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Conserved domains on  [gi|1152391755|ref|WP_078259218|]
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FAD-dependent oxidoreductase [Helicobacter pylori]

Protein Classification

Rossmann-fold NAD(P)-binding domain-containing protein( domain architecture ID 229380)

Rossmann-fold NAD(P)-binding domain-containing protein may function as an oxidoreductase

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NADB_Rossmann super family cl21454
Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a ...
2-443 9.08e-178

Rossmann-fold NAD(P)(+)-binding proteins; A large family of proteins that share a Rossmann-fold NAD(P)H/NAD(P)(+) binding (NADB) domain. The NADB domain is found in numerous dehydrogenases of metabolic pathways such as glycolysis, and many other redox enzymes. NAD binding involves numerous hydrogen-bonds and van der Waals contacts, in particular H-bonding of residues in a turn between the first strand and the subsequent helix of the Rossmann-fold topology. Characteristically, this turn exhibits a consensus binding pattern similar to GXGXXG, in which the first 2 glycines participate in NAD(P)-binding, and the third facilitates close packing of the helix to the beta-strand. Typically, proteins in this family contain a second domain in addition to the NADB domain, which is responsible for specifically binding a substrate and catalyzing a particular enzymatic reaction.


The actual alignment was detected with superfamily member PTZ00383:

Pssm-ID: 473865 [Multi-domain]  Cd Length: 497  Bit Score: 506.58  E-value: 9.08e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   2 SMEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAKKVRLSAYKTRQ 81
Cdd:PTZ00383   43 SDVYDVVIVGGGVTGTALFYTLSKFTNLKKIALIERRSDFALVASHGKNNSQTIHCGDIETNYTLEKARKVKRQADMLRN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  82 YA--LNKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVILGANGIDRHENIIGHGYQ 159
Cdd:PTZ00383  123 YLtkLPPSERDSIIFKMQKMVLGVGEKECEFLEKRYPVFKELFPSMQLLDKKEIHRVEPRVVLKNNHTLREEPLAALYVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 160 KDWSTMNFAKLSENFVEEA--LKLKPNNQV--FLNFKVKKIEKRDDTYALTSEDAEEVYAKFVLVNAGSYALPLAQSMGY 235
Cdd:PTZ00383  203 NELTTVDYQKLSESFVKHArrDALVPGKKIsiNLNTEVLNIERSNDSLYKIHTNRGEIRARFVVVSACGYSLLFAQKMGY 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 236 GLDLGCLPVAGSFYFVPNLLRGKVYTVQNPKLPFAAVHGDPDAVIKGKTRIGPTALTMPKLERNKCWLKGISLELLKMDL 315
Cdd:PTZ00383  283 GLEYSCLPVAGSFYFSGNILNGKVYTVQNPALPFAAVHGDPDIIAKGKTRFGPTALPLPLLERYNMSSLPDFLKVWNPDL 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 316 NrdVFKIAFDLMSDKEIRNYVFKNMVFELPVIGKRKFLKDAQKIIPSLSLEDLEYAHGFGEVRPQVLDRTKRKLELGEKK 395
Cdd:PTZ00383  363 N--LLAVYFDLFKDSTMRKYVLRNFLFEVPLLNKYLFLKDARKIVPSLTRKDLRYCVGYGGVRPQLIDKVSKKLLLGEGK 440
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1152391755 396 ICTHKGITFNMTPSPGATSCLQNALVDSQEIAAYLGESFELERFYKDL 443
Cdd:PTZ00383  441 IDPGKGIIFNITPSPGATTCLGNAESDMREICERLGATIDEKGVKKTL 488
 
Name Accession Description Interval E-value
PTZ00383 PTZ00383
malate:quinone oxidoreductase; Provisional
2-443 9.08e-178

malate:quinone oxidoreductase; Provisional


Pssm-ID: 240393 [Multi-domain]  Cd Length: 497  Bit Score: 506.58  E-value: 9.08e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   2 SMEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAKKVRLSAYKTRQ 81
Cdd:PTZ00383   43 SDVYDVVIVGGGVTGTALFYTLSKFTNLKKIALIERRSDFALVASHGKNNSQTIHCGDIETNYTLEKARKVKRQADMLRN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  82 YA--LNKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVILGANGIDRHENIIGHGYQ 159
Cdd:PTZ00383  123 YLtkLPPSERDSIIFKMQKMVLGVGEKECEFLEKRYPVFKELFPSMQLLDKKEIHRVEPRVVLKNNHTLREEPLAALYVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 160 KDWSTMNFAKLSENFVEEA--LKLKPNNQV--FLNFKVKKIEKRDDTYALTSEDAEEVYAKFVLVNAGSYALPLAQSMGY 235
Cdd:PTZ00383  203 NELTTVDYQKLSESFVKHArrDALVPGKKIsiNLNTEVLNIERSNDSLYKIHTNRGEIRARFVVVSACGYSLLFAQKMGY 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 236 GLDLGCLPVAGSFYFVPNLLRGKVYTVQNPKLPFAAVHGDPDAVIKGKTRIGPTALTMPKLERNKCWLKGISLELLKMDL 315
Cdd:PTZ00383  283 GLEYSCLPVAGSFYFSGNILNGKVYTVQNPALPFAAVHGDPDIIAKGKTRFGPTALPLPLLERYNMSSLPDFLKVWNPDL 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 316 NrdVFKIAFDLMSDKEIRNYVFKNMVFELPVIGKRKFLKDAQKIIPSLSLEDLEYAHGFGEVRPQVLDRTKRKLELGEKK 395
Cdd:PTZ00383  363 N--LLAVYFDLFKDSTMRKYVLRNFLFEVPLLNKYLFLKDARKIVPSLTRKDLRYCVGYGGVRPQLIDKVSKKLLLGEGK 440
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1152391755 396 ICTHKGITFNMTPSPGATSCLQNALVDSQEIAAYLGESFELERFYKDL 443
Cdd:PTZ00383  441 IDPGKGIIFNITPSPGATTCLGNAESDMREICERLGATIDEKGVKKTL 488
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-430 4.64e-96

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 295.13  E-value: 4.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   1 MSMEFDAVIIGGGVSGCATFYTLSEYSSLKrVAIVEKCSKLAQISSsaKANSQTIHDGSIETNYTpEKAKKVRLSAYKTR 80
Cdd:COG0579     1 MMEMYDVVIIGAGIVGLALARELSRYEDLK-VLVLEKEDDVAQESS--GNNSGVIHAGLYYTPGS-LKARLCVEGNELFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  81 QYALNKGLQNEvifETQKMAIGVGDEECEFMKKRYESFKEIFV-GLEEFDKQKIKELEPNV---ILGANGIDrheniigH 156
Cdd:COG0579    77 ELCRELGIPFK---RCGKLVVATGEEEVAFLEKLYERGKANGVpGLEILDREELRELEPLLsdeGVAALYSP-------S 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 157 GYqkdwsTMNFAKLSENFVEEALKlkPNNQVFLNFKVKKIEKRDDTYALTSeDAEEVYAKFVLVNAGSYALPLAQSMGYG 236
Cdd:COG0579   147 TG-----IVDPGALTRALAENAEA--NGVELLLNTEVTGIEREGDGWEVTT-NGGTIRARFVINAAGLYADRLAQMAGIG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 237 LDLGCLPVAGSFYFVPN---LLRGKVYTVQNPKLPFAAVHGDPDavIKGKTRIGPTALTMPKLErnkcwlkgislellkm 313
Cdd:COG0579   219 KDFGIFPVKGEYLVLDKpaeLVNAKVYPVPDPGAPFLGVHLTRT--IDGNLLFGPNAVFVPKKE---------------- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 314 DLNRDVFKIAFDLMSDKEIRNYVFKNMVFELPVIGKRKFLKDAQKIIPSLSLEDLEYAhgFGEVRPQVLDRTKrKLELGE 393
Cdd:COG0579   281 DSLLDLFESLRFPNFWPMLAKNLLTKYLESVTSLSKEAFLEALRKYVPELPDEDLIPA--FAGIRAQIIKPDG-DFVIEE 357
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1152391755 394 KKIctHKGITFNMTPSPGATSCLQNALVDSQEIAAYL 430
Cdd:COG0579   358 ADD--PGSIHVLGIESPGATSALAIAEHVAELLPEKL 392
Mqo pfam06039
Malate:quinone oxidoreductase (Mqo); This family consists of several bacterial Malate:quinone ...
4-248 2.77e-22

Malate:quinone oxidoreductase (Mqo); This family consists of several bacterial Malate:quinone oxidoreductase (Mqo) proteins (EC:1.1.99.16). Mqo takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. The enzyme is therefore called malate:quinone oxidoreductase, abbreviated to Mqo. Mqo is a peripheral membrane protein and can be released from the membrane by addition of chelators.


Pssm-ID: 461809  Cd Length: 488  Bit Score: 99.05  E-value: 2.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   4 EFDAVIIGGGVSGcATFYTLseyssLK------RVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAK-KVRLS- 75
Cdd:pfam06039   1 KVDVVLIGAGIMS-ATLGTL-----LKelepdwSITVFERLDAVAAESSNAWNNAGTGHSALCELNYTPEKPDgSIDISk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  76 AYK-------TRQ---YALNKG-LQN--EVIFETQKMAIGVGDEECEFMKKRYESFKE--IFVGLeEF--DKQKIKELEP 138
Cdd:pfam06039  75 AVKineqfevSRQfwaYLVENGvLPDpkSFINPVPHMSFVWGEDNVAFLRKRYEALSAhpLFEGM-EFseDPAQIAEWAP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 139 nviLGANGIDRHENI----IGHGyqkdwSTMNFAKLSENFVeEALKLKPNNQVFLNFKVKKIEKRDD-TYALTSED---- 209
Cdd:pfam06039 154 ---LMMEGRDPSEPVaatrIELG-----TDVNFGALTRQLV-AYLQKQPGVELHYGHEVTDLKRNSDgRWRVKVKDlntg 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1152391755 210 -AEEVYAKFVLVNAGSYALPLAQ------SMGYGldlGcLPVAGSF 248
Cdd:pfam06039 225 eKRTVRAKFVFIGAGGGALPLLQksgipeAKGYG---G-FPVSGQF 266
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
5-140 2.94e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 39.81  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   5 FDAVIIGGGVSGCATFYTLSEYSslKRVAIVEKCSkLAQISSSAKANSQTIHDGSIETNYTPekakkVRLSAYKTrQYAL 84
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHG--KKTLLLEQFD-LPHSRGSSHGQSRIIRKAYPEDFYTP-----MMLECYQL-WAQL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1152391755  85 NKGLQNEVIFETQKMAIGVGDEecEFMKKRYESFKEIFVGLEEFDKQKIKELEPNV 140
Cdd:TIGR01377  72 EKEAGTKLHRQTGLLLLGPKEN--QFLKTIQATLSRHGLEHELLSSKQLKQRFPNI 125
 
Name Accession Description Interval E-value
PTZ00383 PTZ00383
malate:quinone oxidoreductase; Provisional
2-443 9.08e-178

