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Conserved domains on  [gi|1709980280|ref|WP_143330757|]
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NAD(P)/FAD-dependent oxidoreductase, partial [Cloacibacillus sp. An23]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11422994)

NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant

CATH:  3.50.50.60
EC:  1.-.-.-
Gene Ontology:  GO:0050660|GO:0016491
PubMed:  33684359

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
3-299 5.52e-45

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


:

Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 155.66  E-value: 5.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   3 AGAKVTVIESDlHPGGQLV--KQTHKFFGSRDeyaGTRGYKIADILLNEIASLEdkVTIKcNSTVTGYYPEDGVYTVMEG 80
Cdd:COG0492    22 AGLKTLVIEGG-EPGGQLAttKEIENYPGFPE---GISGPELAERLREQAERFG--AEIL-LEEVTSVDKDDGPFRVTTD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  81 EEDYYRvkAKKAVIATGAQERMIPFPNNDLP---GVYGAGAVQTLMnvygvTPGKRVLMVGAGNIGLIVSYQLAQAGVEV 157
Cdd:COG0492    95 DGTEYE--AKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDGFF-----FRGKDVVVVGGGDSALEEALYLTKFASKV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 158 AAVVEAmPKVGGYWVHAAKIRRL-GIPILLQHTVTEAIGDRVLEGAVIQELDDkfqlkGEPEKIDCDIICMAVGLAPTTE 236
Cdd:COG0492   168 TLIHRR-DELRASKILVERLRANpKIEVLWNTEVTEIEGDGRVEGVTLKNVKT-----GEEKELEVDGVFVAIGLKPNTE 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709980280 237 LFWQAGCEMKyvPQlcGYVPyRDKNMRTSNKDIWVAGDASG--IEEASAAMVEGRIAGHSAAKAL 299
Cdd:COG0492   242 LLKGLGLELD--ED--GYIV-VDEDMETSVPGVFAAGDVRDykYRQAATAAGEGAIAALSAARYL 301
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
3-299 5.52e-45

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 155.66  E-value: 5.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   3 AGAKVTVIESDlHPGGQLV--KQTHKFFGSRDeyaGTRGYKIADILLNEIASLEdkVTIKcNSTVTGYYPEDGVYTVMEG 80
Cdd:COG0492    22 AGLKTLVIEGG-EPGGQLAttKEIENYPGFPE---GISGPELAERLREQAERFG--AEIL-LEEVTSVDKDDGPFRVTTD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  81 EEDYYRvkAKKAVIATGAQERMIPFPNNDLP---GVYGAGAVQTLMnvygvTPGKRVLMVGAGNIGLIVSYQLAQAGVEV 157
Cdd:COG0492    95 DGTEYE--AKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDGFF-----FRGKDVVVVGGGDSALEEALYLTKFASKV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 158 AAVVEAmPKVGGYWVHAAKIRRL-GIPILLQHTVTEAIGDRVLEGAVIQELDDkfqlkGEPEKIDCDIICMAVGLAPTTE 236
Cdd:COG0492   168 TLIHRR-DELRASKILVERLRANpKIEVLWNTEVTEIEGDGRVEGVTLKNVKT-----GEEKELEVDGVFVAIGLKPNTE 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709980280 237 LFWQAGCEMKyvPQlcGYVPyRDKNMRTSNKDIWVAGDASG--IEEASAAMVEGRIAGHSAAKAL 299
Cdd:COG0492   242 LLKGLGLELD--ED--GYIV-VDEDMETSVPGVFAAGDVRDykYRQAATAAGEGAIAALSAARYL 301
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-288 1.85e-28

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 112.03  E-value: 1.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   1 AGAGAKVTVIESD-LHPGGQLVKqtHKFFG--SRDEYAGTRGYKIADILLNEIASLEDKVTIKCNSTVTGYYPEDGVYTV 77
Cdd:pfam07992  20 AQLGGKVTLIEDEgTCPYGGCVL--SKALLgaAEAPEIASLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  78 MEGEE-DYYRVKAKKAVIATGAQERMIPFPNNDLPGVYGagaVQTLMNVYGVTPG---KRVLMVGAGNIGLIVSYQLAQA 153
Cdd:pfam07992  98 EELVDgDGETITYDRLVIATGARPRLPPIPGVELNVGFL---VRTLDSAEALRLKllpKRVVVVGGGYIGVELAAALAKL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 154 GVEVaAVVEAMPKVG-------GYWVHAAkIRRLGIPILLQHTVTEAIGDrvlEGAVIQELDDKfqlkgepEKIDCDIIC 226
Cdd:pfam07992 175 GKEV-TLIEALDRLLrafdeeiSAALEKA-LEKNGVEVRLGTSVKEIIGD---GDGVEVILKDG-------TEIDADLVV 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709980280 227 MAVGLAPTTELFWQAGCEMKYVpqlcGYVPyRDKNMRTSNKDIWVAGDA--SGIEEASAAMVEG 288
Cdd:pfam07992 243 VAIGRRPNTELLEAAGLELDER----GGIV-VDEYLRTSVPGIYAAGDCrvGGPELAQNAVAQG 301
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 75-296 5.12e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 66.35  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  75 YTVMEGEEdyyRVKAKKAVIATGAqeRMIPFPNNDLP---GVYGAGAVQTLMNVygvtpGKRVLMVGAGNIGLivsyQLA 151
Cdd:PRK06292  120 NTVEVNGE---RIEAKNIVIATGS--RVPPIPGVWLIlgdRLLTSDDAFELDKL-----PKSLAVIGGGVIGL----ELG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 152 QA----GVEVAaVVEAMPKVGGYW---VHAAKIRRLG--IPILLQHTVTEAIGDRVlEGAVIQELDdkfqlkGEPEKIDC 222
Cdd:PRK06292  186 QAlsrlGVKVT-VFERGDRILPLEdpeVSKQAQKILSkeFKIKLGAKVTSVEKSGD-EKVEELEKG------GKTETIEA 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709980280 223 DIICMAVGLAPTTEL--FWQAGCEMKYVpqlcGYVPYrDKNMRTSNKDIWVAGDASGIEE-ASAAMVEGRIAGHSAA 296
Cdd:PRK06292  258 DYVLVATGRRPNTDGlgLENTGIELDER----GRPVV-DEHTQTSVPGIYAAGDVNGKPPlLHEAADEGRIAAENAA 329
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 3-299 7.34e-12

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 64.96  E-value: 7.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   3 AGAKVTVIESdLHPGGQLVKQThkffgSRDEYAG----TRGYKIADILLNEIASLEDKVTIKcnsTVTGYYPEDGVYTVM 78
Cdd:TIGR01292  21 ANLKPLLIEG-MEPGGQLTTTT-----EVENYPGfpegISGPELMEKMKEQAVKFGAEIIYE---EVIKVDKSDRPFKVY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  79 EGEEDYYrvKAKKAVIATGAQERMIPFPNNDLpgVYGAGAVqtlmnvYGVT------PGKRVLMVGAGNIGLIVSYQLAQ 152
Cdd:TIGR01292  92 TGDGKEY--TAKAVIIATGASARKLGIPGEDE--FWGRGVS------YCATcdgpffKNKEVAVVGGGDSAIEEALYLTR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 153 AGVEVaavveampkvggYWVH------AAKI------RRLGIPILLQHTVTEAIGDRVLEGAVIQELddkfqLKGEPEKI 220
Cdd:TIGR01292 162 IAKKV------------TLVHrrdkfrAEKIlldrlkKNPKIEFLWNSTVEEIVGDNKVEGVKIKNT-----VTGEEEEL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 221 DCDIICMAVGLAPTTELFWQAGCEMKYvpqlcGYVPYrDKNMRTSNKDIWVAGD--ASGIEEASAAMVEGRIAGHSAAKA 298
Cdd:TIGR01292 225 EVDGVFIAIGHEPNTELLKGLLELDEN-----GYIVT-DEGMRTSVPGVFAAGDvrDKGYRQAVTAAGDGCIAALSAERY 298


                  .
gi 1709980280 299 L 299
Cdd:TIGR01292 299 L 299
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 115-156 3.28e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 37.64  E-value: 3.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1709980280 115 GAGAVQTLMNVYGVTPGKRVLMVGAGNIGLIVSYQLAQAGVE 156
Cdd:cd01065     3 GLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAA 44
 
Name Accession Description Interval E-value
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
3-299 5.52e-45

Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 155.66  E-value: 5.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   3 AGAKVTVIESDlHPGGQLV--KQTHKFFGSRDeyaGTRGYKIADILLNEIASLEdkVTIKcNSTVTGYYPEDGVYTVMEG 80
Cdd:COG0492    22 AGLKTLVIEGG-EPGGQLAttKEIENYPGFPE---GISGPELAERLREQAERFG--AEIL-LEEVTSVDKDDGPFRVTTD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  81 EEDYYRvkAKKAVIATGAQERMIPFPNNDLP---GVYGAGAVQTLMnvygvTPGKRVLMVGAGNIGLIVSYQLAQAGVEV 157
Cdd:COG0492    95 DGTEYE--AKAVIIATGAGPRKLGLPGEEEFegrGVSYCATCDGFF-----FRGKDVVVVGGGDSALEEALYLTKFASKV 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 158 AAVVEAmPKVGGYWVHAAKIRRL-GIPILLQHTVTEAIGDRVLEGAVIQELDDkfqlkGEPEKIDCDIICMAVGLAPTTE 236
Cdd:COG0492   168 TLIHRR-DELRASKILVERLRANpKIEVLWNTEVTEIEGDGRVEGVTLKNVKT-----GEEKELEVDGVFVAIGLKPNTE 241

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709980280 237 LFWQAGCEMKyvPQlcGYVPyRDKNMRTSNKDIWVAGDASG--IEEASAAMVEGRIAGHSAAKAL 299
Cdd:COG0492   242 LLKGLGLELD--ED--GYIV-VDEDMETSVPGVFAAGDVRDykYRQAATAAGEGAIAALSAARYL 301
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
 1-324 3.51e-40

NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase [Lipid transport and metabolism];


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 143.80  E-value: 3.51e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   1 AGAGAKVTVIESDLHPGGQ---LVKqthkffgsrdeYAGTRGYKIADILLNEIASLEDK-VTIKCNSTVTGYYPEDGVYT 76
Cdd:COG0446     2 LGPDAEITVIEKGPHHSYQpcgLPY-----------YVGGGIKDPEDLLVRTPESFERKgIDVRTGTEVTAIDPEAKTVT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  77 VMEGEEDYYRvkakKAVIATGAQERMIPFPNNDLPGVYGAGAVQTLMNVYGV---TPGKRVLMVGAGNIGLIVSYQLAQA 153
Cdd:COG0446    71 LRDGETLSYD----KLVLATGARPRPPPIPGLDLPGVFTLRTLDDADALREAlkeFKGKRAVVIGGGPIGLELAEALRKR 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 154 GVEVaAVVEAMPKV-GGY------WVHAAkIRRLGIPILLQHTVTEAIGDrvlEGAVIQELDDkfqlkgepEKIDCDIIC 226
Cdd:COG0446   147 GLKV-TLVERAPRLlGVLdpemaaLLEEE-LREHGVELRLGETVVAIDGD---DKVAVTLTDG--------EEIPADLVV 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 227 MAVGLAPTTELFWQAGCEMkyvpQLCGYVPyRDKNMRTSNKDIWVAGDASG-----------IEEASAAMVEGRIAGHSA 295
Cdd:COG0446   214 VAPGVRPNTELAKDAGLAL----GERGWIK-VDETLQTSDPDVYAAGDCAEvphpvtgktvyIPLASAANKQGRVAAENI 288

                         330       340
                  ....*....|....*....|....*....
gi 1709980280 296 AkalGLTVDDDKFHEYWERLGHLRAGEVG 324
Cdd:COG0446   289 L---GGPAPFPGLGTFISKVFDLCIASTG 314
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 1-288 1.85e-28

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 112.03  E-value: 1.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   1 AGAGAKVTVIESD-LHPGGQLVKqtHKFFG--SRDEYAGTRGYKIADILLNEIASLEDKVTIKCNSTVTGYYPEDGVYTV 77
Cdd:pfam07992  20 AQLGGKVTLIEDEgTCPYGGCVL--SKALLgaAEAPEIASLWADLYKRKEEVVKKLNNGIEVLLGTEVVSIDPGAKKVVL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  78 MEGEE-DYYRVKAKKAVIATGAQERMIPFPNNDLPGVYGagaVQTLMNVYGVTPG---KRVLMVGAGNIGLIVSYQLAQA 153
Cdd:pfam07992  98 EELVDgDGETITYDRLVIATGARPRLPPIPGVELNVGFL---VRTLDSAEALRLKllpKRVVVVGGGYIGVELAAALAKL 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 154 GVEVaAVVEAMPKVG-------GYWVHAAkIRRLGIPILLQHTVTEAIGDrvlEGAVIQELDDKfqlkgepEKIDCDIIC 226
Cdd:pfam07992 175 GKEV-TLIEALDRLLrafdeeiSAALEKA-LEKNGVEVRLGTSVKEIIGD---GDGVEVILKDG-------TEIDADLVV 242

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1709980280 227 MAVGLAPTTELFWQAGCEMKYVpqlcGYVPyRDKNMRTSNKDIWVAGDA--SGIEEASAAMVEG 288
Cdd:pfam07992 243 VAIGRRPNTELLEAAGLELDER----GGIV-VDEYLRTSVPGIYAAGDCrvGGPELAQNAVAQG 301
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
43-293 1.48e-24

NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 102.91  E-value: 1.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  43 ADILLNEIASLEDK-VTIKCNSTVTGYYPEDGVYTVMEGEEdyyrVKAKKAVIATGAQERMIPFPNNDLPGVYGagaVQT 121
Cdd:COG1251    56 EDLLLRPADFYEENgIDLRLGTRVTAIDRAARTVTLADGET----LPYDKLVLATGSRPRVPPIPGADLPGVFT---LRT 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 122 LMNVYG----VTPGKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMP--------KVGGYWVHAAkIRRLGIPILLQHT 189
Cdd:COG1251   129 LDDADAlraaLAPGKRVVVIGGGLIGLEAAAALRKRGLEV-TVVERAPrllprqldEEAGALLQRL-LEALGVEVRLGTG 206

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 190 VTEAIGDRVLEGAviqELDDKfqlkgepEKIDCDIICMAVGLAPTTELFWQAGCEMKyvpqlcgyvpyR----DKNMRTS 265
Cdd:COG1251   207 VTEIEGDDRVTGV---RLADG-------EELPADLVVVAIGVRPNTELARAAGLAVD-----------RgivvDDYLRTS 265

                         250       260
                  ....*....|....*....|....*...
gi 1709980280 266 NKDIWVAGDasgieeasAAMVEGRIAGH 293
Cdd:COG1251   266 DPDIYAAGD--------CAEHPGPVYGR 285
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
 86-296 1.96e-15

Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase [Energy production and conversion]; Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex or glutathione oxidoreductase is part of the Pathway/BioSystem: Glycine cleavagePyruvate oxidation


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 76.66  E-value: 1.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  86 RVKAKKAVIATGAQERMIPFPNNDLPGVY---GAGAVQTLmnvygvtPgKRVLMVGAGNIGLivsyQLAQA----GVEVa 158
Cdd:COG1249   128 TLTADHIVIATGSRPRVPPIPGLDEVRVLtsdEALELEEL-------P-KSLVVIGGGYIGL----EFAQIfarlGSEV- 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 159 AVVEAMPKVGGYW----VHAAK--IRRLGIPILLQHTVTEAigdRVLEGAVIQELDDkfqlKGEPEKIDCDIICMAVGLA 232
Cdd:COG1249   195 TLVERGDRLLPGEdpeiSEALEkaLEKEGIDILTGAKVTSV---EKTGDGVTVTLED----GGGEEAVEADKVLVATGRR 267

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1709980280 233 PTTELFwqaGCE---MKYVPQlcGYVPYrDKNMRTSNKDIWVAGDASGIEE-ASAAMVEGRIAGHSAA 296
Cdd:COG1249   268 PNTDGL---GLEaagVELDER--GGIKV-DEYLRTSVPGIYAIGDVTGGPQlAHVASAEGRVAAENIL 329
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 1-294 7.35e-15

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 74.79  E-value: 7.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   1 AGAGAKVTVIESDLHPGGQLvkqthkffgsrdEYaGTRGYKI-ADILLNEIASLEDK-VTIKCNSTVtgyypeDGVYTVM 78
Cdd:COG0493   141 ARAGHEVTVFEALDKPGGLL------------RY-GIPEFRLpKDVLDREIELIEALgVEFRTNVEV------GKDITLD 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  79 EGEEDYyrvkakKAV-IATGAQE-RMIPFPNNDLPGVYGA-----GAVQTLMNVYGVTPGKRVLMVGAGNIGLIVSYQLA 151
Cdd:COG0493   202 ELLEEF------DAVfLATGAGKpRDLGIPGEDLKGVHSAmdfltAVNLGEAPDTILAVGKRVVVIGGGNTAMDCARTAL 275

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 152 QAGVEVAAVV-----EAMPkvggywvhaAKIRRL------GIPILLQHTVTEAIGDRvlEGAV---------IQELDDKF 211
Cdd:COG0493   276 RLGAESVTIVyrrtrEEMP---------ASKEEVeealeeGVEFLFLVAPVEIIGDE--NGRVtglecvrmeLGEPDESG 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 212 QLK-----GEPEKIDCDIICMAVGLAPTTElFWQAGCEMKYVPQlcGYVPYRDKNMRTSNKDIWVAGDA-SGIEEASAAM 285
Cdd:COG0493   345 RRRpvpieGSEFTLPADLVILAIGQTPDPS-GLEEELGLELDKR--GTIVVDEETYQTSLPGVFAGGDAvRGPSLVVWAI 421


                  ....*....
gi 1709980280 286 VEGRIAGHS 294
Cdd:COG0493   422 AEGRKAARA 430
PRK06292 PRK06292
dihydrolipoamide dehydrogenase; Validated
 75-296 5.12e-12

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235774 [Multi-domain]  Cd Length: 460  Bit Score: 66.35  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  75 YTVMEGEEdyyRVKAKKAVIATGAqeRMIPFPNNDLP---GVYGAGAVQTLMNVygvtpGKRVLMVGAGNIGLivsyQLA 151
Cdd:PRK06292  120 NTVEVNGE---RIEAKNIVIATGS--RVPPIPGVWLIlgdRLLTSDDAFELDKL-----PKSLAVIGGGVIGL----ELG 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 152 QA----GVEVAaVVEAMPKVGGYW---VHAAKIRRLG--IPILLQHTVTEAIGDRVlEGAVIQELDdkfqlkGEPEKIDC 222
Cdd:PRK06292  186 QAlsrlGVKVT-VFERGDRILPLEdpeVSKQAQKILSkeFKIKLGAKVTSVEKSGD-EKVEELEKG------GKTETIEA 257

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709980280 223 DIICMAVGLAPTTEL--FWQAGCEMKYVpqlcGYVPYrDKNMRTSNKDIWVAGDASGIEE-ASAAMVEGRIAGHSAA 296
Cdd:PRK06292  258 DYVLVATGRRPNTDGlgLENTGIELDER----GRPVV-DEHTQTSVPGIYAAGDVNGKPPlLHEAADEGRIAAENAA 329
TRX_reduct TIGR01292
thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a ...
 3-299 7.34e-12

thioredoxin-disulfide reductase; This model describes thioredoxin-disulfide reductase, a member of the pyridine nucleotide-disulphide oxidoreductases (pfam00070). [Energy metabolism, Electron transport]


Pssm-ID: 273540 [Multi-domain]  Cd Length: 299  Bit Score: 64.96  E-value: 7.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   3 AGAKVTVIESdLHPGGQLVKQThkffgSRDEYAG----TRGYKIADILLNEIASLEDKVTIKcnsTVTGYYPEDGVYTVM 78
Cdd:TIGR01292  21 ANLKPLLIEG-MEPGGQLTTTT-----EVENYPGfpegISGPELMEKMKEQAVKFGAEIIYE---EVIKVDKSDRPFKVY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  79 EGEEDYYrvKAKKAVIATGAQERMIPFPNNDLpgVYGAGAVqtlmnvYGVT------PGKRVLMVGAGNIGLIVSYQLAQ 152
Cdd:TIGR01292  92 TGDGKEY--TAKAVIIATGASARKLGIPGEDE--FWGRGVS------YCATcdgpffKNKEVAVVGGGDSAIEEALYLTR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 153 AGVEVaavveampkvggYWVH------AAKI------RRLGIPILLQHTVTEAIGDRVLEGAVIQELddkfqLKGEPEKI 220
Cdd:TIGR01292 162 IAKKV------------TLVHrrdkfrAEKIlldrlkKNPKIEFLWNSTVEEIVGDNKVEGVKIKNT-----VTGEEEEL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 221 DCDIICMAVGLAPTTELFWQAGCEMKYvpqlcGYVPYrDKNMRTSNKDIWVAGD--ASGIEEASAAMVEGRIAGHSAAKA 298
Cdd:TIGR01292 225 EVDGVFIAIGHEPNTELLKGLLELDEN-----GYIVT-DEGMRTSVPGVFAAGDvrDKGYRQAVTAAGDGCIAALSAERY 298


                  .
gi 1709980280 299 L 299
Cdd:TIGR01292 299 L 299
PRK09564 PRK09564
coenzyme A disulfide reductase; Reviewed
 82-278 4.83e-09

coenzyme A disulfide reductase; Reviewed


Pssm-ID: 181958 [Multi-domain]  Cd Length: 444  Bit Score: 57.36  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  82 EDYYrvkaKKAVIATGAQERMIPFPNNDLPGVYG------AGAVQTLMNVYGVtpgKRVLMVGAGNIGLIVSYQLAQAGV 155
Cdd:PRK09564  101 NDTY----DKLMIATGARPIIPPIKNINLENVYTlksmedGLALKELLKDEEI---KNIVIIGAGFIGLEAVEAAKHLGK 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 156 EVAAVVEAMPKVGGYW------VHAAKIRRLGIPILLQHTVTEAIGDRVLEGAVIQelddkfqlKGEpekIDCDIICMAV 229
Cdd:PRK09564  174 NVRIIQLEDRILPDSFdkeitdVMEEELRENGVELHLNEFVKSLIGEDKVEGVVTD--------KGE---YEADVVIVAT 242

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1709980280 230 GLAPTTELFWQAGCEMkyvpqLCGYVPYRDKNMRTSNKDIWVAGDASGI 278
Cdd:PRK09564  243 GVKPNTEFLEDTGLKT-----LKNGAIIVDEYGETSIENIYAAGDCATI 286
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 94-299 4.11e-08

bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate synthase;


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 54.75  E-value: 4.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  94 IATGAQ-ERMIPFPNNDLPGVYGAGAVQT---LMNVYG------VTPGKRVLMVGAGNIGLIVSYQLAQAGVEVAAVV-- 161
Cdd:PRK12778  523 IASGAGlPNFMNIPGENSNGVMSSNEYLTrvnLMDAASpdsdtpIKFGKKVAVVGGGNTAMDSARTAKRLGAERVTIVyr 602

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 162 ---EAMPKVGGYWVHAakiRRLGIPILLQHTVTEAIGDRvlEGAVIQELDDKFQLkGEP---------------EKIDCD 223
Cdd:PRK12778  603 rseEEMPARLEEVKHA---KEEGIEFLTLHNPIEYLADE--KGWVKQVVLQKMEL-GEPdasgrrrpvaipgstFTVDVD 676

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 224 IICMAVGLAPTTELfwqagceMKYVPQL----CGYVPYrDKNMRTSNKDIWVAGDasgIEEASAAMVEGRIAGHSAAKAL 299
Cdd:PRK12778  677 LVIVSVGVSPNPLV-------PSSIPGLelnrKGTIVV-DEEMQSSIPGIYAGGD---IVRGGATVILAMGDGKRAAAAI 745
PRK04965 PRK04965
NADH:flavorubredoxin reductase NorW;
54-279 7.96e-08

NADH:flavorubredoxin reductase NorW;


Pssm-ID: 179902 [Multi-domain]  Cd Length: 377  Bit Score: 53.38  E-value: 7.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  54 EDKVTIKCNSTVTGYYPEDGVYTVMEGEEDYyrvkaKKAVIATGAQermiPFpnndLPGVYGAGAVQTL--MNVYGVTPG 131
Cdd:PRK04965   70 QFNLRLFPHTWVTDIDAEAQVVKSQGNQWQY-----DKLVLATGAS----AF----VPPIPGRELMLTLnsQQEYRAAET 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 132 -----KRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEampkvggywvHAAKIRRLGIPIL----LQHTVTEAiGDRVLEGA 202
Cdd:PRK04965  137 qlrdaQRVLVVGGGLIGTELAMDLCRAGKAV-TLVD----------NAASLLASLMPPEvssrLQHRLTEM-GVHLLLKS 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 203 VIQEL---DDKFQL---KGEPEKIDCdIICmAVGLAPTTELFWQAGCEMKYvpqlcGYVPyrDKNMRTSNKDIWVAGDAS 276
Cdd:PRK04965  205 QLQGLektDSGIRAtldSGRSIEVDA-VIA-AAGLRPNTALARRAGLAVNR-----GIVV--DSYLQTSAPDIYALGDCA 275


                  ...
gi 1709980280 277 GIE 279
Cdd:PRK04965  276 EIN 278
PRK06416 PRK06416
dihydrolipoamide dehydrogenase; Reviewed
 66-296 6.87e-07

dihydrolipoamide dehydrogenase; Reviewed


Pssm-ID: 235798 [Multi-domain]  Cd Length: 462  Bit Score: 50.53  E-value: 6.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  66 TGYYPEDGVYTVME--GEEDYyrvKAKKAVIATGAQERMIP---FPNNDLPGVYGAGAVQTLmnvygvtPgKRVLMVGAG 140
Cdd:PRK06416  113 EAKLVDPNTVRVMTedGEQTY---TAKNIILATGSRPRELPgieIDGRVIWTSDEALNLDEV-------P-KSLVVIGGG 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 141 NIGLivsyQLAQA----GVEVaAVVEAMPK-VGGYWVHAAKI-----RRLGIPILLQHTVTEAIGDrvlEGAVIQELDDk 210
Cdd:PRK06416  182 YIGV----EFASAyaslGAEV-TIVEALPRiLPGEDKEISKLaeralKKRGIKIKTGAKAKKVEQT---DDGVTVTLED- 252

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 211 fqlKGEPEKIDCDIICMAVGLAPTTEL--FWQAGCEMKYvpqlcGYVPYrDKNMRTSNKDIWVAGDASG------IEEAS 282
Cdd:PRK06416  253 ---GGKEETLEADYVLVAVGRRPNTENlgLEELGVKTDR-----GFIEV-DEQLRTNVPNIYAIGDIVGgpmlahKASAE 323

                         250
                  ....*....|....
gi 1709980280 283 AAMVEGRIAGHSAA 296
Cdd:PRK06416  324 GIIAAEAIAGNPHP 337
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 1-294 1.07e-06

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 50.18  E-value: 1.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   1 AGAGAKVTVIESDLHPGGQLvkqthkffgsrdEYaGTRGYKIA-DILLNEIASLEDK-VTIKCNSTVtgyypeDGVYTVM 78
Cdd:PRK11749  160 ARKGYDVTIFEARDKAGGLL------------RY-GIPEFRLPkDIVDREVERLLKLgVEIRTNTEV------GRDITLD 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  79 EGEEDYyrvkakKAV-IATGAQE-RMIPFPNNDLPGVYGAgaVQTLMNV------YGVTPGKRVLMVGAGNIGLIVSYQL 150
Cdd:PRK11749  221 ELRAGY------DAVfIGTGAGLpRFLGIPGENLGGVYSA--VDFLTRVnqavadYDLPVGKRVVVIGGGNTAMDAARTA 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 151 AQAGVEVAAVV-----EAMPkvgGYW--VHAAKIRrlGIPILLQHTVTEAIGDRVLEGAVI---QELDD-------KFQL 213
Cdd:PRK11749  293 KRLGAESVTIVyrrgrEEMP---ASEeeVEHAKEE--GVEFEWLAAPVEILGDEGRVTGVEfvrMELGEpdasgrrRVPI 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 214 KGEPEKIDCDIICMAVGLAPTTELFW---QAGCEMKyvpqlcGYVPYRDKNMRTSNKDIWVAGDAsgIEEAS---AAMVE 287
Cdd:PRK11749  368 EGSEFTLPADLVIKAIGQTPNPLILSttpGLELNRW------GTIIADDETGRTSLPGVFAGGDI--VTGAAtvvWAVGD 439


                  ....*..
gi 1709980280 288 GRIAGHS 294
Cdd:PRK11749  440 GKDAAEA 446
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
 93-299 1.67e-06

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 49.22  E-value: 1.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  93 VIATGA-QERMIPFPNNDLPGVYGAGA--VQTLMNVYGVTP--------GKRVLMVGAGNIGLIVSYQLAQAGVEVAAVV 161
Cdd:PRK12770  123 LIATGTwKSRKLGIPGEDLPGVYSALEylFRIRAAKLGYLPwekvppveGKKVVVVGAGLTAVDAALEAVLLGAEKVYLA 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 162 ------EAmpKVGGYWVHaaKIRRLGIPILLQHTVTEAIGDRVLEGAVIQ-----ELDDKFQLKGEP-----EKIDCDII 225
Cdd:PRK12770  203 yrrtinEA--PAGKYEIE--RLIARGVEFLELVTPVRIIGEGRVEGVELAkmrlgEPDESGRPRPVPipgseFVLEADTV 278

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1709980280 226 CMAVGLAPTTElFWQAGCEMKYVPQlcGYVPYrDKNMRTSNKDIWVAGDA-SGIEEASAAMVEGRIAGHSAAKAL 299
Cdd:PRK12770  279 VFAIGEIPTPP-FAKECLGIELNRK--GEIVV-DEKHMTSREGVFAAGDVvTGPSKIGKAIKSGLRAAQSIHEWL 349
PRK06370 PRK06370
FAD-containing oxidoreductase;
76-277 2.20e-06

FAD-containing oxidoreductase;


Pssm-ID: 235787 [Multi-domain]  Cd Length: 463  Bit Score: 49.05  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  76 TVMEGEEdyyRVKAKKAVIATGAQERmIPfpnnDLPGVYGAGAV--QTLMNVyGVTPgKRVLMVGAGNIGLivsyQLAQA 153
Cdd:PRK06370  124 TVRVGGE---TLRAKRIFINTGARAA-IP----PIPGLDEVGYLtnETIFSL-DELP-EHLVIIGGGYIGL----EFAQM 189

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 154 ----GVEVAaVVEAMPKV-GGYWVHAAKI-----RRLGIPILLQhtvTEAIGDRVLEGAVIQELDdkfqLKGEPEKIDCD 223
Cdd:PRK06370  190 frrfGSEVT-VIERGPRLlPREDEDVAAAvreilEREGIDVRLN---AECIRVERDGDGIAVGLD----CNGGAPEITGS 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1709980280 224 IICMAVGLAPTTELFW--QAGCEMKYVpqlcGYVPYrDKNMRTSNKDIWVAGDASG 277
Cdd:PRK06370  262 HILVAVGRVPNTDDLGleAAGVETDAR----GYIKV-DDQLRTTNPGIYAAGDCNG 312
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 131-183 3.15e-05

NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport and metabolism, General function prediction only]; NADPH-dependent glutamate synthase beta chain or related oxidoreductase is part of the Pathway/BioSystem: Glutamine biosynthesis


Pssm-ID: 440259 [Multi-domain]  Cd Length: 434  Bit Score: 45.51  E-value: 3.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1709980280 131 GKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGGywvhaakIRRLGIP 183
Cdd:COG0493   121 GKKVAVVGSGPAGLAAAYQLARAGHEV-TVFEALDKPGG-------LLRYGIP 165
PRK09754 PRK09754
phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional
 46-274 3.87e-05

phenylpropionate dioxygenase ferredoxin reductase subunit; Provisional


Pssm-ID: 170080 [Multi-domain]  Cd Length: 396  Bit Score: 44.92  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  46 LLNEIASLEDKVTIKCNSTVTGYYPEDGVYTVMEGEEDYYrvkaKKAVIATGAQERmiPFPNNDLPG--VYG---AGAVQ 120
Cdd:PRK09754   62 VLPANWWQENNVHLHSGVTIKTLGRDTRELVLTNGESWHW----DQLFIATGAAAR--PLPLLDALGerCFTlrhAGDAA 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 121 TLMNVygVTPGKRVLMVGAGNIGLivsyQLAQAGVEVAAVVEAMPKvggywvhAAKIRRLGIPILLQHTV----TEAIGD 196
Cdd:PRK09754  136 RLREV--LQPERSVVIVGAGTIGL----ELAASATQRRCKVTVIEL-------AATVMGRNAPPPVQRYLlqrhQQAGVR 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 197 RVLEGAVIQELD-DKFQLK-GEPEKIDCDIICMAVGLAPTTELFWQAGCEMKyvpqlCGYVPyrDKNMRTSNKDIWVAGD 274
Cdd:PRK09754  203 ILLNNAIEHVVDgEKVELTlQSGETLQADVVIYGIGISANDQLAREANLDTA-----NGIVI--DEACRTCDPAIFAGGD 275
PRK12831 PRK12831
putative oxidoreductase; Provisional
 1-299 6.40e-05

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 44.62  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   1 AGAGAKVTVIESdLH-PGGQLVKQTHKFFGSRDeyagtrgykiaDILLNEIASLED-KVTIKCN----STVTgyypedgV 74
Cdd:PRK12831  160 AKMGYDVTIFEA-LHePGGVLVYGIPEFRLPKE-----------TVVKKEIENIKKlGVKIETNvvvgKTVT-------I 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  75 YTVMEgEEDYyrvkakKAV-IATGA-QERMIPFPNNDLPGVYGAGAVQT---LMNVYG------VTPGKRVLMVGAGNIG 143
Cdd:PRK12831  221 DELLE-EEGF------DAVfIGSGAgLPKFMGIPGENLNGVFSANEFLTrvnLMKAYKpeydtpIKVGKKVAVVGGGNVA 293

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 144 LIVSYQLAQAGVEVAAV----VEAMPkVGGYWVHAAKirRLGIPILLQHTVTEAIGDRvlEGAVIQELDDKFQLkGEPEK 219
Cdd:PRK12831  294 MDAARTALRLGAEVHIVyrrsEEELP-ARVEEVHHAK--EEGVIFDLLTNPVEILGDE--NGWVKGMKCIKMEL-GEPDA 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 220 ---------------IDCDIICMAVGLAPtTELFWQAGCEMKYVPQlcGYVPYRDKNMRTSNKDIWVAGDASgieEASAA 284
Cdd:PRK12831  368 sgrrrpveiegsefvLEVDTVIMSLGTSP-NPLISSTTKGLKINKR--GCIVADEETGLTSKEGVFAGGDAV---TGAAT 441

                         330
                  ....*....|....*
gi 1709980280 285 MVEGRIAGHSAAKAL 299
Cdd:PRK12831  442 VILAMGAGKKAAKAI 456
Pyr_redox pfam00070
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
 133-196 8.60e-05

Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain.


Pssm-ID: 425450 [Multi-domain]  Cd Length: 80  Bit Score: 40.65  E-value: 8.60e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 133 RVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGGYWVHAA------KIRRLGIPILLQHTVTEAIGD 196
Cdd:pfam00070   1 RVVVVGGGYIGLELAGALARLGSKV-TVVERRDRLLPGFDPEIakilqeKLEKNGIEFLLNTTVEAIEGN 69
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 4-230 2.41e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.94  E-value: 2.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280   4 GAKVTVIESDLHPGGQLvkqthkffgsrdEYaGTRGYKIA-DILLNEIASLED-KVTIKCNSTVtgyyPEDGVYTVMEGE 81
Cdd:PRK12771  160 GHAVTIFEAGPKLGGMM------------RY-GIPAYRLPrEVLDAEIQRILDlGVEVRLGVRV----GEDITLEQLEGE 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  82 EDyyrvkakkAV-IATGAQE-RMIPFPNNDLPGVYGAgaVQTLMNVYGVTP---GKRVLMVGAGNIGLIVSYQLAQAGVE 156
Cdd:PRK12771  223 FD--------AVfVAIGAQLgKRLPIPGEDAAGVLDA--VDFLRAVGEGEPpflGKRVVVIGGGNTAMDAARTARRLGAE 292

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 157 VAAVV-----EAMPkvggywVHAAKI---RRLGIPILLQHTVTEAIGD-------RVLEgAVIQELDDKFQ---LKGEPE 218
Cdd:PRK12771  293 EVTIVyrrtrEDMP------AHDEEIeeaLREGVEINWLRTPVEIEGDengatglRVIT-VEKMELDEDGRpspVTGEEE 365

                         250
                  ....*....|..
gi 1709980280 219 KIDCDIICMAVG 230
Cdd:PRK12771  366 TLEADLVVLAIG 377
PRK13512 PRK13512
coenzyme A disulfide reductase; Provisional
 54-275 4.47e-04

coenzyme A disulfide reductase; Provisional


Pssm-ID: 184103 [Multi-domain]  Cd Length: 438  Bit Score: 41.69  E-value: 4.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  54 EDK-VTIKCNSTVTGYYPEDGVYTVMEGEED-YYRVKAKKAVIATGAQERMIPFpNNDLpgvygagaVQTLMNVYGV--- 128
Cdd:PRK13512   69 DRKqITVKTYHEVIAINDERQTVTVLNRKTNeQFEESYDKLILSPGASANSLGF-ESDI--------TFTLRNLEDTdai 139

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 129 ------TPGKRVLMVGAGNIGLIVSYQLAQAGVEVAavveampkvggyWVH-AAKIRRLgipillqhtvteaiGDRVLEG 201
Cdd:PRK13512  140 dqfikaNQVDKALVVGAGYISLEVLENLYERGLHPT------------LIHrSDKINKL--------------MDADMNQ 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 202 AVIQELDDK---FQLKGEPEKID-------------CDIICMAVGLAPTTELFWQAGCEMKYVpqlcGYVPYRDKnMRTS 265
Cdd:PRK13512  194 PILDELDKReipYRLNEEIDAINgnevtfksgkvehYDMIIEGVGTHPNSKFIESSNIKLDDK----GFIPVNDK-FETN 268

                         250
                  ....*....|
gi 1709980280 266 NKDIWVAGDA 275
Cdd:PRK13512  269 VPNIYAIGDI 278
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 131-194 6.00e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 41.40  E-value: 6.00e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1709980280 131 GKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGGYW------------VHAAKIRR---LGIPILLQHTVTEAI 194
Cdd:PRK12771  137 GKRVAVIGGGPAGLSAAYHLRRMGHAV-TIFEAGPKLGGMMrygipayrlpreVLDAEIQRildLGVEVRLGVRVGEDI 214
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 131-183 6.60e-04

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 41.30  E-value: 6.60e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1709980280 131 GKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGGywvhaakIRRLGIP 183
Cdd:PRK12810  143 GKKVAVVGSGPAGLAAADQLARAGHKV-TVFERADRIGG-------LLRYGIP 187
PanE COG1893
Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of ...
 133-199 2.02e-03

Ketopantoate reductase [Coenzyme transport and metabolism]; Ketopantoate reductase is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis


Pssm-ID: 441497 [Multi-domain]  Cd Length: 305  Bit Score: 39.45  E-value: 2.02e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1709980280 133 RVLMVGAGNIGLIVSYQLAQAGVEVAAVVeampkvggYWVHAAKIRRLGIpillqhTVTEAIGDRVL 199
Cdd:COG1893     2 KIAILGAGAIGGLLGARLARAGHDVTLVA--------RGAHAEALRENGL------RLESPDGDRTT 54
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 128-171 2.33e-03

Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ion transport and metabolism];


Pssm-ID: 441675 [Multi-domain]  Cd Length: 414  Bit Score: 39.46  E-value: 2.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1709980280 128 VTPGKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGGYW 171
Cdd:COG2072     3 ATEHVDVVVIGAGQAGLAAAYHLRRAGIDF-VVLEKADDVGGTW 45
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
129-213 2.51e-03

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 39.52  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 129 TPGKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGG------------Y------WVHAAK------IRRLGIPI 184
Cdd:COG1231     5 ARGKDVVIVGAGLAGLAAARELRKAGLDV-TVLEARDRVGGrvwtlrfgddglYaelgamRIPPSHtnllalARELGLPL 83

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1709980280 185 LLQHTVTEAI-----GDRVLEGAVIQELDDKFQL 213
Cdd:COG1231    84 EPFPNENGNAllylgGKRVRAGEIAADLRGVAEL 117
PRK06327 PRK06327
dihydrolipoamide dehydrogenase; Validated
 87-294 2.70e-03

dihydrolipoamide dehydrogenase; Validated


Pssm-ID: 235779 [Multi-domain]  Cd Length: 475  Bit Score: 39.52  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  87 VKAKKAVIATGAQERM---IPFPNNDLPGVYGAGAVQTLmnvygvtPGKRVLmVGAGNIGLIVSYQLAQAGVEVaAVVEA 163
Cdd:PRK06327  144 ITAKHVIIATGSEPRHlpgVPFDNKIILDNTGALNFTEV-------PKKLAV-IGAGVIGLELGSVWRRLGAEV-TILEA 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 164 MPKVGGywvhAA----------KIRRLGIPILLQHTV--TEAIGDRVlegaVIQELDDkfqlKGEPEKIDCDIICMAVGL 231
Cdd:PRK06327  215 LPAFLA----AAdeqvakeaakAFTKQGLDIHLGVKIgeIKTGGKGV----SVAYTDA----DGEAQTLEVDKLIVSIGR 282

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1709980280 232 APTTElfwqaGCEMKYVPQLC---GYVPYrDKNMRTSNKDIWVAGD-ASGIEEASAAMVEG-----RIAGHS 294
Cdd:PRK06327  283 VPNTD-----GLGLEAVGLKLderGFIPV-DDHCRTNVPNVYAIGDvVRGPMLAHKAEEEGvavaeRIAGQK 348
NAD_bind_Shikimate_DH cd01065
NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino ...
 115-156 3.28e-03

NAD(P) binding domain of Shikimate dehydrogenase; Shikimate dehydrogenase (DH) is an amino acid DH family member. Shikimate pathway links metabolism of carbohydrates to de novo biosynthesis of aromatic amino acids, quinones and folate. It is essential in plants, bacteria, and fungi but absent in mammals, thus making enzymes involved in this pathway ideal targets for broad spectrum antibiotics and herbicides. Shikimate DH catalyzes the reduction of 3-hydroshikimate to shikimate using the cofactor NADH. Amino acid DH-like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DHs, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts.


Pssm-ID: 133443 [Multi-domain]  Cd Length: 155  Bit Score: 37.64  E-value: 3.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1709980280 115 GAGAVQTLMNVYGVTPGKRVLMVGAGNIGLIVSYQLAQAGVE 156
Cdd:cd01065     3 GLGFVRALEEAGIELKGKKVLILGAGGAARAVAYALAELGAA 44
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
56-273 3.61e-03

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 38.74  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  56 KVTIKCNSTVTGYYPEDGVYTVMEGEEDYyrvKAKKAVIATGAQErmipFPNndLPGVYGAGAVQTLMNVYGVTPGKRVL 135
Cdd:pfam13738  89 ELPINLFEEVTSVKKEDDGFVVTTSKGTY---QARYVIIATGEFD----FPN--KLGVPELPKHYSYVKDFHPYAGQKVV 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 136 MVGAGNIGLIVSYQLAQAGVEVAAVV-----EAMPKVGGYWVHAAKIRRLGipILLQHTVTEAIGDRVLEGavIQELDDK 210
Cdd:pfam13738 160 VIGGYNSAVDAALELVRKGARVTVLYrgsewEDRDSDPSYSLSPDTLNRLE--ELVKNGKIKAHFNAEVKE--ITEVDVS 235

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1709980280 211 FQLK---GEPEKIDCDIIcMAVGLAPTTELFwqAGCEMKYVPQlcGYVPYRDKNMRTSNKDIWVAG 273
Cdd:pfam13738 236 YKVHtedGRKVTSNDDPI-LATGYHPDLSFL--KKGLFELDED--GRPVLTEETESTNVPGLFLAG 296
PRK07233 PRK07233
hypothetical protein; Provisional
 133-169 4.07e-03

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 38.71  E-value: 4.07e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1709980280 133 RVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGG 169
Cdd:PRK07233    1 KIAIVGGGIAGLAAAYRLAKRGHEV-TVFEADDQLGG 36
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 131-169 5.77e-03

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 38.24  E-value: 5.77e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1709980280 131 GKRVLMVGAGNIGLIVSYQLAQAGVEVaAVVEAMPKVGG 169
Cdd:PRK11749  140 GKKVAVIGAGPAGLTAAHRLARKGYDV-TIFEARDKAGG 177
PRK07251 PRK07251
FAD-containing oxidoreductase;
78-236 6.26e-03

FAD-containing oxidoreductase;


Pssm-ID: 180907 [Multi-domain]  Cd Length: 438  Bit Score: 38.19  E-value: 6.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280  78 MEGEEDYYRVKAKKAVIATGAQERMIPFPN-NDLPGVYGAGAVQTLMnvygvTPGKRVLMVGAGNIGLIVSYQLAQAGVE 156
Cdd:PRK07251  108 VQAGDEKIELTAETIVINTGAVSNVLPIPGlADSKHVYDSTGIQSLE-----TLPERLGIIGGGNIGLEFAGLYNKLGSK 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1709980280 157 VaAVVEAMPKV-GGYWVHAAKIRR-----LGIPILLQHTVTEaigdrvlegavIQELDDKFQLKGEPEKIDCDIICMAVG 230
Cdd:PRK07251  183 V-TVLDAASTIlPREEPSVAALAKqymeeDGITFLLNAHTTE-----------VKNDGDQVLVVTEDETYRFDALLYATG 250


                  ....*.
gi 1709980280 231 LAPTTE 236
Cdd:PRK07251  251 RKPNTE 256
 
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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