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Conserved domains on  [gi|379987950|dbj|BAL70528|]
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L-pantoyl lactone dehydrogenase [Rhodococcus erythropolis]

Protein Classification

alpha-hydroxy-acid oxidizing protein( domain architecture ID 10800424)

FMN-dependent alpha-hydroxyacid oxidizing protein such as bacterial L-lactate dehydrogenase or eukaryotic 2-hydroxy-acid oxidase

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
actino_HemFlav TIGR03966
heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an ...
 3-387 0e+00

heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an N-terminal heme-binding domain and C-terminal flavodehydrogenase domain, and share homology to yeast flavocytochrome b2, to E. coli L-lactate dehydrogenase [cytochrome], to (S)-mandelate dehydrogenase, etc. This enzyme appears only in the context of the mycofactocin system. Interestingly, it is absent from the four species detected so far with mycofactocin but without an F420 biosynthesis system.


:

Pssm-ID: 274885  Cd Length: 385  Bit Score: 716.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950    3 KNAFFETVAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPT 82
Cdd:TIGR03966   1 TRAWFETVAEAQRRARKRLPRSVYAALIAGTEKGVTLADNVAAFDELGFRPHVAGLPPKRELSTTVMGQEISFPVLISPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   83 GVQAVHPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSF 162
Cdd:TIGR03966  81 GVQAVHPDGEVAVARAAAARGTAMGLSSFASKPVEEVVAANPKTFFQIYWVGSRDDILARLERARAAGAKGLILTLDWSF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  163 SYGRDWGSPSIPEKMDLKAMFQFAPEGIMRPKWLLEFAKTGKIPDLTTPNLAAPGQPAPTFFGAYGEWMQTPLPTWEDIA 242
Cdd:TIGR03966 161 ASRRDWGSPEIPEKIDLRTMLRFAPEVLVRPGWLLRYLRSGRIPDLTVPNLALRGETPPTFFGAYGEWMGTPPPTWEDVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  243 WLREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKA 322
Cdd:TIGR03966 241 WLREQWGGPFMLKGITRPDDARRAVDAGATAISVSNHGGNNLDGTPAAIRALPAIAEAVGDQVEVLLDGGIRRGSDVVKA 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379987950  323 LALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLVIPEGFTR 387
Cdd:TIGR03966 321 LALGARAVMIGRAYLWGLAANGEAGVENVLDILRQGIDSALLGLGKASVHELSREDLVIPEGFTR 385
 
Name Accession Description Interval E-value
actino_HemFlav TIGR03966
heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an ...
 3-387 0e+00

heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an N-terminal heme-binding domain and C-terminal flavodehydrogenase domain, and share homology to yeast flavocytochrome b2, to E. coli L-lactate dehydrogenase [cytochrome], to (S)-mandelate dehydrogenase, etc. This enzyme appears only in the context of the mycofactocin system. Interestingly, it is absent from the four species detected so far with mycofactocin but without an F420 biosynthesis system.


Pssm-ID: 274885  Cd Length: 385  Bit Score: 716.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950    3 KNAFFETVAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPT 82
Cdd:TIGR03966   1 TRAWFETVAEAQRRARKRLPRSVYAALIAGTEKGVTLADNVAAFDELGFRPHVAGLPPKRELSTTVMGQEISFPVLISPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   83 GVQAVHPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSF 162
Cdd:TIGR03966  81 GVQAVHPDGEVAVARAAAARGTAMGLSSFASKPVEEVVAANPKTFFQIYWVGSRDDILARLERARAAGAKGLILTLDWSF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  163 SYGRDWGSPSIPEKMDLKAMFQFAPEGIMRPKWLLEFAKTGKIPDLTTPNLAAPGQPAPTFFGAYGEWMQTPLPTWEDIA 242
Cdd:TIGR03966 161 ASRRDWGSPEIPEKIDLRTMLRFAPEVLVRPGWLLRYLRSGRIPDLTVPNLALRGETPPTFFGAYGEWMGTPPPTWEDVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  243 WLREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKA 322
Cdd:TIGR03966 241 WLREQWGGPFMLKGITRPDDARRAVDAGATAISVSNHGGNNLDGTPAAIRALPAIAEAVGDQVEVLLDGGIRRGSDVVKA 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379987950  323 LALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLVIPEGFTR 387
Cdd:TIGR03966 321 LALGARAVMIGRAYLWGLAANGEAGVENVLDILRQGIDSALLGLGKASVHELSREDLVIPEGFTR 385
FMN_dh pfam01070
FMN-dependent dehydrogenase;
17-380 2.10e-127

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 370.71  E-value: 2.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   17 AKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAagLSD--KREMSTTIMGQDISLPVMISPTGVQA-VHPDGEV 93
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRV--LRDvsNRDLSTTLLGQRLSLPFGIAPVGMQGlAHPDGEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   94 AVARAAAARGTAIGLSSFASKSIEEVAAANPQ-VFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSFSYGRDW---G 169
Cdd:pfam01070  79 ALARAAAAAGIPFVLSTVSSTSLEEVAAAAGGpLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERdlrN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  170 SPSIPEKMDLKAMFQFApegiMRPKWLLEFAKTGKIPDlttpnlaapgqpaptfFGAYGEWMQTPLPTWEDIAWLREQWG 249
Cdd:pfam01070 159 GFTLPPRLTPRNLLDLA----LHPRWALGVLRRGGAGG----------------AAAFVGSQFDPALTWDDLAWLRERWK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  250 GPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALGAKA 329
Cdd:pfam01070 219 GPLVVKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADA 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 379987950  330 VMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLV 380
Cdd:pfam01070 299 VLLGRPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 11-376 1.73e-114

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 335.96  E-value: 1.73e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  11 AEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAagLSD--KREMSTTIMGQDISLPVMISPTGVQA-V 87
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRV--LRDvsKRDTSTTLLGQKLAMPFGIAPTGLQGlA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  88 HPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANP-QVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDwsfsygr 166
Cdd:cd02809   79 HPDGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPgPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVD------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 167 dwgspsipekmdlkamfqfapegimrpkwllefaktgkipdlttpnLAAPGQpaptffgaygewmqtpLPTWEDIAWLRE 246
Cdd:cd02809  152 ----------------------------------------------TPVLGR----------------RLTWDDLAWLRS 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 247 QWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALG 326
Cdd:cd02809  170 QWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALG 249

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 379987950 327 AKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSP 376
Cdd:cd02809  250 ADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 9-381 7.37e-114

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 336.33  E-value: 7.37e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   9 TVAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQA-V 87
Cdd:COG1304    6 SIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGlA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  88 HPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQVF-FQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSFSYGR 166
Cdd:COG1304   86 HPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLwFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGRR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 167 DWG---SPSIPEKMDLKAMFQFApegiMRPKWLLEFAKTGKIPDlttpnlaapgqpapTFFgaygewmqTPLPTWEDIAW 243
Cdd:COG1304  166 ERDlreGFSQPPRLTPRNLLEAA----THPRWALGLASLAAWLD--------------TNF--------DPSLTWDDIAW 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 244 LREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKAL 323
Cdd:COG1304  220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 379987950 324 ALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLVI 381
Cdd:COG1304  300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
PLN02535 PLN02535
glycolate oxidase
 10-356 9.78e-68

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 218.55  E-value: 9.78e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  10 VAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQAV-H 88
Cdd:PLN02535   8 VNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLaH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  89 PDGEVAVARAAAARGTAIGLSSFASKSIEEVAAA-NPQVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDwSFSYGRD 167
Cdd:PLN02535  88 PEGEIATARAAAACNTIMVLSFMASCTVEEVASScNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD-VPRLGRR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 168 wgSPSIPEKMDLKAMFQFapEGIMRPKwllefaktgkipdlTTPNLAAPgqpaptfFGAYGEWMQTPLPTWEDIAWLREQ 247
Cdd:PLN02535 167 --EADIKNKMISPQLKNF--EGLLSTE--------------VVSDKGSG-------LEAFASETFDASLSWKDIEWLRSI 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 248 WGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALGA 327
Cdd:PLN02535 222 TNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGA 301

                        330       340
                 ....*....|....*....|....*....
gi 379987950 328 KAVMLGRAYLWGLSANGQAGVENVLDLMR 356
Cdd:PLN02535 302 QAVLVGRPVIYGLAAKGEDGVRKVIEMLK 330
 