malate:quinone oxidoreductase; Provisional


Pssm-ID: 240393 [Multi-domain]  Cd Length: 497  Bit Score: 506.58  E-value: 9.08e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   2 SMEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAKKVRLSAYKTRQ 81
Cdd:PTZ00383   43 SDVYDVVIVGGGVTGTALFYTLSKFTNLKKIALIERRSDFALVASHGKNNSQTIHCGDIETNYTLEKARKVKRQADMLRN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  82 YA--LNKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVILGANGIDRHENIIGHGYQ 159
Cdd:PTZ00383  123 YLtkLPPSERDSIIFKMQKMVLGVGEKECEFLEKRYPVFKELFPSMQLLDKKEIHRVEPRVVLKNNHTLREEPLAALYVP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 160 KDWSTMNFAKLSENFVEEA--LKLKPNNQV--FLNFKVKKIEKRDDTYALTSEDAEEVYAKFVLVNAGSYALPLAQSMGY 235
Cdd:PTZ00383  203 NELTTVDYQKLSESFVKHArrDALVPGKKIsiNLNTEVLNIERSNDSLYKIHTNRGEIRARFVVVSACGYSLLFAQKMGY 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 236 GLDLGCLPVAGSFYFVPNLLRGKVYTVQNPKLPFAAVHGDPDAVIKGKTRIGPTALTMPKLERNKCWLKGISLELLKMDL 315
Cdd:PTZ00383  283 GLEYSCLPVAGSFYFSGNILNGKVYTVQNPALPFAAVHGDPDIIAKGKTRFGPTALPLPLLERYNMSSLPDFLKVWNPDL 362
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 316 NrdVFKIAFDLMSDKEIRNYVFKNMVFELPVIGKRKFLKDAQKIIPSLSLEDLEYAHGFGEVRPQVLDRTKRKLELGEKK 395
Cdd:PTZ00383  363 N--LLAVYFDLFKDSTMRKYVLRNFLFEVPLLNKYLFLKDARKIVPSLTRKDLRYCVGYGGVRPQLIDKVSKKLLLGEGK 440
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 1152391755 396 ICTHKGITFNMTPSPGATSCLQNALVDSQEIAAYLGESFELERFYKDL 443
Cdd:PTZ00383  441 IDPGKGIIFNITPSPGATTCLGNAESDMREICERLGATIDEKGVKKTL 488
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-430 4.64e-96

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 295.13  E-value: 4.64e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   1 MSMEFDAVIIGGGVSGCATFYTLSEYSSLKrVAIVEKCSKLAQISSsaKANSQTIHDGSIETNYTpEKAKKVRLSAYKTR 80
Cdd:COG0579     1 MMEMYDVVIIGAGIVGLALARELSRYEDLK-VLVLEKEDDVAQESS--GNNSGVIHAGLYYTPGS-LKARLCVEGNELFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  81 QYALNKGLQNEvifETQKMAIGVGDEECEFMKKRYESFKEIFV-GLEEFDKQKIKELEPNV---ILGANGIDrheniigH 156
Cdd:COG0579    77 ELCRELGIPFK---RCGKLVVATGEEEVAFLEKLYERGKANGVpGLEILDREELRELEPLLsdeGVAALYSP-------S 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 157 GYqkdwsTMNFAKLSENFVEEALKlkPNNQVFLNFKVKKIEKRDDTYALTSeDAEEVYAKFVLVNAGSYALPLAQSMGYG 236
Cdd:COG0579   147 TG-----IVDPGALTRALAENAEA--NGVELLLNTEVTGIEREGDGWEVTT-NGGTIRARFVINAAGLYADRLAQMAGIG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 237 LDLGCLPVAGSFYFVPN---LLRGKVYTVQNPKLPFAAVHGDPDavIKGKTRIGPTALTMPKLErnkcwlkgislellkm 313
Cdd:COG0579   219 KDFGIFPVKGEYLVLDKpaeLVNAKVYPVPDPGAPFLGVHLTRT--IDGNLLFGPNAVFVPKKE---------------- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 314 DLNRDVFKIAFDLMSDKEIRNYVFKNMVFELPVIGKRKFLKDAQKIIPSLSLEDLEYAhgFGEVRPQVLDRTKrKLELGE 393
Cdd:COG0579   281 DSLLDLFESLRFPNFWPMLAKNLLTKYLESVTSLSKEAFLEALRKYVPELPDEDLIPA--FAGIRAQIIKPDG-DFVIEE 357
                         410       420       430
                  ....*....|....*....|....*....|....*..
gi 1152391755 394 KKIctHKGITFNMTPSPGATSCLQNALVDSQEIAAYL 430
Cdd:COG0579   358 ADD--PGSIHVLGIESPGATSALAIAEHVAELLPEKL 392
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
3-432 1.39e-25

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 107.60  E-value: 1.39e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   3 MEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEKCSKLAQISSSAkaNSQTIHDGsieTNYTP--EKAKKVRLSAYKTR 80
Cdd:PRK11728    1 AMYDFVIIGGGIVGLSTAMQLQERYPGARIAVLEKESGPARHQTGH--NSGVIHAG---VYYTPgsLKARFCRRGNEATK 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  81 QYALNKGLQNEvifETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVI-LGA-----NGIdrhenii 154
Cdd:PRK11728   76 AFCDQHGIPYE---ECGKLLVATSELELERMEALYERARANGIEVERLDAEELREREPNIRgLGAifvpsTGI------- 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 155 ghgyqkdwstMNFAKLSENFVEEALKLkpNNQVFLNFKVKKIEKRDDTYALTSEDAEeVYAKFVLVNAGSYALPLAQSMG 234
Cdd:PRK11728  146 ----------VDYRAVAEAMAELIQAR--GGEIRLGAEVTALDEHANGVVVRTTQGE-YEARTLINCAGLMSDRLAKMAG 212
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 235 YGLDLGCLPVAGSFYFVP----NLLRGKVYTVQNPKLPFAAVHGDPDavIKGKTRIGPTALTMPKLERNKcwlkgislel 310
Cdd:PRK11728  213 LEPDFRIVPFRGEYYRLApeknQLVNHLIYPVPDPAFPFLGVHLTRM--IDGSVTVGPNAVLAFKREGYR---------- 280
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 311 lKMDLN-RDVFKIA----FDLMSDKEIRNYV--FKNMVFelpvigKRKFLKDAQKIIPSLSLEDLEYAHGfGeVRPQVLD 383
Cdd:PRK11728  281 -KRDFSlRDLLEILtypgFWKLAQKHWRSGLgeMKNSLS------KSGYLRLVQKYCPSLTLSDLQPYPA-G-VRAQAVS 351
                         410       420       430       440       450       460
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1152391755 384 R------------TKRKLElgekkICthkgitfNmTPSPGATSCLqnalvdsqEIAAYLGE 432
Cdd:PRK11728  352 RdgklvddflfveTPRSLH-----VC-------N-APSPAATSSL--------PIGEHIVS 391
Mqo pfam06039
Malate:quinone oxidoreductase (Mqo); This family consists of several bacterial Malate:quinone ...
4-248 2.77e-22

Malate:quinone oxidoreductase (Mqo); This family consists of several bacterial Malate:quinone oxidoreductase (Mqo) proteins (EC:1.1.99.16). Mqo takes part in the citric acid cycle. It oxidizes L-malate to oxaloacetate and donates electrons to ubiquinone-1 and other artificial acceptors or, via the electron transfer chain, to oxygen. NAD is not an acceptor and the natural direct acceptor for the enzyme is most likely a quinone. The enzyme is therefore called malate:quinone oxidoreductase, abbreviated to Mqo. Mqo is a peripheral membrane protein and can be released from the membrane by addition of chelators.


Pssm-ID: 461809  Cd Length: 488  Bit Score: 99.05  E-value: 2.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   4 EFDAVIIGGGVSGcATFYTLseyssLK------RVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPEKAK-KVRLS- 75
Cdd:pfam06039   1 KVDVVLIGAGIMS-ATLGTL-----LKelepdwSITVFERLDAVAAESSNAWNNAGTGHSALCELNYTPEKPDgSIDISk 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  76 AYK-------TRQ---YALNKG-LQN--EVIFETQKMAIGVGDEECEFMKKRYESFKE--IFVGLeEF--DKQKIKELEP 138
Cdd:pfam06039  75 AVKineqfevSRQfwaYLVENGvLPDpkSFINPVPHMSFVWGEDNVAFLRKRYEALSAhpLFEGM-EFseDPAQIAEWAP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 139 nviLGANGIDRHENI----IGHGyqkdwSTMNFAKLSENFVeEALKLKPNNQVFLNFKVKKIEKRDD-TYALTSED---- 209
Cdd:pfam06039 154 ---LMMEGRDPSEPVaatrIELG-----TDVNFGALTRQLV-AYLQKQPGVELHYGHEVTDLKRNSDgRWRVKVKDlntg 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1152391755 210 -AEEVYAKFVLVNAGSYALPLAQ------SMGYGldlGcLPVAGSF 248
Cdd:pfam06039 225 eKRTVRAKFVFIGAGGGALPLLQksgipeAKGYG---G-FPVSGQF 266
PRK05257 PRK05257
malate:quinone oxidoreductase; Validated
4-248 3.18e-21

