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Conserved domains on  [gi|1750501969|gb|QES94496|]
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tetracycline-inactivating monooxygenase Tet(X) (plasmid) [Empedobacter brevis]

Protein Classification

FAD-dependent oxidoreductase( domain architecture ID 11428987)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 19-386 1.05e-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: 159.72  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIFGGTLDLhktSGQEAMKKAGLLKAYYDLALPM-GVNIAD-EKG 96
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSP---RSLELLRRLGLWDRLLARGAPIrGIRVRDgSDG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  97 NILSTKNVKPENRFDNPEINRNDLRAILLNSLE--NDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKV 174
Cdd:COG0654    83 RVLARFDAAETGLPAGLVVPRADLERALLEAARalGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGARSAV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 175 RKfvtdteveetgtfniqadihqpeincpgffqlcngnrlmashqgnllfanpnnngalHFGISFktpdewknqTQVDFQ 254
Cdd:COG0654   163 RR---------------------------------------------------------LLGIGF---------TGRDYP 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 255 NRNSVVDF---LLKEFSDWDERYKELIHTT-LSFVGLATRIFPlekPWKSKRplpITMIGDAAHLMPPFAGQGVNSGLVD 330
Cdd:COG0654   177 QRALWAGVrteLRARLAAAGPRLGELLELSpRSAFPLRRRRAE---RWRRGR---VVLLGDAAHTMHPLGGQGANLALRD 250

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1750501969 331 ALILSDNLADGKFN-SIEEAVKNYEQQMFIYGKEAQEESTQNeIEMFKPDFTFQQLL 386
Cdd:COG0654   251 AAALAWKLAAALRGrDDEAALARYERERRPRAARVQRAADAL-GRLFHPDSPPLRLL 306
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 19-386 1.05e-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: 159.72  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIFGGTLDLhktSGQEAMKKAGLLKAYYDLALPM-GVNIAD-EKG 96
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSP---RSLELLRRLGLWDRLLARGAPIrGIRVRDgSDG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  97 NILSTKNVKPENRFDNPEINRNDLRAILLNSLE--NDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKV 174
Cdd:COG0654    83 RVLARFDAAETGLPAGLVVPRADLERALLEAARalGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGARSAV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 175 RKfvtdteveetgtfniqadihqpeincpgffqlcngnrlmashqgnllfanpnnngalHFGISFktpdewknqTQVDFQ 254
Cdd:COG0654   163 RR---------------------------------------------------------LLGIGF---------TGRDYP 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 255 NRNSVVDF---LLKEFSDWDERYKELIHTT-LSFVGLATRIFPlekPWKSKRplpITMIGDAAHLMPPFAGQGVNSGLVD 330
Cdd:COG0654   177 QRALWAGVrteLRARLAAAGPRLGELLELSpRSAFPLRRRRAE---RWRRGR---VVLLGDAAHTMHPLGGQGANLALRD 250

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1750501969 331 ALILSDNLADGKFN-SIEEAVKNYEQQMFIYGKEAQEESTQNeIEMFKPDFTFQQLL 386
Cdd:COG0654   251 AAALAWKLAAALRGrDDEAALARYERERRPRAARVQRAADAL-GRLFHPDSPPLRLL 306
PRK06753 PRK06753
hypothetical protein; Provisional
 18-355 3.64e-24

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 102.46  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYErdKDRQARIFGGTLDLhktsGQEAMKKAGLlkayYDLA---------LPmG 88
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE--KNESVKEVGAGIGI----GDNVIKKLGN----HDLAkgiknagqiLS-T 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  89 VNIADEKGNILSTknVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILAN 168
Cdd:PRK06753   71 MNLLDDKGTLLNK--VKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEAFDLCIGAD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 169 GGMSKVRKFVT-DTEVEETGTFNIQADIHQPEINCPGFFQLCNGNRlmashqGNL-LFANPNNNGALHFGISFKTPD-EW 245
Cdd:PRK06753  149 GIHSKVRQSVNaDSKVRYQGYTCFRGLIDDIDLKLPDCAKEYWGTK------GRFgIVPLLNNQAYWFITINAKERDpKY 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 246 KNQTQVDFQNRnsvvdfllkeFSDWDERYKELIHTTlSFVGLATR-IFPLeKPWKS---KRplpITMIGDAAHLMPPFAG 321
Cdd:PRK06753  223 SSFGKPHLQAY----------FNHYPNEVREILDKQ-SETGILHHdIYDL-KPLKSfvyGR---IVLLGDAAHATTPNMG 287

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1750501969 322 QGVNSGLVDALILSDNLADGKFnsiEEAVKNYEQ 355
Cdd:PRK06753  288 QGAGQAMEDAIVLANCLNAYDF---EKALQRYDK 318
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 19-339 1.44e-13

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: 71.20  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKDR----QARIFG-GTLDLhktsgqeaMKKAGLLKAYYDLALP---MGVN 90
Cdd:pfam01494   4 VLIVGGGPAGLMLALLLARAGVRVVLVERHATTsvlpRAHGLNqRTMEL--------LRQAGLEDRILAEGVPhegMGLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  91 IADEKGNILSTKNVKPENRFDNPEinrNDLRAILLNSLEND--TVIWDRKLVMLEPGKKKWTLTFENKPSET-----ADL 163
Cdd:pfam01494  76 FYNTRRRADLDFLTSPPRVTVYPQ---TELEPILVEHAEARgaQVRFGTEVLSLEQDGDGVTAVVRDRRDGEeytvrAKY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 164 VILANGGMSKVRKFV-TDTEVEET---GTFNIQADIHQPEINCPGFFQLCngnRLMASHQGNLLFAnPNNNGALHFGISF 239
Cdd:pfam01494 153 LVGCDGGRSPVRKTLgIEFEGFEGvpfGSLDVLFDAPDLSDPVERAFVHY---LIYAPHSRGFMVG-PWRSAGRERYYVQ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 240 KTPDEWKNQTQVDFQnrnsvvdfllkefsdwDERYKELIHTTlsfvgLATRIFPLEKPWKSKRPL-----------PITM 308
Cdd:pfam01494 229 VPWDEEVEERPEEFT----------------DEELKQRLRSI-----VGIDLALVEILWKSIWGVasrvatryrkgRVFL 287

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1750501969 309 IGDAAHLMPPFAGQGVNSGLVDALILSDNLA 339
Cdd:pfam01494 288 AGDAAHIHPPTGGQGLNTAIQDAFNLAWKLA 318
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 18-342 3.07e-10

