NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2009424401|ref|XP_040099542|]
View 

L-gulonolactone oxidase isoform X1 [Oryx dammah]

Protein Classification

FAD-binding oxidoreductase( domain architecture ID 1002049)

FAD-binding oxidoreductase catalyzes the oxidation or reduction of a specific substrate using flavin adenine dinucleotide (FAD) as a cofactor

CATH:  3.40.462.40
EC:  1.-.-.-
Gene Ontology:  GO:0071949|GO:0016491
SCOP:  4002178

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
FAD_lactone_ox super family cl36950
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 7-474 0e+00

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


The actual alignment was detected with superfamily member TIGR01678:

Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 666.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401   7 GVKFQNWARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVT 86
Cdd:TIGR01678   1 GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  87 MEAGILLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLTANGTILECSESSNAEVFQA 166
Cdd:TIGR01678  81 VEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 167 ARVHLGCLGVILTVTLQCVPQFHLQETTFPSTLNELwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrvLD 246
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKEL------------------------------------------LD 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 247 NLDSHLKKSEYFRFLWFPHSENVSVIYQDHTNKPPSSSANWFWDYAIGFYLLEFLLWISTFLPGLVGWINRFFFWLLFNG 326
Cdd:TIGR01678 199 NWDSHWKSSEFFRVLWFPYTENVVIWRQNKTNKAPSSPSNSFWDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGE 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 327 K----KENCNLSHKIFNYECRFKQHVQDWAIPREKTKAALLELKATLEANPK---VVAHYPVEVRFTRA---DDILLSPC 396
Cdd:TIGR01678 279 KsstkKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLELKAMLEAHAKnkeVYAHYPVEVRFTRGtlpDECLLSPC 358

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2009424401 397 FQRDSCYMNIIMYRPYGKDVPRLDYWLAYENIMKKVGGRPHWAKAHN-CTRKDFEKMYPAFQKFCAIREKLDPTGMFLN 474
Cdd:TIGR01678 359 FQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHWAKAHNvCKQKDFEEMYPTLHKFCDIRKKLDPTGVFLN 437
 
Name Accession Description Interval E-value
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 7-474 0e+00

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 666.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401   7 GVKFQNWARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVT 86
Cdd:TIGR01678   1 GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  87 MEAGILLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLTANGTILECSESSNAEVFQA 166
Cdd:TIGR01678  81 VEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 167 ARVHLGCLGVILTVTLQCVPQFHLQETTFPSTLNELwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrvLD 246
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKEL------------------------------------------LD 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 247 NLDSHLKKSEYFRFLWFPHSENVSVIYQDHTNKPPSSSANWFWDYAIGFYLLEFLLWISTFLPGLVGWINRFFFWLLFNG 326
Cdd:TIGR01678 199 NWDSHWKSSEFFRVLWFPYTENVVIWRQNKTNKAPSSPSNSFWDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGE 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 327 K----KENCNLSHKIFNYECRFKQHVQDWAIPREKTKAALLELKATLEANPK---VVAHYPVEVRFTRA---DDILLSPC 396
Cdd:TIGR01678 279 KsstkKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLELKAMLEAHAKnkeVYAHYPVEVRFTRGtlpDECLLSPC 358

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2009424401 397 FQRDSCYMNIIMYRPYGKDVPRLDYWLAYENIMKKVGGRPHWAKAHN-CTRKDFEKMYPAFQKFCAIREKLDPTGMFLN 474
Cdd:TIGR01678 359 FQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHWAKAHNvCKQKDFEEMYPTLHKFCDIRKKLDPTGVFLN 437
ALO pfam04030
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ...
 180-480 4.96e-113

D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.


