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Conserved domains on  [gi|1850223513|ref|WP_172963080|]
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MULTISPECIES: 4-hydroxybenzoate 3-monooxygenase [Pseudomonas]

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: 789.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRIRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALD 80
Cdd:PRK08243    1 MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGLVHDGIELRFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  81 GRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADNVRPHDMHSDQPYLTFDYQGEPHRLDCDYIAGCDG 160
Cdd:PRK08243   81 GRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVTYEKDGEEHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 161 FHGVARQSIPADRLKVFERVYPFGWLGILADTPPVHDELVYARHERGFALCSMRSTTRTRYYLQVPAEENVADWSDQRFW 240
Cdd:PRK08243  161 FHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFALCSMRSPTRSRYYLQCPLDDKVEDWSDERFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 241 DELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQ 320
Cdd:PRK08243  241 DELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1850223513 321 RTDLLQKYSQICLRRIWKAERFSWWMTAMLHRFPDSDDFSQRIAESELAYFVDSEAGRKTIAENYVGLPYEA 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: 789.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRIRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALD 80
Cdd:PRK08243    1 MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGLVHDGIELRFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  81 GRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADNVRPHDMHSDQPYLTFDYQGEPHRLDCDYIAGCDG 160
Cdd:PRK08243   81 GRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVTYEKDGEEHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 161 FHGVARQSIPADRLKVFERVYPFGWLGILADTPPVHDELVYARHERGFALCSMRSTTRTRYYLQVPAEENVADWSDQRFW 240
Cdd:PRK08243  161 FHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFALCSMRSPTRSRYYLQCPLDDKVEDWSDERFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 241 DELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQ 320
Cdd:PRK08243  241 DELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1850223513 321 RTDLLQKYSQICLRRIWKAERFSWWMTAMLHRFPDSDDFSQRIAESELAYFVDSEAGRKTIAENYVGLPYEA 392
Cdd:PRK08243  321 DTALLDAYSATALRRVWKAERFSWWMTSMLHRFPDDDPFDQRIQLAELDYLTSSRAAATTLAENYVGLPFED 392
pbenz_hydroxyl TIGR02360
4-hydroxybenzoate 3-monooxygenase; Members of this family are the enzyme 4-hydroxybenzoate ...
 1-390 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: 707.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRIRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALD 80
Cdd:TIGR02360   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQSRDYVLGRIRAGVLEQGTVDLLREAGVDERMDREGLVHEGTEIAFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  81 GRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADNVRPHDMHSDQPYLTFDYQGEPHRLDCDYIAGCDG 160
Cdd:TIGR02360  81 GQRFRIDLKALTGGKTVMVYGQTEVTRDLMEAREAAGLTTVYDADDVRLHDLAGDRPYVTFERDGERHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 161 FHGVARQSIPADRLKVFERVYPFGWLGILADTPPVHDELVYARHERGFALCSMRSTTRTRYYLQVPAEENVADWSDQRFW 240
Cdd:TIGR02360 161 FHGVSRASIPAEVLKEFERVYPFGWLGILSETPPVSHELIYSNHERGFALCSMRSATRSRYYVQVPLTDKVEDWSDDRFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 241 DELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQ 320
Cdd:TIGR02360 241 AELKRRLPSEAAERLVTGPSIEKSIAPLRSFVCEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVHYLYEALLEHYQEG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 321 RTDLLQKYSQICLRRIWKAERFSWWMTAMLHRFPDSDDFSQRIAESELAYFVDSEAGRKTIAENYVGLPY 390
Cdd:TIGR02360 321 SSAGIEGYSARALARVWKAERFSWWMTSLLHRFPDTDAFDQRIQQAELEYLLGSEAAQATLAENYVGLPY 390
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 2-343 3.25e-114

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: 336.99  E-value: 3.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   2 KTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRirAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALDG 81
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPR--AHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  82 RRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGArTLYQADNVR--PHDMHSDQPYLTFDYQGEPHRLDCDYIAGCD 159
Cdd:pfam01494  79 TRRRADLDFLTSPPRVTVYPQTELEPILVEHAEARGA-QVRFGTEVLslEQDGDGVTAVVRDRRDGEEYTVRAKYLVGCD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 160 GFHGVARQSIPADRlKVFERVyPFGWLGILADTPPV--------HDELVYARHERGFALCSMRSTTRTRYYLQVPAEENV 231
Cdd:pfam01494 158 GGRSPVRKTLGIEF-EGFEGV-PFGSLDVLFDAPDLsdpverafVHYLIYAPHSRGFMVGPWRSAGRERYYVQVPWDEEV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 232 ADWSDQRFWDELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFN 311
Cdd:pfam01494 236 EERPEEFTDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAW 315

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1850223513 312 ILLKVYREQRTD-LLQKYSQICLRRIWKAERFS 343
Cdd:pfam01494 316 KLAAVLRGQAGEsLLDTYSAERLPVAWAVVDFA 348
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-351 1.58e-45

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: 159.33  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGriRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFEL--A 78
Cdd:COG0654     2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDG--RGIALSPRSLELLRRLGLWDRLLARGAPIRGIRVrdG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  79 LDGRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADnVRPHDMHSDQPYLTFDyQGEphRLDCDYIAGC 158
Cdd:COG0654    80 SDGRVLARFDAAETGLPAGLVVPRADLERALLEAARALGVELRFGTE-VTGLEQDADGVTVTLA-DGR--TLRADLVVGA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 159 DGFHGVARQSIPADrLKVFERVYPFGWLGILAdtppvhdelvyarhergfalcsmrsttrtryylqvpaeenvadwsdqR 238
Cdd:COG0654   156 DGARSAVRRLLGIG-FTGRDYPQRALWAGVRT-----------------------------------------------E 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 239 FWDELkRRLPEELAERLVTGPSiekSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYR 318
Cdd:COG0654   188 LRARL-AAAGPRLGELLELSPR---SAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALR 263