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: 61.07  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYErdkdrqarifggtldlhktsGQEAMKKAgllKAYYD---LALPMG-VNIAD 93
Cdd:TIGR01988   1 DIVIVGGGMVGLALALALARSGLKVALIE--------------------ATPLPAPA---DPGFDnrvSALSAAsIRLLE 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  94 EKG--NILSTKNVKP-------------ENRFDNPEINRNDL---------RAILLNSLEND---TVIWDRKLVMLEPGK 146
Cdd:TIGR01988  58 KLGvwDKIEPARAQPirdihvsdggsfgALRFDADEIGLEALgyvvenrvlQQALWERLQELpnvTLLCPARVVELPRHS 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 147 KKWTLTFENKPSETADLVILANGGMSKVRKFvtdteveetgtFNIQADIHQPEincpgffQLCngnrLMAshqgNLLFAN 226
Cdd:TIGR01988 138 DHVELTLDDGQQLRARLLVGADGANSKVRQL-----------AGIPTTGWDYG-------QSA----VVA----NVKHER 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 227 PNNNGA----LHFGISFKTPDewknqtqvdFQNRNSVVdfllkeFSDWDERYKELIhtTLS---FVGLATRIFP------ 293
Cdd:TIGR01988 192 PHQGTAwerfTPTGPLALLPL---------PDNRSSLV------WTLPPEEAERLL--ALSdeeFLAELQRAFGsrlgai 254

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750501969 294 -LEKPwKSKRPLPIT-----------MIGDAAHLMPPFAGQGVNSGLVDALILSDNLADGK 342
Cdd:TIGR01988 255 tLVGE-RHAFPLSLThakryvaprlaLIGDAAHTIHPLAGQGLNLGLRDVAALAEVLEDAR 314
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 18-59 2.81e-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: 39.43  E-value: 2.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDID-VTVYERDKDR--QARIFGGT 59
Cdd:cd08234   162 SVLVFGAGPIGLLLAQLLKLNGASrVTVAEPNEEKleLAKKLGAT 206
 
Name Accession Description Interval E-value
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 19-386 1.05e-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: 159.72  E-value: 1.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIFGGTLDLhktSGQEAMKKAGLLKAYYDLALPM-GVNIAD-EKG 96
Cdd:COG0654     6 VLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSP---RSLELLRRLGLWDRLLARGAPIrGIRVRDgSDG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  97 NILSTKNVKPENRFDNPEINRNDLRAILLNSLE--NDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKV 174
Cdd:COG0654    83 RVLARFDAAETGLPAGLVVPRADLERALLEAARalGVELRFGTEVTGLEQDADGVTVTLADGRTLRADLVVGADGARSAV 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 175 RKfvtdteveetgtfniqadihqpeincpgffqlcngnrlmashqgnllfanpnnngalHFGISFktpdewknqTQVDFQ 254
Cdd:COG0654   163 RR---------------------------------------------------------LLGIGF---------TGRDYP 176

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 255 NRNSVVDF---LLKEFSDWDERYKELIHTT-LSFVGLATRIFPlekPWKSKRplpITMIGDAAHLMPPFAGQGVNSGLVD 330
Cdd:COG0654   177 QRALWAGVrteLRARLAAAGPRLGELLELSpRSAFPLRRRRAE---RWRRGR---VVLLGDAAHTMHPLGGQGANLALRD 250

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1750501969 331 ALILSDNLADGKFN-SIEEAVKNYEQQMFIYGKEAQEESTQNeIEMFKPDFTFQQLL 386
Cdd:COG0654   251 AAALAWKLAAALRGrDDEAALARYERERRPRAARVQRAADAL-GRLFHPDSPPLRLL 306
PRK06753 PRK06753
hypothetical protein; Provisional
 18-355 3.64e-24

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 102.46  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYErdKDRQARIFGGTLDLhktsGQEAMKKAGLlkayYDLA---------LPmG 88
Cdd:PRK06753    2 KIAIIGAGIGGLTAAALLQEQGHEVKVFE--KNESVKEVGAGIGI----GDNVIKKLGN----HDLAkgiknagqiLS-T 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  89 VNIADEKGNILSTknVKPENRFDNPEINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILAN 168
Cdd:PRK06753   71 MNLLDDKGTLLNK--VKLKSNTLNVTLHRQTLIDIIKSYVKEDAIFTGKEVTKIENETDKVTIHFADGESEAFDLCIGAD 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 169 GGMSKVRKFVT-DTEVEETGTFNIQADIHQPEINCPGFFQLCNGNRlmashqGNL-LFANPNNNGALHFGISFKTPD-EW 245
Cdd:PRK06753  149 GIHSKVRQSVNaDSKVRYQGYTCFRGLIDDIDLKLPDCAKEYWGTK------GRFgIVPLLNNQAYWFITINAKERDpKY 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 246 KNQTQVDFQNRnsvvdfllkeFSDWDERYKELIHTTlSFVGLATR-IFPLeKPWKS---KRplpITMIGDAAHLMPPFAG 321
Cdd:PRK06753  223 SSFGKPHLQAY----------FNHYPNEVREILDKQ-SETGILHHdIYDL-KPLKSfvyGR---IVLLGDAAHATTPNMG 287

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1750501969 322 QGVNSGLVDALILSDNLADGKFnsiEEAVKNYEQ 355
Cdd:PRK06753  288 QGAGQAMEDAIVLANCLNAYDF---EKALQRYDK 318
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
19-339 2.69e-16

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 80.34  E-value: 2.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKD--RQARifGGTLDlhktsgQEAMK---KAGLLKAYYDLALPM-GVNIA 92
Cdd:PRK06183   13 VVIVGAGPVGLTLANLLGQYGVRVLVLERWPTlyDLPR--AVGID------DEALRvlqAIGLADEVLPHTTPNhGMRFL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  93 DEKGNILSTKNVKPE--------NRFDNPEINRNdLRAiLLNSLENDTVIWDRKLVMLEPGKKKWTLTFEN---KPSE-T 160
Cdd:PRK06183   85 DAKGRCLAEIARPSTgefgwprrNAFHQPLLEAV-LRA-GLARFPHVRVRFGHEVTALTQDDDGVTVTLTDadgQRETvR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 161 ADLVILANGGMSKVRKFVtDTEVEETGTFN----IQADIHQPEINCPGFFQLCNGNRlmashqgnllfanPNNNGALHFG 236
Cdd:PRK06183  163 ARYVVGCDGANSFVRRTL-GVPFEDLTFPErwlvVDVLIANDPLGGPHTYQYCDPAR-------------PYTSVRLPHG 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 237 I---SFK-----TPDEWknqtqvdfqNRNSVVDFLLKEFSDWDERYkELI-HTTLSF-VGLATRifplekpWKSKRPLpi 306
Cdd:PRK06183  229 RrrwEFMllpgeTEEQL---------ASPENVWRLLAPWGPTPDDA-ELIrHAVYTFhARVADR-------WRSGRVL-- 289

