: 343  Bit Score: 38.75  E-value: 4.65e-03
                         10        20
                 ....*....|....*....|....*..
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGIHTVIL 31
Cdd:cd08236  163 VVVIGAGTIGLLAIQWLKILGAKRVIA 189
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 5-122 4.77e-03

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 39.01  E-value: 4.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829   5 VAIIGAGPSGLLLGQLLHNAGiHTV-ILERQ---------------TPQYVLGRIRAGILESG-------------TVDL 55
Cdd:PRK11749 143 VAVIGAGPAGLTAAHRLARKG-YDVtIFEARdkaggllrygipefrLPKDIVDREVERLLKLGveirtntevgrdiTLDE 221

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378976829  56 LREA--------GVAQ----RMDAEGL--VHHGVEFLfdgQRVPVA--LSELTDGKSVMVYGQTEVTRDlmAARAAS--G 117
Cdd:PRK11749 222 LRAGydavfigtGAGLprflGIPGENLggVYSAVDFL---TRVNQAvaDYDLPVGKRVVVIGGGNTAMD--AARTAKrlG 296


                 ....*...
gi 378976829 118 AP---IVY 122
Cdd:PRK11749 297 AEsvtIVY 304
 
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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