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1850223513 319 EQRTD-LLQKYSQICLRRIWKAERFSWWMTAMLH 351
Cdd:COG0654   264 GRDDEaALARYERERRPRAARVQRAADALGRLFH 297
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 5-31 5.69e-03

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: 38.28  E-value: 5.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLIL 31
Cdd:cd08234   163 VLVFGAGPIGLLLAQLLKLNGASRVTV 189
 
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: 789.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRIRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALD 80
Cdd:PRK08243    1 MRTQVAIIGAGPAGLLLGQLLHLAGIDSVVLERRSREYVEGRIRAGVLEQGTVDLLREAGVGERMDREGLVHDGIELRFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  81 GRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADNVRPHDMHSDQPYLTFDYQGEPHRLDCDYIAGCDG 160
Cdd:PRK08243   81 GRRHRIDLTELTGGRAVTVYGQTEVTRDLMAARLAAGGPIRFEASDVALHDFDSDRPYVTYEKDGEEHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 161 FHGVARQSIPADRLKVFERVYPFGWLGILADTPPVHDELVYARHERGFALCSMRSTTRTRYYLQVPAEENVADWSDQRFW 240
Cdd:PRK08243  161 FHGVSRASIPAGALRTFERVYPFGWLGILAEAPPVSDELIYANHERGFALCSMRSPTRSRYYLQCPLDDKVEDWSDERFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 241 DELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQ 320
Cdd:PRK08243  241 DELRRRLPPEDAERLVTGPSIEKSIAPLRSFVAEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVRYLARALVEFYREG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1850223513 321 RTDLLQKYSQICLRRIWKAERFSWWMTAMLHRFPDSDDFSQRIAESELAYFVDSEAGRKTIAENYVGLPYEA 392
Cdd:PRK08243  321 DTALLDAYSATALRRVWKAERFSWWMTSMLHRFPDDDPFDQRIQLAELDYLTSSRAAATTLAENYVGLPFED 392
pbenz_hydroxyl TIGR02360
4-hydroxybenzoate 3-monooxygenase; Members of this family are the enzyme 4-hydroxybenzoate ...
 1-390 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: 707.68  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRIRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALD 80
Cdd:TIGR02360   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDNVILERQSRDYVLGRIRAGVLEQGTVDLLREAGVDERMDREGLVHEGTEIAFD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  81 GRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADNVRPHDMHSDQPYLTFDYQGEPHRLDCDYIAGCDG 160
Cdd:TIGR02360  81 GQRFRIDLKALTGGKTVMVYGQTEVTRDLMEAREAAGLTTVYDADDVRLHDLAGDRPYVTFERDGERHRLDCDFIAGCDG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 161 FHGVARQSIPADRLKVFERVYPFGWLGILADTPPVHDELVYARHERGFALCSMRSTTRTRYYLQVPAEENVADWSDQRFW 240
Cdd:TIGR02360 161 FHGVSRASIPAEVLKEFERVYPFGWLGILSETPPVSHELIYSNHERGFALCSMRSATRSRYYVQVPLTDKVEDWSDDRFW 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 241 DELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQ 320
Cdd:TIGR02360 241 AELKRRLPSEAAERLVTGPSIEKSIAPLRSFVCEPMQYGRLFLAGDAAHIVPPTGAKGLNLAASDVHYLYEALLEHYQEG 320

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 321 RTDLLQKYSQICLRRIWKAERFSWWMTAMLHRFPDSDDFSQRIAESELAYFVDSEAGRKTIAENYVGLPY 390
Cdd:TIGR02360 321 SSAGIEGYSARALARVWKAERFSWWMTSLLHRFPDTDAFDQRIQQAELEYLLGSEAAQATLAENYVGLPY 390
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 2-343 3.25e-114

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: 336.99  E-value: 3.25e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   2 KTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRirAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFELALDG 81
Cdd:pfam01494   1 ETDVLIVGGGPAGLMLALLLARAGVRVVLVERHATTSVLPR--AHGLNQRTMELLRQAGLEDRILAEGVPHEGMGLAFYN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  82 RRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGArTLYQADNVR--PHDMHSDQPYLTFDYQGEPHRLDCDYIAGCD 159
Cdd:pfam01494  79 TRRRADLDFLTSPPRVTVYPQTELEPILVEHAEARGA-QVRFGTEVLslEQDGDGVTAVVRDRRDGEEYTVRAKYLVGCD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 160 GFHGVARQSIPADRlKVFERVyPFGWLGILADTPPV--------HDELVYARHERGFALCSMRSTTRTRYYLQVPAEENV 231
Cdd:pfam01494 158 GGRSPVRKTLGIEF-EGFEGV-PFGSLDVLFDAPDLsdpverafVHYLIYAPHSRGFMVGPWRSAGRERYYVQVPWDEEV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 232 ADWSDQRFWDELKRRLPEELAERLVTGPSIEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFN 311
Cdd:pfam01494 236 EERPEEFTDEELKQRLRSIVGIDLALVEILWKSIWGVASRVATRYRKGRVFLAGDAAHIHPPTGGQGLNTAIQDAFNLAW 315

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1850223513 312 ILLKVYREQRTD-LLQKYSQICLRRIWKAERFS 343
Cdd:pfam01494 316 KLAAVLRGQAGEsLLDTYSAERLPVAWAVVDFA 348
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 1-351 1.58e-45

