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Conserved domains on  [gi|6323587|ref|NP_013658|]
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L-lactate dehydrogenase (cytochrome) [Saccharomyces cerevisiae S288C]

Protein Classification

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

FMN-dependent alpha-hydroxy acid dehydrogenase containing a cytochrome b5-like heme/steroid binding domain, such as Saccharomyces cerevisiae L-lactate dehydrogenase (cytochrome) that catalyzes the oxidation of (S)-lactate (L-lactate) to pyruvate with subsequent transfer of electrons to cytochrome c

EC:  1.1.-.-
Gene Ontology:  GO:0020037|GO:0010181|GO:0016614|GO:0046872
PubMed:  10093730|19850002

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) ...
 206-555 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: 581.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  206 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 285
Cdd:cd02922   1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  286 lEGEKDVARGCGQGvtKVPQMISTLASCSPEEIIEAAPSDkQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 365
Cdd:cd02922  81 -DGELNLARAAGKH--GILQMISTNASCSLEEIVDARPPD-QPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  366 LGQREKDMKLKFSNTKAGPKAMKKTNvEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 445
Cdd:cd02922 157 LGKRERDERLKAEEAVSDGPAGKKTK-AKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGV 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  446 SGVVLSNHGGRQLDFSRAPIEVLAETMPILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 525
Cdd:cd02922 236 DGIVLSNHGGRQLDTAPAPIEVLLEIRKHCPE--VFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEE 313

                       330       340       350
                ....*....|....*....|....*....|
gi 6323587  526 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 555
Cdd:cd02922 314 GVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 92-164 1.77e-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: 1.77e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323587     92 SPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFE-PLHAPNVIDKYIApEKKLGPL 164
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEaIGHSEDAAEKLLK-KYRIGEL 73
 
Name Accession Description Interval E-value
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 206-555 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: 581.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  206 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 285
Cdd:cd02922   1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  286 lEGEKDVARGCGQGvtKVPQMISTLASCSPEEIIEAAPSDkQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 365
Cdd:cd02922  81 -DGELNLARAAGKH--GILQMISTNASCSLEEIVDARPPD-QPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  366 LGQREKDMKLKFSNTKAGPKAMKKTNvEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 445
Cdd:cd02922 157 LGKRERDERLKAEEAVSDGPAGKKTK-AKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGV 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  446 SGVVLSNHGGRQLDFSRAPIEVLAETMPILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 525
Cdd:cd02922 236 DGIVLSNHGGRQLDTAPAPIEVLLEIRKHCPE--VFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEE 313

                       330       340       350
                ....*....|....*....|....*....|
gi 6323587  526 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 555
Cdd:cd02922 314 GVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
FMN_dh pfam01070
FMN-dependent dehydrogenase;
212-560 2.72e-156

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 451.60  E-value: 2.72e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    212 ASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPlEGEKD 291
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHP-DGELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    292 VARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREK 371
Cdd:pfam01070  80 LARAAAA--AGIPFVLSTVSSTSLEEVAAAAGGPL---WFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRER 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    372 DMKLKFS-NTKAGPK-----------AMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIK 439
Cdd:pfam01070 155 DLRNGFTlPPRLTPRnlldlalhprwALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    440 AAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYAN 519
Cdd:pfam01070 235 AVEAGVDGIVVSNHGGRQLDGAPATIDALPE---IVAA--VGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGL 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 6323587    520 SCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDL 560
Cdd:pfam01070 310 AAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 199-558 8.10e-128

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: 379.09  E-value: 8.10e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  199 LDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATA 278
Cdd:COG1304   1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  279 LCKLGNPlEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALF 358
Cdd:COG1304  81 GGGLAHP-DGELALARAAAA--AGIPMGLSTQSTTSLEEVAAAAPAPL---WFQLYVPKDRGFTDDLLRRAEAAGADALV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  359 VTVDAPSLGQREKDMKLKFSntkaGPKAMKKTNVEE----------SQGASRALSKFIDPSLTWKDIEELKKKTKLPIVI 428
Cdd:COG1304 155 LTVDTPVLGRRERDLREGFS----QPPRLTPRNLLEaathprwalgLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIV 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  429 KGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKG 508
Cdd:COG1304 231 KGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIR-----AAVGGRIPVIADGGIRRGLDVAKALALGADA 305

