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Conserved domains on  [gi|440577511|emb|CBX26643|]
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flavin-dependent monooxygenase (ZvFMOa) [Zonocerus variegatus]

Protein Classification

flavin-containing monooxygenase( domain architecture ID 1750397)

flavin-containing monooxygenase (FMO) may act as an xenobiotic-metabolising enzyme that catalyzes the oxygenation of nucleophilic nitrogen, sulphur, phosphorus and selenium atoms in a range of structurally diverse compounds by using an NADPH cofactor and FAD prosthetic group

EC:  1.14.13.8
Gene Ontology:  GO:0004499|GO:0050661|GO:0050660
PubMed:  9538688

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PLN02172 super family cl40780
flavin-containing monooxygenase FMO GS-OX
2-334 1.19e-74

flavin-containing monooxygenase FMO GS-OX


The actual alignment was detected with superfamily member PLN02172:

Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 240.15  E-value: 1.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNYTDETW---MSED-GRPI-YTSLYQNLVVNLPKEIMAFPD 76
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSEsdpLSLDpTRSIvHSSVYESLRTNLPRECMGYRD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  77 FPF-HHVDDS------YVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPCDSGWLVTVTDLTTMMEQSFeFDAVAVCT 149
Cdd:PLN02172  91 FPFvPRFDDEsrdsrrYPSHREVLAYLQDFAREFKIEEMVRFETEVVRVEPVDGKWRVQSKNSGGFSKDEI-FDAVVVCN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 150 GQCWCPLYPNVEGRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRR--ELKTVEGL-FPD 226
Cdd:PLN02172 170 GHYTEPNVAHIPGIKSWPGKQIHSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRasESDTYEKLpVPQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 227 NVtekplLTSLSEY-TAH------FSDGTSTDIDDIIYCTGYRFRFPFLSPECGVIVDEKRVHPLYLHVLNIN-KPTMGF 298
Cdd:PLN02172 250 NN-----LWMHSEIdTAHedgsivFKNGKVVYADTIVHCTGYKYHFPFLETNGYMRIDENRVEPLYKHVFPPAlAPGLSF 324
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 440577511 299 VGVPHDACFSILFDLQAQWFTAVLAGRCTLPDAETM 334
Cdd:PLN02172 325 IGLPAMGIQFVMFEIQSKWVAAVLSGRVTLPSEDKM 360
 
Name Accession Description Interval E-value
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
2-334 1.19e-74

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 240.15  E-value: 1.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNYTDETW---MSED-GRPI-YTSLYQNLVVNLPKEIMAFPD 76
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSEsdpLSLDpTRSIvHSSVYESLRTNLPRECMGYRD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  77 FPF-HHVDDS------YVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPCDSGWLVTVTDLTTMMEQSFeFDAVAVCT 149
Cdd:PLN02172  91 FPFvPRFDDEsrdsrrYPSHREVLAYLQDFAREFKIEEMVRFETEVVRVEPVDGKWRVQSKNSGGFSKDEI-FDAVVVCN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 150 GQCWCPLYPNVEGRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRR--ELKTVEGL-FPD 226
Cdd:PLN02172 170 GHYTEPNVAHIPGIKSWPGKQIHSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRasESDTYEKLpVPQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 227 NVtekplLTSLSEY-TAH------FSDGTSTDIDDIIYCTGYRFRFPFLSPECGVIVDEKRVHPLYLHVLNIN-KPTMGF 298
Cdd:PLN02172 250 NN-----LWMHSEIdTAHedgsivFKNGKVVYADTIVHCTGYKYHFPFLETNGYMRIDENRVEPLYKHVFPPAlAPGLSF 324
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 440577511 299 VGVPHDACFSILFDLQAQWFTAVLAGRCTLPDAETM 334
Cdd:PLN02172 325 IGLPAMGIQFVMFEIQSKWVAAVLSGRVTLPSEDKM 360
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
2-334 1.12e-60

Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.


Pssm-ID: 395602 [Multi-domain]  Cd Length: 531  Bit Score: 205.40  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511    2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNYTDEtwmSEDGRpiyTSLYQNLVVNLPKEIMAFPDFPFHH 81
Cdd:pfam00743   2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRFTEN---VEEGR---ASIYKSVITNTSKEMSCFSDFPFPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   82 VDDSYVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPC----DSG-WlvtvtDLTTMME---QSFEFDAVAVCTGQCW 153
Cdd:pfam00743  76 DYPNFMHNSKFLEYFRMFAKEFDLLKYIQFKTTVCSVKKRpdfsTSGqW-----EVVTEHEgkqESAVFDAVMVCTGHHT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  154 CPLYP--NVEGRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRRE--------------- 216
Cdd:pfam00743 151 NPHLPleSFPGIEKFKGQYFHSRDYKHPEGFTGKRVLVIGIGNSGGDIAVELSHTAAQVFLSTRRgswvlsrvsdhgypw 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  217 -----------LKTV----------------------EGLFPDN---------------------VTEKPLLTSLSEYTA 242
Cdd:pfam00743 231 dmlfstrftsfLRNIlptsisnwlmekqmnrrfnhenYGLKPKNralskepvvnddlpnrilcgaVKVKPNVKEFTETSA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  243 HFSDGT-STDIDDIIYCTGYRFRFPFLSpECGVIVDEKRVHpLYLHV--LNINKPTMGFVGV--PHDACFSILfDLQAQW 317
Cdd:pfam00743 311 IFEDGTvEEDIDVVIFATGYTFAFPFLE-ESLVKVENNKVS-LYKYVfpPNLEKPTLAIIGLiqPLGSIIPTV-ELQARW 387
                         410
                  ....*....|....*..
gi 440577511  318 FTAVLAGRCTLPDAETM 334
Cdd:pfam00743 388 ATRVFKGLCTLPSQSEM 404
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
4-323 5.47e-58