Pssm-ID: 427663 [Multi-domain]  Cd Length: 258  Bit Score: 333.85  E-value: 4.96e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 180 VTLQCVPQFHLQETTFPSTLNElwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrVLDNLDSHLKKSEYFR 259
Cdd:pfam04030   1 VTLRVVPAFTLTSTQEVISFDT------------------------------------------LLENWDELLTSSEHFR 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 260 FLWFPHSENVSVIYQDHTNKPPSSSA-NWFWDYAIGFYLLEFLLWISTFLPGLVGWINRFFFWLLFNGKkENCNLSHKIF 338
Cdd:pfam04030  39 FWWFPYTDKAVVWRANKTDEPEQSRPrKSLYGEWLGNGVYEALLWLSRIFPSLTPWVERFVFKLQYGGD-EAVDDSYKVF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 339 NYECRFKQHVQDWAIPREKTKAALLELKATLEANPkVVAHYPVEVRFTRADDILLSPCFQRDSCYMNIIMYRPYGKDVPR 418
Cdd:pfam04030 118 NMDCLVSQFVMEWAIPLENGPEALRELRAWIRRAA-LRVHFPIEVRCSAADDIYLSTAYGRDTCYINAHMYRPYGRNVPY 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2009424401 419 LDYWLAYENIMKKVGGRPHWAKAHNCTRKDFEKMYPAFQKFCAIREKLDPTGMFLNTYLEKV 480
Cdd:pfam04030 197 HKYFRAFEDIMKKYGGRPHWAKNHTLTAEDLEEWYPDWDRFLQVRKKLDPEGVFLNEYLRRV 258
PLN02465 PLN02465
L-galactono-1,4-lactone dehydrogenase
 12-481 4.89e-59

L-galactono-1,4-lactone dehydrogenase


Pssm-ID: 215258 [Multi-domain]  Cd Length: 573  Bit Score: 203.93  E-value: 4.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  12 NWARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVTMEAGI 91
Cdd:PLN02465   88 NWSGTHEVQTRRYHQPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREGMVNLALMDKVLEVDKEKKRVTVQAGA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  92 LLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLT-ANGTIlECSESSNAEVFQAARVH 170
Cdd:PLN02465  168 RVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIPPIDEQVVSMKLVTpAKGTI-ELSKEDDPELFRLARCG 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 171 LGCLGVILTVTLQCVPQFHLQETTFPSTLNElwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrVLDNLDS 250
Cdd:PLN02465  247 LGGLGVVAEVTLQCVPAHRLVEHTFVSNRKE------------------------------------------IKKNHKK 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 251 HLKKSEYFRFLWFPHSENVSVIYQDHTNKPP-----------------------------SSSANWFWDYAIGF-YLLEF 300
Cdd:PLN02465  285 WLSENKHIRYMWIPYTDTVVVVTCNPLSKWKeppkikpkysedervqplrdlykesagtkSSENPEPDIQEMGFgELRDK 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 301 LLWISTFLPGLVGWINRF--FFWLLFNGKKenCNLSHKIFNYECRFKQHVQDWAIP-------REKTKAALLELKATLEA 371
Cdd:PLN02465  365 LLALDPLDPDHVKRVNAAeaEFWRRSEGYR--VGWSDEILGFDCGGQQWVSEVCFPagtlakpSMKDLEFMEELLALIEK 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 372 NpKVVAHYPVEVRFTRADDILLSPCFQ----RDSCYMNIIMYRPYGKDVPRLD--------YWLAYENIMKKVGGRPHWA 439
Cdd:PLN02465  443 E-GIPAPAPIEQRWTASSSSPMSPASSpspdDLHSWVGIIMYLPTEDERQRKEiteeffhyRKKTQRNLWDKYSAYEHWA 521

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2009424401 440 K--------AHNCTRKDFEKMYPAfQKFCAIREKLDPTGMFLNTYLEKVF 481
Cdd:PLN02465  522 KievpkdkeELEALRERLRKRFPV-DAFNKARKELDPKGILSNNLLEKLF 570
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
13-187 3.18e-30

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 122.31  E-value: 3.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  13 WARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSD--IACTDGFMIHMGKMNRILKVDTEKKQVTMEAG 90
Cdd:COG0277    32 GNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGgaVPLDGGVVLDLSRMNRILEVDPEDRTATVEAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  91 ILLADLNHQLDKHGLAL-SNLGAVSDVTAGGVI---GSGTHntGIKHGILATQVVALTLLTANGTILECSE-----SSNA 161
Cdd:COG0277   112 VTLADLNAALAPHGLFFpPDPSSQGTATIGGNIatnAGGPR--SLKYGLTRDNVLGLEVVLADGEVVRTGGrvpknVTGY 189

                         170       180
                  ....*....|....*....|....*.
gi 2009424401 162 EVFQAARVHLGCLGVILTVTLQCVPQ 187
Cdd:COG0277   190 DLFWLLVGSEGTLGVITEATLRLHPL 215
 
Name Accession Description Interval E-value
FAD_lactone_ox TIGR01678
sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 ...
 7-474 0e+00

sugar 1,4-lactone oxidases; This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.


