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Conserved domains on  [gi|15597391|ref|NP_250885|]
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hydrogen cyanide synthase subunit HcnC [Pseudomonas aeruginosa PAO1]

Protein Classification

NAD(P)/FAD-dependent oxidoreductase( domain architecture ID 11429741)

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

CATH:  3.30.9.10
EC:  1.-.-.-
Gene Ontology:  GO:0016491|GO:0050660
SCOP:  3000055

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
3-404 5.73e-89

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


:

Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 274.09  E-value: 5.73e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   3 RTYDIVIAGGGVIGASCAYQLSRRGnLRIAVVDDKRPGN-ATRASAGGLWAIGESVGlgcgviffrmmssrnrreaqgaa 81
Cdd:COG0665   1 ATADVVVIGGGIAGLSTAYHLARRG-LDVTVLERGRPGSgASGRNAGQLRPGLAALA----------------------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  82 vavdastphilPPAFFDLALQSNALYpelhRELIERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDR 161
Cdd:COG0665  57 -----------DRALVRLAREALDLW----RELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRALGLPVELLDA 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 162 EELRRAEPAV-SHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDNaGVLHCRTLI 240
Cdd:COG0665 122 AELREREPGLgSPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTER-GTVRADAVV 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 241 NAAGAWAAELSEMAtGRRIPVKPVKGQIVLTERMPRLLNG-CLTTSDCYMAQKDNGEILIGSTTEDKGFDVSNTFPEIAG 319
Cdd:COG0665 201 LAAGAWSARLLPML-GLRLPLRPVRGYVLVTEPLPDLPLRpVLDDTGVYLRPTADGRLLVGGTAEPAGFDRAPTPERLEA 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 320 LVQGAVRCVPELQQVNLKRTWAGLRPGSPDELPILGPVAEVEGYLNACGHFRTGILTSAITGVLLDRLVHEETLPLDIAP 399
Cdd:COG0665 280 LLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAP 359

                ....*
gi 15597391 400 FLAAR 404
Cdd:COG0665 360 FSPDR 364
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
3-404 5.73e-89

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 274.09  E-value: 5.73e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   3 RTYDIVIAGGGVIGASCAYQLSRRGnLRIAVVDDKRPGN-ATRASAGGLWAIGESVGlgcgviffrmmssrnrreaqgaa 81
Cdd:COG0665   1 ATADVVVIGGGIAGLSTAYHLARRG-LDVTVLERGRPGSgASGRNAGQLRPGLAALA----------------------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  82 vavdastphilPPAFFDLALQSNALYpelhRELIERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDR 161
Cdd:COG0665  57 -----------DRALVRLAREALDLW----RELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRALGLPVELLDA 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 162 EELRRAEPAV-SHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDNaGVLHCRTLI 240
Cdd:COG0665 122 AELREREPGLgSPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTER-GTVRADAVV 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 241 NAAGAWAAELSEMAtGRRIPVKPVKGQIVLTERMPRLLNG-CLTTSDCYMAQKDNGEILIGSTTEDKGFDVSNTFPEIAG 319
Cdd:COG0665 201 LAAGAWSARLLPML-GLRLPLRPVRGYVLVTEPLPDLPLRpVLDDTGVYLRPTADGRLLVGGTAEPAGFDRAPTPERLEA 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 320 LVQGAVRCVPELQQVNLKRTWAGLRPGSPDELPILGPVAEVEGYLNACGHFRTGILTSAITGVLLDRLVHEETLPLDIAP 399
Cdd:COG0665 280 LLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAP 359

                ....*
gi 15597391 400 FLAAR 404
Cdd:COG0665 360 FSPDR 364
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
90-391 4.04e-61

glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 201.05  E-value: 4.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    90 HILPPAFFDLALQSNALYPELHRELIERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREELRRAEP 169
Cdd:TIGR02352  37 EYAEDPLFDLALESLRLYPEWLEALKELTGLDTGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRALRRLEP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   170 AVSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDnAGVLHCRTLINAAGAWAAE 249
Cdd:TIGR02352 117 YLSGGIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTP-SGDVQADQVVLAAGAWAGE 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   250 LSEMAtGRRIPVKPVKGQIVLTERMPRLLNGCLTTSDCYMAQKDNGEILIGSTTEDKGFDVSNTFPEIAGLVQGAVRCVP 329
Cdd:TIGR02352 196 LLPLP-LRPVRGQPLRLEAPAVPLLNRPLRAVVYGRRVYIVPRRDGRLVVGATMEESGFDTTPTLGGIKELLRDAYTILP 274
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597391   330 ELQQVNLKRTWAGLRPGSPDELPILGPVAEVEGYLNACGHFRTGILTSAITG-VLLDRLVHEE 391
Cdd:TIGR02352 275 ALKEARLLETWAGLRPGTPDNLPYIGEHPEDRRLLIATGHYRNGILLAPATAeVIADLILGKE 337
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
6-384 3.63e-60

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: 198.78  E-value: 3.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391     6 DIVIAGGGVIGASCAYQLSRRGnLRIAVVD-DKRPGNATRASAGGLWAIGESvglgcgviffrmmssrnrreaqgaavav 84
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRG-LSVTLLErGDDPGSGASGRNAGLIHPGLR---------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    85 dastpHILPPAFFDLALQSNALYpelhRELIERHGMDFKFERTGlKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREEL 164
Cdd:pfam01266  52 -----YLEPSELARLALEALDLW----EELEEELGIDCGFRRCG-VLVLARDEEEEALEKLLAALRRLGVPAELLDAEEL 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   165 RRAEPAvSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGrRISGVRTDNagvlHCRTLINAAG 244
Cdd:pfam01266 122 RELEPL-LPGLRGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEG-GVWGVVTTG----EADAVVNAAG 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   245 AWAAELSEmaTGRRIPVKPVKGQIVLTERMPRLLNG--CLTTSDC----YMAQKDNGEILIGSTTEDKGFD-VSNTFPEI 317
Cdd:pfam01266 196 AWADLLAL--PGLRLPVRPVRGQVLVLEPLPEALLIlpVPITVDPgrgvYLRPRADGRLLLGGTDEEDGFDdPTPDPEEI 273
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597391   318 AGLVQGAVRCVPELqqVNLKRTWAGLRPgSPDELPILGPvAEVEGYLNACGHFRTGILTSAITGVLL 384
Cdd:pfam01266 274 EELLEAARRLFPAL--ADIERAWAGLRP-LPDGLPIIGR-PGSPGLYLATGHGGHGLTLAPGIGKLL 336
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
101-350 2.33e-18

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 86.99  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  101 LQSNALY----PELHRELIE---------RHGMdfkfERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREELRRA 167
Cdd:PRK11101  52 LHSGARYavtdAESARECISenqilkriaRHCV----EPTDGLFITLPEDDLAFQATFIRACEEAGIEAEAIDPQQALIL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  168 EPAVSHAAHGALEfLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVR-----TDNAGVLHCRTLINA 242
Cdd:PRK11101 128 EPAVNPALIGAVK-VPDGTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGDTVCGVRvrdhlTGETQEIHAPVVVNA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  243 AGAWAAELSEMATgRRIPVKPVKGQ-IVLTERMPRL-LNGCLTTSDcymaqkdnGEIL--------IGSTTE----DKGF 308
Cdd:PRK11101 207 AGIWGQHIAEYAD-LRIRMFPAKGSlLIMDHRINNHvINRCRKPAD--------ADILvpgdtislIGTTSTridyDQID 277
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15597391  309 DVSNTFPEIAGLVQGAVRCVPELQQVNLKRTWAGLRP--GSPDE 350
Cdd:PRK11101 278 DNRVTAEEVDILLREGEKLAPVMAKTRILRAYAGVRPlvASDDD 321
 
Name Accession Description Interval E-value
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
3-404 5.73e-89

Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 274.09  E-value: 5.73e-89
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   3 RTYDIVIAGGGVIGASCAYQLSRRGnLRIAVVDDKRPGN-ATRASAGGLWAIGESVGlgcgviffrmmssrnrreaqgaa 81
Cdd:COG0665   1 ATADVVVIGGGIAGLSTAYHLARRG-LDVTVLERGRPGSgASGRNAGQLRPGLAALA----------------------- 56
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  82 vavdastphilPPAFFDLALQSNALYpelhRELIERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDR 161
Cdd:COG0665  57 -----------DRALVRLAREALDLW----RELAAELGIDCDFRRTGVLYLARTEAELAALRAEAEALRALGLPVELLDA 121
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 162 EELRRAEPAV-SHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDNaGVLHCRTLI 240
Cdd:COG0665 122 AELREREPGLgSPDYAGGLYDPDDGHVDPAKLVRALARAARAAGVRIREGTPVTGLEREGGRVTGVRTER-GTVRADAVV 200
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 241 NAAGAWAAELSEMAtGRRIPVKPVKGQIVLTERMPRLLNG-CLTTSDCYMAQKDNGEILIGSTTEDKGFDVSNTFPEIAG 319
Cdd:COG0665 201 LAAGAWSARLLPML-GLRLPLRPVRGYVLVTEPLPDLPLRpVLDDTGVYLRPTADGRLLVGGTAEPAGFDRAPTPERLEA 279
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 320 LVQGAVRCVPELQQVNLKRTWAGLRPGSPDELPILGPVAEVEGYLNACGHFRTGILTSAITGVLLDRLVHEETLPLDIAP 399
Cdd:COG0665 280 LLRRLRRLFPALADAEIVRAWAGLRPMTPDGLPIIGRLPGAPGLYVATGHGGHGVTLAPAAGRLLADLILGGEPPLDLAP 359

                ....*
gi 15597391 400 FLAAR 404
Cdd:COG0665 360 FSPDR 364
thiamin_ThiO TIGR02352
glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine ...
90-391 4.04e-61

glycine oxidase ThiO; This family consists of the homotetrameric, FAD-dependent glycine oxidase ThiO, from species such as Bacillus subtilis that use glycine in thiamine biosynthesis. In general, members of this family will not be found in species such as E. coli that instead use tyrosine and the ThiH protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]


Pssm-ID: 274092 [Multi-domain]  Cd Length: 337  Bit Score: 201.05  E-value: 4.04e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    90 HILPPAFFDLALQSNALYPELHRELIERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREELRRAEP 169
Cdd:TIGR02352  37 EYAEDPLFDLALESLRLYPEWLEALKELTGLDTGYHQCGTLVVAFDEDDVEHLRQLADLQSATGMEVEWLSGRALRRLEP 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   170 AVSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDnAGVLHCRTLINAAGAWAAE 249
Cdd:TIGR02352 117 YLSGGIRGAVFYPDDAHVDPRALLKALEKALEKLGVEIIEHTEVQHIEIRGEKVTAIVTP-SGDVQADQVVLAAGAWAGE 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   250 LSEMAtGRRIPVKPVKGQIVLTERMPRLLNGCLTTSDCYMAQKDNGEILIGSTTEDKGFDVSNTFPEIAGLVQGAVRCVP 329
Cdd:TIGR02352 196 LLPLP-LRPVRGQPLRLEAPAVPLLNRPLRAVVYGRRVYIVPRRDGRLVVGATMEESGFDTTPTLGGIKELLRDAYTILP 274
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597391   330 ELQQVNLKRTWAGLRPGSPDELPILGPVAEVEGYLNACGHFRTGILTSAITG-VLLDRLVHEE 391
Cdd:TIGR02352 275 ALKEARLLETWAGLRPGTPDNLPYIGEHPEDRRLLIATGHYRNGILLAPATAeVIADLILGKE 337
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
6-384 3.63e-60

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: 198.78  E-value: 3.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391     6 DIVIAGGGVIGASCAYQLSRRGnLRIAVVD-DKRPGNATRASAGGLWAIGESvglgcgviffrmmssrnrreaqgaavav 84
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRG-LSVTLLErGDDPGSGASGRNAGLIHPGLR---------------------------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    85 dastpHILPPAFFDLALQSNALYpelhRELIERHGMDFKFERTGlKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREEL 164
Cdd:pfam01266  52 -----YLEPSELARLALEALDLW----EELEEELGIDCGFRRCG-VLVLARDEEEEALEKLLAALRRLGVPAELLDAEEL 121
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   165 RRAEPAvSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGrRISGVRTDNagvlHCRTLINAAG 244
Cdd:pfam01266 122 RELEPL-LPGLRGGLFYPDGGHVDPARLLRALARAAEALGVRIIEGTEVTGIEEEG-GVWGVVTTG----EADAVVNAAG 195
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   245 AWAAELSEmaTGRRIPVKPVKGQIVLTERMPRLLNG--CLTTSDC----YMAQKDNGEILIGSTTEDKGFD-VSNTFPEI 317
Cdd:pfam01266 196 AWADLLAL--PGLRLPVRPVRGQVLVLEPLPEALLIlpVPITVDPgrgvYLRPRADGRLLLGGTDEEDGFDdPTPDPEEI 273
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15597391   318 AGLVQGAVRCVPELqqVNLKRTWAGLRPgSPDELPILGPvAEVEGYLNACGHFRTGILTSAITGVLL 384
Cdd:pfam01266 274 EELLEAARRLFPAL--ADIERAWAGLRP-LPDGLPIIGR-PGSPGLYLATGHGGHGLTLAPGIGKLL 336
LhgO COG0579
L-2-hydroxyglutarate oxidase LhgO [Carbohydrate transport and metabolism];
1-280 5.07e-38

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


Pssm-ID: 440344 [Multi-domain]  Cd Length: 418  Bit Score: 142.21  E-value: 5.07e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   1 MNRTYDIVIAGGGVIGASCAYQLSRRGNLRIAVVDdkrpgnatRASAgglwaigesvgLGCGViffrmmSSRNrreaqgA 80
Cdd:COG0579   1 MMEMYDVVIIGAGIVGLALARELSRYEDLKVLVLE--------KEDD-----------VAQES------SGNN------S 49
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  81 AV---AVDAsTPHILPPAffdLALQSNALYPELHRELierhgmDFKFERTGlKYVI-QDDEDRQYAEHIVAQ-IPHLAEQ 155
Cdd:COG0579  50 GVihaGLYY-TPGSLKAR---LCVEGNELFYELCREL------GIPFKRCG-KLVVaTGEEEVAFLEKLYERgKANGVPG 118
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 156 VRWLDREELRRAEPAVSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISgVRTDNaGVLH 235
Cdd:COG0579 119 LEILDREELRELEPLLSDEGVAALYSPSTGIVDPGALTRALAENAEANGVELLLNTEVTGIEREGDGWE-VTTNG-GTIR 196
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 15597391 236 CRTLINAAGAWAAELSEMA-TGRRIPVKPVKGQIVLTERMPRLLNG 280
Cdd:COG0579 197 ARFVINAAGLYADRLAQMAgIGKDFGIFPVKGEYLVLDKPAELVNA 242
glpA PRK11101
anaerobic glycerol-3-phosphate dehydrogenase subunit A;
101-350 2.33e-18

anaerobic glycerol-3-phosphate dehydrogenase subunit A;


Pssm-ID: 236847 [Multi-domain]  Cd Length: 546  Bit Score: 86.99  E-value: 2.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  101 LQSNALY----PELHRELIE---------RHGMdfkfERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREELRRA 167
Cdd:PRK11101  52 LHSGARYavtdAESARECISenqilkriaRHCV----EPTDGLFITLPEDDLAFQATFIRACEEAGIEAEAIDPQQALIL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  168 EPAVSHAAHGALEfLCDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVR-----TDNAGVLHCRTLINA 242
Cdd:PRK11101 128 EPAVNPALIGAVK-VPDGTVDPFRLTAANMLDAKEHGAQILTYHEVTGLIREGDTVCGVRvrdhlTGETQEIHAPVVVNA 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  243 AGAWAAELSEMATgRRIPVKPVKGQ-IVLTERMPRL-LNGCLTTSDcymaqkdnGEIL--------IGSTTE----DKGF 308
Cdd:PRK11101 207 AGIWGQHIAEYAD-LRIRMFPAKGSlLIMDHRINNHvINRCRKPAD--------ADILvpgdtislIGTTSTridyDQID 277
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 15597391  309 DVSNTFPEIAGLVQGAVRCVPELQQVNLKRTWAGLRP--GSPDE 350
Cdd:PRK11101 278 DNRVTAEEVDILLREGEKLAPVMAKTRILRAYAGVRPlvASDDD 321
PRK00711 PRK00711
D-amino acid dehydrogenase;
112-405 1.07e-14

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 75.22  E-value: 1.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  112 RELIERHGMDFKFERTGLKYVIQDDEdrQYaEHIVAQIPHLAE-----QVrwLDREELRRAEPAVSHAAH---GALeFLC 183
Cdd:PRK00711 120 KALRAETGIQYEGRQGGTLQLFRTQQ--QL-DAAAKDIAVLEEagvpyEL--LDRDELAAVEPALAGVRHklvGGL-RLP 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  184 DHQVspfrlADAYL------EAARQNGVELLPGTNVTGVLRQGRRISGVRTDnAGVLHCRTLINAAGAWAAE-LSEMatG 256
Cdd:PRK00711 194 NDET-----GDCQLftqrlaAMAEQLGVKFRFNTPVDGLLVEGGRITGVQTG-GGVITADAYVVALGSYSTAlLKPL--G 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  257 RRIPVKPVKG-----QIVLTERMPRllngcLTTSD-CY---MAQKDNgEILIGSTTEDKGFD--------------VSNT 313
Cdd:PRK00711 266 VDIPVYPLKGysltvPITDEDRAPV-----STVLDeTYkiaITRFDD-RIRVGGMAEIVGFDlrldparretlemvVRDL 339
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  314 FPEIAGLVQGAVrcvpelqqvnlkrtWAGLRPGSPDELPILGPvAEVEG-YLNAcGHFRTGILTSAITGVLLDRLVHEET 392
Cdd:PRK00711 340 FPGGGDLSQATF--------------WTGLRPMTPDGTPIVGA-TRYKNlWLNT-GHGTLGWTMACGSGQLLADLISGRK 403
                        330
                 ....*....|...
gi 15597391  393 LPLDIAPFLAARF 405
Cdd:PRK00711 404 PAIDADDLSVARY 416
GlpA COG0578
Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate ...
157-345 2.32e-14

Glycerol-3-phosphate dehydrogenase [Energy production and conversion]; Glycerol-3-phosphate dehydrogenase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440343 [Multi-domain]  Cd Length: 501  Bit Score: 74.78  E-value: 2.32e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 157 RWLDREELRRAEPAVS-HAAHGALEFLcDHQVSPFRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVR-----TDN 230
Cdd:COG0578 103 RRLSRAEALALAPLLRpDGLRGGFEYY-DAQVDDARLVLELARTAAERGAVVLNYTRVTGLLRDGGRVWGVTvrdrlTGE 181
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 231 AGVLHCRTLINAAGAWAAELSEMATGR-RIPVKPVKG-QIVLtermPRLLNGCltTSDCYMAQKDNGEI----------L 298
Cdd:COG0578 182 EFTVRARVVVNATGPWVDELRALDGPKaPRRVRPSKGsHLVV----PRLFLPL--DDALYIFQNTDGRVvfaipwegrtL 255
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15597391 299 IGSTtedkgfDVsntfpEIAGLVQgAVRCVPE-----LQQVN------LKR-----TWAGLRP 345
Cdd:COG0578 256 IGTT------DT-----DYDGDPD-EPAATEEeidylLEAANryfarpLTRddvvsTYAGVRP 306
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
6-364 4.36e-13

bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent 5-carboxymethylaminomethyl-2-thiouridine(34) oxidoreductase MnmC;


Pssm-ID: 234978 [Multi-domain]  Cd Length: 662  Bit Score: 71.03  E-value: 4.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    6 DIVIAGGGVIGASCAYQLSRRGnlriAVVD--DKRPGNATRASagglwaigesvGLGCGViFFRMMSSRNRREAQgaava 83
Cdd:PRK01747 262 DAAIIGGGIAGAALALALARRG----WQVTlyEADEAPAQGAS-----------GNRQGA-LYPLLSKDDNALSR----- 320
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   84 vdastphiLPPAFFDLALQsnalypelHRELIERHGMDFKFERTGlkyVIQ---DDEDRQYAEHIVAQIPhLAEQVRWLD 160
Cdd:PRK01747 321 --------FFRAAFLFARR--------FYDALPAAGVAFDHDWCG---VLQlawDEKSAEKIAKMLALGL-PAELARALD 380
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  161 REELR-RAEPAVSHA----AHGALeflcdhqVSPFRLADAYLEAArQNGVELLPGTNVTGVLRQGRRISgVRTDNAGVLH 235
Cdd:PRK01747 381 AEEAEeLAGLPVPCGgifyPQGGW-------LCPAELCRALLALA-GQQLTIHFGHEVARLEREDDGWQ-LDFAGGTLAS 451
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  236 CRTLINAAGAwaaELSEMATGRRIPVKPVKGQIVL---TERMPRLlnGCLTTSDCYMA-QKDNGEILIGSTtEDKGfDVS 311
Cdd:PRK01747 452 APVVVLANGH---DAARFAQTAHLPLYSVRGQVSHlptTPALSAL--KQVLCYDGYLTpQPANGTHCIGAS-YDRD-DTD 524
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15597391  312 NTFPEI--AGLVQGAVRCVPELQQV-------NLKRtwAGLRPGSPDELPILGPVAEVEGYL 364
Cdd:PRK01747 525 TAFREAdhQENLERLAECLPQALWAkevdvsaLQGR--VGFRCASRDRLPMVGNVPDEAATL 584
MnmC_Cterm TIGR03197
tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In ...
115-364 9.99e-13

tRNA U-34 5-methylaminomethyl-2-thiouridine biosynthesis protein MnmC, C-terminal domain; In Escherichia coli, the protein previously designated YfcK is now identified as the bifunctional enzyme MnmC. It acts, following the action of the heterotetramer of GidA and MnmE, in the modification of U-34 of certain tRNA to 5-methylaminomethyl-2-thiouridine (mnm5s2U). In other bacterial, the corresponding proteins are usually but always found as a single polypeptide chain, but occasionally as the product of tandem genes. This model represents the C-terminal region of the multifunctional protein. [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 274478 [Multi-domain]  Cd Length: 381  Bit Score: 69.22  E-value: 9.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   115 IERHGMDFKFERTGLKYVIQDDEDRQYAEHIVAQIPHLAEQVRWLDREELrrAEPAVSHAAHGALEFlcdHQ---VSPFR 191
Cdd:TIGR03197  62 LAEAGFPFDHEWCGVLQLAYDEKEAERLQKLLEQLGFPEELARWVDAEQA--SQLAGIPLPYGGLFF---PQggwLSPPQ 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   192 LADAYLEAARQnGVELLPGTNVTGVLRQGRRISgVRTDNAGVLHCRTLINAAGAWAAELSEMAtgrRIPVKPVKGQ---I 268
Cdd:TIGR03197 137 LCRALLAHAGI-RLTLHFNTEITSLERDGEGWQ-LLDANGEVIAASVVVLANGAQAPQLAQTA---HLPLRPVRGQvshL 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   269 VLTERMPRLlnGCLTTSDCYMAQKDNGEILIGSTtedkgFDVSNTFPEI-----AGLVQGAVRCVPELQQVN-----LKR 338
Cdd:TIGR03197 212 PATEALSAL--KTVLCYDGYLTPANNGEHCIGAS-----YDRNDDDLALreadhAENLERLAECLPALAWASevdisALQ 284
                         250       260
                  ....*....|....*....|....*.
gi 15597391   339 TWAGLRPGSPDELPILGPVAEVEGYL 364
Cdd:TIGR03197 285 GRVGVRCASPDHLPLVGAVPDFEAIK 310
solA PRK11259
N-methyl-L-tryptophan oxidase;
3-250 9.05e-10

N-methyl-L-tryptophan oxidase;


Pssm-ID: 236887 [Multi-domain]  Cd Length: 376  Bit Score: 59.85  E-value: 9.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    3 RTYDIVIAGGGVIGASCAYQLSRRGnLRIAVVDDKRPGNATRASAGGLWAIGESVGLGcgviffrmmssrnrreaqgaav 82
Cdd:PRK11259   2 MRYDVIVIGLGSMGSAAGYYLARRG-LRVLGLDRFMPPHQQGSSHGDTRIIRHAYGEG---------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   83 avdastphilpPAFFDLALQSNALYpelhRELIERHGMDFkFERTGLKYVIQDDEDrqyaehIVAQIPHLAEQ----VRW 158
Cdd:PRK11259  59 -----------PAYVPLVLRAQELW----RELERESGEPL-FVRTGVLNLGPADSD------FLANSIRSARQhglpHEV 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  159 LDREELRRAEP--AVSHAAHGALE----FLCdhqvsPFRLADAYLEAARQNGVELLPGTNVTGVLRQGrriSGVR-TDNA 231
Cdd:PRK11259 117 LDAAEIRRRFPqfRLPDGYIALFEpdggFLR-----PELAIKAHLRLAREAGAELLFNEPVTAIEADG---DGVTvTTAD 188
                        250
                 ....*....|....*....
gi 15597391  232 GVLHCRTLINAAGAWAAEL 250
Cdd:PRK11259 189 GTYEAKKLVVSAGAWVKDL 207
PRK11728 PRK11728
L-2-hydroxyglutarate oxidase;
4-254 2.91e-08

L-2-hydroxyglutarate oxidase;


Pssm-ID: 183292 [Multi-domain]  Cd Length: 393  Bit Score: 55.21  E-value: 2.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    4 TYDIVIAGGGVIGASCAYQLSRRG-NLRIAVVDdKRPGNATRASagglwaigesvGLGCGVI----FFRMMSSRNRREAQ 78
Cdd:PRK11728   2 MYDFVIIGGGIVGLSTAMQLQERYpGARIAVLE-KESGPARHQT-----------GHNSGVIhagvYYTPGSLKARFCRR 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   79 GAavavdastphilppaffdlalqsnalypELHRELIERHGMDFkfERTGLKYVIQDDEDRQYAEHIVA-----QIPhla 153
Cdd:PRK11728  70 GN----------------------------EATKAFCDQHGIPY--EECGKLLVATSELELERMEALYEraranGIE--- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  154 eqVRWLDREELRRAEPAVS-----HAAHGAlefLCDHQvspfRLADAYLEAARQNGVELLPGTNVTGVLRQGRRISgVRT 228
Cdd:PRK11728 117 --VERLDAEELREREPNIRglgaiFVPSTG---IVDYR----AVAEAMAELIQARGGEIRLGAEVTALDEHANGVV-VRT 186
                        250       260
                 ....*....|....*....|....*.
gi 15597391  229 dNAGVLHCRTLINAAGAWAAELSEMA 254
Cdd:PRK11728 187 -TQGEYEARTLINCAGLMSDRLAKMA 211
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
7-388 2.47e-07

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 52.33  E-value: 2.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    7 IVIAGGGVIGASCAYQLSRRGnLRIAVVDDKR-PGNATRASAGG--------LWAIGESVGLGcgvifFRMMSSRnrrea 77
Cdd:PRK12409   4 IAVIGAGITGVTTAYALAQRG-YQVTVFDRHRyAAMETSFANGGqlsasnaeVWNHWATVLKG-----LKWMLRK----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   78 qgaavavDAstPHILPPAF----------F---------------DLALQSNalypELHRELIERHGMDFKFERTGLKYV 132
Cdd:PRK12409  73 -------DA--PLLLNPKPswhkyswlaeFlahipnyrantietvRLAIAAR----KHLFDIAEREGIDFDLERRGILHI 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  133 IQDDEDRQYAEHIVAQiphLAE---QVRWLDREELRRAEPAVSHAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLP 209
Cdd:PRK12409 140 YHDKAGFDHAKRVNAL---LAEgglERRAVTPEEMRAIEPTLTGEYYGGYYTPSDSTGDIHKFTTGLAAACARLGVQFRY 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  210 GTNVTGVLRQGRRISgVRTDNAGVLHCRTLIN-----AAGAWAAELSEMaTGRRIPVKPVKG---QIVLTERMPR----- 276
Cdd:PRK12409 217 GQEVTSIKTDGGGVV-LTVQPSAEHPSRTLEFdgvvvCAGVGSRALAAM-LGDRVNVYPVKGysiTVNLDDEASRaaapw 294
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  277 --LLN--GCLTTSdcymaQKDNGEILIGSTTEDKGFDVSNTFPEIAGLVQGAVRCVPElqqVNLKRT--WAGLRPGSPDE 350
Cdd:PRK12409 295 vsLLDdsAKIVTS-----RLGADRFRVAGTAEFNGYNRDIRADRIRPLVDWVRRNFPD---VSTRRVvpWAGLRPMMPNM 366
                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 15597391  351 LPILGPVAEVEGYLNAcGHFRTGILTSAITGVLLDRLV 388
Cdd:PRK12409 367 MPRVGRGRRPGVFYNT-GHGHLGWTLSAATADLVAQVV 403
PRK13369 PRK13369
glycerol-3-phosphate dehydrogenase; Provisional
200-345 8.91e-07

glycerol-3-phosphate dehydrogenase; Provisional


Pssm-ID: 237365 [Multi-domain]  Cd Length: 502  Bit Score: 50.74  E-value: 8.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  200 ARQNGVELLPGTNVTGVLRQGRRISGVRTDNAG---VLHCRTLINAAGAWAAELSEMATGRRIP--VKPVKG-QIVLter 273
Cdd:PRK13369 165 AAERGATILTRTRCVSARREGGLWRVETRDADGetrTVRARALVNAAGPWVTDVIHRVAGSNSSrnVRLVKGsHIVV--- 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  274 mPRLLNGclttSDCYMAQKDNGEI-----------LIGSTTEDKG---FDVSNTFPEIAGLVQGAVRCVPE-LQQVNLKR 338
Cdd:PRK13369 242 -PKFWDG----AQAYLFQNPDKRVifanpyegdftLIGTTDIAYEgdpEDVAADEEEIDYLLDAANRYFKEkLRREDVVH 316

                 ....*..
gi 15597391  339 TWAGLRP 345
Cdd:PRK13369 317 SFSGVRP 323
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
191-250 3.95e-06

Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 48.69  E-value: 3.95e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 191 RLADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDNAGVLHCRTLINAAGAWAAEL 250
Cdd:COG1233 223 ALADALARLAEELGGEIRTGAEVERILVEGGRATGVRLADGEEIRADAVVSNADPAHTYL 282
SdhA COG1053
Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and ...
3-244 1.96e-05

Succinate dehydrogenase/fumarate reductase, flavoprotein subunit [Energy production and conversion]; Succinate dehydrogenase/fumarate reductase, flavoprotein subunit is part of the Pathway/BioSystem: TCA cycle


Pssm-ID: 440673 [Multi-domain]  Cd Length: 443  Bit Score: 46.75  E-value: 1.96e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   3 RTYDIVIAGGGVIGASCAYQLSRRGnLRIAVVD-DKRPGNATRASAGGLWAIGESVGLGCGviffrmmssrnrreaqgaa 81
Cdd:COG1053   2 HEYDVVVVGSGGAGLRAALEAAEAG-LKVLVLEkVPPRGGHTAAAQGGINAAGTNVQKAAG------------------- 61
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  82 vaVDasTPHIlppAFFDLalqsnalypelhrelieRHGMDFKFertglkyviqdDEDRqyAEHIVAQIPhlaEQVRWLDR 161
Cdd:COG1053  62 --ED--SPEE---HFYDT-----------------VKGGDGLA-----------DQDL--VEALAEEAP---EAIDWLEA 101
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391 162 EELRraepaVSHAAHGALEFLCDHQVSpfR-----------LADAYLEAARQNGVELLPGTNVTGVLRQGRRISGVRTDN 230
Cdd:COG1053 102 QGVP-----FSRTPDGRLPQFGGHSVG--RtcyagdgtghaLLATLYQAALRLGVEIFTETEVLDLIVDDGRVVGVVARD 174
                       250
                ....*....|....*...
gi 15597391 231 AG----VLHCRTLINAAG 244
Cdd:COG1053 175 RTgeivRIRAKAVVLATG 192
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
194-245 3.10e-05

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 45.34  E-value: 3.10e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 15597391 194 DAYL-EAARQNGVELLPGTNVTGVLRQGRRISgVRTDNAGVLHCRTLINAAGA 245
Cdd:COG0644  89 DRWLaEQAEEAGAEVRTGTRVTDVLRDDGRVV-VRTGDGEEIRADYVVDADGA 140
FAD_binding_2 pfam00890
FAD binding domain; This family includes members that bind FAD. This family includes the ...
6-54 4.74e-04

FAD binding domain; This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase.


Pssm-ID: 395718 [Multi-domain]  Cd Length: 398  Bit Score: 42.27  E-value: 4.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 15597391     6 DIVIAGGGVIGASCAYQLSRRGnLRIAVVD-DKRPGNATRASAGGLWAIG 54
Cdd:pfam00890   1 DVLVIGGGLAGLAAALAAAEAG-LKVAVVEkGQPFGGATAWSSGGIDALG 49
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
2-52 5.24e-04

2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion]; 2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 440419 [Multi-domain]  Cd Length: 326  Bit Score: 41.85  E-value: 5.24e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15597391   2 NRTYDIVIAGGGVIGASCAYQLSRRGnLRIAVVdDKRPGNATRASAGGLWA 52
Cdd:COG0654   1 MMRTDVLIVGGGPAGLALALALARAG-IRVTVV-ERAPPPRPDGRGIALSP 49
PLN02661 PLN02661
Putative thiazole synthesis
6-55 5.54e-04

Putative thiazole synthesis


Pssm-ID: 178267  Cd Length: 357  Bit Score: 41.74  E-value: 5.54e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 15597391    6 DIVIAGGGVIGASCAYQLSRRGNLRIAVVDDK-RPGnatrasaGGLWAIGE 55
Cdd:PLN02661  94 DVVIVGAGSAGLSCAYELSKNPNVKVAIIEQSvSPG-------GGAWLGGQ 137
PTZ00383 PTZ00383
malate:quinone oxidoreductase; Provisional
5-280 1.09e-03

malate:quinone oxidoreductase; Provisional


Pssm-ID: 240393 [Multi-domain]  Cd Length: 497  Bit Score: 41.26  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391    5 YDIVIAGGGVIGASCAYQLSRRGNL-RIAVVdDKRPGNATRASAGGlwaiGESVGLGCGVIFFRMMSSRNRREAQGAAVA 83
Cdd:PTZ00383  46 YDVVIVGGGVTGTALFYTLSKFTNLkKIALI-ERRSDFALVASHGK----NNSQTIHCGDIETNYTLEKARKVKRQADML 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391   84 VDASTPhiLPPAFFDL---ALQSNAL-YPELHRELIERHGMDFKFERTGLKYViqDDEDRQYAEHIVAqiphlaeqvrwL 159
Cdd:PTZ00383 121 RNYLTK--LPPSERDSiifKMQKMVLgVGEKECEFLEKRYPVFKELFPSMQLL--DKKEIHRVEPRVV-----------L 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  160 DREELRRAEPAVS------HAAhgaleflCDHQvspfRLADAYLEAARQ----NGVELLPGTN--VTGVLRQGRRISGVR 227
Cdd:PTZ00383 186 KNNHTLREEPLAAlyvpneLTT-------VDYQ----KLSESFVKHARRdalvPGKKISINLNteVLNIERSNDSLYKIH 254
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 15597391  228 TdNAGVLHCRTLINAAGAWAAELSE-MATGRRIPVKPVKGQIVLTermPRLLNG 280
Cdd:PTZ00383 255 T-NRGEIRARFVVVSACGYSLLFAQkMGYGLEYSCLPVAGSFYFS---GNILNG 304
PRK07608 PRK07608
UbiH/UbiF family hydroxylase;
4-35 1.38e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181057 [Multi-domain]  Cd Length: 388  Bit Score: 40.71  E-value: 1.38e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15597391    4 TYDIVIAGGGVIGASCAYQLSRRGnLRIAVVD 35
Cdd:PRK07608   5 KFDVVVVGGGLVGASLALALAQSG-LRVALLA 35
PRK05732 PRK05732
2-octaprenyl-6-methoxyphenyl hydroxylase; Validated
1-47 1.71e-03

2-octaprenyl-6-methoxyphenyl hydroxylase; Validated


Pssm-ID: 235584 [Multi-domain]  Cd Length: 395  Bit Score: 40.22  E-value: 1.71e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 15597391    1 MNRtYDIVIAGGGVIGASCAYQLSR--RGNLRIAVV------DDKRPGNATRASA 47
Cdd:PRK05732   1 MSR-MDVIIVGGGMAGATLALALSRlsHGGLPVALIeafapeSDAHPGFDARAIA 54
glpD PRK12266
glycerol-3-phosphate dehydrogenase; Reviewed
199-302 1.94e-03

glycerol-3-phosphate dehydrogenase; Reviewed


Pssm-ID: 237027 [Multi-domain]  Cd Length: 508  Bit Score: 40.51  E-value: 1.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  199 AARQNGVELLPGTNVTGVLRQGRR----ISGVRTDNAGVLHCRTLINAAGAWAAELSEMATGRRIP--VKPVKG-QIVLt 271
Cdd:PRK12266 164 DAAERGAEILTRTRVVSARRENGLwhvtLEDTATGKRYTVRARALVNAAGPWVKQFLDDGLGLPSPygIRLVKGsHIVV- 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 15597391  272 ermPRLLNGclttSDCYMAQKDNGEI-----------LIGST 302
Cdd:PRK12266 243 ---PRLFDH----DQAYILQNPDGRIvfaipyeddftLIGTT 277
PRK07364 PRK07364
FAD-dependent hydroxylase;
4-35 2.10e-03

FAD-dependent hydroxylase;


Pssm-ID: 236001 [Multi-domain]  Cd Length: 415  Bit Score: 40.00  E-value: 2.10e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 15597391    4 TYDIVIAGGGVIGASCAYQLsRRGNLRIAVVD 35
Cdd:PRK07364  18 TYDVAIVGGGIVGLTLAAAL-KDSGLRIALIE 48
PRK08773 PRK08773
UbiH/UbiF family hydroxylase;
1-39 4.67e-03

UbiH/UbiF family hydroxylase;


Pssm-ID: 181552 [Multi-domain]  Cd Length: 392  Bit Score: 39.08  E-value: 4.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 15597391    1 MNRTY--DIVIAGGGVIGASCAYQLSRRGnLRIAVVDDKRP 39
Cdd:PRK08773   1 MSRRSrrDAVIVGGGVVGAACALALADAG-LSVALVEGREP 40
PRK10015 PRK10015
oxidoreductase; Provisional
139-244 4.84e-03

oxidoreductase; Provisional


Pssm-ID: 182194 [Multi-domain]  Cd Length: 429  Bit Score: 38.80  E-value: 4.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15597391  139 RQYAEHIVAQIPHLAEQV---RWLDREELR--RAEPAVS---HAAHGALEFLCDHQVSPFRLADAYLEAARQNGVELLPG 210
Cdd:PRK10015  49 RLYAHTLEAIIPGFAASApveRKVTREKISflTEESAVTldfHREQPDVPQHASYTVLRNRLDPWLMEQAEQAGAQFIPG 128
                         90       100       110
                 ....*....|....*....|....*....|....
gi 15597391  211 TNVTGVLRQGRRISGVRTDNaGVLHCRTLINAAG 244
Cdd:PRK10015 129 VRVDALVREGNKVTGVQAGD-DILEANVVILADG 161
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
6-54 5.34e-03

Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.


Pssm-ID: 460393  Cd Length: 232  Bit Score: 38.22  E-value: 5.34e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 15597391     6 DIVIAGGGVIGASCAYQLSRRGNLRIAVVDdkrpgnATRASAGGLWAIG 54
Cdd:pfam01946  19 DVVIVGAGSSGLTAAYYLAKNRGLKVAIIE------RSVSPGGGAWLGG 61
 
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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