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: 195.08  E-value: 5.47e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWnytdetwmsedgrpiYTSLYQNLVVNLPKEIMAFPDFPFHHVD 83
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTW---------------RDNRYPGLRLDTPSHLYSLPFFPNWSDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  84 DSYVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPC--DSGWLVTVTDlttmmEQSFEFDAVAVCTGQCWCPLYPNVE 161
Cdd:COG2072   74 PDFPTGDEILAYLEAYADKFGLRRPIRFGTEVTSARWDeaDGRWTVTTDD-----GETLTARFVVVATGPLSRPKIPDIP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 162 GRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRRE------------------------- 216
Cdd:COG2072  149 GLEDFAGEQLHSADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRTppwvlprpnydpergrpanylglea 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 217 -------------LKTVEGLFPDNVTEKPL-------------------------------LTSLSEYTAHFSDGTSTDI 252
Cdd:COG2072  229 ppalnrrdarawlRRLLRAQVKDPELGLLTpdyppgckrpllstdyyealrrgnvelvtggIERITEDGVVFADGTEHEV 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440577511 253 DDIIYCTGYRFRFPFLSPEcGVIVDEKRVHP-LYLHVLNINKPTMGFVG--VPHDACFSIL-FDLQAQWFTAVLA 323
Cdd:COG2072  309 DVIVWATGFRADLPWLAPL-DVRGRDGRSGPrAYLGVVVPGFPNLFFLGpnSPSGHSSLTLgAERQARYIARLIA 382
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
4-296 4.24e-11

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 63.74  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511    4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY-TDETWMSedgrpiyTSlyqnlvvnlpkEIMAFPDFPFhhv 82
Cdd:TIGR04018   2 VIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYpTNMTFFS-------TS-----------ERLEIGGIPF--- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   83 ddsyVSS------KEVLKYFNNFCDAFDLRklVKFQHHVENVRPCDSGWLVTVTdlttmmEQSFEFDAVAVCTGQCWCPL 156
Cdd:TIGR04018  61 ----ISEnpkptrNEALEYYRRVAERFKLN--IRLYEEVLKVKKTDGGFEVTTE------KGTYQAKNVIVATGYYDIPN 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  157 YPNVEGRTIFRGRqihaHEFRCPDSFRNRRVLVIGAGPSGHDLAL--------------------NISYVAKQVFISRRE 216
Cdd:TIGR04018 129 LLNVPGEDLPKVS----HYYKEAHPYFGQKVVVVGGSNSAVDAALelyrkgaevtmvhrgdevssSVKYWVRPDIENRIK 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  217 LKTVEGLFPDNVTEkplltsLSEYTAHFS--DGTSTDI--DDIIYCTGYRFRFPFLSpECGVIVDEKRVHPLYlhvlniN 292
Cdd:TIGR04018 205 EGSIKAYFNSRVKE------ITEDSVTLEtpDGEVHTIpnDFVFALTGYRPDFEFLE-SLGVELDEDTGIPVY------N 271

                  ....
gi 440577511  293 KPTM 296
Cdd:TIGR04018 272 PETM 275
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
4-50 2.39e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.61  E-value: 2.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERS-------RHVGGTW--NYTDETWMSE 50
Cdd:cd05188  138 VLVLGAGGVGLLAAQLAKAAGARVIVTDRSdeklelaKELGADHviDYKEEDLEEE 193
 
Name Accession Description Interval E-value
PLN02172 PLN02172
flavin-containing monooxygenase FMO GS-OX
2-334 1.19e-74

flavin-containing monooxygenase FMO GS-OX


Pssm-ID: 215116 [Multi-domain]  Cd Length: 461  Bit Score: 240.15  E-value: 1.19e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNYTDETW---MSED-GRPI-YTSLYQNLVVNLPKEIMAFPD 76
Cdd:PLN02172  11 QHVAVIGAGAAGLVAARELRREGHTVVVFEREKQVGGLWVYTPKSEsdpLSLDpTRSIvHSSVYESLRTNLPRECMGYRD 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  77 FPF-HHVDDS------YVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPCDSGWLVTVTDLTTMMEQSFeFDAVAVCT 149
Cdd:PLN02172  91 FPFvPRFDDEsrdsrrYPSHREVLAYLQDFAREFKIEEMVRFETEVVRVEPVDGKWRVQSKNSGGFSKDEI-FDAVVVCN 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 150 GQCWCPLYPNVEGRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRR--ELKTVEGL-FPD 226
Cdd:PLN02172 170 GHYTEPNVAHIPGIKSWPGKQIHSHNYRVPDPFKNEVVVVIGNFASGADISRDIAKVAKEVHIASRasESDTYEKLpVPQ 249
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 227 NVtekplLTSLSEY-TAH------FSDGTSTDIDDIIYCTGYRFRFPFLSPECGVIVDEKRVHPLYLHVLNIN-KPTMGF 298
Cdd:PLN02172 250 NN-----LWMHSEIdTAHedgsivFKNGKVVYADTIVHCTGYKYHFPFLETNGYMRIDENRVEPLYKHVFPPAlAPGLSF 324
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 440577511 299 VGVPHDACFSILFDLQAQWFTAVLAGRCTLPDAETM 334
Cdd:PLN02172 325 IGLPAMGIQFVMFEIQSKWVAAVLSGRVTLPSEDKM 360
FMO-like pfam00743
Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone ...
2-334 1.12e-60

Flavin-binding monooxygenase-like; This family includes FMO proteins, cyclohexanone mono-oxygenase and a number of different mono-oxygenases.