Pssm-ID: 273751 [Multi-domain]  Cd Length: 438  Bit Score: 666.22  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401   7 GVKFQNWARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVT 86
Cdd:TIGR01678   1 GVQFQNWAKTYSASPEVYYQPTSVEEVREVLALAREQKKKVKVVGGGHSPSDIACTDGFLIHLDKMNKVLQFDKEKKQIT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  87 MEAGILLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLTANGTILECSESSNAEVFQA 166
Cdd:TIGR01678  81 VEAGIRLYQLHEQLDEHGYSMSNLGSISEVSVAGIISTGTHGSSIKHGILATQVVALTIMTADGEVLECSEERNADVFQA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 167 ARVHLGCLGVILTVTLQCVPQFHLQETTFPSTLNELwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrvLD 246
Cdd:TIGR01678 161 ARVSLGCLGIIVTVTIQVVPQFHLQETSFVSTLKEL------------------------------------------LD 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 247 NLDSHLKKSEYFRFLWFPHSENVSVIYQDHTNKPPSSSANWFWDYAIGFYLLEFLLWISTFLPGLVGWINRFFFWLLFNG 326
Cdd:TIGR01678 199 NWDSHWKSSEFFRVLWFPYTENVVIWRQNKTNKAPSSPSNSFWDYKLGFFLYEFLLWTSKYLPCLTPWIERFFFWMLYGE 278

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 327 K----KENCNLSHKIFNYECRFKQHVQDWAIPREKTKAALLELKATLEANPK---VVAHYPVEVRFTRA---DDILLSPC 396
Cdd:TIGR01678 279 KsstkKESSNLSHKIFTMECRFSQHVQEWGIPREKTKEALLELKAMLEAHAKnkeVYAHYPVEVRFTRGtlpDECLLSPC 358

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2009424401 397 FQRDSCYMNIIMYRPYGKDVPRLDYWLAYENIMKKVGGRPHWAKAHN-CTRKDFEKMYPAFQKFCAIREKLDPTGMFLN 474
Cdd:TIGR01678 359 FQVDTCYINAIMYRPFGKDVPRLDYFLAYETIMKKFGGKPHWAKAHNvCKQKDFEEMYPTLHKFCDIRKKLDPTGVFLN 437
ALO pfam04030
D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC: ...
 180-480 4.96e-113

D-arabinono-1,4-lactone oxidase; This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.


Pssm-ID: 427663 [Multi-domain]  Cd Length: 258  Bit Score: 333.85  E-value: 4.96e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 180 VTLQCVPQFHLQETTFPSTLNElwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrVLDNLDSHLKKSEYFR 259
Cdd:pfam04030   1 VTLRVVPAFTLTSTQEVISFDT------------------------------------------LLENWDELLTSSEHFR 38

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 260 FLWFPHSENVSVIYQDHTNKPPSSSA-NWFWDYAIGFYLLEFLLWISTFLPGLVGWINRFFFWLLFNGKkENCNLSHKIF 338
Cdd:pfam04030  39 FWWFPYTDKAVVWRANKTDEPEQSRPrKSLYGEWLGNGVYEALLWLSRIFPSLTPWVERFVFKLQYGGD-EAVDDSYKVF 117

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 339 NYECRFKQHVQDWAIPREKTKAALLELKATLEANPkVVAHYPVEVRFTRADDILLSPCFQRDSCYMNIIMYRPYGKDVPR 418
Cdd:pfam04030 118 NMDCLVSQFVMEWAIPLENGPEALRELRAWIRRAA-LRVHFPIEVRCSAADDIYLSTAYGRDTCYINAHMYRPYGRNVPY 196

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2009424401 419 LDYWLAYENIMKKVGGRPHWAKAHNCTRKDFEKMYPAFQKFCAIREKLDPTGMFLNTYLEKV 480
Cdd:pfam04030 197 HKYFRAFEDIMKKYGGRPHWAKNHTLTAEDLEEWYPDWDRFLQVRKKLDPEGVFLNEYLRRV 258
bact_FAD_ox TIGR01679
FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with ...
 10-481 3.97e-79

FAD-linked oxidoreductase; This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae.


Pssm-ID: 130740 [Multi-domain]  Cd Length: 419  Bit Score: 252.50  E-value: 3.97e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  10 FQNWARTYGCCPEMYFQPTSVEEVKEVLALARqqnKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVTMEA 89
Cdd:TIGR01679   1 WSNWSGEQVAAPSAIVRPTDEGELADVIAQAA---KPVRAVGSGHSFTDLACTDGTMISLTGLQGVVDVDQPTGLATVEA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  90 GILLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLTANGTILECSESSNAEVFQAARV 169
Cdd:TIGR01679  78 GTRLGALGPQLAQRGLGLENQGDIDPQSIGGALGTATHGTGVRFQALHARIVSLRLVTAGGKVLDLSEGDDQDMYLAARV 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 170 HLGCLGVILTVTLQCVPQFHLQEttfpstlnelwllfrpelhgsppgpssvsiitpmdqpslpRLWpqTRTAQRVLDNLD 249
Cdd:TIGR01679 158 SLGALGVISQVTLQTVALFRLRR----------------------------------------RDW--RRPLAQTLERLD 195

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 250 SHLKKSEYFRFLWFPHSENVSVIYQDHTNKPPSSsanWFWDYAIGFY-LLEFLLWISTFLPGLVGWINRFffwLLFNGKK 328
Cdd:TIGR01679 196 EFVDGHRHFEFYVFPFAGKALTITMDRSDEQPKP---RQRDVDENFLgGLRLLRQTLRRFPSLRPRLNRL---MTNMMSS 269

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 329 ENC-NLSHKIFNYECRFKQHVQDWAIPREKTKAALLELKATLEAN-PKVvaHYPVEVRFTRADDILLSPCFQRDSCYMNI 406
Cdd:TIGR01679 270 ETVvDRAYKVFATQRKVRFNEMEYHLPRENGRKALQEVIDLVERRsPPV--MFPIEVRFSAPDDSWLSPFYGRPTCSIAV 347

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2009424401 407 IMYrpYGKDVprLDYWLAYENIMKKVGGRPHWAKAHNCTRKDFEKMYPAFQKFCAIREKLDPTGMFLNTYLEKVF 481
Cdd:TIGR01679 348 HQY--AGMDF--ESYFRAVEPIFRRYAGRPHWGKRHYLTAATLRERYPRWDDFAAVRDDLDPDRRFLNPYTRGLF 418
PLN02465 PLN02465
L-galactono-1,4-lactone dehydrogenase
 12-481 4.89e-59

L-galactono-1,4-lactone dehydrogenase


Pssm-ID: 215258 [Multi-domain]  Cd Length: 573  Bit Score: 203.93  E-value: 4.89e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  12 NWARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVTMEAGI 91
Cdd:PLN02465   88 NWSGTHEVQTRRYHQPESLEELEDIVKEAHEKGRRIRPVGSGLSPNGLAFSREGMVNLALMDKVLEVDKEKKRVTVQAGA 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  92 LLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLT-ANGTIlECSESSNAEVFQAARVH 170
Cdd:PLN02465  168 RVQQVVEALRPHGLTLQNYASIREQQIGGFIQVGAHGTGARIPPIDEQVVSMKLVTpAKGTI-ELSKEDDPELFRLARCG 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 171 LGCLGVILTVTLQCVPQFHLQETTFPSTLNElwllfrpelhgsppgpssvsiitpmdqpslprlwpqtrtaqrVLDNLDS 250
Cdd:PLN02465  247 LGGLGVVAEVTLQCVPAHRLVEHTFVSNRKE------------------------------------------IKKNHKK 284