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: 159.33  E-value: 1.58e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGriRAGVLEQGMVDLLRQAGVSQRMDAEGLVHGGFEL--A 78
Cdd:COG0654     2 MRTDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDG--RGIALSPRSLELLRRLGLWDRLLARGAPIRGIRVrdG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  79 LDGRRVAIDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADnVRPHDMHSDQPYLTFDyQGEphRLDCDYIAGC 158
Cdd:COG0654    80 SDGRVLARFDAAETGLPAGLVVPRADLERALLEAARALGVELRFGTE-VTGLEQDADGVTVTLA-DGR--TLRADLVVGA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 159 DGFHGVARQSIPADrLKVFERVYPFGWLGILAdtppvhdelvyarhergfalcsmrsttrtryylqvpaeenvadwsdqR 238
Cdd:COG0654   156 DGARSAVRRLLGIG-FTGRDYPQRALWAGVRT-----------------------------------------------E 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 239 FWDELkRRLPEELAERLVTGPSiekSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYR 318
Cdd:COG0654   188 LRARL-AAAGPRLGELLELSPR---SAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALAWKLAAALR 263

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1850223513 319 EQRTD-LLQKYSQICLRRIWKAERFSWWMTAMLH 351
Cdd:COG0654   264 GRDDEaALARYERERRPRAARVQRAADALGRLFH 297
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 5-330 1.79e-14

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: 74.16  E-value: 1.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLILERQTP-----DYVLGRIRAgvLEQGMVDLLRQAGVSQR---MDAEGLVH---- 72
Cdd:TIGR01988   2 IVIVGGGMVGLALALALARSGLKVALIEATPLpapadPGFDNRVSA--LSAASIRLLEKLGVWDKiepARAQPIRDihvs 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  73 -GGFELALDGRRVAIDLHALtggksvtiyGQTEVTRDLMQAR----QAVGARTLYQADNVRPHDMHSDQPYLTFDyQGEp 147
Cdd:TIGR01988  80 dGGSFGALRFDADEIGLEAL---------GYVVENRVLQQALwerlQELPNVTLLCPARVVELPRHSDHVELTLD-DGQ- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 148 hRLDCDYIAGCDGFHGVARQS--IPADRlkvfervYPFGWLGILA----DTPpvHDELVYARH--ERGFAL-------CS 212
Cdd:TIGR01988 149 -QLRARLLVGADGANSKVRQLagIPTTG-------WDYGQSAVVAnvkhERP--HQGTAWERFtpTGPLALlplpdnrSS 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 213 MRSTTRTRYylqvpAEEnVADWSDQRFWDELKRRLPEELAERLVTGPsieKSIAPLRSFVVEPMQYGRLFLVGDAAHIVP 292
Cdd:TIGR01988 219 LVWTLPPEE-----AER-LLALSDEEFLAELQRAFGSRLGAITLVGE---RHAFPLSLTHAKRYVAPRLALIGDAAHTIH 289

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1850223513 293 PTGAKGLNLAASDVSTLFNILLKVyREQRTDL-----LQKYSQ 330
Cdd:TIGR01988 290 PLAGQGLNLGLRDVAALAEVLEDA-RRRGEDIgslrvLQRYER 331
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
1-309 6.20e-14

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 73.02  E-value: 6.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRI------------RAGVLEqgmvDLLRQAGVSQRM--- 65
Cdd:PRK06183    9 HDTDVVIVGAGPVGLTLANLLGQYGVRVLVLERWPTLYDLPRAvgiddealrvlqAIGLAD----EVLPHTTPNHGMrfl 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  66 DAEGLVHGGFELALDG-----RRVAID--------LHALTGGKSVTIYGQTEVTrDLMQArqavgartlyqADNVRphdm 132
Cdd:PRK06183   85 DAKGRCLAEIARPSTGefgwpRRNAFHqplleavlRAGLARFPHVRVRFGHEVT-ALTQD-----------DDGVT---- 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 133 hsdqpyLTF-DYQGEPHRLDCDYIAGCDGFHGVARQSIPADRLkvfERVYPFGWLGIlaDTPPVHDEL------VYARHE 205
Cdd:PRK06183  149 ------VTLtDADGQRETVRARYVVGCDGANSFVRRTLGVPFE---DLTFPERWLVV--DVLIANDPLggphtyQYCDPA 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 206 RgfALCSMRS-TTRTRYYLQVPAEENVADWSDqrfwDELKRRLpeeLAERLVTGPSIE---KSIAPLRSFVVEPMQYGRL 281
Cdd:PRK06183  218 R--PYTSVRLpHGRRRWEFMLLPGETEEQLAS----PENVWRL---LAPWGPTPDDAElirHAVYTFHARVADRWRSGRV 288

                         330       340
                  ....*....|....*....|....*...
gi 1850223513 282 FLVGDAAHIVPPTGAKGLNLAASDVSTL 309
Cdd:PRK06183  289 LLAGDAAHLMPPFAGQGMNSGIRDAANL 316
PRK06753 PRK06753
hypothetical protein; Provisional
 1-344 1.29e-11

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 65.48  E-value: 1.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKtqVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGrirAGV-LEQGMVDLLRQAGVSQRMDAEGLVHGGFELAL 79
Cdd:PRK06753    1 MK--IAIIGAGIGGLTAAALLQEQGHEVKVFEKNESVKEVG---AGIgIGDNVIKKLGNHDLAKGIKNAGQILSTMNLLD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  80 DGRRVAIDLHALTGGKSVTIYGQTevtrdLMQARQA-VGARTLYQADNVRPHDMHSDQPYLTFDYQGEPhrlDCDYIAGC 158
Cdd:PRK06753   76 DKGTLLNKVKLKSNTLNVTLHRQT-----LIDIIKSyVKEDAIFTGKEVTKIENETDKVTIHFADGESE---AFDLCIGA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 159 DGFHGVARQSIpADRLKVFERVYPFgWLGI-----LADTppvHDELVYARHERGFALCSMRSTtRTRYYLQVPAEENVAD 233
Cdd:PRK06753  148 DGIHSKVRQSV-NADSKVRYQGYTC-FRGLiddidLKLP---DCAKEYWGTKGRFGIVPLLNN-QAYWFITINAKERDPK 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 234 WSD------QRFWDELKRRLPEELaERLVTGPSIEKSI---APLRSFVvepmqYGRLFLVGDAAHIVPPTGAKGLNLAAS 304
Cdd:PRK06753  222 YSSfgkphlQAYFNHYPNEVREIL-DKQSETGILHHDIydlKPLKSFV-----YGRIVLLGDAAHATTPNMGQGAGQAME 295

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1850223513 305 DVSTLFNILLKVYREQRtdlLQKYSQICLRRIWKAERFSW 344
Cdd:PRK06753  296 DAIVLANCLNAYDFEKA---LQRYDKIRVKHTAKVIKRSR 332
PRK06126 PRK06126
hypothetical protein; Provisional
 1-309 5.54e-11

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 63.86  E-value: 5.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVlgRIRAGVLEQGMVDLLRQAGVSQRMDAEGL---------- 70
Cdd:PRK06126    6 SETPVLIVGGGPVGLALALDLGRRGVDSILVERKDGTAF--NPKANTTSARSMEHFRRLGIADEVRSAGLpvdyptdiay 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  71 --VHGGFELA---LDGRRVAIDLHALTGGKSVTIY-----GQTEVTRDLMQ-ARQAVGARTLYQ---------ADNVRPH 130
Cdd:PRK06126   84 ftRLTGYELArfrLPSAREAITPVGGPDGSWPSPElphriPQKYLEPILLEhAAAQPGVTLRYGhrltdfeqdADGVTAT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 131 DMHSDQpyltfdyqGEPHRLDCDYIAGCDGFHGVARQSIPAdRLkVFERVYPFGwLGILADTPPVHDELVYARHERGFAL 210
Cdd:PRK06126  164 VEDLDG--------GESLTIRADYLVGCDGARSAVRRSLGI-SY-EGTSGLQRD-LSIYIRAPGLAALVGHDPAWMYWLF 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 211 CSMRSTTRTR-------YYLQVPAEENVADWSDqRFWDELKRRLPEELAERLVtgpsIEKSIAPLRSFVVEPMQYGRLFL 283
Cdd:PRK06126  233 NPDRRGVLVAidgrdewLFHQLRGGEDEFTIDD-VDARAFVRRGVGEDIDYEV----LSVVPWTGRRLVADSYRRGRVFL 307

                         330       340
                  ....*....|....*....|....*.
gi 1850223513 284 VGDAAHIVPPTGAKGLNLAASDVSTL 309
Cdd:PRK06126  308 AGDAAHLFTPTGGYGMNTGIGDAVNL 333
PRK08244 PRK08244
monooxygenase;
1-309 3.88e-10

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 61.30  E-value: 3.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILER---QTPDYvlgriRAGVLEQGMVDLLRQAGVSQRMDAEG-LVHGGFE 76
Cdd:PRK08244    1 MKYEVIIIGGGPVGLMLASELALAGVKTCVIERlkeTVPYS-----KALTLHPRTLEILDMRGLLERFLEKGrKLPSGHF 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  77 LALDGRrvaIDLHALTGGKSVTIY-GQTEVTRDLMQARQAVGARTLYQADNVRPHDmHSDQPYLTFDYQGEPHRLDCDYI 155
Cdd:PRK08244   76 AGLDTR---LDFSALDTSSNYTLFlPQAETEKVLEEHARSLGVEIFRGAEVLAVRQ-DGDGVEVVVRGPDGLRTLTSSYV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 156 AGCDGFHGVARQ----SIPADRLKVfervypFGWLG--ILADTPPVHdelVYAR-HERGFALCSMRSTTRTR------YY 222
Cdd:PRK08244  152 VGADGAGSIVRKqagiAFPGTDATF------TAMLGdvVLKDPPPSS---VLSLcTREGGVMIVPLSGGIYRvliidpER 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 223 LQVPAEENVadwSDQRFWDELKRRLPEELAerlVTGPS-------IEKSIAPLRSfvvepmqyGRLFLVGDAAHIVPPTG 295
Cdd:PRK08244  223 PQVPKDEPV---TLEELKTSLIRICGTDFG---LNDPVwmsrfgnATRQAERYRS--------GRIFLAGDAAHIHFPAG 288

                         330
                  ....*....|....
gi 1850223513 296 AKGLNLAASDVSTL 309
Cdd:PRK08244  289 GQGLNVGLQDAMNL 302
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
10-303 1.63e-09

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 58.44  E-value: 1.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  10 AGPSGLLLGQLLHKAGIDTLILERQTpdYVLGRIRAGVLEQGMVDLLRQAGVSQRMDAEgLVHGGFELaLDGRRVAIDlH 89
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGS--FPGDKICGGGLLPRALEELEPLGLDEPLERP-VRGARFYS-PGGKSVELP-P 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  90 ALTGGKSVTiygQTEVTRDLMQARQAVGARTLYQAdNVRPHDMHSDQPYLTFdyqGEPHRLDCDYIAGCDGFHGVARQSI 169
Cdd:COG0644    76 GRGGGYVVD---RARFDRWLAEQAEEAGAEVRTGT-RVTDVLRDDGRVVVRT---GDGEEIRADYVVDADGARSLLARKL 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 170 PADRLKVFERVYPFGWLGILADTPPVHDelvyarhERGFALCSMRSTTRTRYYLQVPAEENVAdwsdqrfwdelkrrlpe 249
Cdd:COG0644   149 GLKRRSDEPQDYALAIKEHWELPPLEGV-------DPGAVEFFFGEGAPGGYGWVFPLGDGRV----------------- 204