                         330       340       350
                  ....*....|....*....|....*....|...
gi 1750501969 307 tMIGDAAHLMPPFAGQGVNSGLVDALilsdNLA 339
Cdd:PRK06183  290 -LAGDAAHLMPPFAGQGMNSGIRDAA----NLA 317
PRK06847 PRK06847
hypothetical protein; Provisional
 17-375 1.37e-14

hypothetical protein; Provisional


Pssm-ID: 235874 [Multi-domain]  Cd Length: 375  Bit Score: 74.52  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQAR-----IFGGTLdlhktsgqEAMKKAGLLKAYYDLALPM-GVN 90
Cdd:PRK06847    5 KKVLIVGGGIGGLSAAIALRRAGIAVDLVEIDPEWRVYgagitLQGNAL--------RALRELGVLDECLEAGFGFdGVD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  91 IADEKGNILSTknvKPENRFDNPE------INRNDLRAILLNSLE--NDTVIWDRKLVMLEPGKKKWTLTFENKPSETAD 162
Cdd:PRK06847   77 LFDPDGTLLAE---LPTPRLAGDDlpggggIMRPALARILADAARaaGADVRLGTTVTAIEQDDDGVTVTFSDGTTGRYD 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 163 LVILANGGMSKVRK--FVTDTEVEETGT----FNIQadiHQPEINCPGFFQlcnGNRL------MASHQGNLLF--ANPN 228
Cdd:PRK06847  154 LVVGADGLYSKVRSlvFPDEPEPEYTGQgvwrAVLP---RPAEVDRSLMYL---GPTTkagvvpLSEDLMYLFVtePRPD 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 229 NngalhfgiSFKTPDEWKNQtqvdfqnrnsvVDFLLKEFSD--WDERYKELIHTT-LSFVGLATRIFPleKPWKSKRplp 305
Cdd:PRK06847  228 N--------PRIEPDTLAAL-----------LRELLAPFGGpvLQELREQITDDAqVVYRPLETLLVP--APWHRGR--- 283

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750501969 306 ITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLADGkfNSIEEAVKNYEQQMFIYGKEAQEESTQ-NEIEM 375
Cdd:PRK06847  284 VVLIGDAAHATTPHLAQGAGMAIEDAIVLAEELARH--DSLEAALQAYYARRWERCRMVVEASARiGRIEI 352
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 19-339 1.44e-13

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: 71.20  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKDR----QARIFG-GTLDLhktsgqeaMKKAGLLKAYYDLALP---MGVN 90
Cdd:pfam01494   4 VLIVGGGPAGLMLALLLARAGVRVVLVERHATTsvlpRAHGLNqRTMEL--------LRQAGLEDRILAEGVPhegMGLA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  91 IADEKGNILSTKNVKPENRFDNPEinrNDLRAILLNSLEND--TVIWDRKLVMLEPGKKKWTLTFENKPSET-----ADL 163
Cdd:pfam01494  76 FYNTRRRADLDFLTSPPRVTVYPQ---TELEPILVEHAEARgaQVRFGTEVLSLEQDGDGVTAVVRDRRDGEeytvrAKY 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 164 VILANGGMSKVRKFV-TDTEVEET---GTFNIQADIHQPEINCPGFFQLCngnRLMASHQGNLLFAnPNNNGALHFGISF 239
Cdd:pfam01494 153 LVGCDGGRSPVRKTLgIEFEGFEGvpfGSLDVLFDAPDLSDPVERAFVHY---LIYAPHSRGFMVG-PWRSAGRERYYVQ 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 240 KTPDEWKNQTQVDFQnrnsvvdfllkefsdwDERYKELIHTTlsfvgLATRIFPLEKPWKSKRPL-----------PITM 308
Cdd:pfam01494 229 VPWDEEVEERPEEFT----------------DEELKQRLRSI-----VGIDLALVEILWKSIWGVasrvatryrkgRVFL 287

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1750501969 309 IGDAAHLMPPFAGQGVNSGLVDALILSDNLA 339
Cdd:pfam01494 288 AGDAAHIHPPTGGQGLNTAIQDAFNLAWKLA 318
PRK05868 PRK05868
FAD-binding protein;
17-371 5.27e-12

FAD-binding protein;


Pssm-ID: 180297 [Multi-domain]  Cd Length: 372  Bit Score: 66.55  E-value: 5.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDkdRQARIFGGTLDLhKTSGQEAMKKAGLLKAYYDLALPM-GVNIADEK 95
Cdd:PRK05868    2 KTVVVSGASVAGTAAAYWLGRHGYSVTMVERH--PGLRPGGQAIDV-RGPALDVLERMGLLAAAQEHKTRIrGASFVDRD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  96 GNILS--TKNVKPENRFDNPEIN--RNDLRAILLNSLENDT-VIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGG 170
Cdd:PRK05868   79 GNELFrdTESTPTGGPVNSPDIEllRDDLVELLYGATQPSVeYLFDDSISTLQDDGDSVRVTFERAAAREFDLVIGADGL 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 171 MSKVRKFVTDTE---VEETGTfniqadiHQPEINCPGFFQLcngNRLMASHQGNLLFA---NPNNNGALHFGISFKtpde 244
Cdd:PRK05868  159 HSNVRRLVFGPEeqfVKRLGT-------HAAIFTVPNFLEL---DYWQTWHYGDSTMAgvySARNNTEARAALAFM---- 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 245 wKNQTQVDFQNRNSvvdfllkEFSDWDERYKE-------LIHTTLS----FVGLATRIfpLEKPWKSKRplpITMIGDAA 313
Cdd:PRK05868  225 -DTELRIDYRDTEA-------QFAELQRRMAEdgwvraqLLHYMRSapdfYFDEMSQI--LMDRWSRGR---VALVGDAG 291

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1750501969 314 HLMPPFAGQGVNSGLVDALILSDNLADGKfNSIEEAVKNYEQQMFIYGKEAQEESTQN 371
Cdd:PRK05868  292 YCCSPLSGQGTSVALLGAYILAGELKAAG-DDYQLGFANYHAEFHGFVERNQWLVSDN 348
Ubi-OHases TIGR01988
Ubiquinone biosynthesis hydroxylase, UbiH/UbiF/VisC/COQ6 family; This model represents a ...
 18-342 3.07e-10

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: 61.07  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYErdkdrqarifggtldlhktsGQEAMKKAgllKAYYD---LALPMG-VNIAD 93
Cdd:TIGR01988   1 DIVIVGGGMVGLALALALARSGLKVALIE--------------------ATPLPAPA---DPGFDnrvSALSAAsIRLLE 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  94 EKG--NILSTKNVKP-------------ENRFDNPEINRNDL---------RAILLNSLEND---TVIWDRKLVMLEPGK 146
Cdd:TIGR01988  58 KLGvwDKIEPARAQPirdihvsdggsfgALRFDADEIGLEALgyvvenrvlQQALWERLQELpnvTLLCPARVVELPRHS 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 147 KKWTLTFENKPSETADLVILANGGMSKVRKFvtdteveetgtFNIQADIHQPEincpgffQLCngnrLMAshqgNLLFAN 226
Cdd:TIGR01988 138 DHVELTLDDGQQLRARLLVGADGANSKVRQL-----------AGIPTTGWDYG-------QSA----VVA----NVKHER 191

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 227 PNNNGA----LHFGISFKTPDewknqtqvdFQNRNSVVdfllkeFSDWDERYKELIhtTLS---FVGLATRIFP------ 293
Cdd:TIGR01988 192 PHQGTAwerfTPTGPLALLPL---------PDNRSSLV------WTLPPEEAERLL--ALSdeeFLAELQRAFGsrlgai 254

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750501969 294 -LEKPwKSKRPLPIT-----------MIGDAAHLMPPFAGQGVNSGLVDALILSDNLADGK 342
Cdd:TIGR01988 255 tLVGE-RHAFPLSLThakryvaprlaLIGDAAHTIHPLAGQGLNLGLRDVAALAEVLEDAR 314
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
17-167 7.95e-08

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 53.34  E-value: 7.95e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYErdKDRQA-------RIFGGTLDL--------HKTSGQ--EAMKKAGLLKA 79
Cdd:COG3380     4 PDIAIIGAGIAGLAAARALQDAGHEVTVFE--KSRGVggrmatrRLDGGRFDHgaqyftarDPRFQAlvEEWLAAGLVAP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  80 YYDlalpmgvNIADEKGNILSTKNVKPENRFdnpeINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKWTLTFEN-KPS 158
Cdd:COG3380    82 WTF-------DFVVLDADGLVSPRDDGEPRY----VGVPGMNALAKHLAAGLDVRLGTRVTALERDGDGWRLTDEDgEEY 150


                  ....*....
gi 1750501969 159 ETADLVILA 167
Cdd:COG3380   151 GPFDAVVLA 159
PRK06126 PRK06126
hypothetical protein; Provisional
 11-339 3.52e-07

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 51.92  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  11 MNLLSDKNVAIIGGGPVGLTMARLLQQNDIDVTVYERdKDRQAriFGGTLDLHKTSGQEAMKKAGLLKAYYDLALPmgVN 90
Cdd:PRK06126    2 MENTSETPVLIVGGGPVGLALALDLGRRGVDSILVER-KDGTA--FNPKANTTSARSMEHFRRLGIADEVRSAGLP--VD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  91 IADEkgNILSTKNVKPE-NRFDNP-----------------------EINRNDLRAILLN---SLENDTVIWDRKLVMLE 143
Cdd:PRK06126   77 YPTD--IAYFTRLTGYElARFRLPsareaitpvggpdgswpspelphRIPQKYLEPILLEhaaAQPGVTLRYGHRLTDFE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 144 PGKKKWTLTFENKPSET-----ADLVILANGGMSKVRK-----FVTDTEVEETGTFNIQAdihqpeincPGFFQLCNGNR 213
Cdd:PRK06126  155 QDADGVTATVEDLDGGEsltirADYLVGCDGARSAVRRslgisYEGTSGLQRDLSIYIRA---------PGLAALVGHDP 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 214 lmashqGNLLFA-NPNNNGALhfgISFKTPDEWKNQTQVDFQNRNSVVDFllkefsDWDERYKELIHTTLSFVGLATrif 292
Cdd:PRK06126  226 ------AWMYWLfNPDRRGVL---VAIDGRDEWLFHQLRGGEDEFTIDDV------DARAFVRRGVGEDIDYEVLSV--- 287

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1750501969 293 pleKPWKSKRPLPITM-------IGDAAHLMPPFAGQGVNSGLVDALILSDNLA 339
Cdd:PRK06126  288 ---VPWTGRRLVADSYrrgrvflAGDAAHLFTPTGGYGMNTGIGDAVNLAWKLA 338
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 17-58 5.20e-07

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: 51.37  E-value: 5.20e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDkDRqariFGG 58
Cdd:COG1232     2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS-DR----VGG 38
PRK07588 PRK07588
FAD-binding domain;
17-386 5.22e-07

FAD-binding domain;


Pssm-ID: 169028 [Multi-domain]  Cd Length: 391  Bit Score: 51.27  E-value: 5.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYER-DKDRQarifGGTLDLHKTSGQEAMKKAGL---LKAY-YDLAlpmGVNI 91
Cdd:PRK07588    1 MKVAISGAGIAGPTLAYWLRRYGHEPTLIERaPELRT----GGYMVDFWGVGYEVAKRMGItdqLREAgYQIE---HVRS 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  92 ADEKGNI---LSTKNVKPENRFDNPEINRNDLRAILLNSLENDT-VIWDRKLVMLEPGKKKWTLTFENKPSETADLVILA 167
Cdd:PRK07588   74 VDPTGRRkadLNVDSFRRMVGDDFTSLPRGDLAAAIYTAIDGQVeTIFDDSIATIDEHRDGVRVTFERGTPRDFDLVIGA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 168 NGGMSKVRKFV----TDTEVE---ETGTFNIQADIHQPEI-----NCPGF----FQLcNGNRLMAShqgnLLFANPNNNG 231
Cdd:PRK07588  154 DGLHSHVRRLVfgpeRDFEHYlgcKVAACVVDGYRPRDERtyvlyNEVGRqvarVAL-RGDRTLFL----FIFRAEHDNP 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 232 ALhfgisfkTPDEWKNQTQVDFQNRNSVVDFLLKEFSDWDERYKElihtTLSFVGLATrifplekpWKSKRplpITMIGD 311
Cdd:PRK07588  229 PL-------TPAEEKQLLRDQFGDVGWETPDILAALDDVEDLYFD----VVSQIRMDR--------WSRGR---VALVGD 286

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1750501969 312 AAHLMPPFAGQGVNSGLVDALILSDNLADGKFNSiEEAVKNYEQQM--FIYGKEAqeeSTQNEIEMFKPDFTFQQLL 386
Cdd:PRK07588  287 AAACPSLLGGEGSGLAITEAYVLAGELARAGGDH-RRAFDAYEKRLrpFIAGKQA---AAAKFLSVFAPKTRFGLYV 359
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 17-105 1.12e-06

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


Pssm-ID: 440335 [Multi-domain]  Cd Length: 296  Bit Score: 49.68  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIFG-GTLDLHK--TSgQEAMKKAGLLKAyyDLALpmgVNIAD 93
Cdd:COG0569    96 MHVIIIGAGRVGRSLARELEEEGHDVVVIDKDPERVERLAEeDVLVIVGdaTD-EEVLEEAGIEDA--DAVI---AATGD 169

                          90
                  ....*....|..
gi 1750501969  94 EKGNILSTKNVK 105
Cdd:COG0569   170 DEANILACLLAK 181
COQ6 TIGR01989
ubiquinone biosynthesis monooxygenase COQ6; This model represents the monooxygenase ...
 18-344 2.93e-06

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: 48.98  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQN----DIDVTVYE--RDKDRQARIF---GGTLDLHKTS----GQEAMKKAG----LLKAY 80
Cdd:TIGR01989   2 DVVIVGGGPVGLALAAALGNNpltkDLKVLLLDavDNPKLKSRNYekpDGPYSNRVSSitpaSISFFKKIGawdhIQSDR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  81 YDLALPMGVNIADEKGNI-LSTKNVKPENRFdnpeINRND-LRAILLNSLE-----NDTVIWDRKLVMLE-PGKKK---- 148
Cdd:TIGR01989  82 IQPFGRMQVWDGCSLALIrFDRDNGKEDMAC----IIENDnIQNSLYNRLQeyngdNVKILNPARLISVTiPSKYPndns 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 149 -WT-LTFENKPSETADLVILANGGMSKVRKFVtdtEVEETG-TFNIQADIHQPEINCPGF----FQ--LCNG-------- 211
Cdd:TIGR01989 158 nWVhITLSDGQVLYTKLLIGADGSNSNVRKAA---NIDTTGwNYNQHAVVATLKLEEATEndvaWQrfLPTGpiallplp 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 212 NRL------MASHQGNLLFANPNN------NGALHFGISfktPDEWKNQTQVDFQNRNSVVDFLlKEFSDWDERYKELIH 279
Cdd:TIGR01989 235 DNNstlvwsTSPEEALRLLSLPPEdfvdalNAAFDLGYS---DHPYSYLLDYAMEKLNEDIGFR-TEGSKSCFQVPPRVI 310

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 280 TTLSfvglATRI-FPLE----KPWKSKRplpITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLADGKFN 344
Cdd:TIGR01989 311 GVVD----KSRAaFPLGlghaDEYVTKR---VALVGDAAHRVHPLAGQGVNLGFGDVASLVKALAEAVSV 373
PRK07208 PRK07208
hypothetical protein; Provisional
 17-48 2.99e-06

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 49.12  E-value: 2.99e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERD 48
Cdd:PRK07208    5 KSVVIIGAGPAGLTAAYELLKRGYPVTVLEAD 36
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
306-340 3.20e-06

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 48.80  E-value: 3.20e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1750501969 306 ITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLAD 340
Cdd:PRK07608  282 VALVGDAAHLIHPLAGQGMNLGLRDVAALADVLAG 316
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 15-60 5.21e-06

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: 48.21  E-value: 5.21e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1750501969  15 SDKNVAIIGGGPVGLTMARLLQQNDIDVTVYERDKdrqarIFGGTL 60
Cdd:COG0493   120 TGKKVAVVGSGPAGLAAAYQLARAGHEVTVFEALD-----KPGGLL 160
trkA PRK09496
Trk system potassium transporter TrkA;
17-51 5.36e-06

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 48.19  E-value: 5.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDR 51
Cdd:PRK09496  232 KRVMIVGGGNIGYYLAKLLEKEGYSVKLIERDPER 266
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 16-59 6.59e-06

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: 47.94  E-value: 6.59e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1750501969  16 DKNVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDrqariFGGT 59
Cdd:COG2072     6 HVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEKADD-----VGGT 44
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 19-61 7.10e-06

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 47.49  E-value: 7.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERdKDRQA---RIFGGTLD 61
Cdd:PRK08243    5 VAIIGAGPAGLLLGQLLHLAGIDSVVLER-RSREYvegRIRAGVLE 49
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 15-60 7.18e-06

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 47.85  E-value: 7.18e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1750501969  15 SDKNVAIIGGGPVGLTMARLLQQNDIDVTVYERDkDRqariFGGTL 60
Cdd:PRK12810  142 TGKKVAVVGSGPAGLAAADQLARAGHKVTVFERA-DR----IGGLL 182
PRK05714 PRK05714
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 306-338 1.42e-05

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


Pssm-ID: 168201 [Multi-domain]  Cd Length: 405  Bit Score: 46.75  E-value: 1.42e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969 306 ITMIGDAAHLMPPFAGQGVNSGLVDALILSDNL 338
Cdd:PRK05714  287 LALIGDAAHTIHPLAGQGVNLGFLDAAVLAEVL 319
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 15-47 1.87e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 46.33  E-value: 1.87e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969  15 SDKNVAIIGGGPVGLTMARLLQQNDIDVTVYER 47
Cdd:PRK11749  139 TGKKVAVIGAGPAGLTAAHRLARKGYDVTIFEA 171
PRK07233 PRK07233
hypothetical protein; Provisional
 18-50 2.24e-05

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 46.03  E-value: 2.24e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYERDKD 50
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQ 33
PRK07045 PRK07045
putative monooxygenase; Reviewed
 18-358 2.81e-05

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 45.67  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYERDkdRQARIFGGTlDLHKTSGQEAMKKAGLL--------------KAYYDL 83
Cdd:PRK07045    7 DVLINGSGIAGVALAHLLGARGHSVTVVERA--ARNRAQNGA-DLLKPSGIGVVRAMGLLddvfaagglrrdamRLYHDK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  84 ALPMGVNI--ADEKGNILStknvkpenrfdnpeINRNDLRAILLNSLENDTVIWDRKLVMLEPGKKKW-----TLTFENK 156
Cdd:PRK07045   84 ELIASLDYrsASALGYFIL--------------IPCEQLRRLLLAKLDGLPNVRLRFETSIERIERDAdgtvtSVTLSDG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 157 PSETADLVILANGGMSKVRKFVTDTEVEET--------GTFNIQADIHQpeincpgffqlCNgnRLMASHQGNLLFANPN 228
Cdd:PRK07045  150 ERVAPTVLVGADGARSMIRDDVLRMPAERVpyatpmafGTIALTDSVRE-----------CN--RLYVDSNQGLAYFYPI 216

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 229 NNGALHFGISFktPDEWKNQTQVDfQNRNSVVDFLLKEFSDWDERYKELIHTTLSFVGLATRIFPLEKPWKSKrplpITM 308
Cdd:PRK07045  217 GDQATRLVVSF--PADEMQGYLAD-TTRTKLLARLNEFVGDESADAMAAIGAGTAFPLIPLGRMNLDRYHKRN----VVL 289

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1750501969 309 IGDAAHLMPPFAGQGVNSGLVDALILSD--NLADGKFNSIEEAVKNYEQQMF 358
Cdd:PRK07045  290 LGDAAHSIHPITGQGMNLAIEDAGELGAclDLHLSGQIALADALERFERIRR 341
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
21-57 2.86e-05

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 41.75  E-value: 2.86e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1750501969  21 IIGGGPVGLTMARLLQQNDIDVTVYErdkdRQARIFG 57
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLE----KRDRLGG 33
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 19-50 4.33e-05

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 45.08  E-value: 4.33e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKD 50
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDD 33
PRK08132 PRK08132
FAD-dependent oxidoreductase; Provisional
 310-339 4.67e-05

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 236158 [Multi-domain]  Cd Length: 547  Bit Score: 45.24  E-value: 4.67e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1750501969 310 GDAAHLMPPFAGQGVNSGLVDAlilsDNLA 339
Cdd:PRK08132  305 GDAAHQVSPFGARGANSGIQDA----DNLA 330
PRK08850 PRK08850
2-octaprenyl-6-methoxyphenol hydroxylase; Validated
 306-338 5.54e-05

2-octaprenyl-6-methoxyphenol hydroxylase; Validated


Pssm-ID: 236341 [Multi-domain]  Cd Length: 405  Bit Score: 44.76  E-value: 5.54e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969 306 ITMIGDAAHLMPPFAGQGVNSGLVDALILSDNL 338
Cdd:PRK08850  284 VALVGDAAHTIHPLAGQGVNLGLLDAASLAQEI 316
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
19-48 6.40e-05

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 44.51  E-value: 6.40e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERD 48
Cdd:COG0665     5 VVVIGGGIAGLSTAYHLARRGLDVTVLERG 34
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
 15-47 1.05e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 44.35  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969  15 SDKNVAIIGGGPVGLTMARLLQQNDIDVTVYER 47
Cdd:PRK12769  326 SDKRVAIIGAGPAGLACADVLARNGVAVTVYDR 358
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
19-47 1.13e-04

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 43.98  E-value: 1.13e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQ-NDIDVTVYER 47
Cdd:COG0579     7 VVIIGAGIVGLALARELSRyEDLKVLVLEK 36
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
17-61 1.21e-04

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 43.95  E-value: 1.21e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDiDVTVYERDkDRqariFGG---TLD 61
Cdd:COG2907     4 MRIAVIGSGISGLTAAWLLSRRH-DVTLFEAN-DR----LGGhthTVD 45
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
24-176 1.56e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.03  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  24 GGPVGLTMARLLQQNDIDVTVYERDKDRQARIFGGTLdlhktsGQEAMKKAGLLKAYYDLALP---MGVNIADEKGNILs 100
Cdd:COG0644     1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGL------LPRALEELEPLGLDEPLERPvrgARFYSPGGKSVEL- 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1750501969 101 tknvkPENRFDNPEINRNDLRAILLNSLEND--TVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKVRK 176
Cdd:COG0644    74 -----PPGRGGGYVVDRARFDRWLAEQAEEAgaEVRTGTRVTDVLRDDGRVVVRTGDGEEIRADYVVDADGARSLLAR 146
PRK06185 PRK06185
FAD-dependent oxidoreductase;
1-86 2.07e-04

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 42.92  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969   1 MTMRIDTDkqmnllsdknVAIIGGGPVGLTMARLLQQNDIDVTVYERDKD--RQARifGGTldLHKTSgQEAMKKAGLLK 78
Cdd:PRK06185    1 MAEVETTD----------CCIVGGGPAGMMLGLLLARAGVDVTVLEKHADflRDFR--GDT--VHPST-LELMDELGLLE 65


                  ....*...
gi 1750501969  79 AYydLALP 86
Cdd:PRK06185   66 RF--LELP 71
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 287-333 2.17e-04

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 43.05  E-value: 2.17e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750501969 287 LATRIFPLEKPWKSKRPLP-ITMIGDAAHLMPPFAGQGVNSGL--VDALI 333
Cdd:PRK08020  263 VAAGAFPLTRRHALQYVQPgLALVGDAAHTINPLAGQGVNLGYrdVDALL 312
TrkA_N pfam02254
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ...
 19-134 2.60e-04

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


Pssm-ID: 426679 [Multi-domain]  Cd Length: 115  Bit Score: 40.20  E-value: 2.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDiDVTVYERDKDR--QARIFGGTLDLHKTSGQEAMKKAGLLKAyyDLALpmgVNIADEKG 96
Cdd:pfam02254   1 IIIIGYGRVGRSLAEELSEGG-DVVVIDKDEERveELREEGVPVVVGDATDEEVLEEAGIEEA--DAVI---AATGDDEA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1750501969  97 NILSTKNVKpeNRFDNPEI---NRNDLRAILLNSLENDTVI 134
Cdd:pfam02254  75 NILIVLLAR--ELNPDKKIiarANDPEHAELLRRLGADHVI 113
PRK08849 PRK08849
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Provisional
 106-334 3.21e-04

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


Pssm-ID: 181564 [Multi-domain]  Cd Length: 384  Bit Score: 42.45  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 106 PE--NRFDNPEINRNDLRAILLNSL------------ENDTVIWDRKLVMLEPGKKKWTLTFENKPSETADLVILANGGM 171
Cdd:PRK08849   87 PEcrTRFHSDELNLDQLGYIVENRLiqlglwqqfaqyPNLTLMCPEKLADLEFSAEGNRVTLESGAEIEAKWVIGADGAN 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 172 SKVRKF----VTDTEVEETGTF-NIQADIHQPEINCPGFFQlcNGNRL---MASHQGNLLFanpnnngalhfgisFKTPD 243
Cdd:PRK08849  167 SQVRQLagigITAWDYRQHCMLiNVETEQPQQDITWQQFTP--SGPRSflpLCGNQGSLVW--------------YDSPK 230

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 244 EWKNQTQV-DFQNRNSVVDFLLKEFSDwderYKELIHTTlsfvglatriFPLEK----PWKSKRplpITMIGDAAHLMPP 318
Cdd:PRK08849  231 RIKQLSAMnPEQLRSEILRHFPAELGE----IKVLQHGS----------FPLTRrhaqQYVKNN---CVLLGDAAHTINP 293

                         250
                  ....*....|....*.
gi 1750501969 319 FAGQGVNSGLVDALIL 334
Cdd:PRK08849  294 LAGQGVNLGFKDVDVL 309
PRK08013 PRK08013
oxidoreductase; Provisional
 308-338 3.55e-04

oxidoreductase; Provisional


Pssm-ID: 236139 [Multi-domain]  Cd Length: 400  Bit Score: 42.34  E-value: 3.55e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1750501969 308 MIGDAAHLMPPFAGQGVNSGLVDALILSDNL 338
Cdd:PRK08013  286 LVGDAAHTIHPLAGQGVNLGFMDAAELIAEL 316
PRK06617 PRK06617
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
 18-366 3.70e-04

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 168629 [Multi-domain]  Cd Length: 374  Bit Score: 42.22  E-value: 3.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIFGgtlDLHKTS----GQEAMKKAGLLKAYYDLALPM-GVNIA 92
Cdd:PRK06617    3 NTVILGCGLSGMLTALSFAQKGIKTTIFESKSVKSPEFFK---DIRTTAltphSKNFLFSIDIWEELEKFVAEMqDIYVV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  93 DEKGN-ILSTKNvkPENRFDNPEINRNDLRAILLNSLEND---TVIWDRKLVMLEPGKKKWTLTFENKPSEtADLVILAN 168
Cdd:PRK06617   80 DNKASeILDLRN--DADAVLGYVVKNSDFKKILLSKITNNpliTLIDNNQYQEVISHNDYSIIKFDDKQIK-CNLLIICD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 169 GGMSKVRKFVTDTEVEETG----TFNIQADihQPEINCP-------GFFQLCNgnrLMASHQGNLLFANPNNNGALHFGI 237
Cdd:PRK06617  157 GANSKVRSHYFANEIEKPYqtalTFNIKHE--KPHENCAmehflplGPFALLP---LKDQYASSVIWSTSSDQAALIVNL 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 238 SFKtpdewknqtQVDFQNRNSVVDFLlkefsdwderYKELIHTTLSFVGLATRIfpLEKPWKSKrplpITMIGDAAHLMP 317
Cdd:PRK06617  232 PVE---------EVRFLTQRNAGNSL----------GKITIDSEISSFPLKARI--ANRYFHNR----IVLIADTAHTVH 286

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1750501969 318 PFAGQGVNSGLVDALILSDNLADGkfNSIEEAVKNYEQQMFIYGKEAQE 366
Cdd:PRK06617  287 PLAGQGLNQGIKDIEILSMIVSNN--GTLQEYQKLRQEDNFIMYKLTDE 333
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
16-58 3.90e-04

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 42.22  E-value: 3.90e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1750501969  16 DKNVAIIGGGPVGLTMARLLQQNDIDVTVYE-RDkdrqaRIfGG 58
Cdd:COG1231     7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRD-----RV-GG 44
PRK09126 PRK09126
FAD-dependent hydroxylase;
19-47 4.66e-04

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 41.85  E-value: 4.66e-04
                          10        20
                  ....*....|....*....|....*....
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYER 47
Cdd:PRK09126    6 IVVVGAGPAGLSFARSLAGSGLKVTLIER 34
PRK06185 PRK06185
FAD-dependent oxidoreductase;
309-341 5.41e-04

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 41.77  E-value: 5.41e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1750501969 309 IGDAAHLMPPFAGQGVNSGLVDAL----ILSDNLADG 341
Cdd:PRK06185  289 IGDAAHAMSPVGGVGINLAIQDAVaaanILAEPLRRG 325
PRK07538 PRK07538
hypothetical protein; Provisional
 255-357 6.62e-04

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 41.42  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 255 NRNSVVDFLLKEFSDWDERYkelihttLSFVGL---ATRIFplEKPWKSKRPLP------ITMIGDAAHLMPPFAGQGVN 325
Cdd:PRK07538  248 NRPGDLEDFLPHFADWRFDW-------LDVPALiraAEAIY--EYPMVDRDPLPrwtrgrVTLLGDAAHPMYPVGSNGAS 318

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1750501969 326 SGLVDALILSDNLADGKfnSIEEAVKNYEQQM 357
Cdd:PRK07538  319 QAILDARALADALAAHG--DPEAALAAYEAER 348
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 17-57 6.79e-04

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


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 41.34  E-value: 6.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYErdkdRQARIFG 57
Cdd:COG0446   125 KRAVVIGGGPIGLELAEALRKRGLKVTLVE----RAPRLLG 161
Kch COG1226
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism];
19-57 8.25e-04

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


Pssm-ID: 440839 [Multi-domain]  Cd Length: 279  Bit Score: 40.87  E-value: 8.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYERDKDR--QARIFG 57
Cdd:COG1226   127 VIIAGFGRVGQIVARLLRAEGIPFVVIDLDPERveELRRFG 167
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
292-340 1.12e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 40.62  E-value: 1.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1750501969 292 FPLEKPW-KSKRPLPITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLAD 340
Cdd:PRK08773  269 FPLRRQLvQQYVSGRVLTLGDAAHVVHPLAGQGVNLGLRDVAALQQLVRQ 318
trkA PRK09496
Trk system potassium transporter TrkA;
18-62 1.19e-03

Trk system potassium transporter TrkA;


Pssm-ID: 236541 [Multi-domain]  Cd Length: 453  Bit Score: 40.88  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIfGGTLDL 62
Cdd:PRK09496    2 KIIIVGAGQVGYTLAENLSGENNDVTVIDTDEERLRRL-QDRLDV 45
PRK08244 PRK08244
monooxygenase;
282-339 1.50e-03

monooxygenase;


Pssm-ID: 236199 [Multi-domain]  Cd Length: 493  Bit Score: 40.50  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1750501969 282 LSFVGLATRifpLEKPWKSKRplpITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLA 339
Cdd:PRK08244  256 MSRFGNATR---QAERYRSGR---IFLAGDAAHIHFPAGGQGLNVGLQDAMNLGWKLA 307
NAD_binding_7 pfam13241
Putative NAD(P)-binding; This domain is found in fungi, plants, archaea and bacteria.
 14-45 1.54e-03

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


Pssm-ID: 433055 [Multi-domain]  Cd Length: 104  Bit Score: 37.84  E-value: 1.54e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1750501969  14 LSDKNVAIIGGGPVGLTMARLLQQNDIDVTVY 45
Cdd:pfam13241   5 LRGKRVLVVGGGEVAARKARKLLEAGAKVTVV 36
PRK07333 PRK07333
ubiquinone biosynthesis hydroxylase;
255-340 1.58e-03

ubiquinone biosynthesis hydroxylase;


Pssm-ID: 180935 [Multi-domain]  Cd Length: 403  Bit Score: 40.35  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 255 NRNSVVdfllkefsdWDERYKelihTTLSFVGLATRIF--PLEK---------PWKSKR---PLPITM-----------I 309
Cdd:PRK07333  219 NRSSLV---------WTERTA----DAERLVALDDLVFeaELEQrfghrlgelKVLGKRrafPLGLTLarsfvaprfalV 285

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1750501969 310 GDAAHLMPPFAGQGVNSGLVDALILSDNLAD 340
Cdd:PRK07333  286 GDAAHGIHPIAGQGLNLGLKDVAALAEVVVE 316
PRK08163 PRK08163
3-hydroxybenzoate 6-monooxygenase;
109-355 1.73e-03

3-hydroxybenzoate 6-monooxygenase;


Pssm-ID: 181262 [Multi-domain]  Cd Length: 396  Bit Score: 40.02  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 109 RFDNPE--INRNDLRAILLNSLENDTVIWDR---KLVMLEPGKKKWTLTFENKPSETADLVILANGGMSKVRKFVTDTEV 183
Cdd:PRK08163   98 RFGNPYavIHRADIHLSLLEAVLDHPLVEFRtstHVVGIEQDGDGVTVFDQQGNRWTGDALIGCDGVKSVVRQSLVGDAP 177

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 184 EETGTFNIQADIHQ---PE---INCPgffqlcngnrlmashqgnLLFANPNNNgALHF----GISF--------KTPDEW 245
Cdd:PRK08163  178 RVTGHVVYRAVIDVddmPEdlrINAP------------------VLWAGPHCH-LVHYplrgGEQYnlvvtfhsREQEEW 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969 246 KNqTQVDFQNrnsvvdfLLKEFSDWDERYKELIH--TTLSFVGLATRIfPLEKpWKSKRplpITMIGDAAHLMPPFAGQG 323
Cdd:PRK08163  239 GV-KDGSKEE-------VLSYFEGIHPRPRQMLDkpTSWKRWATADRE-PVAK-WSTGR---VTLLGDAAHPMTQYMAQG 305

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1750501969 324 VNSGLVDALILSDNLaDGKFNSIEEAVKNYEQ 355
Cdd:PRK08163  306 ACMALEDAVTLGKAL-EGCDGDAEAAFALYES 336
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
 12-49 1.99e-03

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 40.23  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1750501969  12 NLLSDKNVAIIGGGPVGLTMARLLQQNDIDVTVYERDK 49
Cdd:PLN02172    6 NPINSQHVAVIGAGAAGLVAARELRREGHTVVVFEREK 43
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 17-174 2.14e-03

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


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 39.61  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDKdrqarifggtldlHKTSGQEAMKKAglLKAYYDLA--LPMGVNIADE 94
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDEG-------------TCPYGGCVLSKA--LLGAAEAPeiASLWADLYKR 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1750501969  95 KGNILSTKNVKPENRFDNPEInrndlraillnslendTVIWDRKLVMLEPGKKKWTLTFenkpseTADLVILANGGMSKV 174
Cdd:pfam07992  66 KEEVVKKLNNGIEVLLGTEVV----------------SIDPGAKKVVLEELVDGDGETI------TYDRLVIATGARPRL 123
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 15-46 2.33e-03

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 40.10  E-value: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1750501969  15 SDKNVAIIGGGPVGLTMARLLQQNDIDVTVYE 46
Cdd:PRK12814  192 SGKKVAIIGAGPAGLTAAYYLLRKGHDVTIFD 223
PRK07538 PRK07538
hypothetical protein; Provisional
 19-46 2.80e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 39.49  E-value: 2.80e-03
                          10        20
                  ....*....|....*....|....*...
gi 1750501969  19 VAIIGGGPVGLTMARLLQQNDIDVTVYE 46
Cdd:PRK07538    3 VLIAGGGIGGLTLALTLHQRGIEVVVFE 30
threonine_DH_like cd08234
L-threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 18-59 2.81e-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: 39.43  E-value: 2.81e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDID-VTVYERDKDR--QARIFGGT 59
Cdd:cd08234   162 SVLVFGAGPIGLLLAQLLKLNGASrVTVAEPNEEKleLAKKLGAT 206
PLN02976 PLN02976
amine oxidase
 12-46 3.11e-03

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 39.85  E-value: 3.11e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1750501969   12 NLLSD----KNVAIIGGGPVGLTMARLLQQNDIDVTVYE 46
Cdd:PLN02976   685 CVLCDsvdrKKIIVVGAGPAGLTAARHLQRQGFSVTVLE 723
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 15-58 3.52e-03

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 39.45  E-value: 3.52e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1750501969  15 SDKNVAIIGGGPVGLTMARLLQQNDIDVTVYERdkdrqARIFGG 58
Cdd:COG1233     2 MMYDVVVIGAGIGGLAAAALLARAGYRVTVLEK-----NDTPGG 40
YdhS COG4529
Uncharacterized NAD(P)/FAD-binding protein YdhS [General function prediction only];
15-50 4.32e-03

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


Pssm-ID: 443597 [Multi-domain]  Cd Length: 466  Bit Score: 39.17  E-value: 4.32e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1750501969  15 SDKNVAIIGGGPVG-LTMARLLQQ--NDIDVTVYERDKD 50
Cdd:COG4529     4 ARKRIAIIGGGASGtALAIHLLRRapEPLRITLFEPRPE 42
PRK06834 PRK06834
hypothetical protein; Provisional
 310-339 4.43e-03

hypothetical protein; Provisional


Pssm-ID: 235870 [Multi-domain]  Cd Length: 488  Bit Score: 38.85  E-value: 4.43e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1750501969 310 GDAAHLMPPFAGQGVNSGLVDALILSDNLA 339
Cdd:PRK06834  271 GDAAHVHSPVGGQGLNTGVQDAVNLGWKLA 300
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
17-61 4.63e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 38.97  E-value: 4.63e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYErdkdRQARIFGGTLD 61
Cdd:COG1251   143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVE----RAPRLLPRQLD 183
PRK08255 PRK08255
bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;
18-49 5.19e-03

bifunctional salicylyl-CoA 5-hydroxylase/oxidoreductase;


Pssm-ID: 236203 [Multi-domain]  Cd Length: 765  Bit Score: 39.15  E-value: 5.19e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQND--IDVTVYERDK 49
Cdd:PRK08255    2 RIVCIGGGPAGLYFALLMKLLDpaHEVTVVERNR 35
PRK07364 PRK07364
FAD-dependent hydroxylase;
308-340 5.87e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 38.46  E-value: 5.87e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969 308 MIGDAAHLMPPFAGQGVNSGLVDALILSDNLAD 340
Cdd:PRK07364  298 LVGDAAHCCHPVGGQGLNLGIRDAAALAQVLQT 330
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
306-340 6.43e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 38.34  E-value: 6.43e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1750501969 306 ITMIGDAAHLMPPFAGQGVNSGLVDALILSDNLAD 340
Cdd:PRK07494  282 TALVGEAAHVFPPIGAQGLNLGLRDVATLVEIVED 316
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 17-49 7.10e-03

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 38.32  E-value: 7.10e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1750501969  17 KNVAIIGGGPVGLTMARLLQQNDIDVTVYERDK 49
Cdd:PRK12771  138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGP 170
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 18-74 7.19e-03

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


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 38.16  E-value: 7.19e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIFGGTLDLHKTSGQEAMKKA 74
Cdd:cd01620   164 KVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRYSQKEELEKE 220
PRK08306 PRK08306
dipicolinate synthase subunit DpsA;
18-56 8.13e-03

dipicolinate synthase subunit DpsA;


Pssm-ID: 181371 [Multi-domain]  Cd Length: 296  Bit Score: 37.90  E-value: 8.13e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1750501969  18 NVAIIGGGPVGLTMARLLQQNDIDVTVYERDKDRQARIF 56
Cdd:PRK08306  154 NVLVLGFGRTGMTLARTLKALGANVTVGARKSAHLARIT 192
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 9-74 8.19e-03

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


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 37.81  E-value: 8.19e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1750501969   9 KQMNLLSDKNVAIIGGGPVGLTMARLLQQ-NDIDVTVYERDKDRQ--ARIFG--GTLDLHKTSGQEAMKKA 74
Cdd:COG1063   155 ERAGVKPGDTVLVIGAGPIGLLAALAARLaGAARVIVVDRNPERLelARELGadAVVNPREEDLVEAVREL 225
PRK13984 PRK13984
putative oxidoreductase; Provisional
 16-46 8.25e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 38.21  E-value: 8.25e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1750501969  16 DKNVAIIGGGPVGLTMARLLQQNDIDVTVYE 46
Cdd:PRK13984  283 NKKVAIVGSGPAGLSAAYFLATMGYEVTVYE 313
PRK12831 PRK12831
putative oxidoreductase; Provisional
 16-46 8.67e-03

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 38.08  E-value: 8.67e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1750501969  16 DKNVAIIGGGPVGLTMARLLQQNDIDVTVYE 46
Cdd:PRK12831  140 GKKVAVIGSGPAGLTCAGDLAKMGYDVTIFE 170
 
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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