malate:quinone oxidoreductase; Validated


Pssm-ID: 179979  Cd Length: 494  Bit Score: 95.97  E-value: 3.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   4 EFDAVIIGGGVSGcATFYT-LSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTPE---------KAKKVR 73
Cdd:PRK05257    5 KTDVVLIGGGIMS-ATLGTlLKELEPEWSITMFERLDGVALESSNGWNNAGTGHSALCELNYTPEkadgsidisKAVKIN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  74 LSAYKTRQ---YALNKGLQNEV---IFETQKMAIGVGDEECEFMKKRYESFKE--IFVGLeEF--DKQKIKELEPnviLG 143
Cdd:PRK05257   84 EQFQISRQfwaYLVEKGVLPDPrsfINPVPHMSFVWGEDNVAFLKKRYEALKAnpLFAGM-EFseDPAQIKEWAP---LM 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 144 ANGIDRHENI----IGHGyqkdwSTMNFAKLSENFVeEALKLKPNNQVFLNFKVKKIEKRDD-TYALTSED-----AEEV 213
Cdd:PRK05257  160 MEGRDPSQKVaatrIEIG-----TDVNFGALTRQLV-GYLQKQGNFELQLGHEVRDIKRNDDgSWTVTVKDlktgeKRTV 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1152391755 214 YAKFVLVNAGSYALPLAQ------SMGYGldlGcLPVAGSF 248
Cdd:PRK05257  234 RAKFVFIGAGGGALPLLQksgipeAKGYG---G-FPVSGQF 270
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
6-290 7.64e-16

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


Pssm-ID: 426168 [Multi-domain]  Cd Length: 339  Bit Score: 78.21  E-value: 7.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   6 DAVIIGGGVSGCATFYTLSEYSslKRVAIVEKCSKLAQISSSakANSQTIHDGSietnYTPEKAKKVRLSAYKTRQYA-L 84
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRG--LSVTLLERGDDPGSGASG--RNAGLIHPGL----RYLEPSELARLALEALDLWEeL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  85 NKGLQNEVIFETQKMAIGVGDEECEFMKKRYESFKEIFVGLEEFDKQKIKELEPNVilgangidrhENIIGHGYQKDWST 164
Cdd:pfam01266  73 EEELGIDCGFRRCGVLVLARDEEEEALEKLLAALRRLGVPAELLDAEELRELEPLL----------PGLRGGLFYPDGGH 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 165 MNFAKLSENFVEEALKLkpNNQVFLNFKVKKIEKRDDTYALTSEDAeevyAKFVLVNAGSYALPLAQSmgyGLDLGCLPV 244
Cdd:pfam01266 143 VDPARLLRALARAAEAL--GVRIIEGTEVTGIEEEGGVWGVVTTGE----ADAVVNAAGAWADLLALP---GLRLPVRPV 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1152391755 245 AGS-FYFVPNLLRGKVYTVQNPKLPFAAVHGDPDAviKGKTRIGPTA 290
Cdd:pfam01266 214 RGQvLVLEPLPEALLILPVPITVDPGRGVYLRPRA--DGRLLLGGTD 258
PRK13339 PRK13339
malate:quinone oxidoreductase; Reviewed
6-299 2.36e-15

