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Conserved domains on  [gi|75220022|sp|O81000|]
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RecName: Full=Squalene epoxidase 2, mitochondrial; Short=AtSQE2; Flags: Precursor

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PLN02985 super family cl39108
squalene monooxygenase
 77-582 0e+00

squalene monooxygenase


The actual alignment was detected with superfamily member PLN02985:

Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 530.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   77 FIASLFTFLLLYILRRSSNKNKKNRGLVvsqnDTVSknlETEVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFS 156
Cdd:PLN02985   5 CLWTLLAFVLTWTVFYVTNRKKKATELA----DAVA---EERKDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  157 EQDRIVGELLQPGGYLKLIELGLEDCVKKIDAQRVLGYVLFKDGKHTKLAYPLE--TFDSDVAGRSFHNGRFVQRMREKA 234
Cdd:PLN02985  78 EPERMMGEFMQPGGRFMLSKLGLEDCLEGIDAQKATGMAVYKDGKEAVAPFPVDnnNFPYEPSARSFHNGRFVQRLRQKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  235 LTLSNVRLEQGTVTSLLEEHGTIKGVRYRTKEGNEFRSFAPLTIVCDGCFSNLRRSLCKPKVDVPSTFVGLVLENCELPF 314
Cdd:PLN02985 158 SSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTALAPLTVVCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  315 ANHGHVVLGDPSPILMYPISSSEVRCLVDVPGQKLPPIANGEMAKYLKTRVAPQVPTKVREAFITAVEKG-NIRTMPNRS 393
Cdd:PLN02985 238 PEKLHLIMSKPSFTMLYQISSTDVRCVFEVLPDNIPSIANGEMSTFVKNTIAPQVPPKLRKIFLKGIDEGaHIKVVPTKR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  394 MPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVLRDLLRPIRNLNDKEALSKYIESFYTLRKPVASTINTLADAL 473
Cdd:PLN02985 318 MSATLSDKKGVIVLGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNANKVSEVIKSFYDIRKPMSATVNTLGNAF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  474 YKVFLASSDEARTEMREACFDYLSLGGVFSSGPVALLSGLNPRPLSLVLHFFAVAIYAVCRLMLPFPSIESFWLGARIIS 553
Cdd:PLN02985 398 SQVLVASTDEAKEAMRQGCYDYLCSGGFRTSGMMALLGGMNPRPLSLIYHLCAITLSSIGHLLSPFPSPLRIWHSLRLFG 477

                        490       500
                 ....*....|....*....|....*....
gi 75220022  554 SASSIIFPIIKAEGVRQMFFPrTIPAIYR 582
Cdd:PLN02985 478 LALKMLVPHLKAEGVSQMLFP-ANAAAYR 505
 
Name Accession Description Interval E-value
PLN02985 PLN02985
squalene monooxygenase
 77-582 0e+00

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 530.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   77 FIASLFTFLLLYILRRSSNKNKKNRGLVvsqnDTVSknlETEVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFS 156
Cdd:PLN02985   5 CLWTLLAFVLTWTVFYVTNRKKKATELA----DAVA---EERKDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  157 EQDRIVGELLQPGGYLKLIELGLEDCVKKIDAQRVLGYVLFKDGKHTKLAYPLE--TFDSDVAGRSFHNGRFVQRMREKA 234
Cdd:PLN02985  78 EPERMMGEFMQPGGRFMLSKLGLEDCLEGIDAQKATGMAVYKDGKEAVAPFPVDnnNFPYEPSARSFHNGRFVQRLRQKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  235 LTLSNVRLEQGTVTSLLEEHGTIKGVRYRTKEGNEFRSFAPLTIVCDGCFSNLRRSLCKPKVDVPSTFVGLVLENCELPF 314
Cdd:PLN02985 158 SSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTALAPLTVVCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  315 ANHGHVVLGDPSPILMYPISSSEVRCLVDVPGQKLPPIANGEMAKYLKTRVAPQVPTKVREAFITAVEKG-NIRTMPNRS 393
Cdd:PLN02985 238 PEKLHLIMSKPSFTMLYQISSTDVRCVFEVLPDNIPSIANGEMSTFVKNTIAPQVPPKLRKIFLKGIDEGaHIKVVPTKR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  394 MPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVLRDLLRPIRNLNDKEALSKYIESFYTLRKPVASTINTLADAL 473
Cdd:PLN02985 318 MSATLSDKKGVIVLGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNANKVSEVIKSFYDIRKPMSATVNTLGNAF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  474 YKVFLASSDEARTEMREACFDYLSLGGVFSSGPVALLSGLNPRPLSLVLHFFAVAIYAVCRLMLPFPSIESFWLGARIIS 553
Cdd:PLN02985 398 SQVLVASTDEAKEAMRQGCYDYLCSGGFRTSGMMALLGGMNPRPLSLIYHLCAITLSSIGHLLSPFPSPLRIWHSLRLFG 477

                        490       500
                 ....*....|....*....|....*....
gi 75220022  554 SASSIIFPIIKAEGVRQMFFPrTIPAIYR 582
Cdd:PLN02985 478 LALKMLVPHLKAEGVSQMLFP-ANAAAYR 505
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 273-544 9.26e-169

Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.


Pssm-ID: 400679  Cd Length: 276  Bit Score: 480.29  E-value: 9.26e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   273 FAPLTIVCDGCFSNLRRSLCKPKVDVPSTFVGLVLENCELPFANHGHVVLGDPSPILMYPISSSEVRCLVDVPGQKLPPI 352
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPKLPSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   353 ANGEMAKYLKTRVAPQVPTKVREAFITAVEKGNIRTMPNRSMPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVL 432
Cdd:pfam08491  81 ANGELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   433 RDLLRPIRNLNDKEALSKYIESFYTLRKPVASTINTLADALYKVFLASSDEARtEMREACFDYLSLGGVFSSGPVALLSG 512
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKPYDAVINTLSIALYSLFAADSDELK-ALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 75220022   513 LNPRPLSLVLHFFAVAIYAVCRLMLPFPSIES 544
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGS 271
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 123-485 1.18e-22

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: 99.24  E-value: 1.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLKLIELGLEDcvkKIDAQ----RVLGYVLFK 198
Cdd:COG0654   4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWD---RLLARgapiRGIRVRDGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 199 DGKHtklaypLETFDSDV----AGRSFHNGRFVQRMREKALTLsNVRLEQGT-VTSLLEEHGtikGVRYRTKEGNEFRsf 273
Cdd:COG0654  81 DGRV------LARFDAAEtglpAGLVVPRADLERALLEAARAL-GVELRFGTeVTGLEQDAD---GVTVTLADGRTLR-- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 274 APLTIVCDGCFSNLRRSLckpkvdvPSTFVGLVlencelpfANHGHVVLGdpspilmypissseVRClvdvpgqklppia 353
Cdd:COG0654 149 ADLVVGADGARSAVRRLL-------GIGFTGRD--------YPQRALWAG--------------VRT------------- 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 354 ngEMAKYLkTRVAPQVPtKVREAfitavekGNIRTMPNRSMPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVLR 433
Cdd:COG0654 187 --ELRARL-AAAGPRLG-ELLEL-------SPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALA 255

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 75220022 434 DLL-RPIRNLNDKEALSKYiESfytLRKPVASTINTLADALYKVFLASSDEAR 485
Cdd:COG0654 256 WKLaAALRGRDDEAALARY-ER---ERRPRAARVQRAADALGRLFHPDSPPLR 304
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 124-426 1.89e-11

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: 65.03  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLqPGGYLKLIELGLEDCVKKIDAQRVLGyvlfkdGKHT 203
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGAL-SPRALEELDLPGELIVNLVRGARFFS------PNGD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   204 KLAYPLETFDSDVAGRSfHNGRFVQRMREKAltLSNVRLEQgTVTSLLEEHGTIkGVRYRTKEGnEFRsfAPLTIVCDGC 283
Cdd:TIGR02032  75 SVEIPIETELAYVIDRD-AFDEQLAERAQEA--GAELRLGT-RVLDVEIHDDRV-VVIVRGSEG-TVT--AKIVIGADGS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   284 FSNLRRSLCKPKVDVPSTFVglVLENCELPfanhghVVLGDPSPILMY--------------PISSSEVRCLVDVPGQKL 349
Cdd:TIGR02032 147 RSIVAKKLGLKKEPREYGVA--ARAEVEMP------DEEVDEDFVEVYidrgivpggygwvfPKGDGTANVGVGSRSAEE 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75220022   350 PPIANGEMAKYLKTRVAPQ--VPTKVREAFItavekgnirtmPNRsMPADPIPTPGALLLGDAFNMRHPLTGGGMTVAL 426
Cdd:TIGR02032 219 GEDPKKYLKDFLARRPELKdaETVEVCGALI-----------PIG-RPDEKLVRGNVLLVGDAAGHVNPLTGEGIYYAM 285
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 125-176 3.47e-03

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 39.75  E-value: 3.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 75220022 125 VIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLKLIE 176
Cdd:cd08935   9 VITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALA 60
 
Name Accession Description Interval E-value
PLN02985 PLN02985
squalene monooxygenase
 77-582 0e+00

squalene monooxygenase


Pssm-ID: 178566 [Multi-domain]  Cd Length: 514  Bit Score: 530.24  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   77 FIASLFTFLLLYILRRSSNKNKKNRGLVvsqnDTVSknlETEVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFS 156
Cdd:PLN02985   5 CLWTLLAFVLTWTVFYVTNRKKKATELA----DAVA---EERKDGATDVIIVGAGVGGSALAYALAKDGRRVHVIERDLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  157 EQDRIVGELLQPGGYLKLIELGLEDCVKKIDAQRVLGYVLFKDGKHTKLAYPLE--TFDSDVAGRSFHNGRFVQRMREKA 234
Cdd:PLN02985  78 EPERMMGEFMQPGGRFMLSKLGLEDCLEGIDAQKATGMAVYKDGKEAVAPFPVDnnNFPYEPSARSFHNGRFVQRLRQKA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  235 LTLSNVRLEQGTVTSLLEEHGTIKGVRYRTKEGNEFRSFAPLTIVCDGCFSNLRRSLCKPKVDVPSTFVGLVLENCELPF 314
Cdd:PLN02985 158 SSLPNVRLEEGTVKSLIEEKGVIKGVTYKNSAGEETTALAPLTVVCDGCYSNLRRSLNDNNAEVLSYQVGYISKNCRLEE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  315 ANHGHVVLGDPSPILMYPISSSEVRCLVDVPGQKLPPIANGEMAKYLKTRVAPQVPTKVREAFITAVEKG-NIRTMPNRS 393
Cdd:PLN02985 238 PEKLHLIMSKPSFTMLYQISSTDVRCVFEVLPDNIPSIANGEMSTFVKNTIAPQVPPKLRKIFLKGIDEGaHIKVVPTKR 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  394 MPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVLRDLLRPIRNLNDKEALSKYIESFYTLRKPVASTINTLADAL 473
Cdd:PLN02985 318 MSATLSDKKGVIVLGDAFNMRHPAIASGMMVLLSDILILRRLLQPLSNLGNANKVSEVIKSFYDIRKPMSATVNTLGNAF 397

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  474 YKVFLASSDEARTEMREACFDYLSLGGVFSSGPVALLSGLNPRPLSLVLHFFAVAIYAVCRLMLPFPSIESFWLGARIIS 553
Cdd:PLN02985 398 SQVLVASTDEAKEAMRQGCYDYLCSGGFRTSGMMALLGGMNPRPLSLIYHLCAITLSSIGHLLSPFPSPLRIWHSLRLFG 477

                        490       500
                 ....*....|....*....|....*....
gi 75220022  554 SASSIIFPIIKAEGVRQMFFPrTIPAIYR 582
Cdd:PLN02985 478 LALKMLVPHLKAEGVSQMLFP-ANAAAYR 505
SE pfam08491
Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which ...
 273-544 9.26e-169

Squalene epoxidase; This domain is found in squalene epoxidase (SE) and related proteins which are found in taxonomically diverse groups of eukaryotes and also in bacteria. SE was first cloned from Saccharomyces cerevisiae where it was named ERG1. It contains a putative FAD binding site and is a key enzyme in the sterol biosynthetic pathway. Putative transmembrane regions are found to the protein's C-terminus.


Pssm-ID: 400679  Cd Length: 276  Bit Score: 480.29  E-value: 9.26e-169
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   273 FAPLTIVCDGCFSNLRRSLCKPKVDVPSTFVGLVLENCELPFANHGHVVLGDPSPILMYPISSSEVRCLVDVPGQKLPPI 352
Cdd:pfam08491   1 FAPLTIVCDGCFSKFRKSLSDNKPEVGSYFVGLILKNADLPAPNHGHVILGKPSPVLLYQISSTETRILCDYPGPKLPSI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   353 ANGEMAKYLKTRVAPQVPTKVREAFITAVEKGNIRTMPNRSMPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVL 432
Cdd:pfam08491  81 ANGELKEYLKKSVAPQIPKELRPSFLAALEEGKIRSMPNSFLPASKNRKKGLILLGDALNMRHPLTGGGMTVGLNDIVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   433 RDLLRPIRNLNDKEALSKYIESFYTLRKPVASTINTLADALYKVFLASSDEARtEMREACFDYLSLGGVFSSGPVALLSG 512
Cdd:pfam08491 161 RKLLGPLRDLSDREKVSKVLKSFHWKRKPYDAVINTLSIALYSLFAADSDELK-ALRKGCFDYFKLGGDCVSGPVALLSG 239

                         250       260       270
                  ....*....|....*....|....*....|..
gi 75220022   513 LNPRPLSLVLHFFAVAIYAVCRLMLPFPSIES 544
Cdd:pfam08491 240 LLPRPLLLFGHFFAVALYSIYQNFIPRPILGS 271
PTZ00367 PTZ00367
squalene epoxidase; Provisional
 124-538 4.05e-143

squalene epoxidase; Provisional


Pssm-ID: 240384 [Multi-domain]  Cd Length: 567  Bit Score: 425.80  E-value: 4.05e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERD-FSEQDRIVGELLQPGGYLKLIELGLEDCVKKIDAQrVLGYVLFK-DGK 201
Cdd:PTZ00367  35 DVIIVGGSIAGPVLAKALSKQGRKVLMLERDlFSKPDRIVGELLQPGGVNALKELGMEECAEGIGMP-CFGYVVFDhKGK 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  202 HTKLAYpletfDSDVAGRSFHNGRFVQRMREKALTLS--NVRLEQGTVTSLLEEHG----TIKGVRYRTKE-----GNEF 270
Cdd:PTZ00367 114 QVKLPY-----GAGASGVSFHFGDFVQNLRSHVFHNCqdNVTMLEGTVNSLLEEGPgfseRAYGVEYTEAEkydvpENPF 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  271 RSF----------------APLTIVCDGCFSNLRRSL--CKPKVDVPSTFVGLVLENCELPFANHGHVVLGDPSPILMYP 332
Cdd:PTZ00367 189 REDppsanpsattvrkvatAPLVVMCDGGMSKFKSRYqhYTPASENHSHFVGLVLKNVRLPKEQHGTVFLGKTGPILSYR 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  333 ISSSEVRCLVDVPGQKLPPIanGEMAKYLKTRVAPQVPTKVREAFITA-VEKGNIRTMPNRSMPADPIPTPGALLLGDAF 411
Cdd:PTZ00367 269 LDDNELRVLVDYNKPTLPSL--EEQSEWLIEDVAPHLPENMRESFIRAsKDTKRIRSMPNARYPPAFPSIKGYVGIGDHA 346

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  412 NMRHPLTGGGMTVALADIVVLRDLLRPIR-----NLND----KEALSKYIESFYTLRKPVASTINTLADALYKVFLASSd 482
Cdd:PTZ00367 347 NQRHPLTGGGMTCCFSDCIRLAKSLTGIKslrsiDQNEmaeiEDAIQAAILSYARNRKTHASTINILSWALYSVFSSPA- 425

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 75220022  483 earteMREACFDYLSLGGVFSSGPVALLSGLNPRPLSLVLHFFAVAIYAVCRLMLP 538
Cdd:PTZ00367 426 -----LRDACLDYFSLGGECVTGPMSLLSGLDPSPGGLLFHYFSVALYGVLNLIME 476
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 123-485 1.18e-22

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: 99.24  E-value: 1.18e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLKLIELGLEDcvkKIDAQ----RVLGYVLFK 198
Cdd:COG0654   4 TDVLIVGGGPAGLALALALARAGIRVTVVERAPPPRPDGRGIALSPRSLELLRRLGLWD---RLLARgapiRGIRVRDGS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 199 DGKHtklaypLETFDSDV----AGRSFHNGRFVQRMREKALTLsNVRLEQGT-VTSLLEEHGtikGVRYRTKEGNEFRsf 273
Cdd:COG0654  81 DGRV------LARFDAAEtglpAGLVVPRADLERALLEAARAL-GVELRFGTeVTGLEQDAD---GVTVTLADGRTLR-- 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 274 APLTIVCDGCFSNLRRSLckpkvdvPSTFVGLVlencelpfANHGHVVLGdpspilmypissseVRClvdvpgqklppia 353
Cdd:COG0654 149 ADLVVGADGARSAVRRLL-------GIGFTGRD--------YPQRALWAG--------------VRT------------- 186

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 354 ngEMAKYLkTRVAPQVPtKVREAfitavekGNIRTMPNRSMPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVLR 433
Cdd:COG0654 187 --ELRARL-AAAGPRLG-ELLEL-------SPRSAFPLRRRRAERWRRGRVVLLGDAAHTMHPLGGQGANLALRDAAALA 255

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|...
gi 75220022 434 DLL-RPIRNLNDKEALSKYiESfytLRKPVASTINTLADALYKVFLASSDEAR 485
Cdd:COG0654 256 WKLaAALRGRDDEAALARY-ER---ERRPRAARVQRAADALGRLFHPDSPPLR 304
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
130-460 1.11e-21

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 95.42  E-value: 1.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 130 AGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLKLIELGLEDCV-KKIDAQRvlgyVLFKDGKHTKLAYP 208
Cdd:COG0644   1 AGPAGSAAARRLARAGLSVLLLEKGSFPGDKICGGGLLPRALEELEPLGLDEPLeRPVRGAR----FYSPGGKSVELPPG 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 209 LETfdsdvaGRSFHNGRFVQRMREKALTLsNVRLEQGT-VTSLLEEHGTikgVRYRTKEGNEFRsfAPLTIVCDGCFSNL 287
Cdd:COG0644  77 RGG------GYVVDRARFDRWLAEQAEEA-GAEVRTGTrVTDVLRDDGR---VVVRTGDGEEIR--ADYVVDADGARSLL 144

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 288 RRSL-CKPKVDVPSTFVGLVLENCELPFANHghvvlGDPSPILMYpisssevrclvdvpgqklppIANGEMAKYlktrva 366
Cdd:COG0644 145 ARKLgLKRRSDEPQDYALAIKEHWELPPLEG-----VDPGAVEFF--------------------FGEGAPGGY------ 193

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 367 pqvptkvreAFITAVEKGNIR-TMPNRSmPADPIPTPGALLLGDAFNMRHPLTGGGMTVALADIVVLRDLLRPIRNLND- 444
Cdd:COG0644 194 ---------GWVFPLGDGRVSvGIPLGG-PRPRLVGDGVLLVGDAAGFVDPLTGEGIHLAMKSGRLAAEAIAEALEGGDf 263

                       330
                ....*....|....*..
gi 75220022 445 -KEALSKYIESFYTLRK 460
Cdd:COG0644 264 sAEALAEYERRLRELLK 280
PRK07045 PRK07045
putative monooxygenase; Reviewed
 120-473 9.04e-19

putative monooxygenase; Reviewed


Pssm-ID: 136171 [Multi-domain]  Cd Length: 388  Bit Score: 88.43  E-value: 9.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  120 DSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLKLIELGLEDCVKKIDAQRVLGYVLFKD 199
Cdd:PRK07045   3 NNPVDVLINGSGIAGVALAHLLGARGHSVTVVERAARNRAQNGADLLKPSGIGVVRAMGLLDDVFAAGGLRRDAMRLYHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  200 GKhtklayPLETFD-SDVAGRSFHNGRFVQRMR----EKALTLSNVRLEQGTVTSLLE--EHGTIKGVRYrtkegNEFRS 272
Cdd:PRK07045  83 KE------LIASLDyRSASALGYFILIPCEQLRrlllAKLDGLPNVRLRFETSIERIErdADGTVTSVTL-----SDGER 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  273 FAPLTIV-CDGCFSNLRRSLCKPKVD-----VPSTFVGLVLENCeLPFANHGHVvlgDPSPIL--MYPISSSEVRCLVDV 344
Cdd:PRK07045 152 VAPTVLVgADGARSMIRDDVLRMPAErvpyaTPMAFGTIALTDS-VRECNRLYV---DSNQGLayFYPIGDQATRLVVSF 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  345 PGQKLPPIANGEMAKYLKTRVAPQVPTKVREAfITAVEKGN-IRTMPNRSMPADPIPTPGALLLGDAFNMRHPLTGGGMT 423
Cdd:PRK07045 228 PADEMQGYLADTTRTKLLARLNEFVGDESADA-MAAIGAGTaFPLIPLGRMNLDRYHKRNVVLLGDAAHSIHPITGQGMN 306

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 75220022  424 VALADIVVLRDLLRpiRNLNDKEALSKYIESFYTLRKPVASTINTLADAL 473
Cdd:PRK07045 307 LAIEDAGELGACLD--LHLSGQIALADALERFERIRRPVNEAVISYGHAL 354
PRK06185 PRK06185
FAD-dependent oxidoreductase;
123-290 2.14e-13

FAD-dependent oxidoreductase;


Pssm-ID: 235729 [Multi-domain]  Cd Length: 407  Bit Score: 72.20  E-value: 2.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIE------RDFseqdRivGELLQPGGyLKLI-ELGLEDCVKKIDAQRVL--- 192
Cdd:PRK06185   7 TDCCIVGGGPAGMMLGLLLARAGVDVTVLEkhadflRDF----R--GDTVHPST-LELMdELGLLERFLELPHQKVRtlr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  193 -----GYVLFKDGKHTKLAYPLETFDSDVAgrsfhngrFVQRMREKALTLSNVRLEQGT-VTSLLEEHGTIKGVRYRTKE 266
Cdd:PRK06185  80 feiggRTVTLADFSRLPTPYPYIAMMPQWD--------FLDFLAEEASAYPNFTLRMGAeVTGLIEEGGRVTGVRARTPD 151

                        170       180
                 ....*....|....*....|....*
gi 75220022  267 GN-EFRsfAPLTIVCDGCFSNLRRS 290
Cdd:PRK06185 152 GPgEIR--ADLVVGADGRHSRVRAL 174
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 123-463 1.16e-11

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: 66.19  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIER--DFSEQDRIVG------ELLQpggylkliELGLEDCVKKIDAQRVLGy 194
Cdd:pfam01494   2 TDVLIVGGGPAGLMLALLLARAGVRVVLVERhaTTSVLPRAHGlnqrtmELLR--------QAGLEDRILAEGVPHEGM- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   195 vlfkdGKHTKLAYPLETFDSDVAGRSFHNgrFVQRMREKAL----TLSNVRLEQGT-VTSLLEEHGTIKGVRYRTKEGNE 269
Cdd:pfam01494  73 -----GLAFYNTRRRADLDFLTSPPRVTV--YPQTELEPILvehaEARGAQVRFGTeVLSLEQDGDGVTAVVRDRRDGEE 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   270 FRSFAPLTIVCDGCFSNLRRSL---CKPKVDVPSTFVGLVLENCELPFANHGHVV----LGDPSPILMYPISSSEVRCLV 342
Cdd:pfam01494 146 YTVRAKYLVGCDGGRSPVRKTLgieFEGFEGVPFGSLDVLFDAPDLSDPVERAFVhyliYAPHSRGFMVGPWRSAGRERY 225

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   343 DVPGQKLPPIANGEmAKYLKTRVAPQVPTKVREAFITaVEKGNIRTMPNRSMPADPIPTPGALLLGDAFNmRHPLTGG-G 421
Cdd:pfam01494 226 YVQVPWDEEVEERP-EEFTDEELKQRLRSIVGIDLAL-VEILWKSIWGVASRVATRYRKGRVFLAGDAAH-IHPPTGGqG 302

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 75220022   422 MTVALADIVVL-RDLLRPIRNlndkEALSKYIESFYTLRKPVA 463
Cdd:pfam01494 303 LNTAIQDAFNLaWKLAAVLRG----QAGESLLDTYSAERLPVA 341
GG-red-SF TIGR02032
geranylgeranyl reductase family; This model represents a subfamily which includes ...
 124-426 1.89e-11

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: 65.03  E-value: 1.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLqPGGYLKLIELGLEDCVKKIDAQRVLGyvlfkdGKHT 203
Cdd:TIGR02032   2 DVVVVGAGPAGASAAYRLADKGLRVLLLEKKSFPRYKPCGGAL-SPRALEELDLPGELIVNLVRGARFFS------PNGD 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   204 KLAYPLETFDSDVAGRSfHNGRFVQRMREKAltLSNVRLEQgTVTSLLEEHGTIkGVRYRTKEGnEFRsfAPLTIVCDGC 283
Cdd:TIGR02032  75 SVEIPIETELAYVIDRD-AFDEQLAERAQEA--GAELRLGT-RVLDVEIHDDRV-VVIVRGSEG-TVT--AKIVIGADGS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   284 FSNLRRSLCKPKVDVPSTFVglVLENCELPfanhghVVLGDPSPILMY--------------PISSSEVRCLVDVPGQKL 349
Cdd:TIGR02032 147 RSIVAKKLGLKKEPREYGVA--ARAEVEMP------DEEVDEDFVEVYidrgivpggygwvfPKGDGTANVGVGSRSAEE 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75220022   350 PPIANGEMAKYLKTRVAPQ--VPTKVREAFItavekgnirtmPNRsMPADPIPTPGALLLGDAFNMRHPLTGGGMTVAL 426
Cdd:TIGR02032 219 GEDPKKYLKDFLARRPELKdaETVEVCGALI-----------PIG-RPDEKLVRGNVLLVGDAAGHVNPLTGEGIYYAM 285
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
123-286 2.46e-08

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 56.07  E-value: 2.46e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERD----------------------------FSEQ-----DRIVGEL---- 165
Cdd:COG0665   3 ADVVVIGGGIAGLSTAYHLARRGLDVTVLERGrpgsgasgrnagqlrpglaaladralvrLAREaldlwRELAAELgidc 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 166 -LQPGGYLKLI--ELGLEDCVKKIDAQRVLGY-VLFKDGKHTKLAYPLETFDSDVAG------RSFHNGRFVQRMREKAL 235
Cdd:COG0665  83 dFRRTGVLYLArtEAELAALRAEAEALRALGLpVELLDAAELREREPGLGSPDYAGGlydpddGHVDPAKLVRALARAAR 162

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 75220022 236 TLsNVRLEQGT-VTSLLEEHGTIKGVryRTKEGnEFRsfAPLTIVCDGCFSN 286
Cdd:COG0665 163 AA-GVRIREGTpVTGLEREGGRVTGV--RTERG-TVR--ADAVVLAAGAWSA 208
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
 123-293 1.05e-06

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 51.37  E-value: 1.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERDF-----------------SEQDRIVGE---------LLQPGGYL---K 173
Cdd:COG1053   4 YDVVVVGSGGAGLRAALEAAEAGLKVLVLEKVPprgghtaaaqgginaagTNVQKAAGEdspeehfydTVKGGDGLadqD 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 174 LIELGLEDCVKKIDAQRVLGyVLFKDGKHTKLAypleTFDSDVAGRSFHNGR-----FVQRMREKALTLsNVRLEQGT-V 247
Cdd:COG1053  84 LVEALAEEAPEAIDWLEAQG-VPFSRTPDGRLP----QFGGHSVGRTCYAGDgtghaLLATLYQAALRL-GVEIFTETeV 157

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 75220022 248 TSLLEEHGTIKGVRYRTKEGNEFRSFAPLTIVCDGCFSNLRRSLCK 293
Cdd:COG1053 158 LDLIVDDGRVVGVVARDRTGEIVRIRAKAVVLATGGFGRNYEMRAE 203
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
 124-175 2.09e-06

Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General function prediction only]; Choline dehydrogenase or related flavoprotein is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 50.60  E-value: 2.09e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75220022 124 DVIIVGAGVAGSALAHTLGK-EGRRVHVIE---RDFSEQDRIvgellqPGGYLKLI 175
Cdd:COG2303   6 DYVIVGAGSAGCVLANRLSEdAGLRVLLLEaggRDDDPLIRM------PAGYAKLL 55
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 124-155 6.91e-06

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 48.55  E-value: 6.91e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 75220022   124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDF 155
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGLSVTLLERGD 32
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
127-153 7.28e-06

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 43.67  E-value: 7.28e-06
                          10        20
                  ....*....|....*....|....*..
gi 75220022   127 IVGAGVAGSALAHTLGKEGRRVHVIER 153
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEK 27
mhpA PRK06183
bifunctional 3-(3-hydroxy-phenyl)propionate/3-hydroxycinnamic acid hydroxylase;
123-297 1.58e-05

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


Pssm-ID: 235727 [Multi-domain]  Cd Length: 500  Bit Score: 47.59  E-value: 1.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERdfseQDRIVGellQPGGylklieLGLEDcvkkiDAQRVLGYVLFKD--G 200
Cdd:PRK06183  11 TDVVIVGAGPVGLTLANLLGQYGVRVLVLER----WPTLYD---LPRA------VGIDD-----EALRVLQAIGLADevL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  201 KHTKLAYPLETFDSDvaGRSF---------HNG-----RFVQRMREKAL-----TLSNVRLEQG-TVTSLLEEHGtikGV 260
Cdd:PRK06183  73 PHTTPNHGMRFLDAK--GRCLaeiarpstgEFGwprrnAFHQPLLEAVLraglaRFPHVRVRFGhEVTALTQDDD---GV 147

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 75220022  261 R--YRTKEGNEFRSFAPLTIVCDGCFSNLRRSLCKPKVD 297
Cdd:PRK06183 148 TvtLTDADGQRETVRARYVVGCDGANSFVRRTLGVPFED 186
Lycopene_cycl pfam05834
Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. ...
 124-437 2.51e-05

Lycopene cyclase protein; This family consists of lycopene beta and epsilon cyclase proteins. Carotenoids with cyclic end groups are essential components of the photosynthetic membranes in all plants, algae, and cyanobacteria. These lipid-soluble compounds protect against photo-oxidation, harvest light for photosynthesis, and dissipate excess light energy absorbed by the antenna pigments. The cyclization of lycopene (psi, psi-carotene) is a key branch point in the pathway of carotenoid biosynthesis. Two types of cyclic end groups are found in higher plant carotenoids: the beta and epsilon rings. Carotenoids with two beta rings are ubiquitous, and those with one beta and one epsilon ring are common; however, carotenoids with two epsilon rings are rare.


Pssm-ID: 310433 [Multi-domain]  Cd Length: 380  Bit Score: 46.64  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEqdrivgELLQPGGYLKLIEL----GLEDCVkkidAQRVLGYVLFKD 199
Cdd:pfam05834   1 DVVIIGAGPAGLSLAARLAAAKPGLSVVLIEPGP------SLLRPNNYVWSDEFedlgALEDCV----GHSWPGTRVHFD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   200 GKHTKLaypletfdSDVAGRSFHNGRFVQRMREKaLTLSNVRLEQGTVTSLLEEHGtikGVRYRTKEGNEfRSFAPLTIV 279
Cdd:pfam05834  71 DGKPIL--------IGRAYGRVSSKRLEEEMLQR-CVENGVIRLNAKVESVEADPV---GESLVVCEGGR-TIRARLVFD 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   280 CDGCFsnlrrSLCKPKVDVPSTFVGLVLEncelpFANHGHvvlgDPS-PILM--------------Y--PISSS----EV 338
Cdd:pfam05834 138 ARGLG-----SLPPGRTLGYQTFYGVEVE-----VDNPPF----DPDvMVLMdarvpqplkgptflYalPLDPDrllvEE 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   339 RCLVDVPGqkLPPIA-NGEMAKYLKTRvapqvptKVREAFITAVEKGNIRTMPNRSMPADPIPTPGAlllGDAFNMRHPL 417
Cdd:pfam05834 204 TYLSSGPV--LPFDAlKKRLAAYLRAL-------GIRILEVVEEEQGVIPMTLGGDLPNTPQKVLRI---GAAAGMVHPA 271

                         330       340
                  ....*....|....*....|....
gi 75220022   418 TGGGM--TVALADIV--VLRDLLR 437
Cdd:pfam05834 272 TGYSVarSLRLAPKLasAIAAALR 295
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
123-153 4.06e-05

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 46.29  E-value: 4.06e-05
                        10        20        30
                ....*....|....*....|....*....|..
gi 75220022 123 TDVIIVGAGVAGSALAHTLGK-EGRRVHVIER 153
Cdd:COG0579   5 YDVVIIGAGIVGLALARELSRyEDLKVLVLEK 36
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
 124-330 4.89e-05

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 45.74  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDFS------------------EQDRIVGELLQP------GGYL---KLIE 176
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAGLKVAVVEKGQPfggatawssggidalgnpPQGGIDSPELHPtdtlkgLDELadhPYVE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   177 LGLEDCVKKID--AQRVLGYVLFKDGKH------TKLAYPLETFDSDVAGRSFHNG-----RFVQRMREKALTLsnvrLE 243
Cdd:pfam00890  81 AFVEAAPEAVDwlEALGVPFSRTEDGHLdlrplgGLSATWRTPHDAADRRRGLGTGhallaRLLEGLRKAGVDF----QP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022   244 QGTVTSLLEEHGTIKGVRYRT-KEGNEFRSFAPL-TIVCDGCFSNLRRSLCKPKVDVPSTF--------------VGLVL 307
Cdd:pfam00890 157 RTAADDLIVEDGRVTGAVVENrRNGREVRIRAIAaVLLATGGFGRLAELLLPAAGYADTTNppantgdglalalrAGAAL 236

                         250       260
                  ....*....|....*....|....*.
gi 75220022   308 ENC---ELPFANHGHVVLGDPSPILM 330
Cdd:pfam00890 237 TDDlmeFVQFHPTSLVGIRLGSGLLI 262
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
117-262 5.33e-05

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 46.07  E-value: 5.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 117 TEVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIE-RD------FSEQDRIVGELLQPGG---------YLKLI-ELGL 179
Cdd:COG1231   2 SRRARGKDVVIVGAGLAGLAAARELRKAGLDVTVLEaRDrvggrvWTLRFGDDGLYAELGAmrippshtnLLALArELGL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 180 EDCVKKIDAQRVlgyVLFKDGKHtklaYPLETFDSDVAGRSFHNGRFVQRMREKALTLSNV--RLEQGTVTSLLEEHGTI 257
Cdd:COG1231  82 PLEPFPNENGNA---LLYLGGKR----VRAGEIAADLRGVAELLAKLLRALAAALDPWAHPaaELDRESLAEWLRRNGAS 154


                ....*
gi 75220022 258 KGVRY 262
Cdd:COG1231 155 PSARR 159
PRK07494 PRK07494
UbiH/UbiF family hydroxylase;
123-293 6.82e-05

UbiH/UbiF family hydroxylase;


Pssm-ID: 181001 [Multi-domain]  Cd Length: 388  Bit Score: 45.28  E-value: 6.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLkLIELGL-EDCVKKIDAQRVLGYVlfkDGK 201
Cdd:PRK07494   8 TDIAVIGGGPAGLAAAIALARAGASVALVAPEPPYADLRTTALLGPSIRF-LERLGLwARLAPHAAPLQSMRIV---DAT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  202 HTKLAYPLETFDS-----DVAGRSFHNGRFVQRMREKALTLSNV-RLEQGTVTSLLEEhgtiKGVRYRTKEGNEFRsfAP 275
Cdd:PRK07494  84 GRLIRAPEVRFRAaeigeDAFGYNIPNWLLNRALEARVAELPNItRFGDEAESVRPRE----DEVTVTLADGTTLS--AR 157

                        170
                 ....*....|....*...
gi 75220022  276 LTIVCDGcfsnlRRSLCK 293
Cdd:PRK07494 158 LVVGADG-----RNSPVR 170
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 123-178 9.84e-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: 45.21  E-value: 9.84e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERDfseqDRIvgellqpGGYLKLIELG 178
Cdd:COG1232   2 KRVAVIGGGIAGLTAAYRLAKAGHEVTVLEAS----DRV-------GGLIRTVEVD 46
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 117-153 1.13e-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: 44.85  E-value: 1.13e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 75220022 117 TEVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIER 153
Cdd:COG2072   1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGIDFVVLEK 37
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 120-201 1.21e-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: 44.42  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 120 DSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIERD---FSEQDRIVGELLQPggYLKL--IELGLEDCVKKIDAQRVLGy 194
Cdd:COG0446 122 FKGKRAVVIGGGPIGLELAEALRKRGLKVTLVERAprlLGVLDPEMAALLEE--ELREhgVELRLGETVVAIDGDDKVA- 198


                ....*..
gi 75220022 195 VLFKDGK 201
Cdd:COG0446 199 VTLTDGE 205
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 123-154 2.54e-04

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


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 43.46  E-value: 2.54e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 75220022   123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERD 154
Cdd:pfam07992   1 YDVVVIGGGPAGLAAALTLAQLGGKVTLIEDE 32
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 124-154 2.63e-04

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


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 44.07  E-value: 2.63e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 75220022  124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERD 154
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRGWQVTLYEAD 292
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 124-153 6.18e-04

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 42.53  E-value: 6.18e-04
                        10        20        30
                ....*....|....*....|....*....|
gi 75220022 124 DVIIVGAGVAGSALAHTLGKEGRRVHVIER 153
Cdd:COG1233   5 DVVVIGAGIGGLAAAALLARAGYRVTVLEK 34
PLN02576 PLN02576
protoporphyrinogen oxidase
 118-181 6.59e-04

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 42.31  E-value: 6.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  118 EVDSGTDVIIVGAGVAGSALAHTLG-KEGRRVHVIERdfseQDRIVGEL--LQPGGYL----------------KLIELG 178
Cdd:PLN02576   8 AAASSKDVAVVGAGVSGLAAAYALAsKHGVNVLVTEA----RDRVGGNItsVSEDGFIweegpnsfqpsdpeltSAVDSG 83


                 ...
gi 75220022  179 LED 181
Cdd:PLN02576  84 LRD 86
PRK12834 PRK12834
putative FAD-binding dehydrogenase; Reviewed
 123-152 7.39e-04

putative FAD-binding dehydrogenase; Reviewed


Pssm-ID: 183782 [Multi-domain]  Cd Length: 549  Bit Score: 42.58  E-value: 7.39e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIE 152
Cdd:PRK12834   5 ADVIVVGAGLAGLVAAAELADAGKRVLLLD 34
COG3573 COG3573
Predicted oxidoreductase [General function prediction only];
123-154 1.10e-03

Predicted oxidoreductase [General function prediction only];


Pssm-ID: 442794 [Multi-domain]  Cd Length: 551  Bit Score: 41.70  E-value: 1.10e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERD 154
Cdd:COG3573   6 ADVIVVGAGLAGLVAAAELADAGRRVLLLDQE 37
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
115-202 1.42e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 41.28  E-value: 1.42e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022 115 LETEVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIERdfseQDRIVGELL-QPGGYL---KLIELG----LEDCVKKI 186
Cdd:COG1251 135 LRAALAPGKRVVVIGGGLIGLEAAAALRKRGLEVTVVER----APRLLPRQLdEEAGALlqrLLEALGvevrLGTGVTEI 210

                        90
                ....*....|....*..
gi 75220022 187 DAQ-RVLGyVLFKDGKH 202
Cdd:COG1251 211 EGDdRVTG-VRLADGEE 226
PRK10157 PRK10157
putative oxidoreductase FixC; Provisional
 124-313 1.49e-03

putative oxidoreductase FixC; Provisional


Pssm-ID: 182273 [Multi-domain]  Cd Length: 428  Bit Score: 41.43  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVgellqPGG--YLKLIELGLEDCVKKIDAQRVLgyvlfkdgK 201
Cdd:PRK10157   7 DAIIVGAGLAGSVAALVLAREGAQVLVIERGNSAGAKNV-----TGGrlYAHSLEHIIPGFADSAPVERLI--------T 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  202 HTKLAYPLETF----------DSDVAGRSFH--NGRFVQRMREKALTLSNVRLEQGTVTSLLEEHGTIKGVRyrtKEGNE 269
Cdd:PRK10157  74 HEKLAFMTEKSamtmdycngdETSPSQRSYSvlRSKFDAWLMEQAEEAGAQLITGIRVDNLVQRDGKVVGVE---ADGDV 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 75220022  270 FRsfAPLTIVCDGCFSNLRRSLCKPK-VDVPSTFVGlVLENCELP 313
Cdd:PRK10157 151 IE--AKTVILADGVNSILAEKLGMAKrVKPTDVAVG-VKELIELP 192
TrkA COG0569
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ...
 125-154 1.88e-03

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: 40.44  E-value: 1.88e-03
                        10        20        30
                ....*....|....*....|....*....|
gi 75220022 125 VIIVGAGVAGSALAHTLGKEGRRVHVIERD 154
Cdd:COG0569  98 VIIIGAGRVGRSLARELEEEGHDVVVIDKD 127
PRK09126 PRK09126
FAD-dependent hydroxylase;
123-153 2.49e-03

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 40.31  E-value: 2.49e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIER 153
Cdd:PRK09126   4 SDIVVVGAGPAGLSFARSLAGSGLKVTLIER 34
PRK06370 PRK06370
FAD-containing oxidoreductase;
124-155 3.07e-03

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 40.19  E-value: 3.07e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 75220022  124 DVIIVGAGVAGSALAHTLGKEGRRVHVIERDF 155
Cdd:PRK06370   7 DAIVIGAGQAGPPLAARAAGLGMKVALIERGL 38
mannonate_red_SDR_c cd08935
putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes ...
 125-176 3.47e-03

putative D-mannonate oxidoreductase, classical (c) SDR; D-mannonate oxidoreductase catalyzes the NAD-dependent interconversion of D-mannonate and D-fructuronate. This subgroup includes Bacillus subtitils UxuB/YjmF, a putative D-mannonate oxidoreductase; the B. subtilis UxuB gene is part of a putative ten-gene operon (the Yjm operon) involved in hexuronate catabolism. Escherichia coli UxuB does not belong to this subgroup. This subgroup has a canonical active site tetrad and a typical Gly-rich NAD-binding motif. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold (alpha/beta folding pattern with a central beta-sheet), an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Classical SDRs are typically about 250 residues long, while extended SDRs are approximately 350 residues. Sequence identity between different SDR enzymes are typically in the 15-30% range, but the enzymes share the Rossmann fold NAD-binding motif and characteristic NAD-binding and catalytic sequence patterns. These enzymes catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase (15-PGDH) numbering). In addition to the Tyr and Lys, there is often an upstream Ser (Ser-138, 15-PGDH numbering) and/or an Asn (Asn-107, 15-PGDH numbering) contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. Extended SDRs have additional elements in the C-terminal region, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Some atypical SDRs have lost catalytic activity and/or have an unusual NAD(P)-binding motif and missing or unusual active site residues. Reactions catalyzed within the SDR family include isomerization, decarboxylation, epimerization, C=N bond reduction, dehydratase activity, dehalogenation, Enoyl-CoA reduction, and carbonyl-alcohol oxidoreduction.


Pssm-ID: 187640 [Multi-domain]  Cd Length: 271  Bit Score: 39.75  E-value: 3.47e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
gi 75220022 125 VIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGGYLKLIE 176
Cdd:cd08935   9 VITGGTGVLGGAMARALAQAGAKVAALGRNQEKGDKVAKEITALGGRAIALA 60
MnmG COG0445
tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal ...
 228-272 3.69e-03

tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA [Translation, ribosomal structure and biogenesis]; tRNA U34 5-carboxymethylaminomethyl modifying enzyme MnmG/GidA is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 440214 [Multi-domain]  Cd Length: 626  Bit Score: 40.37  E-value: 3.69e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 75220022 228 QRMREKALTLSNVRLEQGTVTSLLEEHGTIKGVryRTKEGNEFRS 272
Cdd:COG0445 106 AAMRETLENQPNLDLIQGEVEDLIVEDGRVTGV--VTADGIEFRA 148
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
123-172 4.88e-03

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 39.33  E-value: 4.88e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERDfseqdrivgellQPGGYL 172
Cdd:COG0492   1 YDVVIIGAGPAGLTAAIYAARAGLKTLVIEGG------------EPGGQL 38
PRK06184 PRK06184
hypothetical protein; Provisional
 123-153 5.33e-03

hypothetical protein; Provisional


Pssm-ID: 235728 [Multi-domain]  Cd Length: 502  Bit Score: 39.58  E-value: 5.33e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIER 153
Cdd:PRK06184   4 TDVLIVGAGPTGLTLAIELARRGVSFRLIEK 34
PRK07233 PRK07233
hypothetical protein; Provisional
 127-154 5.49e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 39.48  E-value: 5.49e-03
                         10        20
                 ....*....|....*....|....*...
gi 75220022  127 IVGAGVAGSALAHTLGKEGRRVHVIERD 154
Cdd:PRK07233   4 IVGGGIAGLAAAYRLAKRGHEVTVFEAD 31
ubiF PRK08020
2-octaprenyl-3-methyl-6-methoxy-1,4-benzoquinol hydroxylase; Reviewed
 118-153 6.47e-03

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


Pssm-ID: 181199 [Multi-domain]  Cd Length: 391  Bit Score: 39.20  E-value: 6.47e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 75220022  118 EVDSGTDVIIVGAGVAGSALAHTLGKEGRRVHVIER 153
Cdd:PRK08020   1 MTNQPTDIAIVGGGMVGAALALGLAQHGFSVAVLEH 36
PRK06475 PRK06475
FAD-binding protein;
126-288 6.61e-03

FAD-binding protein;


Pssm-ID: 180582 [Multi-domain]  Cd Length: 400  Bit Score: 39.04  E-value: 6.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  126 IIVGAGVAGSALAHTLGKEGRRVHVIERdfSEQDRIVGELLQ--PGGYLKLIELGLEDcvkKIDAQRVLGYVLF-KDGKh 202
Cdd:PRK06475   6 LIAGAGVAGLSAALELAARGWAVTIIEK--AQELSEVGAGLQlaPNAMRHLERLGVAD---RLSGTGVTPKALYlMDGR- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  203 tKLAYPLETFDSDVAGRSFHNGRFV-QRMREKALTLSNVRLEQG-------TVTSLLEEHGTIKGVRYRTkEGNEFRSfA 274
Cdd:PRK06475  80 -KARPLLAMQLGDLARKRWHHPYIVcHRADLQSALLDACRNNPGieiklgaEMTSQRQTGNSITATIIRT-NSVETVS-A 156

                        170
                 ....*....|....
gi 75220022  275 PLTIVCDGCFSNLR 288
Cdd:PRK06475 157 AYLIACDGVWSMLR 170
PRK07538 PRK07538
hypothetical protein; Provisional
 123-291 8.14e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 38.72  E-value: 8.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERdfSEQDRI--VGELLQPGGYLKLIELGLEDcvkKIDAQRV----LGYVl 196
Cdd:PRK07538   1 MKVLIAGGGIGGLTLALTLHQRGIEVVVFEA--APELRPlgVGINLLPHAVRELAELGLLD---ALDAIGIrtreLAYF- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75220022  197 fkdGKHTKLAYpletfdSDVAGR---------SFHNGRFVQRMREKALTlsnvRLEQGTV------TSLLEEHGTIKGVR 261
Cdd:PRK07538  75 ---NRHGQRIW------SEPRGLaagydwpqySIHRGELQMLLLDAVRE----RLGPDAVrtghrvVGFEQDADVTVVFL 141

                        170       180       190
                 ....*....|....*....|....*....|
gi 75220022  262 YRTKEGNEFRSFAPLTIVCDGCFSNLRRSL 291
Cdd:PRK07538 142 GDRAGGDLVSVRGDVLIGADGIHSAVRAQL 171
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 123-154 8.35e-03

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


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 38.91  E-value: 8.35e-03
                        10        20        30
                ....*....|....*....|....*....|..
gi 75220022 123 TDVIIVGAGVAGSALAHTLGKEGRRVHVIERD 154
Cdd:COG1249   4 YDLVVIGAGPGGYVAAIRAAQLGLKVALVEKG 35
PRK08277 PRK08277
D-mannonate oxidoreductase; Provisional
 125-170 8.62e-03

D-mannonate oxidoreductase; Provisional


Pssm-ID: 236216 [Multi-domain]  Cd Length: 278  Bit Score: 38.34  E-value: 8.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 75220022  125 VIIVGAGVAGSALAHTLGKEGRRVHVIERDFSEQDRIVGELLQPGG 170
Cdd:PRK08277  14 VITGGGGVLGGAMAKELARAGAKVAILDRNQEKAEAVVAEIKAAGG 59
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 125-166 8.91e-03

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 38.99  E-value: 8.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 75220022  125 VIIVGAGVAGSALAHTLGKEGRRVHVIERDfseqDRIvGELL 166
Cdd:PRK12810 146 VAVVGSGPAGLAAADQLARAGHKVTVFERA----DRI-GGLL 182
 
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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