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 251 HLKKSEYFRFLWFPHSENVSVIYQDHTNKPP-----------------------------SSSANWFWDYAIGF-YLLEF 300
Cdd:PLN02465  285 WLSENKHIRYMWIPYTDTVVVVTCNPLSKWKeppkikpkysedervqplrdlykesagtkSSENPEPDIQEMGFgELRDK 364

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 301 LLWISTFLPGLVGWINRF--FFWLLFNGKKenCNLSHKIFNYECRFKQHVQDWAIP-------REKTKAALLELKATLEA 371
Cdd:PLN02465  365 LLALDPLDPDHVKRVNAAeaEFWRRSEGYR--VGWSDEILGFDCGGQQWVSEVCFPagtlakpSMKDLEFMEELLALIEK 442

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 372 NpKVVAHYPVEVRFTRADDILLSPCFQ----RDSCYMNIIMYRPYGKDVPRLD--------YWLAYENIMKKVGGRPHWA 439
Cdd:PLN02465  443 E-GIPAPAPIEQRWTASSSSPMSPASSpspdDLHSWVGIIMYLPTEDERQRKEiteeffhyRKKTQRNLWDKYSAYEHWA 521

                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|
gi 2009424401 440 K--------AHNCTRKDFEKMYPAfQKFCAIREKLDPTGMFLNTYLEKVF 481
Cdd:PLN02465  522 KievpkdkeELEALRERLRKRFPV-DAFNKARKELDPKGILSNNLLEKLF 570
GLDHase TIGR01676
galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase ...
 12-481 1.18e-40

galactonolactone dehydrogenase; This model represents L-Galactono-gamma-lactone dehydrogenase (EC 1.3.2.3). This enzyme catalyzes the final step in ascorbic acid biosynthesis in higher plants. This protein is homologous to ascorbic acid biosynthesis enzymes of other species: L-gulono-gamma-lactone oxidase in rat and L-galactono-gamma-lactone oxidase in yeast. All three covalently bind the cofactor FAD.


Pssm-ID: 130737 [Multi-domain]  Cd Length: 541  Bit Score: 153.29  E-value: 1.18e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  12 NWARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVTMEAGI 91
Cdd:TIGR01676  53 NWSGTHEVLTRTFHQPEAIEELEGIVKQANEKKARIRPVGSGLSPNGIGLSRAGMVNLALMDKVLEVDEEKKRVRVQAGI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  92 LLADLNHQLDKHGLALSNLGAVSDVTAGGVIGSGTHNTGIKHGILATQVVALTLLT-ANGTIlECSESSNAEVFQAARVH 170
Cdd:TIGR01676 133 RVQQLVDAIKEYGITLQNFASIREQQIGGIIQVGAHGTGAKLPPIDEQVIAMKLVTpAKGTI-EISKDKDPELFFLARCG 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 171 LGCLGVILTVTLQCVPQFHLQETTFPSTLNELWLLFRPELHGSP-------PGPSSVSIIT--PMDQPSLPRLWPQTRTA 241
Cdd:TIGR01676 212 LGGLGVVAEVTLQCVERQELVEHTFISNMKDIKKNHKKFLADNKhvkylhiPYTDAIVVVTcnPISKSRGPPKFKPKYTS 291

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 242 QRVLdnldshlkksEYFRFLWFPHSENVSVIYQDHTNKPPSSSANWFWDyaigfyLLEFLLWISTFLPGLVGWINR--FF 319
Cdd:TIGR01676 292 EEAI----------QHVRDLYRESLKKYRGQVADSASEEPDIDEFSFTE------LRDKLLALDPLNKEHVIEINKaeAE 355

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 320 FWLLFNGKKenCNLSHKIFNYECRFKQHVQD-------WAIPREKTKAALLELKATLEANpKVVAHYPVEVRFTRADDIL 392
Cdd:TIGR01676 356 FWRKSEGYK--VGWSDEILGFDCGGHQWVSEtcfpagtLAKPNMKDIEYIEELKQLIEKE-NIPAPAPIEQRWTACSKSP 432

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 393 LSPCFQRDS----CYMNIIMYRPYGKDVPR---LDYWLAYENIMK-----KVGGRPHWAKAHNCTRKD--------FEKM 452
Cdd:TIGR01676 433 MSPASSSADddifSWVGIIMYLPTMDARQRkeiTEEFFHYRHLTQallwdHFSAFEHWAKIEVPKDKDelaalqarLKKK 512

                         490       500
                  ....*....|....*....|....*....
gi 2009424401 453 YPAfQKFCAIREKLDPTGMFLNTYLEKVF 481
Cdd:TIGR01676 513 FPV-DASNKARKALDPNKILSNNKLEKLF 540
FAD_binding_4 pfam01565
FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most ...
 21-156 1.23e-39

FAD binding domain; This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidizes the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan.