Name Accession Description Interval E-value
actino_HemFlav TIGR03966
heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an ...
 3-387 0e+00

heme/flavin dehydrogenase, mycofactocin system; Members of this protein family possess an N-terminal heme-binding domain and C-terminal flavodehydrogenase domain, and share homology to yeast flavocytochrome b2, to E. coli L-lactate dehydrogenase [cytochrome], to (S)-mandelate dehydrogenase, etc. This enzyme appears only in the context of the mycofactocin system. Interestingly, it is absent from the four species detected so far with mycofactocin but without an F420 biosynthesis system.


Pssm-ID: 274885  Cd Length: 385  Bit Score: 716.16  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950    3 KNAFFETVAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPT 82
Cdd:TIGR03966   1 TRAWFETVAEAQRRARKRLPRSVYAALIAGTEKGVTLADNVAAFDELGFRPHVAGLPPKRELSTTVMGQEISFPVLISPT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   83 GVQAVHPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSF 162
Cdd:TIGR03966  81 GVQAVHPDGEVAVARAAAARGTAMGLSSFASKPVEEVVAANPKTFFQIYWVGSRDDILARLERARAAGAKGLILTLDWSF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  163 SYGRDWGSPSIPEKMDLKAMFQFAPEGIMRPKWLLEFAKTGKIPDLTTPNLAAPGQPAPTFFGAYGEWMQTPLPTWEDIA 242
Cdd:TIGR03966 161 ASRRDWGSPEIPEKIDLRTMLRFAPEVLVRPGWLLRYLRSGRIPDLTVPNLALRGETPPTFFGAYGEWMGTPPPTWEDVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  243 WLREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKA 322
Cdd:TIGR03966 241 WLREQWGGPFMLKGITRPDDARRAVDAGATAISVSNHGGNNLDGTPAAIRALPAIAEAVGDQVEVLLDGGIRRGSDVVKA 320

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 379987950  323 LALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLVIPEGFTR 387
Cdd:TIGR03966 321 LALGARAVMIGRAYLWGLAANGEAGVENVLDILRQGIDSALLGLGKASVHELSREDLVIPEGFTR 385
FMN_dh pfam01070
FMN-dependent dehydrogenase;
17-380 2.10e-127

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 370.71  E-value: 2.10e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   17 AKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAagLSD--KREMSTTIMGQDISLPVMISPTGVQA-VHPDGEV 93
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRV--LRDvsNRDLSTTLLGQRLSLPFGIAPVGMQGlAHPDGEL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   94 AVARAAAARGTAIGLSSFASKSIEEVAAANPQ-VFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSFSYGRDW---G 169
Cdd:pfam01070  79 ALARAAAAAGIPFVLSTVSSTSLEEVAAAAGGpLWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERdlrN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  170 SPSIPEKMDLKAMFQFApegiMRPKWLLEFAKTGKIPDlttpnlaapgqpaptfFGAYGEWMQTPLPTWEDIAWLREQWG 249
Cdd:pfam01070 159 GFTLPPRLTPRNLLDLA----LHPRWALGVLRRGGAGG----------------AAAFVGSQFDPALTWDDLAWLRERWK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  250 GPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALGAKA 329
Cdd:pfam01070 219 GPLVVKGILSPEDAKRAVEAGVDGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIPVLVDGGIRRGTDVLKALALGADA 298

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 379987950  330 VMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLV 380
Cdd:pfam01070 299 VLLGRPFLYGLAAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 11-376 1.73e-114

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 335.96  E-value: 1.73e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  11 AEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAagLSD--KREMSTTIMGQDISLPVMISPTGVQA-V 87
Cdd:cd02809    1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRV--LRDvsKRDTSTTLLGQKLAMPFGIAPTGLQGlA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  88 HPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANP-QVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDwsfsygr 166
Cdd:cd02809   79 HPDGELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPgPRWFQLYVPRDREITEDLLRRAEAAGYKALVLTVD------- 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 167 dwgspsipekmdlkamfqfapegimrpkwllefaktgkipdlttpnLAAPGQpaptffgaygewmqtpLPTWEDIAWLRE 246
Cdd:cd02809  152 ----------------------------------------------TPVLGR----------------RLTWDDLAWLRS 169

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 247 QWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALG 326
Cdd:cd02809  170 QWKGPLILKGILTPEDALRAVDAGADGIVVSNHGGRQLDGAPATIDALPEIVAAVGGRIEVLLDGGIRRGTDVLKALALG 249

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 379987950 327 AKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSP 376
Cdd:cd02809  250 ADAVLIGRPFLYGLAAGGEAGVAHVLEILRDELERAMALLGCASLADLDP 299
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 9-381 7.37e-114

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 336.33  E-value: 7.37e-114
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950   9 TVAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQA-V 87
Cdd:COG1304    6 SIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMGGGGlA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  88 HPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQVF-FQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSFSYGR 166
Cdd:COG1304   86 HPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAPLwFQLYVPKDRGFTDDLLRRAEAAGADALVLTVDTPVLGRR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 167 DWG---SPSIPEKMDLKAMFQFApegiMRPKWLLEFAKTGKIPDlttpnlaapgqpapTFFgaygewmqTPLPTWEDIAW 243
Cdd:COG1304  166 ERDlreGFSQPPRLTPRNLLEAA----THPRWALGLASLAAWLD--------------TNF--------DPSLTWDDIAW 219

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 244 LREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKAL 323
Cdd:COG1304  220 LRERWPGPLIVKGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIRAAVGGRIPVIADGGIRRGLDVAKAL 299

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 379987950 324 ALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLVI 381
Cdd:COG1304  300 ALGADAVGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALLVL 357
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 14-379 2.32e-86

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448 [Multi-domain]  Cd Length: 383  Bit Score: 266.84  E-value: 2.32e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  14 QRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQ-AVHPDGE 92
Cdd:cd03332   25 EALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQeLFHPDAE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  93 VAVARAAAARGTAIGLSSFASKSIEEVAAANPQV--FFQMYWVGSRDVLLQRMERARAAGAKGLIITTD-WSFSygrdWG 169
Cdd:cd03332  105 LATARAAAELGVPYILSTASSSSIEDVAAAAGDAprWFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDtWSLG----WR 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 170 spsiPEKMDLKAMFQFAPEGIMR----PKWLLEFAK-TGKIPDLTTPNLAAPGQPAPTFFGAYgewmqtplPTWEDIAWL 244
Cdd:cd03332  181 ----PRDLDLGYLPFLRGIGIANyfsdPVFRKKLAEpVGEDPEAPPPMEAAVARFVSVFSGPS--------LTWEDLAFL 248

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 245 REQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALA 324
Cdd:cd03332  249 REWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVGDRLTVLFDSGVRTGADIMKALA 328

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 379987950 325 LGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSgLMGL-GHSSITELSPADL 379
Cdd:cd03332  329 LGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDL-TMGLaGIRSIAELTRDAL 383
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 17-376 6.38e-81

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238 [Multi-domain]  Cd Length: 344  Bit Score: 251.75  E-value: 6.38e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  17 AKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAagLSDKRE--MSTTIMGQDISLPVMISPTGV-QAVHPDGEV 93
Cdd:cd02922    7 AKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRV--LRDVEKvdTSTTILGHKVSLPFFISPAALaKLAHPDGEL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  94 AVARAAAARGTAIGLSSFASKSIEEV--AAANPQVFFQMYWVGS-RDVLLQRMERARAAGAKGLIITTDwsfsygrdwgS 170
Cdd:cd02922   85 NLARAAGKHGILQMISTNASCSLEEIvdARPPDQPLFFQLYVNKdRTKTEELLKRAEKLGAKAIFLTVD----------A 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 171 PSIPEK-MDLKAMFQFAPEGIMRPKwllefaktgkipdlttpNLAAPGQPAPTFFGAYGEwmqtPLPTWEDIAWLREQWG 249
Cdd:cd02922  155 PVLGKReRDERLKAEEAVSDGPAGK-----------------KTKAKGGGAGRAMSGFID----PTLTWDDIKWLRKHTK 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 250 GPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGI---AEAVGDQVEVVLDGGIRRGGDVVKALALG 326
Cdd:cd02922  214 LPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGGRQLDTAPAPIEVLLEIrkhCPEVFDKIEVYVDGGVRRGTDVLKALCLG 293

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 379987950 327 AKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSP 376
Cdd:cd02922  294 AKAVGLGRPFLYALSAYGEEGVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 14-376 8.79e-76

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240087  Cd Length: 361  Bit Score: 238.96  E-value: 8.79e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  14 QRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQ-AVHPDGE 92
Cdd:cd04736    4 RSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNgAFWPNGD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  93 VAVARAAAARGTAIGLSSFASKSIEEVA-AANPQVFFQMYWVgSRDVLLQRMERARAAGAKGLIITTDWSFSYGRDWGSP 171
Cdd:cd04736   84 LALARAAAKAGIPFVLSTASNMSIEDVArQADGDLWFQLYVV-HRELAELLVKRALAAGYTTLVLTTDVAVNGYRERDLR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 172 SiPEKMDLKAMFQFAPEGIMRPKWLLEFAKTGkipdltTPNLAAPGQPAPTFFGAYGEWMQTPLPT---WEDIAWLREQW 248
Cdd:cd04736  163 N-GFAIPFRYTPRVLLDGILHPRWLLRFLRNG------MPQLANFASDDAIDVEVQAALMSRQMDAsfnWQDLRWLRDLW 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 249 GGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGdqVEVVLDGGIRRGGDVVKALALGAK 328
Cdd:cd04736  236 PHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIVAATY--KPVLIDSGIRRGSDIVKALALGAN 313

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 379987950 329 AVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSP 376
Cdd:cd04736  314 AVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
PLN02535 PLN02535
glycolate oxidase
 10-356 9.78e-68

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 218.55  E-value: 9.78e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  10 VAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQAV-H 88
Cdd:PLN02535   8 VNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLaH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  89 PDGEVAVARAAAARGTAIGLSSFASKSIEEVAAA-NPQVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDwSFSYGRD 167
Cdd:PLN02535  88 PEGEIATARAAAACNTIMVLSFMASCTVEEVASScNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTAD-VPRLGRR 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 168 wgSPSIPEKMDLKAMFQFapEGIMRPKwllefaktgkipdlTTPNLAAPgqpaptfFGAYGEWMQTPLPTWEDIAWLREQ 247
Cdd:PLN02535 167 --EADIKNKMISPQLKNF--EGLLSTE--------------VVSDKGSG-------LEAFASETFDASLSWKDIEWLRSI 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 248 WGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALGA 327
Cdd:PLN02535 222 TNLPILIKGVLTREDAIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVVQAVGGRVPVLLDGGVRRGTDVFKALALGA 301

                        330       340
                 ....*....|....*....|....*....
gi 379987950 328 KAVMLGRAYLWGLSANGQAGVENVLDLMR 356
Cdd:PLN02535 302 QAVLVGRPVIYGLAAKGEDGVRKVIEMLK 330
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 10-379 3.47e-64

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 208.84  E-value: 3.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  10 VAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQA-VH 88
Cdd:cd04737    8 LYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGlAH 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  89 PDGEVAVARAAAARGTAIGLSSFASKSIEEVAAA---NPQvFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSFSYG 165
Cdd:cd04737   88 ATGEVATARGMAEVGSLFSISTYSNTSLEEIAKAsngGPK-WFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGGN 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 166 RDwgspsipekMDLKAMFQFaPEGImrpkwllefaktgkipdlttPNLAAPGQPAP---TFFGAYGEWMQTPLPtwEDIA 242
Cdd:cd04737  167 RE---------ADIRNKFQF-PFGM--------------------PNLNHFSEGTGkgkGISEIYAAAKQKLSP--ADIE 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 243 WLREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKA 322
Cdd:cd04737  215 FIAKISGLPVIVKGIQSPEDADVAINAGADGIWVSNHGGRQLDGGPASFDSLPEIAEAVNHRVPIIFDSGVRRGEHVFKA 294

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 379987950 323 LALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADL 379
Cdd:cd04737  295 LASGADAVAVGRPVLYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVKRTFL 351
lldD PRK11197
L-lactate dehydrogenase; Provisional
 16-380 9.54e-64

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 208.72  E-value: 9.54e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  16 RAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELgfAPHAAGLSDKREMS--TTIMGQDISLPVMISPTGVQAVHPD-GE 92
Cdd:PRK11197  12 AAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADI--ALRQRVLKDMSDLSleTTLFGEKLSMPVALAPVGLTGMYARrGE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  93 VAVARAAAARGTAIGLSSFASKSIEEVAAA-NPQVFFQMYWVGSRDVLLQRMERARAAGAKGLIITTDWSF--SYGRDWG 169
Cdd:PRK11197  90 VQAARAADAKGIPFTLSTVSVCPIEEVAPAiKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVpgARYRDAH 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 170 SPSIPEKMDLKAMFQfapeGIMRPKWLLEFAKTGKIPDLTTpnlAAPGQPAPTFFGAYGEWMQT---PLPTWEDIAWLRE 246
Cdd:PRK11197 170 SGMSGPNAAMRRYLQ----AVTHPQWAWDVGLNGRPHDLGN---ISAYLGKPTGLEDYIGWLGNnfdPSISWKDLEWIRD 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 247 QWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALALG 326
Cdd:PRK11197 243 FWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALPAIADAVKGDITILADSGIRNGLDVVRMIALG 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 379987950 327 AKAVMLGRAYLWGLSANGQAGVENVLDL----MRMGidsglMGL-GHSSITELSPADLV 380
Cdd:PRK11197 323 ADTVLLGRAFVYALAAAGQAGVANLLDLiekeMRVA-----MTLtGAKSISEITRDSLV 376
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 10-380 8.30e-63

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 205.74  E-value: 8.30e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  10 VAEAQRRAKKRLPKSVYAALVAGSEKGLTVDDNVAAFSELGFAPHAAGLSDKREMSTTIMGQDISLPVMISPTGVQAV-H 88
Cdd:PLN02493   6 VTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMaH 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  89 PDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQV-FFQMYWVGSRDVLLQRMERARAAGAKGLIITTDwSFSYGRd 167
Cdd:PLN02493  86 PDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIrFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVD-TPRLGR- 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 168 wgspsipEKMDLKAMFQFAPEGIMRPkwlLEFAKTGKIPDLTTPNLAA--PGQPAPTFfgaygewmqtplpTWEDIAWLR 245
Cdd:PLN02493 164 -------RESDIKNRFTLPPNLTLKN---FEGLDLGKMDEANDSGLASyvAGQIDRTL-------------SWKDVQWLQ 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 246 EQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIRRGGDVVKALAL 325
Cdd:PLN02493 221 TITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGRIPVFLDGGVRRGTDVFKALAL 300

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 379987950 326 GAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELSPADLV 380
Cdd:PLN02493 301 GASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEISRNHIT 355
PLN02979 PLN02979
glycolate oxidase
 61-375 2.83e-52

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 178.38  E-value: 2.83e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  61 KREMSTTIMGQDISLPVMISPTGVQAV-HPDGEVAVARAAAARGTAIGLSSFASKSIEEVAAANPQV-FFQMYWVGSRDV 138
Cdd:PLN02979  56 KIDMTTTVLGFKISMPIMVAPTAMQKMaHPDGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIrFFQLYVYKNRNV 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 139 LLQRMERARAAGAKGLIITTDwSFSYGRdwgspsipEKMDLKAMFQFAPEGIMRPkwlLEFAKTGKIPDLTTPNLAA--P 216
Cdd:PLN02979 136 VEQLVRRAERAGFKAIALTVD-TPRLGR--------RESDIKNRFTLPPNLTLKN---FEGLDLGKMDEANDSGLASyvA 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 217 GQPAPTFfgaygewmqtplpTWEDIAWLREQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAPIRVLPG 296
Cdd:PLN02979 204 GQIDRTL-------------SWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEE 270

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 379987950 297 IAEAVGDQVEVVLDGGIRRGGDVVKALALGAKAVMLGRAYLWGLSANGQAGVENVLDLMRMGIDSGLMGLGHSSITELS 375
Cdd:PLN02979 271 VVKATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEIS 349
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 237-334 1.37e-09