Pssm-ID: 395602 [Multi-domain]  Cd Length: 531  Bit Score: 205.40  E-value: 1.12e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511    2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNYTDEtwmSEDGRpiyTSLYQNLVVNLPKEIMAFPDFPFHH 81
Cdd:pfam00743   2 KKVAVIGAGVSGLASIKCCLEEGLEPTCFERSDDIGGLWRFTEN---VEEGR---ASIYKSVITNTSKEMSCFSDFPFPE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   82 VDDSYVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPC----DSG-WlvtvtDLTTMME---QSFEFDAVAVCTGQCW 153
Cdd:pfam00743  76 DYPNFMHNSKFLEYFRMFAKEFDLLKYIQFKTTVCSVKKRpdfsTSGqW-----EVVTEHEgkqESAVFDAVMVCTGHHT 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  154 CPLYP--NVEGRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRRE--------------- 216
Cdd:pfam00743 151 NPHLPleSFPGIEKFKGQYFHSRDYKHPEGFTGKRVLVIGIGNSGGDIAVELSHTAAQVFLSTRRgswvlsrvsdhgypw 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  217 -----------LKTV----------------------EGLFPDN---------------------VTEKPLLTSLSEYTA 242
Cdd:pfam00743 231 dmlfstrftsfLRNIlptsisnwlmekqmnrrfnhenYGLKPKNralskepvvnddlpnrilcgaVKVKPNVKEFTETSA 310
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  243 HFSDGT-STDIDDIIYCTGYRFRFPFLSpECGVIVDEKRVHpLYLHV--LNINKPTMGFVGV--PHDACFSILfDLQAQW 317
Cdd:pfam00743 311 IFEDGTvEEDIDVVIFATGYTFAFPFLE-ESLVKVENNKVS-LYKYVfpPNLEKPTLAIIGLiqPLGSIIPTV-ELQARW 387
                         410
                  ....*....|....*..
gi 440577511  318 FTAVLAGRCTLPDAETM 334
Cdd:pfam00743 388 ATRVFKGLCTLPSQSEM 404
CzcO COG2072
Predicted flavoprotein CzcO associated with the cation diffusion facilitator CzcD [Inorganic ...
4-323 5.47e-58

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: 195.08  E-value: 5.47e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWnytdetwmsedgrpiYTSLYQNLVVNLPKEIMAFPDFPFHHVD 83
Cdd:COG2072    9 VVVIGAGQAGLAAAYHLRRAGIDFVVLEKADDVGGTW---------------RDNRYPGLRLDTPSHLYSLPFFPNWSDD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  84 DSYVSSKEVLKYFNNFCDAFDLRKLVKFQHHVENVRPC--DSGWLVTVTDlttmmEQSFEFDAVAVCTGQCWCPLYPNVE 161
Cdd:COG2072   74 PDFPTGDEILAYLEAYADKFGLRRPIRFGTEVTSARWDeaDGRWTVTTDD-----GETLTARFVVVATGPLSRPKIPDIP 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 162 GRTIFRGRQIHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQVFISRRE------------------------- 216
Cdd:COG2072  149 GLEDFAGEQLHSADWRNPVDLAGKRVLVVGTGASAVQIAPELARVAAHVTVFQRTppwvlprpnydpergrpanylglea 228
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 217 -------------LKTVEGLFPDNVTEKPL-------------------------------LTSLSEYTAHFSDGTSTDI 252
Cdd:COG2072  229 ppalnrrdarawlRRLLRAQVKDPELGLLTpdyppgckrpllstdyyealrrgnvelvtggIERITEDGVVFADGTEHEV 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 440577511 253 DDIIYCTGYRFRFPFLSPEcGVIVDEKRVHP-LYLHVLNINKPTMGFVG--VPHDACFSIL-FDLQAQWFTAVLA 323
Cdd:COG2072  309 DVIVWATGFRADLPWLAPL-DVRGRDGRSGPrAYLGVVVPGFPNLFFLGpnSPSGHSSLTLgAERQARYIARLIA 382
Pyr_redox_3 pfam13738
Pyridine nucleotide-disulphide oxidoreductase;
11-285 4.55e-18

Pyridine nucleotide-disulphide oxidoreductase;


Pssm-ID: 404603 [Multi-domain]  Cd Length: 296  Bit Score: 83.81  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   11 PCGLATARHLKHAGFE-VTVFERSRHVGGTWNY-TDETWMSedgrPIYTSlyqnlvvnlpkEIMAFPDFPFHHVDDS--- 85
Cdd:pfam13738   1 PAGIGCAIALKKAGLEdYLILEKGNIGNSFYRYpTHMTFFS----PSFTS-----------NGFGIPDLNAISPGTSpaf 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   86 -----YVSSKEVLKYFNNFCDAFDLRklVKFQHHVENVRPCDSGWLVTvTDlttmmEQSFEFDAVAVCTGQCWCPLYPNV 160
Cdd:pfam13738  66 tfnreHPSGNEYAEYLRRVADHFELP--INLFEEVTSVKKEDDGFVVT-TS-----KGTYQARYVIIATGEFDFPNKLGV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  161 EGRTIfrgrqiHAHEFRCPDSFRNRRVLVIGAGPSGHDLALNISYVAKQV-------FISRRELKTVEGLFPDN------ 227
Cdd:pfam13738 138 PELPK------HYSYVKDFHPYAGQKVVVIGGYNSAVDAALELVRKGARVtvlyrgsEWEDRDSDPSYSLSPDTlnrlee 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 440577511  228 -----------------VTEKPlltslSEYTAHFSDGTSTDI-DDIIYCTGYRFRFPFLSPeCGVIVDEKRvHPLY 285
Cdd:pfam13738 212 lvkngkikahfnaevkeITEVD-----VSYKVHTEDGRKVTSnDDPILATGYHPDLSFLKK-GLFELDEDG-RPVL 280
Pyr_redox_2 pfam07992
Pyridine nucleotide-disulphide oxidoreductase; This family includes both class I and class II ...
3-262 7.15e-13

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


Pssm-ID: 400379 [Multi-domain]  Cd Length: 301  Bit Score: 68.88  E-value: 7.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511    3 QVAVLGAGPCGLATARHLKHAGFEVTVFErsrhVGGTWNYtdetwmsedGRPIytslyqnlvvnLPKEIMAFPDFP--FH 80
Cdd:pfam07992   2 DVVVIGGGPAGLAAALTLAQLGGKVTLIE----DEGTCPY---------GGCV-----------LSKALLGAAEAPeiAS 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   81 HVDDSYVSSKEVLKYFNNfcdafDLRKLvkFQHHVENVrpcDSGW-LVTVTDLTTMMEQSFEFDAVAVCTGqCWcPLYPN 159
Cdd:pfam07992  58 LWADLYKRKEEVVKKLNN-----GIEVL--LGTEVVSI---DPGAkKVVLEELVDGDGETITYDRLVIATG-AR-PRLPP 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  160 VEGRTIFRGRQIHAHE----FRcpDSFRNRRVLVIGAGPSG-------HDLALNISYVAKQVFISRRELKTVEGLFPDNV 228
Cdd:pfam07992 126 IPGVELNVGFLVRTLDsaeaLR--LKLLPKRVVVVGGGYIGvelaaalAKLGKEVTLIEALDRLLRAFDEEISAALEKAL 203
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 440577511  229 TEK----PLLTSLSE-------YTAHFSDGTSTDIDDIIYCTGYR 262
Cdd:pfam07992 204 EKNgvevRLGTSVKEiigdgdgVEVILKDGTEIDADLVVVAIGRR 248
NAD_binding_9 pfam13454
FAD-NAD(P)-binding;
5-150 1.28e-12

FAD-NAD(P)-binding;


Pssm-ID: 433222 [Multi-domain]  Cd Length: 155  Bit Score: 64.99  E-value: 1.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511    5 AVLGAGPCGLATARHL----KHAGFEVTVFERSRH-VGGTWNYTDETWmsedgrpiytslyqnLVVNLPKEIM-AFPDFP 78
Cdd:pfam13454   1 AIVGGGPSGLALLERLlaraPKRPLEITLFDPSPPgAGGVYRTDQSPE---------------HLLNVPASRMsLFPDDP 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   79 FH----------------HVDDSYVSSKEVLKYFNNFCDAF--DLRKLVKFQHH---VENVRPCDSGWLVTVTDlttmmE 137
Cdd:pfam13454  66 PHflewlrargaldeapgLDPDDFPPRALYGRYLRDRFEEAlaRAPAGVTVRVHrarVTDLRPRGDGYRVLLAD-----G 140
                         170
                  ....*....|...
gi 440577511  138 QSFEFDAVAVCTG 150
Cdd:pfam13454 141 RTLAADAVVLATG 153
GltD COG0493
NADPH-dependent glutamate synthase beta chain or related oxidoreductase [Amino acid transport ...
4-193 5.32e-12

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: 67.08  E-value: 5.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGtwnytdetwMSEDGRPIYtslyqnlvvNLPKEIMAfpdfpfhhvd 83
Cdd:COG0493  124 VAVVGSGPAGLAAAYQLARAGHEVTVFEALDKPGG---------LLRYGIPEF---------RLPKDVLD---------- 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  84 dsyvssKEVLKyfnnfcdafdLRKL-VKFQHHVEnVrpcdsGWLVTVTDLTTmmeqsfEFDAVAVCTGqCWCPLYPNVEG 162
Cdd:COG0493  176 ------REIEL----------IEALgVEFRTNVE-V-----GKDITLDELLE------EFDAVFLATG-AGKPRDLGIPG 226
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 440577511 163 RT---IFRG----RQIHAHEFRCPDSFRNRRVLVIGAG 193
Cdd:COG0493  227 EDlkgVHSAmdflTAVNLGEAPDTILAVGKRVVVIGGG 264
HemY COG1232
Protoporphyrinogen oxidase HemY/PPOX [Coenzyme transport and metabolism]; Protoporphyrinogen ...
1-38 6.86e-12

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: 66.78  E-value: 6.86e-12
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:COG1232    1 MKRVAVIGGGIAGLTAAYRLAKAGHEVTVLEASDRVGG 38
COG3380 COG3380
Predicted NAD/FAD-dependent oxidoreductase [General function prediction only];
1-38 3.15e-11

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


Pssm-ID: 442607 [Multi-domain]  Cd Length: 331  Bit Score: 64.13  E-value: 3.15e-11
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:COG3380    3 MPDIAIIGAGIAGLAAARALQDAGHEVTVFEKSRGVGG 40
Bthiol_YpdA TIGR04018
putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, ...
4-296 4.24e-11

putative bacillithiol system oxidoreductase, YpdA family; Members of this protein family, including YpdA from Bacillus subtilis, are apparent oxidoreductases present only in species with an active bacillithiol system. They have been suggested actually to be thiol disulfide oxidoreductases (TDOR), although the evidence is incomplete. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 188533 [Multi-domain]  Cd Length: 316  Bit Score: 63.74  E-value: 4.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511    4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY-TDETWMSedgrpiyTSlyqnlvvnlpkEIMAFPDFPFhhv 82
Cdd:TIGR04018   2 VIIIGAGPCGLACAIEAQKAGLSYLIIEKGNLVNSIYRYpTNMTFFS-------TS-----------ERLEIGGIPF--- 60
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   83 ddsyVSS------KEVLKYFNNFCDAFDLRklVKFQHHVENVRPCDSGWLVTVTdlttmmEQSFEFDAVAVCTGQCWCPL 156
Cdd:TIGR04018  61 ----ISEnpkptrNEALEYYRRVAERFKLN--IRLYEEVLKVKKTDGGFEVTTE------KGTYQAKNVIVATGYYDIPN 128
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  157 YPNVEGRTIFRGRqihaHEFRCPDSFRNRRVLVIGAGPSGHDLAL--------------------NISYVAKQVFISRRE 216
Cdd:TIGR04018 129 LLNVPGEDLPKVS----HYYKEAHPYFGQKVVVVGGSNSAVDAALelyrkgaevtmvhrgdevssSVKYWVRPDIENRIK 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  217 LKTVEGLFPDNVTEkplltsLSEYTAHFS--DGTSTDI--DDIIYCTGYRFRFPFLSpECGVIVDEKRVHPLYlhvlniN 292
Cdd:TIGR04018 205 EGSIKAYFNSRVKE------ITEDSVTLEtpDGEVHTIpnDFVFALTGYRPDFEFLE-SLGVELDEDTGIPVY------N 271

                  ....
gi 440577511  293 KPTM 296
Cdd:TIGR04018 272 PETM 275
TrxB COG0492
Thioredoxin reductase [Posttranslational modification, protein turnover, chaperones];
4-216 2.17e-10

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


Pssm-ID: 440258 [Multi-domain]  Cd Length: 305  Bit Score: 61.29  E-value: 2.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRhVGGTWNYTDETWmsedgrpiytslyqnlvvNlpkeimaFPDFPFHhvd 83
Cdd:COG0492    3 VVIIGAGPAGLTAAIYAARAGLKTLVIEGGE-PGGQLATTKEIE------------------N-------YPGFPEG--- 53
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  84 dsyVSSKEVLKYFNNFCDAFDLRklVKFQHhVENVRPCDSGWLVTVTDLTTmmeqsFEFDAVAVCTGqcwC-PLYPNVEG 162
Cdd:COG0492   54 ---ISGPELAERLREQAERFGAE--ILLEE-VTSVDKDDGPFRVTTDDGTE-----YEAKAVIIATG---AgPRKLGLPG 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 440577511 163 RTIFRGRQIHAhefrCP----DSFRNRRVLVIGAGPSGHDLALNISYVAKQV-FISRRE 216
Cdd:COG0492  120 EEEFEGRGVSY----CAtcdgFFFRGKDVVVVGGGDSALEEALYLTKFASKVtLIHRRD 174
YobN COG1231
Monoamine oxidase [Amino acid transport and metabolism];
1-44 4.50e-09

Monoamine oxidase [Amino acid transport and metabolism];


Pssm-ID: 440844 [Multi-domain]  Cd Length: 440  Bit Score: 58.01  E-value: 4.50e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG-TWNYTD 44
Cdd:COG1231    7 GKDVVIVGAGLAGLAAARELRKAGLDVTVLEARDRVGGrVWTLRF 51
PRK07233 PRK07233
hypothetical protein; Provisional
4-47 2.39e-08

hypothetical protein; Provisional


Pssm-ID: 235977 [Multi-domain]  Cd Length: 434  Bit Score: 55.66  E-value: 2.39e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG---TWNYTDETW 47
Cdd:PRK07233   2 IAIVGGGIAGLAAAYRLAKRGHEVTVFEADDQLGGlaaSFEFGGLPI 48
NAD_binding_8 pfam13450
NAD(P)-binding Rossmann-like domain;
6-40 2.52e-08

NAD(P)-binding Rossmann-like domain;


Pssm-ID: 433218 [Multi-domain]  Cd Length: 67  Bit Score: 50.22  E-value: 2.52e-08
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 440577511    6 VLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTW 40
Cdd:pfam13450   1 IVGAGLAGLVAAALLAKRGFRVLVLEKRDRLGGNA 35
PRK11749 PRK11749
dihydropyrimidine dehydrogenase subunit A; Provisional
2-193 4.64e-08

dihydropyrimidine dehydrogenase subunit A; Provisional


Pssm-ID: 236967 [Multi-domain]  Cd Length: 457  Bit Score: 54.80  E-value: 4.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERsRHVGGTWN-YtdetwmsedGRPIYtslyqnlvvNLPKEImafpdfpfh 80
Cdd:PRK11749 141 KKVAVIGAGPAGLTAAHRLARKGYDVTIFEA-RDKAGGLLrY---------GIPEF---------RLPKDI--------- 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  81 hVDdsyvssKEVLKyfnnfcdafdLRKL-VKFQHHVEnVrpcdsGWLVTVTDLttmMEQsfeFDAVAVCTGqCWCPLYPN 159
Cdd:PRK11749 193 -VD------REVER----------LLKLgVEIRTNTE-V-----GRDITLDEL---RAG---YDAVFIGTG-AGLPRFLG 242
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 440577511 160 VEGRTiFRGrqIH-AHEF------RCPDS--FRNRRVLVIGAG 193
Cdd:PRK11749 243 IPGEN-LGG--VYsAVDFltrvnqAVADYdlPVGKRVVVIGGG 282
COG3349 COG3349
Uncharacterized protein, contains NAD-binding domain and a Fe-S cluster [General function ...
1-38 5.39e-08

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: 54.48  E-value: 5.39e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:COG3349    3 PPRVVVVGGGLAGLAAAVELAEAGFRVTLLEARPRLGG 40
COG1233 COG1233
Phytoene dehydrogenase-related protein [Secondary metabolites biosynthesis, transport and ...
1-38 8.42e-08

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


Pssm-ID: 440846 [Multi-domain]  Cd Length: 491  Bit Score: 54.09  E-value: 8.42e-08
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:COG1233    3 MYDVVVIGAGIGGLAAAALLARAGYRVTVLEKNDTPGG 40
PLN02976 PLN02976
amine oxidase
2-49 1.11e-07

amine oxidase


Pssm-ID: 215527 [Multi-domain]  Cd Length: 1713  Bit Score: 54.10  E-value: 1.11e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 440577511    2 RQVAVLGAGPCGLATARHLKHAGFEVTVFE-RSRhVGGTWnYTDETWMS 49
Cdd:PLN02976  694 KKIIVVGAGPAGLTAARHLQRQGFSVTVLEaRSR-IGGRV-YTDRSSLS 740
PRK12770 PRK12770
putative glutamate synthase subunit beta; Provisional
2-218 1.58e-07

putative glutamate synthase subunit beta; Provisional


Pssm-ID: 237197 [Multi-domain]  Cd Length: 352  Bit Score: 52.68  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGtwnytdetwmsedgrpiytslyqnlvvnlpkeIMAF--PDF-- 77
Cdd:PRK12770  19 KKVAIIGAGPAGLAAAGYLACLGYEVHVYDKLPEPGG--------------------------------LMLFgiPEFri 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  78 PFHHVDDSY--VSSKEVLKYFNNF--CDAFDLRKLVkfQHHVENVRpcdsgwlvtvtDLTTMMEqsfEFDAVAVCTGQcW 153
Cdd:PRK12770  67 PIERVREGVkeLEEAGVVFHTRTKvcCGEPLHEEEG--DEFVERIV-----------SLEELVK---KYDAVLIATGT-W 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 154 CPLYPNVEGRT----------IFRgrqIHAHEF------RCPDSfRNRRVLVIGAGPSGHDLAL--NISYVAKQVFISRR 215
Cdd:PRK12770 130 KSRKLGIPGEDlpgvysaleyLFR---IRAAKLgylpweKVPPV-EGKKVVVVGAGLTAVDAALeaVLLGAEKVYLAYRR 205

                 ...
gi 440577511 216 ELK 218
Cdd:PRK12770 206 TIN 208
PRK07208 PRK07208
hypothetical protein; Provisional
1-38 1.93e-07

hypothetical protein; Provisional


Pssm-ID: 235967 [Multi-domain]  Cd Length: 479  Bit Score: 52.97  E-value: 1.93e-07
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:PRK07208   4 KKSVVIIGAGPAGLTAAYELLKRGYPVTVLEADPVVGG 41
gltD PRK12810
glutamate synthase subunit beta; Reviewed
2-38 2.07e-07

glutamate synthase subunit beta; Reviewed


Pssm-ID: 237213 [Multi-domain]  Cd Length: 471  Bit Score: 52.86  E-value: 2.07e-07
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:PRK12810 144 KKVAVVGSGPAGLAAADQLARAGHKVTVFERADRIGG 180
UbiH COG0654
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme ...
1-34 8.85e-07

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: 50.32  E-value: 8.85e-07
                         10        20        30
                 ....*....|....*....|....*....|....
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSR 34
Cdd:COG0654    3 RTDVLIVGGGPAGLALALALARAGIRVTVVERAP 36
DadA COG0665
Glycine/D-amino acid oxidase (deaminating) [Amino acid transport and metabolism];
1-34 4.24e-06

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


Pssm-ID: 440429 [Multi-domain]  Cd Length: 364  Bit Score: 48.36  E-value: 4.24e-06
                         10        20        30
                 ....*....|....*....|....*....|....
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSR 34
Cdd:COG0665    2 TADVVVIGGGIAGLSTAYHLARRGLDVTVLERGR 35
Amino_oxidase pfam01593
Flavin containing amine oxidoreductase; This family consists of various amine oxidases, ...
13-38 5.92e-06

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: 48.26  E-value: 5.92e-06
                          10        20
                  ....*....|....*....|....*.
gi 440577511   13 GLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:pfam01593   3 GLAAARELLRAGHDVTVLEARDRVGG 28
PRK12771 PRK12771
putative glutamate synthase (NADPH) small subunit; Provisional
2-38 7.10e-06

putative glutamate synthase (NADPH) small subunit; Provisional


Pssm-ID: 237198 [Multi-domain]  Cd Length: 564  Bit Score: 47.95  E-value: 7.10e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:PRK12771 138 KRVAVIGGGPAGLSAAYHLRRMGHAVTIFEAGPKLGG 174
DAO pfam01266
FAD dependent oxidoreductase; This family includes various FAD dependent oxidoreductases: ...
4-38 2.19e-05

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: 46.24  E-value: 2.19e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 440577511    4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:pfam01266   2 VVVIGGGIVGLSTAYELARRGLSVTLLERGDDPGS 36
crtI_fam TIGR02734
phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two ...
4-38 4.21e-05

phytoene desaturase; Phytoene is converted to lycopene by desaturation at four (two symmetrical pairs of) sites. This is achieved by two enzymes (crtP and crtQ) in cyanobacteria (Gloeobacter being an exception) and plants, but by a single enzyme in most other bacteria and in fungi. This single enzyme is called the bacterial-type phytoene desaturase, or CrtI. Most members of this family, part of the larger pfam01593, which also contains amino oxidases, are CrtI itself; it is likely that all members act on either phytoene or on related compounds such as dehydrosqualene, for carotenoid biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 274273 [Multi-domain]  Cd Length: 495  Bit Score: 45.73  E-value: 4.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 440577511    4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:TIGR02734   1 AVVIGAGFGGLALAIRLAAAGIPVTVVEQRDKPGG 35
PRK12409 PRK12409
D-amino acid dehydrogenase small subunit; Provisional
1-35 7.35e-05

D-amino acid dehydrogenase small subunit; Provisional


Pssm-ID: 237093 [Multi-domain]  Cd Length: 410  Bit Score: 44.63  E-value: 7.35e-05
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSRH 35
Cdd:PRK12409   1 MSHIAVIGAGITGVTTAYALAQRGYQVTVFDRHRY 35
PRK09126 PRK09126
FAD-dependent hydroxylase;
4-33 8.47e-05

FAD-dependent hydroxylase;


Pssm-ID: 236385 [Multi-domain]  Cd Length: 392  Bit Score: 44.55  E-value: 8.47e-05
                         10        20        30
                 ....*....|....*....|....*....|
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERS 33
Cdd:PRK09126   6 IVVVGAGPAGLSFARSLAGSGLKVTLIERQ 35
PRK13984 PRK13984
putative oxidoreductase; Provisional
2-42 8.91e-05

putative oxidoreductase; Provisional


Pssm-ID: 172486 [Multi-domain]  Cd Length: 604  Bit Score: 44.76  E-value: 8.91e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY 42
Cdd:PRK13984 284 KKVAIVGSGPAGLSAAYFLATMGYEVTVYESLSKPGGVMRY 324
MmsB COG2084
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ...
1-34 9.16e-05

3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];


Pssm-ID: 441687 [Multi-domain]  Cd Length: 285  Bit Score: 43.95  E-value: 9.16e-05
                         10        20        30
                 ....*....|....*....|....*....|....
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERSR 34
Cdd:COG2084    1 MMKVGFIGLGAMGAPMARNLLKAGHEVTVWNRTP 34
FixC COG0644
Dehydrogenase (flavoprotein) [Energy production and conversion];
9-37 1.02e-04

Dehydrogenase (flavoprotein) [Energy production and conversion];


Pssm-ID: 440409 [Multi-domain]  Cd Length: 281  Bit Score: 43.80  E-value: 1.02e-04
                         10        20
                 ....*....|....*....|....*....
gi 440577511   9 AGPCGLATARHLKHAGFEVTVFERSRHVG 37
Cdd:COG0644    1 AGPAGSAAARRLARAGLSVLLLEKGSFPG 29
Ppro0129 COG2907
Predicted flavin-containing amine oxidase [General function prediction only];
1-38 1.87e-04

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


Pssm-ID: 442151 [Multi-domain]  Cd Length: 423  Bit Score: 43.57  E-value: 1.87e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAgFEVTVFERSRHVGG 38
Cdd:COG2907    3 RMRIAVIGSGISGLTAAWLLSRR-HDVTLFEANDRLGG 39
PRK12778 PRK12778
bifunctional dihydroorotate dehydrogenase B NAD binding subunit/NADPH-dependent glutamate ...
3-42 1.99e-04

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


Pssm-ID: 237200 [Multi-domain]  Cd Length: 752  Bit Score: 43.58  E-value: 1.99e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 440577511   3 QVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY 42
Cdd:PRK12778 433 KVAVIGSGPAGLSFAGDLAKRGYDVTVFEALHEIGGVLKY 472
PRK12809 PRK12809
putative oxidoreductase Fe-S binding subunit; Reviewed
3-59 2.43e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183762 [Multi-domain]  Cd Length: 639  Bit Score: 43.48  E-value: 2.43e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 440577511   3 QVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY------TDETWMSEDgRPIYTSL 59
Cdd:PRK12809 312 KVAVIGAGPAGLGCADILARAGVQVDVFDRHPEIGGMLTFgippfkLDKTVLSQR-REIFTAM 373
PLN02268 PLN02268
probable polyamine oxidase
4-38 3.13e-04

probable polyamine oxidase


Pssm-ID: 177909 [Multi-domain]  Cd Length: 435  Bit Score: 42.75  E-value: 3.13e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:PLN02268   3 VIVIGGGIAGIAAARALHDASFKVTLLESRDRIGG 37
PRK12814 PRK12814
putative NADPH-dependent glutamate synthase small subunit; Provisional
2-42 3.74e-04

putative NADPH-dependent glutamate synthase small subunit; Provisional


Pssm-ID: 139246 [Multi-domain]  Cd Length: 652  Bit Score: 42.79  E-value: 3.74e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY 42
Cdd:PRK12814 194 KKVAIIGAGPAGLTAAYYLLRKGHDVTIFDANEQAGGMMRY 234
Thi4 pfam01946
Thi4 family; This family includes Swiss:P32318 a putative thiamine biosynthetic enzyme.
4-40 4.00e-04

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


Pssm-ID: 460393  Cd Length: 232  Bit Score: 41.69  E-value: 4.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 440577511    4 VAVLGAGPCGLATARHL-KHAGFEVTVFERSRHV-GGTW 40
Cdd:pfam01946  20 VVIVGAGSSGLTAAYYLaKNRGLKVAIIERSVSPgGGAW 58
PRK12831 PRK12831
putative oxidoreductase; Provisional
3-42 5.63e-04

putative oxidoreductase; Provisional


Pssm-ID: 183780 [Multi-domain]  Cd Length: 464  Bit Score: 41.93  E-value: 5.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 440577511   3 QVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY 42
Cdd:PRK12831 142 KVAVIGSGPAGLTCAGDLAKMGYDVTIFEALHEPGGVLVY 181
PRK12775 PRK12775
putative trifunctional 2-polyprenylphenol hydroxylase/glutamate synthase subunit beta/ferritin ...
3-42 7.00e-04

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


Pssm-ID: 183738 [Multi-domain]  Cd Length: 1006  Bit Score: 41.85  E-value: 7.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 440577511    3 QVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY 42
Cdd:PRK12775  432 KVAICGSGPAGLAAAADLVKYGVDVTVYEALHVVGGVLQY 471
Ndh COG1252
NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];
1-215 7.01e-04

NADH dehydrogenase, FAD-containing subunit [Energy production and conversion];


Pssm-ID: 440864 [Multi-domain]  Cd Length: 386  Bit Score: 41.66  E-value: 7.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511   1 MRQVAVLGAGPCGLATARHLKH---AGFEVTVFERSRHvggtWNYTdetwmsedgrpiyTSLYQnlvvnlpkeimafpdF 77
Cdd:COG1252    1 MKRIVIVGGGFAGLEAARRLRKklgGDAEVTLIDPNPY----HLFQ-------------PLLPE---------------V 48
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511  78 PFHHVDDSYVsskevlkyfnnfcdAFDLRKLVKFQH------HVENVRP------CDSGwlvtvtdlttmmeQSFEFDAV 145
Cdd:COG1252   49 AAGTLSPDDI--------------AIPLRELLRRAGvrfiqgEVTGIDPeartvtLADG-------------RTLSYDYL 101
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 440577511 146 AVCTGQcwCPLYPNVEG--------RTIFRGRQIHAH-EFRCPDSFRNR--RVLVIGAGPSGHDLALNISYVAKQVFISR 214
Cdd:COG1252  102 VIATGS--VTNFFGIPGlaehalplKTLEDALALRERlLAAFERAERRRllTIVVVGGGPTGVELAGELAELLRKLLRYP 179

                 .
gi 440577511 215 R 215
Cdd:COG1252  180 G 180
PRK12769 PRK12769
putative oxidoreductase Fe-S binding subunit; Reviewed
2-38 7.53e-04

putative oxidoreductase Fe-S binding subunit; Reviewed


Pssm-ID: 183733 [Multi-domain]  Cd Length: 654  Bit Score: 41.66  E-value: 7.53e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:PRK12769 328 KRVAIIGAGPAGLACADVLARNGVAVTVYDRHPEIGG 364
Lpd COG1249
Dihydrolipoamide dehydrogenase (E3) component of pyruvate/2-oxoglutarate dehydrogenase complex ...
4-39 8.57e-04

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


Pssm-ID: 440861 [Multi-domain]  Cd Length: 456  Bit Score: 41.23  E-value: 8.57e-04
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERsRHVGGT 39
Cdd:COG1249    6 LVVIGAGPGGYVAAIRAAQLGLKVALVEK-GRLGGT 40
PRK00711 PRK00711
D-amino acid dehydrogenase;
1-32 9.27e-04

D-amino acid dehydrogenase;


Pssm-ID: 234819 [Multi-domain]  Cd Length: 416  Bit Score: 41.32  E-value: 9.27e-04
                         10        20        30
                 ....*....|....*....|....*....|..
gi 440577511   1 MRqVAVLGAGPCGLATARHLKHAGFEVTVFER 32
Cdd:PRK00711   1 MR-VVVLGSGVIGVTSAWYLAQAGHEVTVIDR 31
PRK12779 PRK12779
putative bifunctional glutamate synthase subunit beta/2-polyprenylphenol hydroxylase; ...
4-42 9.68e-04

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


Pssm-ID: 183740 [Multi-domain]  Cd Length: 944  Bit Score: 41.36  E-value: 9.68e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGGTWNY 42
Cdd:PRK12779 309 IAVVGSGPSGLINAYLLAVEGFPVTVFEAFHDLGGVLRY 347
NirB COG1251
NAD(P)H-nitrite reductase, large subunit [Energy production and conversion];
2-36 1.44e-03

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


Pssm-ID: 440863 [Multi-domain]  Cd Length: 402  Bit Score: 40.51  E-value: 1.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHV 36
Cdd:COG1251  143 KRVVVIGGGLIGLEAAAALRKRGLEVTVVERAPRL 177
FadH2 COG0446
NADPH-dependent 2,4-dienoyl-CoA reductase, sulfur reductase, or a related oxidoreductase ...
2-36 2.05e-03

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


Pssm-ID: 440215 [Multi-domain]  Cd Length: 322  Bit Score: 39.79  E-value: 2.05e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFERSRHV 36
Cdd:COG0446  125 KRAVVIGGGPIGLELAEALRKRGLKVTLVERAPRL 159
PLN03000 PLN03000
amine oxidase
4-38 2.10e-03

amine oxidase


Pssm-ID: 178578 [Multi-domain]  Cd Length: 881  Bit Score: 40.39  E-value: 2.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERSRHVGG 38
Cdd:PLN03000 187 VVIVGAGLSGLAAARQLMRFGFKVTVLEGRKRPGG 221
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
4-50 2.39e-03

Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 39.61  E-value: 2.39e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFERS-------RHVGGTW--NYTDETWMSE 50
Cdd:cd05188  138 VLVLGAGGVGLLAAQLAKAAGARVIVTDRSdeklelaKELGADHviDYKEEDLEEE 193
proto_IX_ox TIGR00562
protoporphyrinogen oxidase; This enzyme oxidizes protoporphyrinogen IX to protoporphyrin IX, a ...
1-52 2.39e-03

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: 39.82  E-value: 2.39e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 440577511    1 MRQVAVLGAGPCGLATARHLK----HAGFEVTVFERSRHVGGTWNYTDET-WMSEDG 52
Cdd:TIGR00562   2 KKHVVIIGGGISGLCAAYYLEkeipELPVELTLVEASDRVGGKIQTVKEDgYLIERG 58
PLN02576 PLN02576
protoporphyrinogen oxidase
4-52 2.43e-03

protoporphyrinogen oxidase


Pssm-ID: 215314 [Multi-domain]  Cd Length: 496  Bit Score: 40.00  E-value: 2.43e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 440577511   4 VAVLGAGPCGLATARHLK-HAGFEVTVFERSRHVGGtwNYTDetwMSEDG 52
Cdd:PLN02576  15 VAVVGAGVSGLAAAYALAsKHGVNVLVTEARDRVGG--NITS---VSEDG 59
COG2509 COG2509
FAD-dependent dehydrogenase [General function prediction only];
4-32 4.96e-03

FAD-dependent dehydrogenase [General function prediction only];


Pssm-ID: 441999 [Multi-domain]  Cd Length: 466  Bit Score: 38.94  E-value: 4.96e-03
                         10        20
                 ....*....|....*....|....*....
gi 440577511   4 VAVLGAGPCGLATARHLKHAGFEVTVFER 32
Cdd:COG2509   33 VVIVGAGPAGLFAALELAEAGLKPLVLER 61
PRK07538 PRK07538
hypothetical protein; Provisional
3-34 5.39e-03

hypothetical protein; Provisional


Pssm-ID: 236046 [Multi-domain]  Cd Length: 413  Bit Score: 38.72  E-value: 5.39e-03
                         10        20        30
                 ....*....|....*....|....*....|..
gi 440577511   3 QVAVLGAGPCGLATARHLKHAGFEVTVFERSR 34
Cdd:PRK07538   2 KVLIAGGGIGGLTLALTLHQRGIEVVVFEAAP 33
NAD_binding_2 pfam03446
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ...
3-34 6.10e-03

NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.


Pssm-ID: 427298 [Multi-domain]  Cd Length: 159  Bit Score: 37.06  E-value: 6.10e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 440577511    3 QVAVLGAGPCGLATARHLKHAGFEVTVFERSR 34
Cdd:pfam03446   1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTP 32
mnmC PRK01747
bifunctional tRNA (5-methylaminomethyl-2-thiouridine)(34)-methyltransferase MnmD/FAD-dependent ...
2-32 6.89e-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: 38.67  E-value: 6.89e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 440577511   2 RQVAVLGAGPCGLATARHLKHAGFEVTVFER 32
Cdd:PRK01747 261 RDAAIIGGGIAGAALALALARRGWQVTLYEA 291
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
1-33 7.30e-03

UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 38.52  E-value: 7.30e-03
                         10        20        30
                 ....*....|....*....|....*....|...
gi 440577511   1 MRQVAVLGAGPCGLATARHLKHAGFEVTVFERS 33
Cdd:COG0771    4 GKKVLVLGLGKSGLAAARLLAKLGAEVTVSDDR 36
PRK06126 PRK06126
hypothetical protein; Provisional
3-32 8.40e-03

hypothetical protein; Provisional


Pssm-ID: 235704 [Multi-domain]  Cd Length: 545  Bit Score: 38.44  E-value: 8.40e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 440577511   3 QVAVLGAGPCGLATARHLKHAGFEVTVFER 32
Cdd:PRK06126   9 PVLIVGGGPVGLALALDLGRRGVDSILVER 38
 
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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