Pssm-ID: 426326 [Multi-domain]  Cd Length: 139  Bit Score: 139.64  E-value: 1.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  21 PEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSDIAC-TDGFMIHMGKMNRILKVDTEKKQVTMEAGILLADLNHQ 99
Cdd:pfam01565   1 PAAVVLPESEEEVAAIVRLANENGLPVLPRGGGSSLLGGAVqTGGIVLDLSRLNGILEIDPEDGTATVEAGVTLGDLVRA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2009424401 100 LDKHGLALS-NLGAVSDVTAGGVIGSGTHNTG-IKHGILATQVVALTLLTANGTILECS 156
Cdd:pfam01565  81 LAAKGLLLGlDPGSGIPGTVGGAIATNAGGYGsEKYGLTRDNVLGLEVVLADGEVVRLG 139
GlcD COG0277
FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];
13-187 3.18e-30

FAD/FMN-containing lactate dehydrogenase/glycolate oxidase [Energy production and conversion];


Pssm-ID: 440046 [Multi-domain]  Cd Length: 462  Bit Score: 122.31  E-value: 3.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  13 WARTYGCCPEMYFQPTSVEEVKEVLALARQQNKRVKVVGGGHSPSD--IACTDGFMIHMGKMNRILKVDTEKKQVTMEAG 90
Cdd:COG0277    32 GNSLYRGRPDAVVRPRSTEDVAAVVRLAAEHGVPVVPRGGGTGLAGgaVPLDGGVVLDLSRMNRILEVDPEDRTATVEAG 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  91 ILLADLNHQLDKHGLAL-SNLGAVSDVTAGGVI---GSGTHntGIKHGILATQVVALTLLTANGTILECSE-----SSNA 161
Cdd:COG0277   112 VTLADLNAALAPHGLFFpPDPSSQGTATIGGNIatnAGGPR--SLKYGLTRDNVLGLEVVLADGEVVRTGGrvpknVTGY 189

                         170       180
                  ....*....|....*....|....*.
gi 2009424401 162 EVFQAARVHLGCLGVILTVTLQCVPQ 187
Cdd:COG0277   190 DLFWLLVGSEGTLGVITEATLRLHPL 215
pln_FAD_oxido TIGR01677
plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized ...
 27-472 9.62e-29

plant-specific FAD-dependent oxidoreductase; This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.


Pssm-ID: 273750 [Multi-domain]  Cd Length: 557  Bit Score: 119.20  E-value: 9.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  27 PTSVEEVKEVLALARQQNKRVKVVGG-GHSPSDIACTDG----FMIHMGKMNRILKVDTEKKQVTMEAGILLADLNHQLD 101
Cdd:TIGR01677  38 PKTEAELVSVVAAATAAGRKMKVVTRySHSIPKLACPDGsdgaLLISTKRLNHVVAVDATAMTVTVESGMSLRELIVEAE 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 102 KHGLALSNLGAVSDVTAGGVIGSGTHNTGI--KHGILATQVVALTLLTANGT------ILECSESSNAEVFQAARVHLGC 173
Cdd:TIGR01677 118 KAGLALPYAPYWWGLTVGGMMGTGAHGSSLwgKGSAVHDYVVGIRLVVPASAaegfakVRILSEGDTPNEFNAAKVSLGV 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 174 LGVILTVTLQCVPQFHlqettfpstlnelwllfrpelhgsppgpSSVSIitpmdqpslprlwpQTRTAQRVLDNLDSHLK 253
Cdd:TIGR01677 198 LGVISQVTLALQPMFK----------------------------RSVTY--------------TMRDDSDFEDQFVTFGK 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 254 KSEYFRFLWFPHSEnvSVIYQDHTNKPPSSSANWFWDYaIGFYllefllwiSTflPGLVGWINRFFFWLLFNGKKEN--C 331
Cdd:TIGR01677 236 KHEFADITWYPSQG--KAVYRRDDRVPVNASGNGVNDF-LGFR--------ST--LIAAIAGIRALEETFERSRNANgkC 302