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6323587  509 VGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 558
Cdd:COG1304 306 VGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
PLN02535 PLN02535
glycolate oxidase
 200-553 3.34e-96

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 298.29  E-value: 3.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   200 DNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATAL 279
Cdd:PLN02535   3 DEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   280 CKLGNPlEGEKDVARGCGQGVTKVpqMISTLASCSPEEIieaAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFV 359
Cdd:PLN02535  83 HKLAHP-EGEIATARAAAACNTIM--VLSFMASCTVEEV---ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   360 TVDAPSLGQREKDMKLK-FSNTKAGPKAMKKTNVEESQGAS-RAL-SKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTED 436
Cdd:PLN02535 157 TADVPRLGRREADIKNKmISPQLKNFEGLLSTEVVSDKGSGlEAFaSETFDASLSWKDIEWLRSITNLPILIKGVLTRED 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   437 VIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFL 516
Cdd:PLN02535 237 AIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVV-----QAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 6323587   517 YANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 553
Cdd:PLN02535 312 YGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDI 348
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 92-164 1.77e-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: 1.77e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323587     92 SPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFE-PLHAPNVIDKYIApEKKLGPL 164
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEaIGHSEDAAEKLLK-KYRIGEL 73
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 91-166 8.77e-20

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


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 84.32  E-value: 8.77e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323587   91 ISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPLHA-PNVIDKYIApEKKLGPLQG 166
Cdd:COG5274  18 YTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPhSPKAERLLE-SYRIGRLAQ 93
PLN02252 PLN02252
nitrate reductase [NADPH]
 91-146 1.67e-17

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 86.65  E-value: 1.67e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323587    91 ISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPLH 146
Cdd:PLN02252 520 YTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIH 575
 
Name Accession Description Interval E-value
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 206-555 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: 581.48  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  206 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 285
Cdd:cd02922   1 HDFEAAAKKYLSKKAWAYYSSGADDEITLRENLEAFQRIRFRPRVLRDVEKVDTSTTILGHKVSLPFFISPAALAKLAHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  286 lEGEKDVARGCGQGvtKVPQMISTLASCSPEEIIEAAPSDkQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 365
Cdd:cd02922  81 -DGELNLARAAGKH--GILQMISTNASCSLEEIVDARPPD-QPLFFQLYVNKDRTKTEELLKRAEKLGAKAIFLTVDAPV 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  366 LGQREKDMKLKFSNTKAGPKAMKKTNvEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 445
Cdd:cd02922 157 LGKRERDERLKAEEAVSDGPAGKKTK-AKGGGAGRAMSGFIDPTLTWDDIKWLRKHTKLPIVLKGVQTVEDAVLAAEYGV 235

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  446 SGVVLSNHGGRQLDFSRAPIEVLAETMPILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 525
Cdd:cd02922 236 DGIVLSNHGGRQLDTAPAPIEVLLEIRKHCPE--VFDKIEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYGEE 313

                       330       340       350
                ....*....|....*....|....*....|
gi 6323587  526 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 555
Cdd:cd02922 314 GVEKAIQILKDEIETTMRLLGVTSLDQLGP 343
FMN_dh pfam01070
FMN-dependent dehydrogenase;
212-560 2.72e-156

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 451.60  E-value: 2.72e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    212 ASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPlEGEKD 291
Cdd:pfam01070   1 ARKRLPRFAFDYLDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSNRDLSTTLLGQRLSLPFGIAPVGMQGLAHP-DGELA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    292 VARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREK 371
Cdd:pfam01070  80 LARAAAA--AGIPFVLSTVSSTSLEEVAAAAGGPL---WFQLYVPRDRELTEDLLERAEAAGYKALVLTVDTPVLGRRER 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    372 DMKLKFS-NTKAGPK-----------AMKKTNVEESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIK 439
Cdd:pfam01070 155 DLRNGFTlPPRLTPRnlldlalhprwALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRERWKGPLVVKGILSPEDAKR 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    440 AAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQrnLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYAN 519
Cdd:pfam01070 235 AVEAGVDGIVVSNHGGRQLDGAPATIDALPE---IVAA--VGGRIPVLVDGGIRRGTDVLKALALGADAVLLGRPFLYGL 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 6323587    520 SCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLLDL 560
Cdd:pfam01070 310 AAGGEAGVAHALEILRDELERTMALLGCKSIADLTPSLLRR 350
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 206-555 1.53e-135

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: 396.82  E-value: 1.53e-135
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  206 YDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNP 285
Cdd:cd02809   1 ADLRALARRRLPKAVFDYIDGGAGDEVTLRRNRAAFDRIRLRPRVLRDVSKRDTSTTLLGQKLAMPFGIAPTGLQGLAHP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  286 lEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPS 365
Cdd:cd02809  81 -DGELATARAAAA--AGIPFTLSTVSTTSLEEVAAAAPGPR---WFQLYVPRDREITEDLLRRAEAAGYKALVLTVDTPV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  366 LGQRekdmklkfsntkagpkamkktnveesqgasralskfidpsLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGV 445
Cdd:cd02809 155 LGRR----------------------------------------LTWDDLAWLRSQWKGPLILKGILTPEDALRAVDAGA 194

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  446 SGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRN 525
Cdd:cd02809 195 DGIVVSNHGGRQLDGAPATIDALPEIV-----AAVGGRIEVLLDGGIRRGTDVLKALALGADAVLIGRPFLYGLAAGGEA 269

                       330       340       350
                ....*....|....*....|....*....|
gi 6323587  526 GVEKAIEILRDEIEMSMRLLGVTSIAELKP 555
Cdd:cd02809 270 GVAHVLEILRDELERAMALLGCASLADLDP 299
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 199-558 8.10e-128

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: 379.09  E-value: 8.10e-128
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  199 LDNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATA 278
Cdd:COG1304   1 MSRILSIEDLRRIARRKLPRFAFDYIDGGAGDEVTLRRNRAAFDRVRLRPRVLEDVSEIDLSTTLLGKRLAAPFLIAPMG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  279 LCKLGNPlEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVNSDRKITDDLVKNVEKLGVKALF 358
Cdd:COG1304  81 GGGLAHP-DGELALARAAAA--AGIPMGLSTQSTTSLEEVAAAAPAPL---WFQLYVPKDRGFTDDLLRRAEAAGADALV 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  359 VTVDAPSLGQREKDMKLKFSntkaGPKAMKKTNVEE----------SQGASRALSKFIDPSLTWKDIEELKKKTKLPIVI 428
Cdd:COG1304 155 LTVDTPVLGRRERDLREGFS----QPPRLTPRNLLEaathprwalgLASLAAWLDTNFDPSLTWDDIAWLRERWPGPLIV 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  429 KGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKG 508
Cdd:COG1304 231 KGVLSPEDARRAVDAGVDGIDVSNHGGRQLDGGPPTIDALPEIR-----AAVGGRIPVIADGGIRRGLDVAKALALGADA 305

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 6323587  509 VGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 558
Cdd:COG1304 306 VGLGRPFLYGLAAGGEAGVARVLELLRAELRRAMALTGCRSLAELRRALL 355
PLN02535 PLN02535
glycolate oxidase
 200-553 3.34e-96

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 298.29  E-value: 3.34e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   200 DNIINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATAL 279
Cdd:PLN02535   3 DEIVNVNEFQELAKQALPKMYYDFYAGGAEDQHTLKENVQAFRRITFRPRVLVDVSKIDMSTTILGYTISAPIMIAPTAM 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   280 CKLGNPlEGEKDVARGCGQGVTKVpqMISTLASCSPEEIieaAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFV 359
Cdd:PLN02535  83 HKLAHP-EGEIATARAAAACNTIM--VLSFMASCTVEEV---ASSCNAVRFLQLYVYKRRDIAAQLVQRAEKNGYKAIVL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   360 TVDAPSLGQREKDMKLK-FSNTKAGPKAMKKTNVEESQGAS-RAL-SKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTED 436
Cdd:PLN02535 157 TADVPRLGRREADIKNKmISPQLKNFEGLLSTEVVSDKGSGlEAFaSETFDASLSWKDIEWLRSITNLPILIKGVLTRED 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   437 VIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileqRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFL 516
Cdd:PLN02535 237 AIKAVEVGVAGIIVSNHGARQLDYSPATISVLEEVV-----QAVGGRVPVLLDGGVRRGTDVFKALALGAQAVLVGRPVI 311

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 6323587   517 YANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 553
Cdd:PLN02535 312 YGLAAKGEDGVRKVIEMLKDELEITMALSGCPSVKDI 348
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 204-558 8.57e-93

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: 290.34  E-value: 8.57e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  204 NLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLG 283
Cdd:cd03332  20 DPERLEALAREALSPGAFAYVAGGAGSESTARANRDAFSRWRIVPRMLRGVTERDLSVELFGRTLAAPLLLAPIGVQELF 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  284 NPlEGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKQiqWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDA 363
Cdd:cd03332 100 HP-DAELATARAAAE--LGVPYILSTASSSSIEDVAAAAGDAPR--WFQLYWPKDDDLTESLLRRAEKAGYRVLVVTLDT 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  364 PSLGQREKDMKL------------------KFSNTKAGPKAMKKTNVEESQGA-SRALSKFIDPSLTWKDIEELKKKTKL 424
Cdd:cd03332 175 WSLGWRPRDLDLgylpflrgigianyfsdpVFRKKLAEPVGEDPEAPPPMEAAvARFVSVFSGPSLTWEDLAFLREWTDL 254

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  425 PIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQrnLKDKLEVFVDGGVRRGTDVLKALCL 504
Cdd:cd03332 255 PIVLKGILHPDDARRAVEAGVDGVVVSNHGGRQVDGSIAALDALPE---IVEA--VGDRLTVLFDSGVRTGADIMKALAL 329

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 6323587  505 GAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 558
Cdd:cd03332 330 GAKAVLIGRPYAYGLALGGEDGVEHVLRNLLAELDLTMGLAGIRSIAELTRDAL 383
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 202-553 7.54e-84

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


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 266.60  E-value: 7.54e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   202 IINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCK 281
Cdd:PLN02493   3 ITNVTEYDAIAKQKLPKMVYDYYASGAEDQWTLQENRNAFARILFRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   282 LGNPlEGEKDVARGCGQGVTkvpqmISTLASCSPEEIIEAAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTV 361
Cdd:PLN02493  83 MAHP-DGEYATARAASAAGT-----IMTLSSWATSSVEEVASTGPGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   362 DAPSLGQREKDMKLKFSNtkagPKAMKKTNVE----------ESQGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGV 431
Cdd:PLN02493 157 DTPRLGRRESDIKNRFTL----PPNLTLKNFEgldlgkmdeaNDSGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGV 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   432 QRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPILEQRnlkdkLEVFVDGGVRRGTDVLKALCLGAKGVGL 511
Cdd:PLN02493 233 LTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKATQGR-----IPVFLDGGVRRGTDVFKALALGASGIFI 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 6323587   512 GRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 553
Cdd:PLN02493 308 GRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 349
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 202-554 1.20e-75