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1850223513 250 elaerlvtgpsiekSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAA 303
Cdd:COG0644   205 --------------SVGIPLGGPRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAM 244
PRK07364 PRK07364
FAD-dependent hydroxylase;
5-328 3.15e-09

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 58.11  E-value: 3.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRIRAGVLEQGMVDLLRQAGVSQRM---------------DAEG 69
Cdd:PRK07364   21 VAIVGGGIVGLTLAAALKDSGLRIALIEAQPAEAAAAKGQAYALSLLSARIFEGIGVWEKIlpqigkfrqirlsdaDYPG 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  70 LVHggFELAldgrrvaiDLHALTGGKSvtiyGQTEVtrdLMQARQAVgartLYQADNVRPH--------DMHSDQPYLTF 141
Cdd:PRK07364  101 VVK--FQPT--------DLGTEALGYV----GEHQV---LLEALQEF----LQSCPNITWLcpaevvsvEYQQDAATVTL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 142 DYQGEPHRLDCDYIAGCDGFHGVARQS--IPADRLK-------------------VFERVYPFGWLGILadtpPVHD--- 197
Cdd:PRK07364  160 EIEGKQQTLQSKLVVAADGARSPIRQAagIKTKGWKywqscvtatvkheaphndiAYERFWPSGPFAIL----PLPGnrc 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 198 ELVY-ARHERGFALCSMrsttrtryylqvpaeenvadwSDQRFWDELKRRLPEELAE-RLVTGPSIeksiaplrsFVVEP 275
Cdd:PRK07364  236 QIVWtAPHAQAKALLAL---------------------PEAEFLAELQQRYGDQLGKlELLGDRFL---------FPVQL 285

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1850223513 276 MQ---Y--GRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQ----RTDLLQKY 328
Cdd:PRK07364  286 MQsdrYvqHRLALVGDAAHCCHPVGGQGLNLGIRDAAALAQVLQTAHQRGedigSLAVLKRY 347
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-99 6.54e-07

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 51.01  E-value: 6.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTpdyvlgriragvleqgmvDLLR-------QAGVSQRMDAEGLvhg 73
Cdd:PRK06185    5 ETTDCCIVGGGPAGMMLGLLLARAGVDVTVLEKHA------------------DFLRdfrgdtvHPSTLELMDELGL--- 63

                          90       100
                  ....*....|....*....|....*...
gi 1850223513  74 gFE--LALDGRRVAiDLHALTGGKSVTI 99
Cdd:PRK06185   64 -LErfLELPHQKVR-TLRFEIGGRTVTL 89
PRK06834 PRK06834
hypothetical protein; Provisional
 1-305 1.17e-06

hypothetical protein; Provisional


Pssm-ID: 235870 [Multi-domain]  Cd Length: 488  Bit Score: 50.40  E-value: 1.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGRiRAGVLEQGMVDLLRQAGVSQRMDAEGL---VHG---- 73
Cdd:PRK06834    2 TEHAVVIAGGGPTGLMLAGELALAGVDVAIVERRPNQELVGS-RAGGLHARTLEVLDQRGIADRFLAQGQvaqVTGfaat 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  74 -----------GFELALDGRRVAIDLHALTGGKSVTIYGQTEVTrDLMQARQAVgartlyqadnvrphDMH-SDqpyltf 141
Cdd:PRK06834   81 rldisdfptrhNYGLALWQNHIERILAEWVGELGVPIYRGREVT-GFAQDDTGV--------------DVElSD------ 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 142 dyqGEPHRldCDYIAGCDGFHGVARQSIPADrlkvfervYPfGW----LGILAD-----TPP--VHdelvyaRHERGF-A 209
Cdd:PRK06834  140 ---GRTLR--AQYLVGCDGGRSLVRKAAGID--------FP-GWdpttSYLIAEvemteEPEwgVH------RDALGIhA 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 210 LCSMRSTTRTRYylqVPAEENVadwsdqrfwdelkRRLPE----ELAERLVT------GPSIEKSIAPLRSFVVEPMQY- 278
Cdd:PRK06834  200 FGRLEDEGPVRV---MVTEKQV-------------GATGEptldDLREALIAvygtdyGIHSPTWISRFTDMARQAASYr 263

                         330       340
                  ....*....|....*....|....*...
gi 1850223513 279 -GRLFLVGDAAHIVPPTGAKGLNLAASD 305
Cdd:PRK06834  264 dGRVLLAGDAAHVHSPVGGQGLNTGVQD 291
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
267-313 1.36e-06

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 49.90  E-value: 1.36e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1850223513 267 PLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNIL 313
Cdd:PRK07494  268 PLSGQVAHRFAAGRTALVGEAAHVFPPIGAQGLNLGLRDVATLVEIV 314
PRK06847 PRK06847
hypothetical protein; Provisional
 4-305 1.98e-06