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 332 ------------------NLSHKIFN----------------------------------YECRFKQHVQDWAIPREKTK 359
Cdd:TIGR01677 303 vtatitsaalflpgygltNSGGIIFTgypvvgsqgrmqtsgscldspqdglltacawdprYKGLFFFHQTTLSVPVSRFR 382

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 360 AALLELKATLEANPK----VVAHYPVEVRFTRADDILLSPcfQRDSCYMNIIMYRPYGKDVPRL--DYWLAYENI-MKKV 432
Cdd:TIGR01677 383 DFVLDVKRLRDMEPKslcgVELYNGILIRYVKASPAYLGK--EEDAVDFDFTYYRAKDPLTPRLyeDVIEEIEQMaFFKY 460

                         490       500       510       520
                  ....*....|....*....|....*....|....*....|
gi 2009424401 433 GGRPHWAKAHNCTRKDFEKMYPAFQKFCAIREKLDPTGMF 472
Cdd:TIGR01677 461 GALPHWGKNRNLAFDGVIRKYPNADKFLKVKDSYDPKGLF 500
MurB COG0812
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; ...
 24-183 6.30e-09

UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylenolpyruvoylglucosamine reductase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440574 [Multi-domain]  Cd Length: 279  Bit Score: 56.95  E-value: 6.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  24 YFQPTSVEEVKEVLALARQQNKRVKVVGGGhspSDIACTD----GFMIHMGKMNRIlKVDtEKKQVTMEAGILLADLNHQ 99
Cdd:COG0812    18 LVEPASEEELAALLRAAREAGLPVLVLGGG---SNLLVRDdgfdGLVIRLGRLKGI-EVD-DGVLVTAGAGENWHDLVRF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 100 LDKHGLA-LSNLgavsdvtAG--GVIGS------GTHNTGIKHgilatQVVALTLLTANGTILecsESSNAE-------- 162
Cdd:COG0812    93 ALEAGLSgLEFL-------AGipGTVGGapvmnaGAYGGEIKD-----VLESVEVLDRTGEVR---TLSAEEcgfgyrds 157

                         170       180
                  ....*....|....*....|.
gi 2009424401 163 VFQAARvhlgclGVILTVTLQ 183
Cdd:COG0812   158 IFKRER------YIILSVTFR 172
PLN00107 PLN00107
FAD-dependent oxidoreductase; Provisional
 352-481 1.69e-08

FAD-dependent oxidoreductase; Provisional


Pssm-ID: 165679  Cd Length: 257  Bit Score: 55.37  E-value: 1.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401 352 AIPREKTKAALLELKATLEANPKVVA----HYPVEVRFTRAddillSPCFQR---DSCYMNIIMYRpyGKD---VPRL-- 419
Cdd:PLN00107   68 SVPLSGAAAFINDIKALRDIEPDALCglelNYGVLLRYVRA-----SPAHLGkeeDALDFDLTYYR--SKDdpaAPRLhe 140

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2009424401 420 DYWLAYENI-MKKVGGRPHWAKAHNCTRKDFEKMYPAFQKFCAIREKLDPTGMFLNTYLEKVF 481
Cdd:PLN00107  141 DAMEEIEQMaILKYGALPHWGKNRNAAFDGAIAKYKKAGEFLKVKERLDPEGLFSSEWSDKIL 203
murB PRK13905
UDP-N-acetylmuramate dehydrogenase;
24-106 2.09e-07

UDP-N-acetylmuramate dehydrogenase;


Pssm-ID: 237553 [Multi-domain]  Cd Length: 298  Bit Score: 52.42  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  24 YFQPTSVEEVKEVLALARQQNKRVKVVGGGhspSDIACTD----GFMIHMGKMNRILKVDTEkkQVTMEAGILLADLNHQ 99
Cdd:PRK13905   34 LVEPADIEDLQEFLKLLKENNIPVTVLGNG---SNLLVRDggirGVVIRLGKGLNEIEVEGN--RITAGAGAPLIKLARF 108