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: 244.66  E-value: 1.20e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  202 IINLYDFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCK 281
Cdd:cd04737   5 IINLYDLEAEAKKVIPKGAFGYIAGGSEDEWTLRENTRAFNHKQIVPRVLQGVESPDTSTELLGIKLKTPIIMAPIAAHG 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  282 LGNPlEGEKDVARGCGQGVTKVPqmISTLASCSPEEIIEAAPsdKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTV 361
Cdd:cd04737  85 LAHA-TGEVATARGMAEVGSLFS--ISTYSNTSLEEIAKASN--GGPKWFQLYMSKDDGFNRSLLDRAKAAGAKAIILTA 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  362 DAPSLGQREKDMKLKFSNtkagPKAMkkTNVE---ESQGASRALS---KFIDPSLTWKDIEELKKKTKLPIVIKGVQRTE 435
Cdd:cd04737 160 DATVGGNREADIRNKFQF----PFGM--PNLNhfsEGTGKGKGISeiyAAAKQKLSPADIEFIAKISGLPVIVKGIQSPE 233

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  436 DVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAEtmpILEQRNlkDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPF 515
Cdd:cd04737 234 DADVAINAGADGIWVSNHGGRQLDGGPASFDSLPE---IAEAVN--HRVPIIFDSGVRRGEHVFKALASGADAVAVGRPV 308

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 6323587  516 LYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELK 554
Cdd:cd04737 309 LYGLALGGAQGVASVLEHLNKELKIVMQLAGTRTIEDVK 347
PLN02979 PLN02979
glycolate oxidase
 246-553 1.08e-67

glycolate oxidase


Pssm-ID: 166620  Cd Length: 366  Bit Score: 224.22  E-value: 1.08e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   246 FKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPlEGEKDVARGCGQGVTkvpqmISTLASCSPEEIIEAAPSD 325
Cdd:PLN02979  46 FRPRILIDVSKIDMTTTVLGFKISMPIMVAPTAMQKMAHP-DGEYATARAASAAGT-----IMTLSSWATSSVEEVASTG 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   326 KQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSLGQREKDMKLKFSNtkagPKAMKKTNVE----------ES 395
Cdd:PLN02979 120 PGIRFFQLYVYKNRNVVEQLVRRAERAGFKAIALTVDTPRLGRRESDIKNRFTL----PPNLTLKNFEgldlgkmdeaND 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   396 QGASRALSKFIDPSLTWKDIEELKKKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMPIL 475
Cdd:PLN02979 196 SGLASYVAGQIDRTLSWKDVQWLQTITKLPILVKGVLTGEDARIAIQAGAAGIIVSNHGARQLDYVPATISALEEVVKAT 275

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 6323587   476 EQRnlkdkLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAEL 553
Cdd:PLN02979 276 QGR-----IPVFLDGGVRRGTDVFKALALGASGIFIGRPVVFSLAAEGEAGVRKVLQMLRDEFELTMALSGCRSLKEI 348
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
 207-555 2.57e-64

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: 215.08  E-value: 2.57e-64
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  207 DFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLGNPl 286
Cdd:cd04736   2 DYRSLAKKRLPRMVFDYLEGGAEDEKGLRHNRDAFDRWRFIPRRLVDVSKRDISASLFGKVWSAPLVIAPTGLNGAFWP- 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  287 EGEKDVARGCGQgvTKVPQMISTLASCSPEEIIEAAPSDKqiqWYQLYVnSDRKITDDLVKNVEKLGVKALFVTVDAPSL 366
Cdd:cd04736  81 NGDLALARAAAK--AGIPFVLSTASNMSIEDVARQADGDL---WFQLYV-VHRELAELLVKRALAAGYTTLVLTTDVAVN 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  367 GQREKDMKLKFS----------------------------NTKAGPKAMKKTNVEeSQGAsrALSKFIDPSLTWKDIEEL 418
Cdd:cd04736 155 GYRERDLRNGFAipfrytprvlldgilhprwllrflrngmPQLANFASDDAIDVE-VQAA--LMSRQMDASFNWQDLRWL 231