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 57.21  E-value: 1.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 237 TWEDIAWLREQWGG-PFMLKGIMRIDDAKR-AVDAGVSAISVSNHGGNNLDGTPAPIRVLPGIAEAVGDQVEVVLDGGIR 314
Cdd:cd04722  101 DLELIRELREAVPDvKVVVKLSPTGELAAAaAEEAGVDEVGLGNGGGGGGGRDAVPIADLLLILAKRGSKVPVIAGGGIN 180

                         90       100
                 ....*....|....*....|
gi 379987950 315 RGGDVVKALALGAKAVMLGR 334
Cdd:cd04722  181 DPEDAAEALALGADGVIVGS 200
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 241-380 8.50e-09

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 56.78  E-value: 8.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 241 IAWLREQWGG-PFMLK--GIMRIDDAKRAVDAG-VSAISVSNHGGnnldGT---PAPIR------VLPGIAEAV------ 301
Cdd:cd02808  205 IEDLREATGGkPIGVKlvAGHGEGDIAAGVAAAgADFITIDGAEG----GTgaaPLTFIdhvglpTELGLARAHqalvkn 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 302 --GDQVEVVLDGGIRRGGDVVKALALGAKAVMLGRAYL-----------------WGLSAN------------GQAGVEN 350
Cdd:cd02808  281 glRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALialgciqarkchtntcpVGVATQdpelrrrldvegKAERVAN 360

                        170       180       190
                 ....*....|....*....|....*....|
gi 379987950 351 VLDLMRMGIDSGLMGLGHSSITELSPADLV 380
Cdd:cd02808  361 YLKSLAEELRELAAALGKRSLELLGRSDLL 390
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 238-374 1.46e-08

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 55.58  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 238 WEDIAWLREQWGGPFMLK----GIMRiDDAKRAVDAGVSAISVSNHGGNN--------------------LD-GTPAPiR 292
Cdd:cd02811  167 LERIEELVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGGTSwarvenyrakdsdqrlaeyfADwGIPTA-A 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 293 VLPGIAEAVGDqVEVVLDGGIRRGGDVVKALALGAKAV-----MLGRAYlwglsaNGQAGVENVLDLMRMGIDSGLMGLG 367
Cdd:cd02811  245 SLLEVRSALPD-LPLIASGGIRNGLDIAKALALGADLVgmagpFLKAAL------EGEEAVIETIEQIIEELRTAMFLTG 317


                 ....*..
gi 379987950 368 HSSITEL 374
Cdd:cd02811  318 AKNLAEL 324
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 266-337 8.31e-08

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 53.49  E-value: 8.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  266 AVDAGVSAISVSNHGGnnldGTPA-PIRV-----LP---GIAEAV--------GDQVEVVLDGGIRRGGDVVKALALGAK 328
Cdd:pfam01645 222 VAKAGADIILIDGYDG----GTGAsPKTSikhagLPwelALAEAHqtlkenglRDRVSLIADGGLRTGADVAKAAALGAD 297


                  ....*....
gi 379987950  329 AVMLGRAYL 337
Cdd:pfam01645 298 AVYIGTAAL 306
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 222-337 5.07e-07

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 50.17  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950 222 TFFGAYGEWmqtplptwedIAWLREqWGGPFMLKgIMRIDDAKRAVDAGVSAISVSN-----HGGNNLDGTPApirVLPG 296
Cdd:cd04730   86 FSFGPPAEV----------VERLKA-AGIKVIPT-VTSVEEARKAEAAGADALVAQGaeaggHRGTFDIGTFA---LVPE 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 379987950 297 IAEAVGdqVEVVLDGGIRRGGDVVKALALGAKAVMLGRAYL 337
Cdd:cd04730  151 VRDAVD--IPVIAAGGIADGRGIAAALALGADGVQMGTRFL 189
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 305-334 5.09e-07

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 50.98  E-value: 5.09e-07
                         10        20        30
                 ....*....|....*....|....*....|
gi 379987950 305 VEVVLDGGIRRGGDVVKALALGAKAVMLGR 334
Cdd:cd00381  198 VPVIADGGIRTSGDIVKALAAGADAVMLGS 227
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 305-334 5.86e-07

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 51.24  E-value: 5.86e-07
                          10        20        30
                  ....*....|....*....|....*....|
gi 379987950  305 VEVVLDGGIRRGGDVVKALALGAKAVMLGR 334
Cdd:pfam00478 324 VPVIADGGIKYSGDIVKALAAGADAVMLGS 353
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
 305-333 1.46e-06

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 50.04  E-value: 1.46e-06
                          10        20
                  ....*....|....*....|....*....
gi 379987950  305 VEVVLDGGIRRGGDVVKALALGAKAVMLG 333
Cdd:TIGR01302 328 IPVIADGGIRYSGDIVKALAAGADAVMLG 356
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 304-334 1.83e-06

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 49.58  E-value: 1.83e-06
                         10        20        30
                 ....*....|....*....|....*....|.
gi 379987950 304 QVEVVLDGGIRRGGDVVKALALGAKAVMLGR 334
Cdd:PTZ00314 344 GVPCIADGGIKNSGDICKALALGADCVMLGS 374
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
 263-337 3.64e-06

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 48.18  E-value: 3.64e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 379987950 263 AKRAVDAGVSAISVSNH--GGNNLDGTPAPIRVLPGIAEAVgdQVEVVLDGGIRRGGDVVKALALGAKAVMLGRAYL 337
Cdd:COG2070  117 ARKAEKAGADAVVAEGAeaGGHRGADEVSTFALVPEVRDAV--DIPVIAAGGIADGRGIAAALALGADGVQMGTRFL 191
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
 245-337 2.89e-05

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 45.58  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  245 REQWGGPFMLKGIMRIDDAKRAVDAGVSAISVSNHGGNNLDGTPAP-----IRVLPGIAEAVgdQVEVVLDGGIRRGGDV 319
Cdd:pfam03060 131 RLHFAGVALIPTISSAKEARIAEARGADALIVQGPEAGGHQGTPEYgdkglFRLVPQVPDAV--DIPVIAAGGIWDRRGV 208

                          90
                  ....*....|....*...
gi 379987950  320 VKALALGAKAVMLGRAYL 337
Cdd:pfam03060 209 AAALALGASGVQMGTRFL 226
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 297-333 1.51e-04

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 43.89  E-value: 1.51e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 379987950 297 IAEAVGdqVEVVLDGGIRRGGDVVKALALGAKAVMLG 333
Cdd:PLN02274 346 IAAQHG--VPVIADGGISNSGHIVKALTLGASTVMMG 380
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
 307-336 2.13e-04

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 43.10  E-value: 2.13e-04
                         10        20        30
                 ....*....|....*....|....*....|
gi 379987950 307 VVLDGGIRRGGDVVKALALGAKAVMLGRAY 336
Cdd:PRK06843 259 IIADGGIRFSGDVVKAIAAGADSVMIGNLF 288
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 298-334 8.10e-04

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 40.96  E-value: 8.10e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 379987950 298 AEAVGDQVEVVLDGGIRRGGDVVKALALGAKAVMLGR 334
Cdd:COG0516  191 VTEARMAIAIAADGGIGYIHDNAKALAAGADAVMLGS 227
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 303-337 4.38e-03

Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439839  Cd Length: 728  Bit Score: 39.08  E-value: 4.38e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 379987950 303 DQVEVVLDGGIRRGGDVVKALALGAKAVMLGRAYL 337
Cdd:COG0069  439 DRIRLIADGKLKTGRDVAIAAALGADEFGFARAFM 473
GltB3 COG0070
Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 ...
 267-327 8.88e-03

Glutamate synthase domain 3 [Amino acid transport and metabolism]; Glutamate synthase domain 3 is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 439840 [Multi-domain]  Cd Length: 1508  Bit Score: 38.35  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 379987950  267 VDAGVSA-----ISVSNHGGnnlDGTPAPIRV-----LP---GIAEAV--------GDQVEVVLDGGIRRGGDVVKALAL 325
Cdd:COG0070  1034 IAAGVAKaaadvILISGHDG---GTGASPLSSikhagLPwelGLAETQqtlvlnnlRRRVVVQTDGGLKTGRDVVIAALL 1110


                  ..
gi 379987950  326 GA 327
Cdd:COG0070  1111 GA 1112
 
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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