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 49.49  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   4 QVAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGrirAGVLEQG-MVDLLRQAGVSQRMDAEGLVHGGFEL-ALDG 81
Cdd:PRK06847    6 KVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYG---AGITLQGnALRALRELGVLDECLEAGFGFDGVDLfDPDG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  82 RRVA-IDLHALTGGK---SVTIYgQTEVTRDLMQARQAVGARTLYqADNVRPHDMHSDQPYLTFDyQGEPHRLdcDYIAG 157
Cdd:PRK06847   83 TLLAeLPTPRLAGDDlpgGGGIM-RPALARILADAARAAGADVRL-GTTVTAIEQDDDGVTVTFS-DGTTGRY--DLVVG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 158 CDGFHGVARQSIPADRLK-----------VFERVYPFG----WLG--ILADTPPVHDELVYArhergFalcsmrsttrtr 220
Cdd:PRK06847  158 ADGLYSKVRSLVFPDEPEpeytgqgvwraVLPRPAEVDrslmYLGptTKAGVVPLSEDLMYL-----F------------ 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 221 yylqvpaeenVADWSDQRFWDElKRRLPEELAERLV--TGPSIEKSIAPL------------RSFVVEPMQYGRLFLVGD 286
Cdd:PRK06847  221 ----------VTEPRPDNPRIE-PDTLAALLRELLApfGGPVLQELREQItddaqvvyrpleTLLVPAPWHRGRVVLIGD 289

                         330
                  ....*....|....*....
gi 1850223513 287 AAHIVPPTGAKGLNLAASD 305
Cdd:PRK06847  290 AAHATTPHLAQGAGMAIED 308
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
235-309 1.09e-05

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 47.28  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 235 SDQRFWDELKRRLPEELAERLVTGpsiEKSIAPL-----RSFVVEpmqygRLFLVGDAAHIVPPTGAKGLNLAASDVSTL 309
Cdd:PRK07333  239 DDLVFEAELEQRFGHRLGELKVLG---KRRAFPLgltlaRSFVAP-----RFALVGDAAHGIHPIAGQGLNLGLKDVAAL 310
PRK06184 PRK06184
hypothetical protein; Provisional
 279-300 1.92e-05

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 46.52  E-value: 1.92e-05
                          10        20
                  ....*....|....*....|..
gi 1850223513 279 GRLFLVGDAAHIVPPTGAKGLN 300
Cdd:PRK06184  281 GRVFLAGDAAHVHPPAGGQGLN 302
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 5-321 2.16e-05

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 46.30  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLILERQTPDYVLGR---IRAGVLEQGMVDLLRQ----AGVSQR------------- 64
Cdd:PRK08850    7 VAIIGGGMVGLALAAALKESDLRIAVIEGQLPEEALNElpdVRVSALSRSSEHILRNlgawQGIEARraapyiamevweq 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  65 -------MDAEGLVHGGFELALDGRRVAIDL-HALTGGKSVTIY----------GQTEVTRdLMQARQAVGARTLYQADN 126
Cdd:PRK08850   87 dsfarieFDAESMAQPDLGHIVENRVIQLALlEQVQKQDNVTLLmparcqsiavGESEAWL-TLDNGQALTAKLVVGADG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 127 ----VRphdMHSDQPYLTFDYQgepHRLDCDYIAGCDGFHGVARQSIPADRLKVFERVYPFGWLGILADTPPVHDElvya 202
Cdd:PRK08850  166 answLR---RQMDIPLTHWDYG---HSALVANVRTVDPHNSVARQIFTPQGPLAFLPMSEPNMSSIVWSTEPLRAE---- 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 203 rhergfALCSMrsttrtryylqvpaeenvadwSDQRFwdelKRRLPEELAERL----VTGpsiEKSIAPL-----RSFVV 273
Cdd:PRK08850  236 ------ALLAM---------------------SDEQF----NKALTAEFDNRLglceVVG---ERQAFPLkmryaRDFVR 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1850223513 274 EpmqygRLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQR 321
Cdd:PRK08850  282 E-----RVALVGDAAHTIHPLAGQGVNLGLLDAASLAQEILALWQQGR 324
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
7-55 4.01e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 41.36  E-value: 4.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1850223513   7 IIGAGPSGLLLGQLLHKAGIDTLILERQtpDYVLGRIRAGVLEQGMVDL 55
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKR--DRLGGNAYSYRVPGYVFDY 47
PRK07045 PRK07045
putative monooxygenase; Reviewed
 5-331 5.08e-05

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 44.90  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLILERQTpdyvlgRIRAgvleQGMVDLLRQAGV----------------SQRMDAE 68
Cdd:PRK07045    8 VLINGSGIAGVALAHLLGARGHSVTVVERAA------RNRA----QNGADLLKPSGIgvvramgllddvfaagGLRRDAM 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  69 GLVHGGFELA-LDGRRVA---------------IDLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTLYQADNVRPHdm 132
Cdd:PRK07045   78 RLYHDKELIAsLDYRSASalgyfilipceqlrrLLLAKLDGLPNVRLRFETSIERIERDADGTVTSVTLSDGERVAPT-- 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 133 hsdqpyltfdyqgephrldcdYIAGCDGfhgvARQSIPADRLKV-FERV-YPFGWL-GILADTPPVHD-ELVYARHERGF 208
Cdd:PRK07045  156 ---------------------VLVGADG----ARSMIRDDVLRMpAERVpYATPMAfGTIALTDSVREcNRLYVDSNQGL 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 209 ALCSMRSTTRTRYYLQVPAEEN---VADWSDQRFWDELKRRLPEELAERL--VTGPSIEKSIaPLRSFVVEPMQYGRLFL 283
Cdd:PRK07045  211 AYFYPIGDQATRLVVSFPADEMqgyLADTTRTKLLARLNEFVGDESADAMaaIGAGTAFPLI-PLGRMNLDRYHKRNVVL 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1850223513 284 VGDAAHIVPPTGAKGLNLAASDVSTLFNILLKVYREQRT--DLLQKYSQI 331
Cdd:PRK07045  290 LGDAAHSIHPITGQGMNLAIEDAGELGACLDLHLSGQIAlaDALERFERI 339
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
229-309 6.46e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 44.85  E-value: 6.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 229 ENVADWSDQRFWDELKRRLPEELAERLVTGPsieKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVST 308
Cdd:PRK08773  235 ERVLALDEAAFSRELTQAFAARLGEVRVASP---RTAFPLRRQLVQQYVSGRVLTLGDAAHVVHPLAGQGVNLGLRDVAA 311


                  .
gi 1850223513 309 L 309
Cdd:PRK08773  312 L 312
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 5-302 7.97e-05

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: 44.23  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLILER-QTPDYVL--GRIRAGVLEQgMVDLLRQAGVSQRmdaEGLVHGGFELALDG 81
Cdd:TIGR02032   3 VVVVGAGPAGASAAYRLADKGLRVLLLEKkSFPRYKPcgGALSPRALEE-LDLPGELIVNLVR---GARFFSPNGDSVEI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  82 RRVAIDLHALTggksvtiygQTEVTRDLMQARQAVGARTLYQADNVRPHDmHSDQPYLTfdYQGEPHRLDCDYIAGCDGF 161
Cdd:TIGR02032  79 PIETELAYVID---------RDAFDEQLAERAQEAGAELRLGTRVLDVEI-HDDRVVVI--VRGSEGTVTAKIVIGADGS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 162 HGVARQSIPADRLKV-----FERVYPFGWLGILADTPPVHDELVYArhERGFALCSMRSTTRTRYYLQVPAEENVADWsd 236
Cdd:TIGR02032 147 RSIVAKKLGLKKEPReygvaARAEVEMPDEEVDEDFVEVYIDRGIV--PGGYGWVFPKGDGTANVGVGSRSAEEGEDP-- 222

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1850223513 237 QRFWDELKRRLPEelAERLVTGPSIEKSIaPLRSFvVEPMQYGRLFLVGDAAHIVPPTGAKGLNLA 302
Cdd:TIGR02032 223 KKYLKDFLARRPE--LKDAETVEVCGALI-PIGRP-DEKLVRGNVLLVGDAAGHVNPLTGEGIYYA 284
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 2-65 9.52e-05

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: 44.44  E-value: 9.52e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1850223513   2 KTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQtpDYVLGRIR----AG-VLEQG----------MVDLLRQAGVSQRM 65
Cdd:COG1232     1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS--DRVGGLIRtvevDGfRIDRGphsfltrdpeVLELLRELGLGDEL 77
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
1-309 1.41e-04

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 43.79  E-value: 1.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQTP-----DYVLGRIRAgvLEQGMVDLLRQAGVSQRMDAEGL----- 70
Cdd:PRK07608    4 MKFDVVVVGGGLVGASLALALAQSGLRVALLAPRAPprpadDAWDSRVYA--ISPSSQAFLERLGVWQALDAARLapvyd 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  71 --VHG--GFELALDGRRVAIDLHALTGGKSvtiygqtEVTRDLMQARQAVGARTLYQADNVRpHDMHSDQPYLTFDyQGE 146
Cdd:PRK07608   82 mrVFGdaHARLHFSAYQAGVPQLAWIVESS-------LIERALWAALRFQPNLTWFPARAQG-LEVDPDAATLTLA-DGQ 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 147 phRLDCDYIAGCDGFHGVARQS--IPADRlkvfervYPFGWLGILA--DTPPVHDELVYARHERGFALCsmrsttrtryY 222
Cdd:PRK07608  153 --VLRADLVVGADGAHSWVRSQagIKAER-------RPYRQTGVVAnfKAERPHRGTAYQWFRDDGILA----------L 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 223 LQVPAEENVADWS-DQRFWDELKRRLPEELAERLVTGPSIE----KSIAPLRSF---------VVEPmqygRLFLVGDAA 288
Cdd:PRK07608  214 LPLPDGHVSMVWSaRTAHADELLALSPEALAARVERASGGRlgrlECVTPAAGFplrlqrvdrLVAP----RVALVGDAA 289

                         330       340
                  ....*....|....*....|.
gi 1850223513 289 HIVPPTGAKGLNLAASDVSTL 309
Cdd:PRK07608  290 HLIHPLAGQGMNLGLRDVAAL 310
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 3-33 1.88e-04

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: 43.31  E-value: 1.88e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1850223513   3 TQVAIIGAGPSGLLLGQLLHKAGIDTLILER 33
Cdd:COG2072     7 VDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
PRK06617 PRK06617
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 3-323 1.99e-04

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 168629 [Multi-domain]  Cd Length: 374  Bit Score: 42.99  E-value: 1.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   3 TQVAIIGAGPSGLLLGQLLHKAGIDTLILERQ---TPDYvLGRIRAGVLEQGMVDLLRQAGVSQRMDaEGLVHGGFELAL 79
Cdd:PRK06617    2 SNTVILGCGLSGMLTALSFAQKGIKTTIFESKsvkSPEF-FKDIRTTALTPHSKNFLFSIDIWEELE-KFVAEMQDIYVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513  80 DGRRVAI-DLHALTGGKSVTIYGQTEVTRDLMQARQAVGARTL---YQADNVRPHDMHSdqpYLTFDYQgephRLDCDYI 155
Cdd:PRK06617   80 DNKASEIlDLRNDADAVLGYVVKNSDFKKILLSKITNNPLITLidnNQYQEVISHNDYS---IIKFDDK----QIKCNLL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 156 AGCDGFHGVARQSIPADRLKvfervypfgwlgiladtPPVHDELVY-ARHERGFALCSMRSTTRTRYYLQVPAEENVAD- 233
Cdd:PRK06617  153 IICDGANSKVRSHYFANEIE-----------------KPYQTALTFnIKHEKPHENCAMEHFLPLGPFALLPLKDQYASs 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 234 --WSDQRFWDELKRRLPEELAERLV---TGPSI-------EKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNL 301
Cdd:PRK06617  216 viWSTSSDQAALIVNLPVEEVRFLTqrnAGNSLgkitidsEISSFPLKARIANRYFHNRIVLIADTAHTVHPLAGQGLNQ 295

                         330       340
                  ....*....|....*....|....*..
gi 1850223513 302 AASDVSTLF-----NILLKVYREQRTD 323
Cdd:PRK06617  296 GIKDIEILSmivsnNGTLQEYQKLRQE 322
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-33 2.70e-04

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 42.56  E-value: 2.70e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILER 33
Cdd:COG3380     2 SMPDIAIIGAGIAGLAAARALQDAGHEVTVFEK 34
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 229-335 9.03e-04

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 40.99  E-value: 9.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513 229 ENVADWSDQRFWDELKRRLPEELAERLVTGpsiEKSIAPLRSFVVEPMQYGRLFLVGDAAHIVPPTGAKGLNLAASDVST 308
Cdd:PRK05732  235 EEVLSWSDAQFLAELQQAFGWRLGRITHAG---KRSAYPLALVTAAQQISHRLALVGNAAQTLHPIAGQGFNLGLRDVMS 311

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1850223513 309 LFNILLKVYReQRTD-----LLQKYSQiclRR 335
Cdd:PRK05732  312 LAETLTQALA-RGEDigdyaVLQRYQQ---RR 339
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
2-84 9.62e-04

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 41.06  E-value: 9.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   2 KTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQtpDYVLGRIR-------AGVLEQG----------MVDLLRQAGVSQR 64
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEAR--DRVGGRVWtlrfgddGLYAELGamrippshtnLLALARELGLPLE 84

                          90       100
                  ....*....|....*....|
gi 1850223513  65 MDAEGlvHGGFELALDGRRV 84
Cdd:COG1231    85 PFPNE--NGNALLYLGGKRV 102
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
1-33 1.28e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 40.87  E-value: 1.28e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILER 33
Cdd:COG2509    29 LKYDVVIVGAGPAGLFAALELAEAGLKPLVLER 61
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 280-313 1.75e-03

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: 40.13  E-value: 1.75e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1850223513 280 RLFLVGDAAHIVPPTGAKGLNLAASDVSTLFNIL 313
Cdd:TIGR01989 334 RVALVGDAAHRVHPLAGQGVNLGFGDVASLVKAL 367
PRK09126 PRK09126
FAD-dependent hydroxylase;
1-67 1.93e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 39.92  E-value: 1.93e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILERQtPDYVL------GRIRAgvLEQGMVDLLRQAGVSQRMDA 67
Cdd:PRK09126    2 MHSDIVVVGAGPAGLSFARSLAGSGLKVTLIERQ-PLAALadpafdGREIA--LTHASREILQRLGAWDRIPE 71
PRK07208 PRK07208
hypothetical protein; Provisional
 1-33 1.99e-03

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 40.26  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILER 33
Cdd:PRK07208    3 NKKSVVIIGAGPAGLTAAYELLKRGYPVTVLEA 35
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 278-300 2.48e-03

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 39.85  E-value: 2.48e-03
                          10        20
                  ....*....|....*....|...
gi 1850223513 278 YGRLFLVGDAAHIVPPTGAKGLN 300
Cdd:PRK08132  298 HGRVLFAGDAAHQVSPFGARGAN 320
PLN02676 PLN02676
polyamine oxidase
 5-44 4.44e-03

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 38.93  E-value: 4.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGI-DTLILErqTPDYVLGRIR 44
Cdd:PLN02676   29 VIIVGAGMSGISAAKTLSEAGIeDILILE--ATDRIGGRMR 67
PLN00093 PLN00093
geranylgeranyl diphosphate reductase; Provisional
 1-33 4.99e-03

geranylgeranyl diphosphate reductase; Provisional


Pssm-ID: 177713 [Multi-domain]  Cd Length: 450  Bit Score: 38.96  E-value: 4.99e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1850223513   1 MKTQVAIIGAGPSGLLLGQLLHKAGIDTLILER 33
Cdd:PLN00093   38 RKLRVAVIGGGPAGACAAETLAKGGIETFLIER 70
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 5-97 5.44e-03

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: 38.64  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLILERQtpDYVLGRIRAGVLEQgMVDLLRQAGVSqrmdaeglVHGGFEL-ALDG-R 82
Cdd:COG0446   127 AVVIGGGPIGLELAEALRKRGLKVTLVERA--PRLLGVLDPEMAAL-LEEELREHGVE--------LRLGETVvAIDGdD 195

                          90
                  ....*....|....*
gi 1850223513  83 RVAIdlhALTGGKSV 97
Cdd:COG0446   196 KVAV---TLTDGEEI 207
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 5-31 5.69e-03

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: 38.28  E-value: 5.69e-03
                          10        20
                  ....*....|....*....|....*..
gi 1850223513   5 VAIIGAGPSGLLLGQLLHKAGIDTLIL 31
Cdd:cd08234   163 VLVFGAGPIGLLLAQLLKLNGASRVTV 189
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 281-313 6.88e-03

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 38.43  E-value: 6.88e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1850223513 281 LFLVGDAAHIVPPTGAKGLNLAASDVSTLFNIL 313
Cdd:PRK08020  283 LALVGDAAHTINPLAGQGVNLGYRDVDALLDVL 315
 
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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