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  419 KKKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAETMpileQRNLKDkleVFVDGGVRRGTDV 498
Cdd:cd04736 232 RDLWPHKLLVKGIVTAEDAKRCIELGADGVILSNHGGRQLDDAIAPIEALAEIV----AATYKP---VLIDSGIRRGSDI 304

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 6323587  499 LKALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKP 555
Cdd:cd04736 305 VKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLKEEIDRTLALIGCPDIASLTP 361
lldD PRK11197
L-lactate dehydrogenase; Provisional
 207-558 8.08e-60

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 203.72  E-value: 8.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   207 DFEYLASQTLTKQAWAYYSSGANDEVTHRENHNAYHRIFFKPKILVDVRKVDISTDMLGSHVDVPFYVSATALCKLgNPL 286
Cdd:PRK11197   8 DYRAAAQRRLPPFLFHYIDGGAYAEYTLRRNVEDLADIALRQRVLKDMSDLSLETTLFGEKLSMPVALAPVGLTGM-YAR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   287 EGEKDVARGCGQgvTKVPQMISTLASCSPEEIieaAPSDKQIQWYQLYVNSDRKITDDLVKNVEKLGVKALFVTVDAPSL 366
Cdd:PRK11197  87 RGEVQAARAADA--KGIPFTLSTVSVCPIEEV---APAIKRPMWFQLYVLRDRGFMRNALERAKAAGCSTLVFTVDMPVP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   367 GQREKDMKLKFSNTKAGPK----AMKKT----------------NVEESQGASRALSKFI-------DPSLTWKDIEELK 419
Cdd:PRK11197 162 GARYRDAHSGMSGPNAAMRrylqAVTHPqwawdvglngrphdlgNISAYLGKPTGLEDYIgwlgnnfDPSISWKDLEWIR 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587   420 KKTKLPIVIKGVQRTEDVIKAAEIGVSGVVLSNHGGRQLDFSRAPIEVLAetmPILEQrnLKDKLEVFVDGGVRRGTDVL 499
Cdd:PRK11197 242 DFWDGPMVIKGILDPEDARDAVRFGADGIVVSNHGGRQLDGVLSSARALP---AIADA--VKGDITILADSGIRNGLDVV 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 6323587   500 KALCLGAKGVGLGRPFLYANSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAELKPDLL 558
Cdd:PRK11197 317 RMIALGADTVLLGRAFVYALAAAGQAGVANLLDLIEKEMRVAMTLTGAKSISEITRDSL 375
Cyt-b5 pfam00173
Cytochrome b5-like Heme/Steroid binding domain; This family includes heme binding domains from ...
 92-164 1.77e-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: 1.77e-26
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6323587     92 SPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFE-PLHAPNVIDKYIApEKKLGPL 164
Cdd:pfam00173   1 TLEELSKHNGDGDCWVAINGKVYDVTKFLKEHPGGEDVILSAAGKDATDAFEaIGHSEDAAEKLLK-KYRIGEL 73
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
 272-513 3.10e-20

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: 89.18  E-value: 3.10e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  272 FYVSATALCKLGNPLEgekdVARGCGQGvTKVPQMISTLASCSPEE-------IIEAAPSDKQIQWYQLYVNSDRKITDD 344
Cdd:cd04722   1 VILALLAGGPSGDPVE----LAKAAAEA-GADAIIVGTRSSDPEEAetddkevLKEVAAETDLPLGVQLAINDAAAAVDI 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  345 LVKNVEKLGVKALFVTVDAPSLgqrekdmklkfsntkagpkamkktnveesqgasralskfidPSLTWKDIEELKKKT-K 423
Cdd:cd04722  76 AAAAARAAGADGVEIHGAVGYL-----------------------------------------AREDLELIRELREAVpD 114

