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Conserved domains on  [gi|2301322313|ref|XP_661505|]
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hypothetical protein [Aspergillus nidulans FGSC A4]

Protein Classification

FMN-dependent alpha-hydroxy acid dehydrogenase family protein( domain architecture ID 10445753)

FMN-dependent alpha-hydroxy acid dehydrogenase family protein similar to Rhodotorula graminis mitochondrial (S)-mandelate dehydrogenase that is involved in the reduction of (S)-mandelate to benzoylformate and enables utilization of mandelate as a substrate for growth

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 116-461 0e+00

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: 582.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02922     2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd02922    82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQAtGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02922   162 RDERLKAEEAVSDGPA-GKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02922   241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVF--DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKA 318

                         330       340
                  ....*....|....*....|....*.
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd02922   319 IQILKDEIETTMRLLGVTSLDQLGPS 344
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 9-80 1.03e-26

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


:

Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 102.70  E-value: 1.03e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313   9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEF-DPIHPPDTLDKYLDSSkHLGEVD 80
Cdd:pfam00173   3 EELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKY-RIGELA 74
 
Name Accession Description Interval E-value
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 116-461 0e+00

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: 582.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02922     2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd02922    82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQAtGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02922   162 RDERLKAEEAVSDGPA-GKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02922   241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVF--DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKA 318

                         330       340
                  ....*....|....*....|....*.
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd02922   319 IQILKDEIETTMRLLGVTSLDQLGPS 344
FMN_dh pfam01070
FMN-dependent dehydrogenase;
121-464 9.55e-157

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 449.29  E-value: 9.55e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 121 ARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPEGEVVL 200
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 201 TRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRREKDMRS 280
Cdd:pfam01070  81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGP--LWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 281 KFS------------DVGSNVQATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEA 348
Cdd:pfam01070 159 GFTlpprltprnlldLALHPRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 349 GVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYG 428
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVG-----GRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGG 313

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2301322313 429 QPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMVD 464
Cdd:pfam01070 314 EAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 108-463 4.75e-126

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: 371.39  E-value: 4.75e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 108 LSACYNLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATA 187
Cdd:COG1304     1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 188 LGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVD 267
Cdd:COG1304    81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAP--LWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 268 APQLGRREKDMRSKFS----DVGSNVQ--ATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVED 341
Cdd:COG1304   159 TPVLGRRERDLREGFSqpprLTPRNLLeaATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 342 VLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQvmpILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFL 421
Cdd:COG1304   239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPE---IRAAVG--GRIPVIADGGIRRGLDVAKALALGADAVGLGRPFL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2301322313 422 FAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:COG1304   314 YGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
PLN02535 PLN02535
glycolate oxidase
 113-463 2.02e-106

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 321.78  E-value: 2.02e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:PLN02535    7 NVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:PLN02535   87 HPEGEIATARAAAACNTIMVLSFMASCTVEEV--ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSK-FSDVGSNVQATGGDEV--DRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAG 349
Cdd:PLN02535  165 RREADIKNKmISPQLKNFEGLLSTEVvsDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 350 VQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRErgwenRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQ 429
Cdd:PLN02535  245 VAGIIVSNHGARQLDYSPATISVLEEVVQAVGG-----RVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE 319

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2301322313 430 PGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:PLN02535  320 DGVRKVIEMLKDELEITMALSGCPSVKDITRSHV 353
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 9-80 1.03e-26

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 102.70  E-value: 1.03e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313   9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEF-DPIHPPDTLDKYLDSSkHLGEVD 80
Cdd:pfam00173   3 EELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKY-RIGELA 74
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 3-62 8.25e-24

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 95.10  E-value: 8.25e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313   3 NNKLTGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHP 62
Cdd:COG5274    15 EKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHP 74
PLN02252 PLN02252
nitrate reductase [NADPH]
 7-97 1.59e-21

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 98.21  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313   7 TGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHPP---DTLDKYldsskHLGEVDMAT 83
Cdd:PLN02252  521 TMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDkakKMLEDY-----RIGELVTTG 595

                          90
                  ....*....|....
gi 2301322313  84 VEQEEKAHDPEEDA 97
Cdd:PLN02252  596 AAASSSASSHPLSA 609
 
Name Accession Description Interval E-value
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 116-461 0e+00

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: 582.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02922     2 DFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd02922    82 GELNLARAAGKHGILQMISTNASCSLEEIVDARPPDQPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPVLGKRE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQAtGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02922   162 RDERLKAEEAVSDGPA-GKKTKAKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGVDGIVL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02922   241 SNHGGRQLDTAPAPIEVLLEIRKHCPEVF--DKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEEGVEKA 318

                         330       340
                  ....*....|....*....|....*.
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd02922   319 IQILKDEIETTMRLLGVTSLDQLGPS 344
FMN_dh pfam01070
FMN-dependent dehydrogenase;
121-464 9.55e-157

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 449.29  E-value: 9.55e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 121 ARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPEGEVVL 200
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHPDGELAL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 201 TRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRREKDMRS 280
Cdd:pfam01070  81 ARAAAAAGIPFVLSTVSSTSLEEVAAAAGGP--LWFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRERDLRN 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 281 KFS------------DVGSNVQATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEA 348
Cdd:pfam01070 159 GFTlpprltprnlldLALHPRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKRAVEA 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 349 GVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYG 428
Cdd:pfam01070 239 GVDGIVVSNHGGRQLDGAPATIDALPEIVAAVG-----GRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGLAAGG 313

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 2301322313 429 QPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMVD 464
Cdd:pfam01070 314 EAGVAHALEILRDELERTMALLGCKSIADLTPSLLR 349
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 116-460 9.36e-132

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: 383.72  E-value: 9.36e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd02809     2 DLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQvqWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRe 275
Cdd:cd02809    82 GELATARAAAAAGIPFTLSTVSTTSLEEVAAAAPGPR--WFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPVLGRR- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 kdmrskfsdvgsnvqatggdevdrsqgaaraissfidpsLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVL 355
Cdd:cd02809   159 ---------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGADGIVV 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 356 SNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRA 435
Cdd:cd02809   200 SNHGGRQLDGAPATIDALPEIVAAVG-----GRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEAGVAHV 274

                         330       340
                  ....*....|....*....|....*
gi 2301322313 436 MQLLKDELEMNMRLIGAQKIADLNP 460
Cdd:cd02809   275 LEILRDELERAMALLGCASLADLDP 299
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 108-463 4.75e-126

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: 371.39  E-value: 4.75e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 108 LSACYNLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATA 187
Cdd:COG1304     1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 188 LGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDqvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVD 267
Cdd:COG1304    81 GGGLAHPDGELALARAAAAAGIPMGLSTQSTTSLEEVAAAAPAP--LWFQLYVPKDRGFTDDLLRRAEAAGADALVLTVD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 268 APQLGRREKDMRSKFS----DVGSNVQ--ATGGDEVDRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVED 341
Cdd:COG1304   159 TPVLGRRERDLREGFSqpprLTPRNLLeaATHPRWALGLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIVKGVLSPED 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 342 VLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQvmpILRERGweNRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFL 421
Cdd:COG1304   239 ARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPE---IRAAVG--GRIPVIADGGIRRGLDVAKALALGADAVGLGRPFL 313

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 2301322313 422 FAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:COG1304   314 YGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
PLN02535 PLN02535
glycolate oxidase
 113-463 2.02e-106

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 321.78  E-value: 2.02e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:PLN02535    7 NVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAMHKLA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:PLN02535   87 HPEGEIATARAAAACNTIMVLSFMASCTVEEV--ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVLTADVPRLG 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSK-FSDVGSNVQATGGDEV--DRSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAG 349
Cdd:PLN02535  165 RREADIKNKmISPQLKNFEGLLSTEVvsDKGSGLEAFASETFDASLSWKDIEWLRSITNLPILIKGVLTREDAIKAVEVG 244

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 350 VQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRErgwenRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQ 429
Cdd:PLN02535  245 VAGIIVSNHGARQLDYSPATISVLEEVVQAVGG-----RVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVIYGLAAKGE 319

                         330       340       350
                  ....*....|....*....|....*....|....
gi 2301322313 430 PGVNRAMQLLKDELEMNMRLIGAQKIADLNPSMV 463
Cdd:PLN02535  320 DGVRKVIEMLKDELEITMALSGCPSVKDITRSHV 353
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 113-458 8.65e-95

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


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 292.02  E-value: 8.65e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:PLN02493    5 NVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:PLN02493   85 HPDGEYATARAASAAGTIMTLSSWATSSVEEV--ASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSKFSdVGSNVQATGGDEVD-------RSQGAARAISSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRA 345
Cdd:PLN02493  163 RRESDIKNRFT-LPPNLTLKNFEGLDlgkmdeaNDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 346 VEAGVQGVVLSNHGGRQLDTAPSGIEVLAQVMpilreRGWENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMS 425
Cdd:PLN02493  242 IQAGAAGIIVSNHGARQLDYVPATISALEEVV-----KATQGRIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLA 316

                         330       340       350
                  ....*....|....*....|....*....|...
gi 2301322313 426 AYGQPGVNRAMQLLKDELEMNMRLIGAQKIADL 458
Cdd:PLN02493  317 AEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 349
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 98-461 8.34e-92

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: 284.56  E-value: 8.34e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313  98 RQERIERMPPLSAcyNLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKC 177
Cdd:cd03332     7 LAGLLGRRPDLPV--DPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 178 SIPFYVTATALGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARrGDQVQWLQLYVNKDRAITKRIIEHAEAR 257
Cdd:cd03332    85 AAPLLLAPIGVQELFHPDAELATARAAAELGVPYILSTASSSSIEDVAAAA-GDAPRWFQLYWPKDDDLTESLLRRAEKA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 258 GCKGLFITVDAPQLGRREKDMRSK-------------FSD------VGSNVQATGGDEVDRSQGAARAISSFIDPSLSWK 318
Cdd:cd03332   164 GYRVLVVTLDTWSLGWRPRDLDLGylpflrgigianyFSDpvfrkkLAEPVGEDPEAPPPMEAAVARFVSVFSGPSLTWE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 319 DIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILRergweNRIEIFIDGGIR 398
Cdd:cd03332   244 DLAFLREWTDLPIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPEIVEAVG-----DRLTVLFDSGVR 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313 399 RATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:cd03332   319 TGADIMKALALGAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRD 381
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 113-458 3.27e-82

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: 258.91  E-value: 3.27e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 113 NLLDFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLG 192
Cdd:cd04737     7 NLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHGLA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 193 NPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIVDARRGDQvQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLG 272
Cdd:cd04737    87 HATGEVATARGMAEVGSLFSISTYSNTSLEEIAKASNGGP-KWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTADATVGG 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 273 RREKDMRSKFSdvgSNVQATGGDEVDRSQGAARAIsSFIDPS----LSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEA 348
Cdd:cd04737   166 NREADIRNKFQ---FPFGMPNLNHFSEGTGKGKGI-SEIYAAakqkLSPADIEFIAKISGLPVIVKGIQSPEDADVAINA 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 349 GVQGVVLSNHGGRQLDTAPSGIEVLAQVMPILrergwENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYG 428
Cdd:cd04737   242 GADGIWVSNHGGRQLDGGPASFDSLPEIAEAV-----NHRVPIIFDSGVRRGEHVFKALASGADAVAVGRPVLYGLALGG 316

                         330       340       350
                  ....*....|....*....|....*....|
gi 2301322313 429 QPGVNRAMQLLKDELEMNMRLIGAQKIADL 458
Cdd:cd04737   317 AQGVASVLEHLNKELKIVMQLAGTRTIEDV 346
PLN02979 PLN02979
glycolate oxidase
 155-459 1.36e-78

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 250.02  E-value: 1.36e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 155 FRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPEGEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQ 234
Cdd:PLN02979   46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHPDGEYATARAASAAGTIMTLSSWATSSVEEV--ASTGPGIR 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 235 WLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRREKDMRSKFSdVGSNVQATGGDEVD-------RSQGAARAI 307
Cdd:PLN02979  124 FFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFT-LPPNLTLKNFEGLDlgkmdeaNDSGLASYV 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 308 SSFIDPSLSWKDIPWFQSVTKMPIVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQVMpilreRGWEN 387
Cdd:PLN02979  203 AGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVV-----KATQG 277

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301322313 388 RIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLN 459
Cdd:PLN02979  278 RIPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEIS 349
lldD PRK11197
L-lactate dehydrogenase; Provisional
 116-461 3.66e-66

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 217.97  E-value: 3.66e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:PRK11197    8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGMYARR 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKDRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:PRK11197   88 GEVQAARAADAKGIPFTLSTVSVCPIEEV--APAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVPGARY 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFS--------------------DVGSNVQATGGDEVDRSQGAARAISSFI-------DPSLSWKDIPWFQSVTK 328
Cdd:PRK11197  166 RDAHSGMSgpnaamrrylqavthpqwawDVGLNGRPHDLGNISAYLGKPTGLEDYIgwlgnnfDPSISWKDLEWIRDFWD 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 329 MPIVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGievlAQVMPILRErGWENRIEIFIDGGIRRATDILKALC 408
Cdd:PRK11197  246 GPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSS----ARALPAIAD-AVKGDITILADSGIRNGLDVVRMIA 320

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2301322313 409 LGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNPS 461
Cdd:PRK11197  321 LGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRD 373
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 116-460 3.83e-66

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: 217.39  E-value: 3.83e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 116 DFETVARSVMKKTAWAYYSSGADDEITMRENHQAFQKIWFRPRVLVDVENVDFSTKMLGTKCSIPFYVTATALGKLGNPE 195
Cdd:cd04736     2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWPN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 196 GEVVLTRAAHDHDVIQMIPTLASCSFDEIvdARRGDQVQWLQLYVNKdRAITKRIIEHAEARGCKGLFITVDAPQLGRRE 275
Cdd:cd04736    82 GDLALARAAAKAGIPFVLSTASNMSIEDV--ARQADGDLWFQLYVVH-RELAELLVKRALAAGYTTLVLTTDVAVNGYRE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 276 KDMRSKFSDVGSNVQATGGDEV-----------------------DRSQGAARA--ISSFIDPSLSWKDIPWFQSVTKMP 330
Cdd:cd04736   159 RDLRNGFAIPFRYTPRVLLDGIlhprwllrflrngmpqlanfasdDAIDVEVQAalMSRQMDASFNWQDLRWLRDLWPHK 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 331 IVLKGVQCVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQV-----MPILrergwenrieifIDGGIRRATDILK 405
Cdd:cd04736   239 LLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIvaatyKPVL------------IDSGIRRGSDIVK 306

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2301322313 406 ALCLGAKGVGIGRPFLFAMSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADLNP 460
Cdd:cd04736   307 ALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 9-80 1.03e-26

Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from a diverse range of proteins. This family also includes proteins that bind to steroids. The family includes progesterone receptors. Many members of this subfamily are membrane anchored by an N-terminal transmembrane alpha helix. This family also includes a domain in some chitin synthases. There is no known ligand for this domain in the chitin synthases.


Pssm-ID: 459698 [Multi-domain]  Cd Length: 74  Bit Score: 102.70  E-value: 1.03e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2301322313   9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEF-DPIHPPDTLDKYLDSSkHLGEVD 80
Cdd:pfam00173   3 EELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFeAIGHSEDAAEKLLKKY-RIGELA 74
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 3-62 8.25e-24

Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport and metabolism];


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 95.10  E-value: 8.25e-24
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313   3 NNKLTGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHP 62
Cdd:COG5274    15 EKTYTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHP 74
PLN02252 PLN02252
nitrate reductase [NADPH]
 7-97 1.59e-21

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 98.21  E-value: 1.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313   7 TGADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQKIILKYAGKDATEEFDPIHPP---DTLDKYldsskHLGEVDMAT 83
Cdd:PLN02252  521 TMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIHSDkakKMLEDY-----RIGELVTTG 595

                          90
                  ....*....|....
gi 2301322313  84 VEQEEKAHDPEEDA 97
Cdd:PLN02252  596 AAASSSASSHPLSA 609
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 330-458 3.81e-12

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: 67.14  E-value: 3.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 330 PIVLKGVQC---VEDVLRAVEAGVQGVVLSNHGG-------------RQLDTAPS----GI---EVLAQVMPILRErgwe 386
Cdd:cd02811   180 PVIVKEVGFgisRETAKRLADAGVKAIDVAGAGGtswarvenyrakdSDQRLAEYfadwGIptaASLLEVRSALPD---- 255

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2301322313 387 nrIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAmSAYGQPGVNRAMQLLKDELEMNMRLIGAQKIADL 458
Cdd:cd02811   256 --LPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEELRTAMFLTGAKNLAEL 324
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 9-101 5.26e-10

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 61.63  E-value: 5.26e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313   9 ADVAKHNSKDSCWVIVHGKAYDVTEFLPEHPGGQkIILKYAGKDATEEFDPIHPPDTLdkyldssKHLGEVDMATVEQEE 88
Cdd:PLN03198  109 SEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFHAASTW-------KILQDFYIGDVDNVE 180

                          90
                  ....*....|...
gi 2301322313  89 KAHDPEEDARQER 101
Cdd:PLN03198  181 PTPELLKDFRDLR 193
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 370-424 1.42e-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: 59.86  E-value: 1.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2301322313 370 IEVLAQVMPILRERGWENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAM 424
Cdd:cd02808   267 ELGLARAHQALVKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIAL 321
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 318-424 8.54e-09

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: 57.34  E-value: 8.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 318 KDIPWfqsvtKMPIVLKGV--QCVEDV-LRAVEAGVQGVVLSNHGG-------RQLDTAPSGIEV-LAQVMPILRERGWE 386
Cdd:pfam01645 197 KEINP-----KAPISVKLVsgHGVGTIaAGVAKAGADIILIDGYDGgtgaspkTSIKHAGLPWELaLAEAHQTLKENGLR 271

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2301322313 387 NRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAM 424
Cdd:pfam01645 272 DRVSLIADGGLRTGADVAKAAALGADAVYIGTAALIAL 309
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 313-418 3.06e-07

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: 51.05  E-value: 3.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 313 PSLSWKDIPWF-QSVTKMPIVLKGVQ-CVEDVLRAVEAGVQGVVLSNHGGRQLDTAPSGIEVLAQvmpILRERGWenRIE 390
Cdd:cd04722    98 AREDLELIRELrEAVPDVKVVVKLSPtGELAAAAAEEAGVDEVGLGNGGGGGGGRDAVPIADLLL---ILAKRGS--KVP 172

                          90       100
                  ....*....|....*....|....*...
gi 2301322313 391 IFIDGGIRRATDILKALCLGAKGVGIGR 418
Cdd:cd04722   173 VIAGGGINDPEDAAEALALGADGVIVGS 200
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 5-89 4.72e-07

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 52.35  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313   5 KLTGADVAKHNSKDSCWVIVHGKAYDVTEFLpEHPGGqKIILKYAGKDATEEFDPIHPPDTldKYLDSSKHLGEVDMATV 84
Cdd:PLN03199   25 KISWQEVKKHASPDDAWIIHQNKVYDVSNWH-DHPGG-AVIFTHAGDDMTDIFAAFHAPGS--QALMKKFYIGDLIPEST 100


                  ....*
gi 2301322313  85 EQEEK 89
Cdd:PLN03199  101 EHKDP 105
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 371-424 1.34e-05

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: 47.94  E-value: 1.34e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2301322313 371 EVLAQVMPILRERGWENRIEIFIDGGIRRATDILKALCLGAKGVGIGRPFLFAM 424
Cdd:COG0069   423 LGLAEVHQTLVGNGLRDRIRLIADGKLKTGRDVAIAAALGADEFGFARAFMVAL 476
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 336-423 3.75e-03

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: 39.00  E-value: 3.75e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2301322313 336 VQCVEDVLRAVEAGVQGVVLSNH--GGRQLDTAPSGIEVLAQVMPILRergwenrIEIFIDGGIRRATDILKALCLGAKG 413
Cdd:cd04730   109 VTSVEEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPEVRDAVD-------IPVIAAGGIADGRGIAAALALGADG 181

                          90
                  ....*....|
gi 2301322313 414 VGIGRPFLFA 423
Cdd:cd04730   182 VQMGTRFLAT 191
 
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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