malate:quinone oxidoreductase; Reviewed


Pssm-ID: 183983  Cd Length: 497  Bit Score: 77.81  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   6 DAVIIGGGVSGcATFYT-LSEYSSLKRVAIVEKCSKLAQISSSAKANSQTIHDGSIETNYTP---------EKAKKVRLS 75
Cdd:PRK13339    8 DVVLVGAGILS-TTFGVlLKELDPDWNIEVVERLDSPAIESSNEWNNAGTGHAALCELNYTVqqpdgsidiEKAKEINEQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755  76 AYKTRQY----ALNKGLQN--EVIFETQKMAIGVGDEECEFMKKRYESFKE--IFVGLE--EfDKQKIKELEPNVILGan 145
Cdd:PRK13339   87 FEISKQFwghlVKSGTIGNprEFINPLPHISFVRGKNNVKFLKKRYEALKQhpMFDNIEytE-DIEVMAKWMPLMMPG-- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 146 gidRHENIIGHGYQKDWST-MNFAKLSENFVEEaLKLKPNNQVFLNFKVKKIEKRDD------TYALTSEDAEEVYAKFV 218
Cdd:PRK13339  164 ---REANEIMAASKIDEGTdVNFGALTRKLAKH-LESHPNAQVKYNHEVVDLERLSDggwevtVKDRNTGEKREQVADYV 239
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 219 LVNAGSYALPLAQSMGY--GLDLGCLPVAGSFYFV--PNLLR---GKVYTVQNPKLPFAAV-HGDpDAVIKGKTRI--GP 288
Cdd:PRK13339  240 FIGAGGGAIPLLQKSGIpeSKHLGGFPISGQFLRCtnPEVVKqhqAKVYSKEPVGTPPMTVpHLD-TRYIDGKRSLlfGP 318
                         330
                  ....*....|.
gi 1152391755 289 TALTMPKLERN 299
Cdd:PRK13339  319 YAGFGPKFLKH 329
PRK06854 PRK06854
adenylyl-sulfate reductase subunit alpha;
3-37 1.42e-03

adenylyl-sulfate reductase subunit alpha;


Pssm-ID: 235879 [Multi-domain]  Cd Length: 608  Bit Score: 41.06  E-value: 1.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1152391755   3 MEFDAVIIGGGVSGCATFYTLSEYSSLKRVAIVEK 37
Cdd:PRK06854   10 VDTDILIIGGGMAGCGAAFEAKEWAPDLKVLIVEK 44
soxA_mon TIGR01377
sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of ...
5-140 2.94e-03

sarcosine oxidase, monomeric form; Sarcosine oxidase catalyzes the oxidative demethylation of sarcosine to glycine. The reaction converts tetrahydrofolate to 5,10-methylene-tetrahydrofolate. The enzyme is known in monomeric and heterotetrameric (alpha,beta,gamma,delta) forms [Energy metabolism, Amino acids and amines]


Pssm-ID: 130444 [Multi-domain]  Cd Length: 380  Bit Score: 39.81  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755   5 FDAVIIGGGVSGCATFYTLSEYSslKRVAIVEKCSkLAQISSSAKANSQTIHDGSIETNYTPekakkVRLSAYKTrQYAL 84
Cdd:TIGR01377   1 FDVIVVGAGIMGCFAAYHLAKHG--KKTLLLEQFD-LPHSRGSSHGQSRIIRKAYPEDFYTP-----MMLECYQL-WAQL 71
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1152391755  85 NKGLQNEVIFETQKMAIGVGDEecEFMKKRYESFKEIFVGLEEFDKQKIKELEPNV 140
Cdd:TIGR01377  72 EKEAGTKLHRQTGLLLLGPKEN--QFLKTIQATLSRHGLEHELLSSKQLKQRFPNI 125
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
170-272 5.18e-03

Flavin containing amine oxidoreductase; This family consists of various amine oxidases, including maze polyamine oxidase (PAO)and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins.


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 39.01  E-value: 5.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1152391755 170 LSENFVEEALKLKpnnqVFLNFKVKKIEKRDDTYALTSEDAEEVYAKFVLVnagsyALPlaqsmgygldlgcLPVAGSFY 249
Cdd:pfam01593 208 LPDALAAQLLGGD----VRLNTRVRSIDREGDGVTVTLTDGEVIEADAVIV-----TVP-------------LGVLKRIL 265
                          90       100
                  ....*....|....*....|...
gi 1152391755 250 FVPNLLRGKVYTVQNpkLPFAAV 272
Cdd:pfam01593 266 FTPPLPPEKARAIRN--LGYGPV 286
BetA COG2303
Choline dehydrogenase or related flavoprotein [Lipid transport and metabolism, General ...
1-36 7.74e-03

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


Pssm-ID: 441878 [Multi-domain]  Cd Length: 531  Bit Score: 38.66  E-value: 7.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1152391755   1 MSMEFDAVIIGGGVSGCATFYTLSEYSSLkRVAIVE 36
Cdd:COG2303     1 MLEEYDYVIVGAGSAGCVLANRLSEDAGL-RVLLLE 35
 
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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