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  424 LPIVIKGVQRTEDV-IKAAEIGVSGVVLSNHGGRQLDFSRAPIevlaeTMPILEQRNLKDKLEVFVDGGVRRGTDVLKAL 502
Cdd:cd04722 115 VKVVVKLSPTGELAaAAAEEAGVDEVGLGNGGGGGGGRDAVPI-----ADLLLILAKRGSKVPVIAGGGINDPEDAAEAL 189

                       250
                ....*....|.
gi 6323587  503 CLGAKGVGLGR 513
Cdd:cd04722 190 ALGADGVIVGS 200
CYB5 COG5274
Cytochrome b involved in lipid metabolism [Energy production and conversion, Lipid transport ...
 91-166 8.77e-20

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


Pssm-ID: 444085 [Multi-domain]  Cd Length: 93  Bit Score: 84.32  E-value: 8.77e-20
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 6323587   91 ISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPLHA-PNVIDKYIApEKKLGPLQG 166
Cdd:COG5274  18 YTLAEVATHNTLSDCWMAIDGNVYDLTEYIPKHPGGEAVILRWCGKDATEAFNTKHPhSPKAERLLE-SYRIGRLAQ 93
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
 415-554 3.04e-19

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: 89.09  E-value: 3.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  415 IEELKKKTKLPIVIK----GVQRtEDVIKAAEIGVSGVVLSNHGGrqLDFSRapIEV---------LAET-----MP--- 473
Cdd:cd02811 170 IEELVKALSVPVIVKevgfGISR-ETAKRLADAGVKAIDVAGAGG--TSWAR--VENyrakdsdqrLAEYfadwgIPtaa 244

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  474 -ILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYAnSCYGRNGVEKAIEILRDEIEMSMRLLGVTSIAE 552
Cdd:cd02811 245 sLLEVRSALPDLPLIASGGIRNGLDIAKALALGADLVGMAGPFLKA-ALEGEEAVIETIEQIIEELRTAMFLTGAKNLAE 323


                ..
gi 6323587  553 LK 554
Cdd:cd02811 324 LK 325
PLN02252 PLN02252
nitrate reductase [NADPH]
 91-146 1.67e-17

nitrate reductase [NADPH]


Pssm-ID: 215141 [Multi-domain]  Cd Length: 888  Bit Score: 86.65  E-value: 1.67e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 6323587    91 ISPAEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQDVIKFNAGKDVTAIFEPLH 146
Cdd:PLN02252 520 YTMSEVRKHNSEDSCWIVVHGHVYDCTRFLKDHPGGADSILINAGTDCTEEFDAIH 575
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 415-560 1.31e-11

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: 66.41  E-value: 1.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  415 IEELKKKT-KLPIVIK-----GVQRTEDVIKAAE---IGVSG---------VVLSNHGGRqldfsraPIEV-LAETMPIL 475
Cdd:cd02808 205 IEDLREATgGKPIGVKlvaghGEGDIAAGVAAAGadfITIDGaeggtgaapLTFIDHVGL-------PTELgLARAHQAL 277

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  476 EQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYA-----------NSC-YG----------RNGVEKA--- 530
Cdd:cd02808 278 VKNGLRDRVSLIASGGLRTGADVAKALALGADAVGIGTAALIAlgciqarkchtNTCpVGvatqdpelrrRLDVEGKaer 357

                       170       180       190
                ....*....|....*....|....*....|....*
gi 6323587  531 ----IEILRDEIEMSMRLLGVTSIAELKP-DLLDL 560
Cdd:cd02808 358 vanyLKSLAEELRELAAALGKRSLELLGRsDLLAL 392
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 415-521 6.95e-11

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: 64.28  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    415 IEELKKKT-KLPIVIK-GVQRTEDVIKA--AEIGVSGVVLSNHGG-------RQLDFSRAPIEV-LAETMPILEQRNLKD 482
Cdd:pfam01645 193 IYDLKEINpKAPISVKlVSGHGVGTIAAgvAKAGADIILIDGYDGgtgaspkTSIKHAGLPWELaLAEAHQTLKENGLRD 272

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 6323587    483 KLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSC 521
Cdd:pfam01645 273 RVSLIADGGLRTGADVAKAAALGADAVYIGTAALIALGC 311
PLN03198 PLN03198
delta6-acyl-lipid desaturase; Provisional
 94-173 2.36e-10

delta6-acyl-lipid desaturase; Provisional


Pssm-ID: 178739 [Multi-domain]  Cd Length: 526  Bit Score: 63.17  E-value: 2.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    94 AEVAKHNKPDDCWVVINGYVYDLTRFLPNHPGGQdVIKFNAGKDVTAIFEPLHAPN----VIDKYIAPEKKLGPlqgsmP 169
Cdd:PLN03198 109 SEVAAHNKPNDCWIVIKNKVYDVSDFAAEHPGGS-VISTYFGRDGTDAFSSFHAAStwkiLQDFYIGDVDNVEP-----T 182


                 ....
gi 6323587   170 PELV 173
Cdd:PLN03198 183 PELL 186
PLN03199 PLN03199
delta6-acyl-lipid desaturase-like protein; Provisional
 83-148 1.33e-09

delta6-acyl-lipid desaturase-like protein; Provisional


Pssm-ID: 178740 [Multi-domain]  Cd Length: 485  Bit Score: 60.82  E-value: 1.33e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 6323587    83 KLDMNKQKISPAEVAKHNKPDDCWVVINGYVYDLTRFLpNHPGGQdVIKFNAGKDVTAIFEPLHAP 148
Cdd:PLN03199  18 KLAEKPQKISWQEVKKHASPDDAWIIHQNKVYDVSNWH-DHPGGA-VIFTHAGDDMTDIFAAFHAP 81
GltB2 COG0069
Glutamate synthase domain 2 [Amino acid transport and metabolism]; Glutamate synthase domain 2 ...
 429-518 3.89e-06

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: 49.86  E-value: 3.89e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  429 KGVQRTEdvIKAAEIGVSG---------VVLSNHGGrqldfsrAPIEV-LAETMPILEQRNLKDKLEVFVDGGVRRGTDV 498
Cdd:COG0069 385 KGVAKTG--AYADFITIDGgeggtgaapLESIKHAG-------LPWELgLAEVHQTLVGNGLRDRIRLIADGKLKTGRDV 455

                        90       100
                ....*....|....*....|
gi 6323587  499 LKALCLGAKGVGLGRPFLYA 518
Cdd:COG0069 456 AIAAALGADEFGFARAFMVA 475
gltB PRK11750
glutamate synthase subunit alpha; Provisional
 468-560 4.31e-05

glutamate synthase subunit alpha; Provisional


Pssm-ID: 236968 [Multi-domain]  Cd Length: 1485  Bit Score: 46.79  E-value: 4.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587    468 LAETMPILEQRNLKDKLEVFVDGGVRRGTDVLKALCLGAKGVGLGRPFLYANSC-YGR--------NGVEKAIEILRDE- 537
Cdd:PRK11750 1052 LAETHQALVANGLRHKIRLQVDGGLKTGLDVIKAAILGAESFGFGTGPMVALGCkYLRichlnncaTGVATQDEKLRKNh 1131

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 6323587    538 ----IEMS--------------MRLLGVTSIAEL--KPDLLDL 560
Cdd:PRK11750 1132 yhglPEMVmnyfefiaeetrewMAQLGVRSLEDLigRTDLLEE 1174
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 435-516 2.75e-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: 39.77  E-value: 2.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6323587  435 EDVIKAAEIGVSGVVLSNH--GGRQLDFSRAPIEVLAEtmpileqrnLKDKLEVFV--DGGVRRGTDVLKALCLGAKGVG 510
Cdd:cd04730 113 EEARKAEAAGADALVAQGAeaGGHRGTFDIGTFALVPE---------VRDAVDIPViaAGGIADGRGIAAALALGADGVQ 183


                ....*.
gi 6323587  511 LGRPFL 516
Cdd:cd04730 184 MGTRFL 189
 
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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