                  ....*..
gi 2009424401 100 LDKHGLA 106
Cdd:PRK13905  109 AAEAGLS 115
PLN02805 PLN02805
D-lactate dehydrogenase [cytochrome]
 21-187 4.79e-07

D-lactate dehydrogenase [cytochrome]


Pssm-ID: 178402 [Multi-domain]  Cd Length: 555  Bit Score: 52.32  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  21 PEMYFQPTSVEEVKEVLALARQQNKRVKVVGG-----GHSpsdIACTDGFMIHMGKMNRILKVDTEKKQVTMEAGILLAD 95
Cdd:PLN02805  134 PDVVVFPRSEEEVSKIVKSCNKYKVPIVPYGGatsieGHT---LAPHGGVCIDMSLMKSVKALHVEDMDVVVEPGIGWLE 210

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  96 LNHQLDKHGLALSnLGAVSDVTAGGVIGSGTHNT-GIKHGILATQVVALTLLTANGTILECSESS--NAEVFQAARVHL- 171
Cdd:PLN02805  211 LNEYLEPYGLFFP-LDPGPGATIGGMCATRCSGSlAVRYGTMRDNVISLKVVLPNGDVVKTASRArkSAAGYDLTRLVIg 289

                         170       180
                  ....*....|....*....|
gi 2009424401 172 --GCLGVILTVT--LQCVPQ 187
Cdd:PLN02805  290 seGTLGVITEVTlrLQKIPQ 309
PRK11230 PRK11230
glycolate oxidase subunit GlcD; Provisional
 17-187 4.23e-05

glycolate oxidase subunit GlcD; Provisional


Pssm-ID: 183043 [Multi-domain]  Cd Length: 499  Bit Score: 45.92  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  17 YGCCPEMYFQPTSVEEVKEVLALARQQnkRVKVV----GGGHSPSDIACTDGFMIHMGKMNRILKVDTEKKQVTMEAGIL 92
Cdd:PRK11230   52 YRTRPLLVVLPKQMEQVQALLAVCHRL--RVPVVargaGTGLSGGALPLEKGVLLVMARFNRILDINPVGRRARVQPGVR 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  93 LADLNHQLDKHGL----------ALSNLGAVSDvTAGGVigsgtHntGIKHGILATQVVALTLLTANGTILEC-SESSNA 161
Cdd:PRK11230  130 NLAISQAAAPHGLyyapdpssqiACSIGGNVAE-NAGGV-----H--CLKYGLTVHNLLKVEILTLDGEALTLgSDALDS 201

                         170       180
                  ....*....|....*....|....*....
gi 2009424401 162 EVFQAARVHLGC---LGVILTVTLQCVPQ 187
Cdd:PRK11230  202 PGFDLLALFTGSegmLGVVTEVTVKLLPK 230
PLN02441 PLN02441
cytokinin dehydrogenase
 21-177 2.35e-04

cytokinin dehydrogenase


Pssm-ID: 215242 [Multi-domain]  Cd Length: 525  Bit Score: 43.75  E-value: 2.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  21 PEMYFQPTSVEEVKEVL--ALARQQNKRVKVVGGGHSPSDIACT-DGFMIHMGKMNRIL------KVDTEKKQVTMEAGI 91
Cdd:PLN02441   65 PAAVLYPSSVEDIASLVraAYGSSSPLTVAARGHGHSLNGQAQApGGVVVDMRSLRGGVrgppviVVSGDGPYVDVSGGE 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2009424401  92 LLADLNHQLDKHGLAlsnlgAVS--D---VTAGGVIGsgthNTGI-----KHGILATQVVALTLLTANGTILECSESSNA 161
Cdd:PLN02441  145 LWIDVLKATLKHGLA-----PRSwtDylyLTVGGTLS----NAGIsgqafRHGPQISNVLELDVVTGKGEVVTCSPTQNS 215

                         170
                  ....*....|....*.
gi 2009424401 162 EVFQAARVHLGCLGVI 177
Cdd:PLN02441  216 DLFFAVLGGLGQFGII 231
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH