NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|149129|gb|AAA98149|]
View 

tryptophan monooxygenase (plasmid) [Plasmid pTiS4]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 217-701 5.59e-104

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


:

Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 325.21  E-value: 5.59e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     217 ISGLVSATLLLRNGiDDVTIFEAKNVVGGRAHTHFFKGEPsvcAELGAMRFPRSQACLFYLLEYLGINAMTKFPNPGTVD 296
Cdd:pfam01593   1 LAGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFL---IELGAMWFHGAQPPLLALLKELGLEDRLVLPDPAPFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     297 TGLYYRGRSYnwkahslpPAIFNRVHKGWRTFLhagfvdgvaAFASPFTLTECLRLRNYEFASslwqKWLDAFSSETFSS 376
Cdd:pfam01593  77 TVLFAGGRRY--------PGDFRRVPAGWEGLL---------EFGRLLSIPEKLRLGLAALAS----DALDEFDLDDFSL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     377 GIERIFRGAHPPGG-EKWTRDVDMELFKELGVGSGGFG---PVFGCGFIEILRLIVNGYEDNVMLLLDGIEEIPRRLSQQ 452
Cdd:pfam01593 136 AESLLFLGRRGPGDvEVWDRLIDPELFAALPFASGAFAgdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQ 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     453 KVGSySIRDRiihKEVKEIIRTESGISLAIGEGMHATFDRVIVTSGFTNIQlRHLLTNDdsfFSYDVNQAIENSHMTGSS 532
Cdd:pfam01593 216 LLGG-DVRLN---TRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLK-RILFTPP---LPPEKARAIRNLGYGPVN 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     533 KLFVLTQNKFWKAEEL--PSCILTTGVAKAVYCLDYEPDKPSGKGLVLLSYTWEDDSHKLL-TFDKGERFQILKRDLAKS 609
Cdd:pfam01593 288 KVHLEFDRKFWPDLGLlgLLSELLTGLGTAFSWLTFPNRAPPGKGLLLLVYVGPGDRARELeGLSDEELLQAVLRDLRKL 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     610 YprfadllePADGDYDNNIIQHDWILDPYAGGAFKLNRRCEDvyskRLFFQPLRLngEPDGRVCLAGCSCSFSG-GWVEG 688
Cdd:pfam01593 368 F--------GEEAPEPLRVLVSDWHTDPWPRGSYSLPQYGPG----HDDYRPLAR--TPDPGLFFAGEHTSTGYpGTVEG 433

                         490
                  ....*....|...
gi 149129     689 AIQTACNAAMATI 701
Cdd:pfam01593 434 AIESGRRAARAVL 446
RolB_RolC super family cl03410
RolB/RolC glucosidase family; This family of proteins includes RolB and RolC. RolC releases ...
 9-166 1.72e-29

RolB/RolC glucosidase family; This family of proteins includes RolB and RolC. RolC releases cytokinins from glucoside conjugates. Whereas RolB hydrolyses indole glucosides.


The actual alignment was detected with superfamily member pfam02027:

Pssm-ID: 366884  Cd Length: 184  Bit Score: 115.62  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129       9 ITNRSYSTKNLLNIEDKGRLKDELEKTRQTniceiclhprgHRASVCRQILMG--------------------------- 61
Cdd:pfam02027   1 MTRPVFTVIDLSNITDREELKLRLEQARSD-----------YRAFVERDLLFAqrswvarflrkpcldgprlpgifdgdt 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129      62 --------FAYTSKTVLEGLLSTMPHDDAPLGKIFVTDLPPYDEQVPQVLLMQAAALV-TSYEYSFEDLAYFLVLPLQMA 132
Cdd:pfam02027  70 illddsplYVYCSREILRQCAESRPLSSSSPSGLVATTLPPYREDITREQMRQLLNLVsVGYYQGPHDLSHFVAILPSKS 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 149129     133 LMQKS-------------PSLGKDFPvisgYSItkdsvhspVAFGRN 166
Cdd:pfam02027 150 FRRKGafhtsgevygffaRSLGDAFP----YDI--------VAVGRA 184
 
Name Accession Description Interval E-value
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 217-701 5.59e-104

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


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 325.21  E-value: 5.59e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     217 ISGLVSATLLLRNGiDDVTIFEAKNVVGGRAHTHFFKGEPsvcAELGAMRFPRSQACLFYLLEYLGINAMTKFPNPGTVD 296
Cdd:pfam01593   1 LAGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFL---IELGAMWFHGAQPPLLALLKELGLEDRLVLPDPAPFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     297 TGLYYRGRSYnwkahslpPAIFNRVHKGWRTFLhagfvdgvaAFASPFTLTECLRLRNYEFASslwqKWLDAFSSETFSS 376
Cdd:pfam01593  77 TVLFAGGRRY--------PGDFRRVPAGWEGLL---------EFGRLLSIPEKLRLGLAALAS----DALDEFDLDDFSL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     377 GIERIFRGAHPPGG-EKWTRDVDMELFKELGVGSGGFG---PVFGCGFIEILRLIVNGYEDNVMLLLDGIEEIPRRLSQQ 452
Cdd:pfam01593 136 AESLLFLGRRGPGDvEVWDRLIDPELFAALPFASGAFAgdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQ 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     453 KVGSySIRDRiihKEVKEIIRTESGISLAIGEGMHATFDRVIVTSGFTNIQlRHLLTNDdsfFSYDVNQAIENSHMTGSS 532
Cdd:pfam01593 216 LLGG-DVRLN---TRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLK-RILFTPP---LPPEKARAIRNLGYGPVN 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     533 KLFVLTQNKFWKAEEL--PSCILTTGVAKAVYCLDYEPDKPSGKGLVLLSYTWEDDSHKLL-TFDKGERFQILKRDLAKS 609
Cdd:pfam01593 288 KVHLEFDRKFWPDLGLlgLLSELLTGLGTAFSWLTFPNRAPPGKGLLLLVYVGPGDRARELeGLSDEELLQAVLRDLRKL 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     610 YprfadllePADGDYDNNIIQHDWILDPYAGGAFKLNRRCEDvyskRLFFQPLRLngEPDGRVCLAGCSCSFSG-GWVEG 688
Cdd:pfam01593 368 F--------GEEAPEPLRVLVSDWHTDPWPRGSYSLPQYGPG----HDDYRPLAR--TPDPGLFFAGEHTSTGYpGTVEG 433

                         490
                  ....*....|...
gi 149129     689 AIQTACNAAMATI 701
Cdd:pfam01593 434 AIESGRRAARAVL 446
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
205-706 5.53e-67

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 227.50  E-value: 5.53e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   205 TKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFkGEPSVCAELGAMRFPRSQACLFYLLEYLGIn 284
Cdd:COG1231   5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRF-GDDGLYAELGAMRIPPSHTNLLALARELGL- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   285 AMTKFPNpGTVDTGLYYRGRSYNWKAHSlppAIFNRVHKGWRTFLHAgfvdgVAAFASPftlteclrlrnyefasslWQK 364
Cdd:COG1231  82 PLEPFPN-ENGNALLYLGGKRVRAGEIA---ADLRGVAELLAKLLRA-----LAAALDP------------------WAH 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   365 WLDAFSSETFSSGIERifrgahpPGGEKWTRDVdMELFKELGVGsGGFGPVfgcGFIEILRLIV-NGYEDNVMLLLDGIE 443
Cdd:COG1231 135 PAAELDRESLAEWLRR-------NGASPSARRL-LGLLGAGEYG-ADPDEL---SLLDLLRYAAsAGGGAQQFRIVGGMD 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   444 EIPRRLSQQkvgsysIRDRIIH-KEVKEIIRTESGISLAIGEGMHATFDRVIVTsgftnIQLRHLLTND-DSFFSYDVNQ 521
Cdd:COG1231 203 QLPRALAAE------LGDRIRLgAPVTRIRQDGDGVTVTTDDGGTVRADAVIVT-----VPPSVLRRIEfDPPLPAAKRA 271

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   522 AIENSHMTGSSKLFVLTQNKFWKAEELPS-CILTTGVAKAVYCLDYEPDKPSGkglVLLSYTWEDDSHKLLTFDKGERFQ 600
Cdd:COG1231 272 AIQRLPYGAAIKVFLQFDRPFWEEDGLYGgISLTDLPIRQTWYPSNGPDGGAG---VLLGYVGGDDARALAALSPEERVA 348

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   601 ILKRDLAKSYPRFAdlLEPADGdydnniIQHDWILDPYAGGAFKLNRrcedVYSKRLFFQPLRlngEPDGRVCLAGCSCS 680
Cdd:COG1231 349 AALEQLARIFGVYA--AEPVDY------VSTDWGRDPWSRGAYAAAP----PGQLTAAGPALA---EPDGRIHFAGEHTS 413

                       490       500
                ....*....|....*....|....*..
gi 149129   681 FSG-GWVEGAIQTACNAAMATIRDAGG 706
Cdd:COG1231 414 DEWpGWVEGALESGERAAAEILARLGG 440
RolB_RolC pfam02027
RolB/RolC glucosidase family; This family of proteins includes RolB and RolC. RolC releases ...
 9-166 1.72e-29

RolB/RolC glucosidase family; This family of proteins includes RolB and RolC. RolC releases cytokinins from glucoside conjugates. Whereas RolB hydrolyses indole glucosides.


Pssm-ID: 366884  Cd Length: 184  Bit Score: 115.62  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129       9 ITNRSYSTKNLLNIEDKGRLKDELEKTRQTniceiclhprgHRASVCRQILMG--------------------------- 61
Cdd:pfam02027   1 MTRPVFTVIDLSNITDREELKLRLEQARSD-----------YRAFVERDLLFAqrswvarflrkpcldgprlpgifdgdt 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129      62 --------FAYTSKTVLEGLLSTMPHDDAPLGKIFVTDLPPYDEQVPQVLLMQAAALV-TSYEYSFEDLAYFLVLPLQMA 132
Cdd:pfam02027  70 illddsplYVYCSREILRQCAESRPLSSSSPSGLVATTLPPYREDITREQMRQLLNLVsVGYYQGPHDLSHFVAILPSKS 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 149129     133 LMQKS-------------PSLGKDFPvisgYSItkdsvhspVAFGRN 166
Cdd:pfam02027 150 FRRKGafhtsgevygffaRSLGDAFP----YDI--------VAVGRA 184
PLN02676 PLN02676
polyamine oxidase
 205-264 2.49e-09

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 60.11  E-value: 2.49e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129    205 TKKPKVAVIGAGISGLVSATLLLRNGIDDVTIFEAKNVVGGRAHTHFFKGepsVCAELGA 264
Cdd:PLN02676  24 KPSPSVIIVGAGMSGISAAKTLSEAGIEDILILEATDRIGGRMRKANFAG---VSVELGA 80
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 207-285 1.31e-04

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 45.21  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     207 KPKVAVIGAGISGLVSATLLLRNGID---DVTIFEAKNVVGGRAHTHFFKGepsVCAELGAMRFPRSQACLFYLLEYLGI 283
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDG---YLIERGPDSFLERKKSAPDLVKDLGL 78


                  ..
gi 149129     284 NA 285
Cdd:TIGR00562  79 EH 80
PBP2_SyrM cd08467
The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates ...
 366-460 1.80e-03

The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates expression of nodulation gene NodD3, contains the type 2 periplasmic binding fold; Rhizobium is a nitrogen fixing bacteria present in the roots of leguminous plants, which fixes atmospheric nitrogen to the soil. Most Rhizobium species possess multiple nodulation (nod) genes for the development of nodules. For example, Rhizobium meliloti possesses three copies of nodD genes. NodD1 and NodD2 activate nod operons when Rhizobium is exposed to inducers synthesized by the host plant, while NodD3 acts independent of plant inducers and requires the symbiotic regulator SyrM for nod gene expression. SyrM activates the expression of the regulatory nodulation gene nodD3. In turn, NodD3 activates expression of syrM. In addition, SyrM is involved in exopolysaccharide synthesis. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176156 [Multi-domain]  Cd Length: 200  Bit Score: 40.11  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   366 LDAFSSETFSSGIERIFRGAHPPGGEKWTRDvDMELFKELGVGSGG--FGPVFGcgfieilRLIVNGYEDNVMLLL---- 439
Cdd:cd08467  62 DGLVVRRLYDDGFACLVRHGHPALAQEWTLD-DFATLRHVAIAPPGrlFGGIYK-------RLENLGLKRNVAIAVssfl 133

                        90       100       110
                ....*....|....*....|....*....|
gi 149129   440 ---------DGIEEIPRRLSQQKVGSYSIR 460
Cdd:cd08467 134 taaatvaatDLIATVPRRVATQVAAMLPLR 163
 
Name Accession Description Interval E-value
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
 217-701 5.59e-104

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


Pssm-ID: 396255 [Multi-domain]  Cd Length: 446  Bit Score: 325.21  E-value: 5.59e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     217 ISGLVSATLLLRNGiDDVTIFEAKNVVGGRAHTHFFKGEPsvcAELGAMRFPRSQACLFYLLEYLGINAMTKFPNPGTVD 296
Cdd:pfam01593   1 LAGLAAARELLRAG-HDVTVLEARDRVGGRIRTVRDDGFL---IELGAMWFHGAQPPLLALLKELGLEDRLVLPDPAPFY 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     297 TGLYYRGRSYnwkahslpPAIFNRVHKGWRTFLhagfvdgvaAFASPFTLTECLRLRNYEFASslwqKWLDAFSSETFSS 376
Cdd:pfam01593  77 TVLFAGGRRY--------PGDFRRVPAGWEGLL---------EFGRLLSIPEKLRLGLAALAS----DALDEFDLDDFSL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     377 GIERIFRGAHPPGG-EKWTRDVDMELFKELGVGSGGFG---PVFGCGFIEILRLIVNGYEDNVMLLLDGIEEIPRRLSQQ 452
Cdd:pfam01593 136 AESLLFLGRRGPGDvEVWDRLIDPELFAALPFASGAFAgdpSELSAGLALPLLWALLGEGGSLLLPRGGLGALPDALAAQ 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     453 KVGSySIRDRiihKEVKEIIRTESGISLAIGEGMHATFDRVIVTSGFTNIQlRHLLTNDdsfFSYDVNQAIENSHMTGSS 532
Cdd:pfam01593 216 LLGG-DVRLN---TRVRSIDREGDGVTVTLTDGEVIEADAVIVTVPLGVLK-RILFTPP---LPPEKARAIRNLGYGPVN 287

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     533 KLFVLTQNKFWKAEEL--PSCILTTGVAKAVYCLDYEPDKPSGKGLVLLSYTWEDDSHKLL-TFDKGERFQILKRDLAKS 609
Cdd:pfam01593 288 KVHLEFDRKFWPDLGLlgLLSELLTGLGTAFSWLTFPNRAPPGKGLLLLVYVGPGDRARELeGLSDEELLQAVLRDLRKL 367

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     610 YprfadllePADGDYDNNIIQHDWILDPYAGGAFKLNRRCEDvyskRLFFQPLRLngEPDGRVCLAGCSCSFSG-GWVEG 688
Cdd:pfam01593 368 F--------GEEAPEPLRVLVSDWHTDPWPRGSYSLPQYGPG----HDDYRPLAR--TPDPGLFFAGEHTSTGYpGTVEG 433

                         490
                  ....*....|...
gi 149129     689 AIQTACNAAMATI 701
Cdd:pfam01593 434 AIESGRRAARAVL 446
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
205-706 5.53e-67

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 227.50  E-value: 5.53e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   205 TKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFkGEPSVCAELGAMRFPRSQACLFYLLEYLGIn 284
Cdd:COG1231   5 ARGKDVVIVGAGLAGLAAARELRKAGL-DVTVLEARDRVGGRVWTLRF-GDDGLYAELGAMRIPPSHTNLLALARELGL- 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   285 AMTKFPNpGTVDTGLYYRGRSYNWKAHSlppAIFNRVHKGWRTFLHAgfvdgVAAFASPftlteclrlrnyefasslWQK 364
Cdd:COG1231  82 PLEPFPN-ENGNALLYLGGKRVRAGEIA---ADLRGVAELLAKLLRA-----LAAALDP------------------WAH 134

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   365 WLDAFSSETFSSGIERifrgahpPGGEKWTRDVdMELFKELGVGsGGFGPVfgcGFIEILRLIV-NGYEDNVMLLLDGIE 443
Cdd:COG1231 135 PAAELDRESLAEWLRR-------NGASPSARRL-LGLLGAGEYG-ADPDEL---SLLDLLRYAAsAGGGAQQFRIVGGMD 202

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   444 EIPRRLSQQkvgsysIRDRIIH-KEVKEIIRTESGISLAIGEGMHATFDRVIVTsgftnIQLRHLLTND-DSFFSYDVNQ 521
Cdd:COG1231 203 QLPRALAAE------LGDRIRLgAPVTRIRQDGDGVTVTTDDGGTVRADAVIVT-----VPPSVLRRIEfDPPLPAAKRA 271

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   522 AIENSHMTGSSKLFVLTQNKFWKAEELPS-CILTTGVAKAVYCLDYEPDKPSGkglVLLSYTWEDDSHKLLTFDKGERFQ 600
Cdd:COG1231 272 AIQRLPYGAAIKVFLQFDRPFWEEDGLYGgISLTDLPIRQTWYPSNGPDGGAG---VLLGYVGGDDARALAALSPEERVA 348

                       410       420       430       440       450       460       470       480
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   601 ILKRDLAKSYPRFAdlLEPADGdydnniIQHDWILDPYAGGAFKLNRrcedVYSKRLFFQPLRlngEPDGRVCLAGCSCS 680
Cdd:COG1231 349 AALEQLARIFGVYA--AEPVDY------VSTDWGRDPWSRGAYAAAP----PGQLTAAGPALA---EPDGRIHFAGEHTS 413

                       490       500
                ....*....|....*....|....*..
gi 149129   681 FSG-GWVEGAIQTACNAAMATIRDAGG 706
Cdd:COG1231 414 DEWpGWVEGALESGERAAAEILARLGG 440
RolB_RolC pfam02027
RolB/RolC glucosidase family; This family of proteins includes RolB and RolC. RolC releases ...
 9-166 1.72e-29

RolB/RolC glucosidase family; This family of proteins includes RolB and RolC. RolC releases cytokinins from glucoside conjugates. Whereas RolB hydrolyses indole glucosides.


Pssm-ID: 366884  Cd Length: 184  Bit Score: 115.62  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129       9 ITNRSYSTKNLLNIEDKGRLKDELEKTRQTniceiclhprgHRASVCRQILMG--------------------------- 61
Cdd:pfam02027   1 MTRPVFTVIDLSNITDREELKLRLEQARSD-----------YRAFVERDLLFAqrswvarflrkpcldgprlpgifdgdt 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129      62 --------FAYTSKTVLEGLLSTMPHDDAPLGKIFVTDLPPYDEQVPQVLLMQAAALV-TSYEYSFEDLAYFLVLPLQMA 132
Cdd:pfam02027  70 illddsplYVYCSREILRQCAESRPLSSSSPSGLVATTLPPYREDITREQMRQLLNLVsVGYYQGPHDLSHFVAILPSKS 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 149129     133 LMQKS-------------PSLGKDFPvisgYSItkdsvhspVAFGRN 166
Cdd:pfam02027 150 FRRKGafhtsgevygffaRSLGDAFP----YDI--------VAVGRA 184
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
 207-496 1.50e-11

Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen oxidase HemY/PPOX is part of the Pathway/BioSystem: Heme biosynthesis


Pssm-ID: 440845 [Multi-domain]  Cd Length: 443  Bit Score: 67.16  E-value: 1.50e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   207 KPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFKGepsVCAELGAMRF-PRSQAcLFYLLEYLGINA 285
Cdd:COG1232   1 MKRVAVIGGGIAGLTAAYRLAKAGH-EVTVLEASDRVGGLIRTVEVDG---FRIDRGPHSFlTRDPE-VLELLRELGLGD 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   286 MTKFPNPGtvdTGLYYRGRsynwKAHSLPPAIFNRVHK---GWRTFLHAGFvdgvAAFASPF------TLTECLRLRnye 356
Cdd:COG1232  76 ELVWPNTR---KSYIYYGG----KLHPLPQGPLALLRSpllSLAGKLRALL----ELLAPRRppgedeSLAEFVRRR--- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   357 FASSLWQKWLDAFSSETFSSGIERI-FRGAHP--PGGEKWTRDV--DMELFKELGVGSGGFGPVFGcgfieilrlivngy 431
Cdd:COG1232 142 FGREVYERLVEPLLEGVYAGDPDELsADWAFPrlKRLELEHGSLikGALALRKGAKAGEVFGYLRG-------------- 207

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 149129   432 ednvmllldGIEEIPRRLSQQkvgsysIRDRIIHK--EVKEIIRTESGISLAIGEGMHATFDRVIVT 496
Cdd:COG1232 208 ---------GLGTLVEALAEA------LEAGEIRLgtRVTAIEREGGGWRVTTSDGETIEADAVVSA 259
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
 205-254 4.31e-11

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 66.03  E-value: 4.31e-11
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|
gi 149129   205 TKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFKG 254
Cdd:COG1233   1 MMMYDVVVIGAGIGGLAAAALLARAGY-RVTVLEKNDTPGGRARTFERPG 49
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
206-250 4.12e-10

Predicted flavin-containing amine oxidase [General function prediction only];


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 62.44  E-value: 4.12e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 149129   206 KKPKVAVIGAGISGLVSATLLLRNgiDDVTIFEAKNVVGGRAHTH 250
Cdd:COG2907   2 ARMRIAVIGSGISGLTAAWLLSRR--HDVTLFEANDRLGGHTHTV 44
PLN02676 PLN02676
polyamine oxidase
 205-264 2.49e-09

polyamine oxidase


Pssm-ID: 215362 [Multi-domain]  Cd Length: 487  Bit Score: 60.11  E-value: 2.49e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129    205 TKKPKVAVIGAGISGLVSATLLLRNGIDDVTIFEAKNVVGGRAHTHFFKGepsVCAELGA 264
Cdd:PLN02676  24 KPSPSVIIVGAGMSGISAAKTLSEAGIEDILILEATDRIGGRMRKANFAG---VSVELGA 80
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
212-281 2.94e-09

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 53.69  E-value: 2.94e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 149129     212 VIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFKGEPsvcAELGAMRF-PRSQACLFYLLEYL 281
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGF-RVLVLEKRDRLGGNAYSYRVPGYV---FDYGAHIFhGSDEPNVRDLLDEL 67
PRK07233 PRK07233
hypothetical protein; Provisional
 209-308 9.45e-09

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 58.36  E-value: 9.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129    209 KVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFKGEPsvcAElgamRF----PRSQACLFYLLEYLGIN 284
Cdd:PRK07233   1 KIAIVGGGIAGLAAAYRLAKRGH-EVTVFEADDQLGGLAASFEFGGLP---IE----RFyhhiFKSDEALLELLDELGLE 72

                         90       100
                 ....*....|....*....|....
gi 149129    285 AMTKFPNPgtvDTGLYYRGRSYNW 308
Cdd:PRK07233  73 DKLRWRET---KTGYYVDGKLYPL 93
PRK07208 PRK07208
hypothetical protein; Provisional
 205-254 4.21e-07

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 52.97  E-value: 4.21e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 149129    205 TKKPKVAVIGAGISGLVSATLLLRNGIDdVTIFEAKNVVGGRAHTHFFKG 254
Cdd:PRK07208   2 TNKKSVVIIGAGPAGLTAAYELLKRGYP-VTVLEADPVVGGISRTVTYKG 50
PRK11883 PRK11883
protoporphyrinogen oxidase; Reviewed
 208-264 4.95e-07

protoporphyrinogen oxidase; Reviewed


Pssm-ID: 237009 [Multi-domain]  Cd Length: 451  Bit Score: 52.93  E-value: 4.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 149129    208 PKVAVIGAGISGLVSATLLLRNGID-DVTIFEAKNVVGGRAHTHFFKGEPsvcAELGA 264
Cdd:PRK11883   1 KKVAIIGGGITGLSAAYRLHKKGPDaDITLLEASDRLGGKIQTVRKDGFP---IELGP 55
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
 193-245 7.72e-07

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: 52.06  E-value: 7.72e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 149129   193 AFSEGVTSFPK---ETKKpKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:COG0493 105 AFEEGWVKPPPpapRTGK-KVAVVGSGPAGLAAAYQLARAGH-EVTVFEALDKPGG 158
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
207-249 9.31e-07

Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 51.42  E-value: 9.31e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 149129   207 KPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHT 249
Cdd:COG3380   3 MPDIAIIGAGIAGLAAARALQDAGH-EVTVFEKSRGVGGRMAT 44
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
 208-251 1.14e-06

Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function prediction only];


Pssm-ID: 442577 [Multi-domain]  Cd Length: 445  Bit Score: 51.78  E-value: 1.14e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 149129   208 PKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHF 251
Cdd:COG3349   4 PRVVVVGGGLAGLAAAVELAEAGF-RVTLLEARPRLGGRARSFP 46
PLN03000 PLN03000
amine oxidase
 179-263 2.69e-06

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 50.79  E-value: 2.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129    179 IDVLYDY---RGFLEGGAFSEGVTSFPKETKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFKG- 254
Cdd:PLN03000 153 LDSAYNYlvtHGYINFGIAQAIKDKFPAQSSKSSVVIVGAGLSGLAAARQLMRFGF-KVTVLEGRKRPGGRVYTKKMEAn 231


                 ....*....
gi 149129    255 EPSVCAELG 263
Cdd:PLN03000 232 RVGAAADLG 240
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
 209-351 5.91e-06

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: 48.93  E-value: 5.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     209 KVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVG----GRA----HTHFFKGEPSVCAELGAmrfpRSQACLFYLLEY 280
Cdd:pfam01266   1 DVVVIGGGIVGLSTAYELARRGL-SVTLLERGDDPGsgasGRNagliHPGLRYLEPSELARLAL----EALDLWEELEEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     281 LGINAMtkFPNPGTVDTG----------LYYRGRSYNWKAHSLPPAIFNRVHKGWRTFLHAGFVDGvAAFASPFTLTECL 350
Cdd:pfam01266  76 LGIDCG--FRRCGVLVLArdeeeealekLLAALRRLGVPAELLDAEELRELEPLLPGLRGGLFYPD-GGHVDPARLLRAL 152


                  .
gi 149129     351 R 351
Cdd:pfam01266 153 A 153
PLN02328 PLN02328
lysine-specific histone demethylase 1 homolog
 179-263 6.03e-06

lysine-specific histone demethylase 1 homolog


Pssm-ID: 215187 [Multi-domain]  Cd Length: 808  Bit Score: 49.61  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129    179 IDVLYDYrgFLEGGAFSEGVTSFPKETK--------KPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTH 250
Cdd:PLN02328 204 VDSAYNF--LLEHGYINFGVAPVIKEAQlrsfegvePANVVVVGAGLAGLVAARQLLSMGF-KVVVLEGRARPGGRVKTM 280

                         90
                 ....*....|....
gi 149129    251 FFKGEPSVC-AELG 263
Cdd:PLN02328 281 KMKGDGVVAaADLG 294
PLN02576 PLN02576
protoporphyrinogen oxidase
 210-245 9.89e-06

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 48.86  E-value: 9.89e-06
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 149129    210 VAVIGAGISGLVSATLLLRNGIDDVTIFEAKNVVGG 245
Cdd:PLN02576  15 VAVVGAGVSGLAAAYALASKHGVNVLVTEARDRVGG 50
gltD PRK12810
glutamate synthase subunit beta; Reviewed
 193-245 1.30e-05

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 48.24  E-value: 1.30e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149129    193 AFSEG-VTSFPKE--TKKpKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK12810 127 AFEEGwVKPDPPVkrTGK-KVAVVGSGPAGLAAADQLARAGH-KVTVFERADRIGG 180
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
 193-245 1.32e-05

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 48.25  E-value: 1.32e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 149129    193 AFSEGVTSF--PKETKKpKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK11749 125 AMETGWVLFkrAPKTGK-KVAVIGAGPAGLTAAHRLARKGY-DVTIFEARDKAGG 177
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
 202-245 3.23e-05

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: 46.78  E-value: 3.23e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 149129   202 PKETKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:COG2072   1 TAATEHVDVVVIGAGQAGLAAAYHLRRAGI-DFVVLEKADDVGG 43
PLN02568 PLN02568
polyamine oxidase
 206-264 3.34e-05

polyamine oxidase


Pssm-ID: 215308 [Multi-domain]  Cd Length: 539  Bit Score: 47.13  E-value: 3.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149129    206 KKPKVAVIGAGISGLVSATLLLRNGID----DVTIFEAKNVVGGRAHTHFFKGEPsvcAELGA 264
Cdd:PLN02568   4 KKPRIVIIGAGMAGLTAANKLYTSSAAndmfELTVVEGGDRIGGRINTSEFGGER---IEMGA 63
PLN02268 PLN02268
probable polyamine oxidase
 208-264 4.00e-05

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 46.60  E-value: 4.00e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 149129    208 PKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRAHTHFFKGEPsvcAELGA 264
Cdd:PLN02268   1 PSVIVIGGGIAGIAAARALHDASF-KVTLLESRDRIGGRVHTDYSFGFP---VDMGA 53
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
 202-245 4.06e-05

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 47.03  E-value: 4.06e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 149129    202 PKETKKpkVAVIGAGISGLVSATLLLRNGiDDVTIFEAKNVVGG 245
Cdd:PRK12814 190 PKSGKK--VAIIGAGPAGLTAAYYLLRKG-HDVTIFDANEQAGG 230
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
 205-249 4.86e-05

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: 46.08  E-value: 4.86e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 149129   205 TKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVV--GGRAHT 249
Cdd:COG0654   1 MMRTDVLIVGGGPAGLALALALARAGI-RVTVVERAPPPrpDGRGIA 46
PRK12831 PRK12831
putative oxidoreductase; Provisional
 202-245 7.80e-05

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 45.78  E-value: 7.80e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 149129    202 PKETKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK12831 135 TEEKKGKKVAVIGSGPAGLTCAGDLAKMGY-DVTIFEALHEPGG 177
PLN02976 PLN02976
amine oxidase
 209-264 1.09e-04

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 46.01  E-value: 1.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 149129     209 KVAVIGAGISGLVSATLLLRNGIDdVTIFEAKNVVGGRAHTHffKGEPSVCAELGA 264
Cdd:PLN02976  695 KIIVVGAGPAGLTAARHLQRQGFS-VTVLEARSRIGGRVYTD--RSSLSVPVDLGA 747
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
 207-285 1.31e-04

protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a precursor of heme and chlorophyll. Bacillus subtilis HemY also has coproporphyrinogen III to coproporphyrin III oxidase activity in a heterologous expression system, although the role for this activity in vivo is unclear. This protein is a flavoprotein and has a beta-alpha-beta dinucleotide binding motif near the amino end. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 213540 [Multi-domain]  Cd Length: 462  Bit Score: 45.21  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129     207 KPKVAVIGAGISGLVSATLLLRNGID---DVTIFEAKNVVGGRAHTHFFKGepsVCAELGAMRFPRSQACLFYLLEYLGI 283
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAYYLEKEIPElpvELTLVEASDRVGGKIQTVKEDG---YLIERGPDSFLERKKSAPDLVKDLGL 78


                  ..
gi 149129     284 NA 285
Cdd:TIGR00562  79 EH 80
PLN02612 PLN02612
phytoene desaturase
 103-246 2.15e-04

phytoene desaturase


Pssm-ID: 215330 [Multi-domain]  Cd Length: 567  Bit Score: 44.45  E-value: 2.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129    103 LLMQAAALVTSYEYSFEDLayflvlplQMALMQKSPSLGKDFPVISGYSITK----DSVHSPVafgrnlmpRGVSCEFPQ 178
Cdd:PLN02612   2 VFGNVSALNLSWHSGFLDA--------QALAFRGSESMGHSLRVPTSSSSRTrrrrNSGRGPL--------QVVCVDYPR 65

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 149129    179 IDvLYDYRGFLEGGAFSEGVTSFPKETKKPKVAVIGAGISGLVSATLLLRNGIDDVtIFEAKNVVGGR 246
Cdd:PLN02612  66 PE-LENTVNFLEAAALSASFRSAPRPAKPLKVVIAGAGLAGLSTAKYLADAGHKPI-LLEARDVLGGK 131
PRK07236 PRK07236
hypothetical protein; Provisional
 203-238 3.52e-04

hypothetical protein; Provisional


Pssm-ID: 235980 [Multi-domain]  Cd Length: 386  Bit Score: 43.37  E-value: 3.52e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 149129    203 KETKKPKVAVIGAGISGLVSATLLLRNGIDdVTIFE 238
Cdd:PRK07236   2 THMSGPRAVVIGGSLGGLFAALLLRRAGWD-VDVFE 36
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
 193-245 6.36e-04

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 42.94  E-value: 6.36e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 149129    193 AFSEGVTsFPK---ETKKpKVAVIGAGISGLVSATLLLRNGiDDVTIFEAKNVVGG 245
Cdd:PRK12771 122 AIANGWK-FPApapDTGK-RVAVIGGGPAGLSAAYHLRRMG-HAVTIFEAGPKLGG 174
PRK06753 PRK06753
hypothetical protein; Provisional
 209-243 6.41e-04

hypothetical protein; Provisional


Pssm-ID: 168661 [Multi-domain]  Cd Length: 373  Bit Score: 42.75  E-value: 6.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 149129    209 KVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVV 243
Cdd:PRK06753   2 KIAIIGAGIGGLTAAALLQEQGH-EVKVFEKNESV 35
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
 207-245 9.71e-04

putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; Provisional


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 42.51  E-value: 9.71e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 149129    207 KPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK12779 306 KPPIAVVGSGPSGLINAYLLAVEGF-PVTVFEAFHDLGG 343
PLN02487 PLN02487
zeta-carotene desaturase
 201-247 1.05e-03

zeta-carotene desaturase


Pssm-ID: 215268 [Multi-domain]  Cd Length: 569  Bit Score: 42.48  E-value: 1.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 149129    201 FPKETKKP-----KVAVIGAGISGLVSATLLLRNGiDDVTIFEAKNVVGGRA 247
Cdd:PLN02487  64 FPPEPEAYkgpklKVAIIGAGLAGMSTAVELLDQG-HEVDIYESRPFIGGKV 114
HdrA COG1148
Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];
208-259 1.38e-03

Heterodisulfide reductase, subunit A (polyferredoxin) [Energy production and conversion];


Pssm-ID: 440762 [Multi-domain]  Cd Length: 563  Bit Score: 41.77  E-value: 1.38e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 149129   208 PKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRA---HTHFFKGEPSVC 259
Cdd:COG1148 141 KRALVIGGGIAGMTAALELAEQGY-EVYLVEKEPELGGRAaqlHKTFPGLDCPQC 194
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
 200-245 1.42e-03

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 42.04  E-value: 1.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 149129    200 SFP--KETKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK12778 422 SVPevAEKNGKKVAVIGSGPAGLSFAGDLAKRGY-DVTVFEALHEIGG 468
PBP2_SyrM cd08467
The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates ...
 366-460 1.80e-03

The C-terminal substrate binding of LysR-type symbiotic regulator SyrM, which activates expression of nodulation gene NodD3, contains the type 2 periplasmic binding fold; Rhizobium is a nitrogen fixing bacteria present in the roots of leguminous plants, which fixes atmospheric nitrogen to the soil. Most Rhizobium species possess multiple nodulation (nod) genes for the development of nodules. For example, Rhizobium meliloti possesses three copies of nodD genes. NodD1 and NodD2 activate nod operons when Rhizobium is exposed to inducers synthesized by the host plant, while NodD3 acts independent of plant inducers and requires the symbiotic regulator SyrM for nod gene expression. SyrM activates the expression of the regulatory nodulation gene nodD3. In turn, NodD3 activates expression of syrM. In addition, SyrM is involved in exopolysaccharide synthesis. This substrate-binding domain shows significant homology to the type 2 periplasmic binding proteins (PBP2), which are responsible for the uptake of a variety of substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. The PBP2 bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis.


Pssm-ID: 176156 [Multi-domain]  Cd Length: 200  Bit Score: 40.11  E-value: 1.80e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149129   366 LDAFSSETFSSGIERIFRGAHPPGGEKWTRDvDMELFKELGVGSGG--FGPVFGcgfieilRLIVNGYEDNVMLLL---- 439
Cdd:cd08467  62 DGLVVRRLYDDGFACLVRHGHPALAQEWTLD-DFATLRHVAIAPPGrlFGGIYK-------RLENLGLKRNVAIAVssfl 133

                        90       100       110
                ....*....|....*....|....*....|
gi 149129   440 ---------DGIEEIPRRLSQQKVGSYSIR 460
Cdd:cd08467 134 taaatvaatDLIATVPRRVATQVAAMLPLR 163
PRK08243 PRK08243
4-hydroxybenzoate 3-monooxygenase; Validated
 209-241 1.85e-03

4-hydroxybenzoate 3-monooxygenase; Validated


Pssm-ID: 236198 [Multi-domain]  Cd Length: 392  Bit Score: 41.32  E-value: 1.85e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 149129    209 KVAVIGAGISGLVSATLLLRNGIDDVtIFEAKN 241
Cdd:PRK08243   4 QVAIIGAGPAGLLLGQLLHLAGIDSV-VLERRS 35
PRK13984 PRK13984
putative oxidoreductase; Provisional
 198-245 1.93e-03

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 41.68  E-value: 1.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 149129    198 VTSFPKETKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK13984 274 ILDDEPEKKNKKVAIVGSGPAGLSAAYFLATMGY-EVTVYESLSKPGG 320
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
 209-245 2.35e-03

putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin domain-containing protein; Provisional


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 41.47  E-value: 2.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 149129     209 KVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGG 245
Cdd:PRK12775  432 KVAICGSGPAGLAAAADLVKYGV-DVTVYEALHVVGG 467
FAD_binding_3 pfam01494
FAD binding domain; This domain is involved in FAD binding in a number of enzymes.
 209-249 3.47e-03

FAD binding domain; This domain is involved in FAD binding in a number of enzymes.


Pssm-ID: 396193 [Multi-domain]  Cd Length: 348  Bit Score: 40.39  E-value: 3.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 149129     209 KVAVIGAGISGLVSATLLLRNGIdDVTIFE--AKNVVGGRAHT 249
Cdd:pfam01494   3 DVLIVGGGPAGLMLALLLARAGV-RVVLVErhATTSVLPRAHG 44
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
 202-247 3.91e-03

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: 40.60  E-value: 3.91e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 149129    202 PKETKKPKVAVIGAGISGLVSATLLLRNGIdDVTIFEAKNVVGGRA 247
Cdd:PRK01747 255 PGSPKARDAAIIGGGIAGAALALALARRGW-QVTLYEADEAPAQGA 299
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
209-250 8.47e-03

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 39.12  E-value: 8.47e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 149129   209 KVAVIGAGISGLVSATLLLRNGIdDVTIFEAkNVVGGRAHTH 250
Cdd:COG0665   4 DVVVIGGGIAGLSTAYHLARRGL-DVTVLER-GRPGSGASGR 43
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH