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Conserved domains on  [gi|488471102|ref|WP_002514772|]
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MULTISPECIES: GuaB3 family IMP dehydrogenase-related protein [Cutibacterium]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IMP_DH_rel_2 super family cl36865
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ...
 3-366 0e+00

IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302. [Unknown function, General]


The actual alignment was detected with superfamily member TIGR01304:

Pssm-ID: 273547 [Multi-domain]  Cd Length: 369  Bit Score: 515.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102    3 DIGRSKRATRAYSLDDIALIPSRRTRGTEMVNLEWRIDALTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVLNLEGLWTR 82
Cdd:TIGR01304   2 EIGRGRTARRTYSLDDISVVPSRRTRSSKDVDTAWQIDAYRFELPFIAHPMDALVSPEFAIELGELGGLGVLNLEGLWGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102   83 YEDPTPYLEELAGL---SDDVATTRRMQEIYAEPIKAELITERMAEIRAAGVPVAGSLSPKNASRFSETVVNAGADFFVI 159
Cdd:TIGR01304  82 HEDPDPAIAKIAEAyeeGDQAAATRLLQELHAAPLKPELLGERIAEVRDSGVITAVRVSPQNAREIAPIVVKAGADLLVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  160 RGTTVSAEHVANGDDVLDLRKFIYDLDVPVIVGGCATYQAALHLMRTGAAGVLVGfgGGATHTTRQVLGIQVSMASAIAD 239
Cdd:TIGR01304 162 QGTLVSAEHVSTSGEPLNLKEFIGELDVPVIAGGVNDYTTALHLMRTGAAGVIVG--PGGANTTRLVLGIEVPMATAIAD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  240 VAEARRDYMDESGGRYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGRGWHWGAEAWHPDLPRGARVHFEP 319
Cdd:TIGR01304 240 VAAARRDYLDETGGRYVHVIADGGIETSGDLVKAIACGADAVVLGSPLARAAEAPGRGYFWPAAAAHPRLPRGVVTESGT 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 488471102  320 VG---TLAEVLNGPSRVPDGTMNLVGGLRQAMATTGYSEVKEFQRIELTI 366
Cdd:TIGR01304 320 VGeapTLEEILHGPSTLPDGVENFEGGLKRAMAKCGYTDLKEFQKVSLTV 369
 
Name Accession Description Interval E-value
IMP_DH_rel_2 TIGR01304
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ...
 3-366 0e+00

IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302. [Unknown function, General]


Pssm-ID: 273547 [Multi-domain]  Cd Length: 369  Bit Score: 515.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102    3 DIGRSKRATRAYSLDDIALIPSRRTRGTEMVNLEWRIDALTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVLNLEGLWTR 82
Cdd:TIGR01304   2 EIGRGRTARRTYSLDDISVVPSRRTRSSKDVDTAWQIDAYRFELPFIAHPMDALVSPEFAIELGELGGLGVLNLEGLWGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102   83 YEDPTPYLEELAGL---SDDVATTRRMQEIYAEPIKAELITERMAEIRAAGVPVAGSLSPKNASRFSETVVNAGADFFVI 159
Cdd:TIGR01304  82 HEDPDPAIAKIAEAyeeGDQAAATRLLQELHAAPLKPELLGERIAEVRDSGVITAVRVSPQNAREIAPIVVKAGADLLVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  160 RGTTVSAEHVANGDDVLDLRKFIYDLDVPVIVGGCATYQAALHLMRTGAAGVLVGfgGGATHTTRQVLGIQVSMASAIAD 239
Cdd:TIGR01304 162 QGTLVSAEHVSTSGEPLNLKEFIGELDVPVIAGGVNDYTTALHLMRTGAAGVIVG--PGGANTTRLVLGIEVPMATAIAD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  240 VAEARRDYMDESGGRYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGRGWHWGAEAWHPDLPRGARVHFEP 319
Cdd:TIGR01304 240 VAAARRDYLDETGGRYVHVIADGGIETSGDLVKAIACGADAVVLGSPLARAAEAPGRGYFWPAAAAHPRLPRGVVTESGT 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 488471102  320 VG---TLAEVLNGPSRVPDGTMNLVGGLRQAMATTGYSEVKEFQRIELTI 366
Cdd:TIGR01304 320 VGeapTLEEILHGPSTLPDGVENFEGGLKRAMAKCGYTDLKEFQKVSLTV 369
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 13-367 2.33e-92

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 279.40  E-value: 2.33e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  13 AYSLDDIALIPSRRTRGTEMVNLEWRIDA-LTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVLNLEGLWTRYEDPTPyle 91
Cdd:cd00381    1 GLTFDDVLLVPGYSTVLPSEVDLSTKLTKnITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVR--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  92 elaglsddvattrrmqeiyaepikaelitermaeiRAAGVPVAGSLSP--KNASRFSETVVNAGADffvirGTTVSAEHV 169
Cdd:cd00381   78 -----------------------------------KVKGRLLVGAAVGtrEDDKERAEALVEAGVD-----VIVIDSAHG 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 170 aNGDDVLDLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVSMASAIADVAEARRDY 247
Cdd:cd00381  118 -HSVYVIEMIKFIKKKypNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDY 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 248 mdesggrYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPG---------RGWHWGAEAWHPDLPRGARVHFE 318
Cdd:cd00381  197 -------GVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGeyieingkrYKEYRGMGSLGAMKKGGGDRYFG 269

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488471102 319 PVGT------LAEVLNGPSRVPDGTMNLVGGLRQAMATTGYSEVKEFQRIELTIR 367
Cdd:cd00381  270 EEAKklvpegVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFVR 324
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 150-296 4.59e-30

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 119.80  E-value: 4.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  150 VNAGADFFVIrgttvsaeHVANG--DDVLDLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQ 225
Cdd:pfam00478 229 VEAGVDVLVV--------DTAHGhsKGVIDTVKWIKKKypDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRV 300

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488471102  226 VLGIQVSMASAIADVAEARRDYmdesgGryVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGR 296
Cdd:pfam00478 301 VAGVGVPQLTAIYDVAEAAKKY-----G--VPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGE 364
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 13-296 4.62e-27

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 111.60  E-value: 4.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  13 AYSLDDIALIPSRRTRGTEMVNLEWRI-DALTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVL----------------- 74
Cdd:PTZ00314  17 GLTYDDVILLPGYIDFSRDDVDLSTRLtRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIhnncsieeqveevrkvk 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  75 --------------------------------------------NLEGLWTRYEdpTPYLEELAGLSDDVATTRRMQEIY 110
Cdd:PTZ00314  97 rfengfimdpyvlspnhtvadvleikekkgfssilitvdgkvggKLLGIVTSRD--IDFVKDKSTPVSEVMTPREKLVVG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 111 AEPIKAELITERMAEIRAAGVPVAG---------SLSP-------KNASRFSE--------------------TVVNAGA 154
Cdd:PTZ00314 175 NTPISLEEANEVLRESRKGKLPIVNdngelvalvSRSDlkknrgyPNASLDSNgqllvgaaistrpedieraaALIEAGV 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 155 DFFVIrgttvsaeHVANGDDVL--DLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQ 230
Cdd:PTZ00314 255 DVLVV--------DSSQGNSIYqiDMIKKLKSNypHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVG 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471102 231 VSMASAIADVAEARRDYmdesggrYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGR 296
Cdd:PTZ00314 327 RPQASAVYHVARYARER-------GVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGE 385
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 160-361 5.13e-25

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 103.75  E-value: 5.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 160 RGTTVSAEHVANGDDVLDLRKFIYDlDVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVSMASAIAD 239
Cdd:COG0516  111 DVLVIDAAHGHSGGDAMKKIKLTFD-DVLLIPGNSATVEPARALVDAGADLTKVGIGPGSICTTRVVIGLGIPQLSAAMD 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 240 VAEARRDYmdesggryVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPG-------------RGWHWGAEAWH 306
Cdd:COG0516  190 TVTEARMA--------IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGevilyqgrsvkryRGMGSDAKKLV 261

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488471102 307 PDlprGARVHFEPVGTLAEVLNgpsrvpdgtmNLVGGLRQAMATTGYSEVKEFQR 361
Cdd:COG0516  262 PE---GIEGRVPYKGPLEDTLH----------QLLGGLRSGMGYCGARTIEELRE 303
 
Name Accession Description Interval E-value
IMP_DH_rel_2 TIGR01304
IMP dehydrogenase family protein; This model represents a family of proteins, often annotated ...
 3-366 0e+00

IMP dehydrogenase family protein; This model represents a family of proteins, often annotated as a putative IMP dehydrogenase, related to IMP dehydrogenase and GMP reductase. Most species with a member of this family belong to the high GC Gram-positive bacteria, and these also have the IMP dehydrogenase described by TIGRFAMs equivalog model TIGR01302. [Unknown function, General]


Pssm-ID: 273547 [Multi-domain]  Cd Length: 369  Bit Score: 515.54  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102    3 DIGRSKRATRAYSLDDIALIPSRRTRGTEMVNLEWRIDALTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVLNLEGLWTR 82
Cdd:TIGR01304   2 EIGRGRTARRTYSLDDISVVPSRRTRSSKDVDTAWQIDAYRFELPFIAHPMDALVSPEFAIELGELGGLGVLNLEGLWGR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102   83 YEDPTPYLEELAGL---SDDVATTRRMQEIYAEPIKAELITERMAEIRAAGVPVAGSLSPKNASRFSETVVNAGADFFVI 159
Cdd:TIGR01304  82 HEDPDPAIAKIAEAyeeGDQAAATRLLQELHAAPLKPELLGERIAEVRDSGVITAVRVSPQNAREIAPIVVKAGADLLVI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  160 RGTTVSAEHVANGDDVLDLRKFIYDLDVPVIVGGCATYQAALHLMRTGAAGVLVGfgGGATHTTRQVLGIQVSMASAIAD 239
Cdd:TIGR01304 162 QGTLVSAEHVSTSGEPLNLKEFIGELDVPVIAGGVNDYTTALHLMRTGAAGVIVG--PGGANTTRLVLGIEVPMATAIAD 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  240 VAEARRDYMDESGGRYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGRGWHWGAEAWHPDLPRGARVHFEP 319
Cdd:TIGR01304 240 VAAARRDYLDETGGRYVHVIADGGIETSGDLVKAIACGADAVVLGSPLARAAEAPGRGYFWPAAAAHPRLPRGVVTESGT 319

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 488471102  320 VG---TLAEVLNGPSRVPDGTMNLVGGLRQAMATTGYSEVKEFQRIELTI 366
Cdd:TIGR01304 320 VGeapTLEEILHGPSTLPDGVENFEGGLKRAMAKCGYTDLKEFQKVSLTV 369
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
 13-367 2.33e-92

IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the NAD-dependent oxidation of inosine 5'-monophosphate (IMP) to xanthosine 5' monophosphate (XMP). It is a rate-limiting step in the de novo synthesis of the guanine nucleotides. There is often a CBS domain inserted in the middle of this domain, which is proposed to play a regulatory role. IMPDH is a key enzyme in the regulation of cell proliferation and differentiation. It has been identified as an attractive target for developing chemotherapeutic agents.


Pssm-ID: 238223 [Multi-domain]  Cd Length: 325  Bit Score: 279.40  E-value: 2.33e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  13 AYSLDDIALIPSRRTRGTEMVNLEWRIDA-LTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVLNLEGLWTRYEDPTPyle 91
Cdd:cd00381    1 GLTFDDVLLVPGYSTVLPSEVDLSTKLTKnITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVR--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  92 elaglsddvattrrmqeiyaepikaelitermaeiRAAGVPVAGSLSP--KNASRFSETVVNAGADffvirGTTVSAEHV 169
Cdd:cd00381   78 -----------------------------------KVKGRLLVGAAVGtrEDDKERAEALVEAGVD-----VIVIDSAHG 117

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 170 aNGDDVLDLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVSMASAIADVAEARRDY 247
Cdd:cd00381  118 -HSVYVIEMIKFIKKKypNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVADVAAAARDY 196

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 248 mdesggrYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPG---------RGWHWGAEAWHPDLPRGARVHFE 318
Cdd:cd00381  197 -------GVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGeyieingkrYKEYRGMGSLGAMKKGGGDRYFG 269

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488471102 319 PVGT------LAEVLNGPSRVPDGTMNLVGGLRQAMATTGYSEVKEFQRIELTIR 367
Cdd:cd00381  270 EEAKklvpegVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQEKARFVR 324
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
 150-296 4.59e-30

IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine nucleotide. Members of this family contain a TIM barrel structure. In the inosine monophosphate dehydrogenases 2 CBS domains pfam00571 are inserted in the TIM barrel. This family is a member of the common phosphate binding site TIM barrel family.


Pssm-ID: 459826 [Multi-domain]  Cd Length: 463  Bit Score: 119.80  E-value: 4.59e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  150 VNAGADFFVIrgttvsaeHVANG--DDVLDLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQ 225
Cdd:pfam00478 229 VEAGVDVLVV--------DTAHGhsKGVIDTVKWIKKKypDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRV 300

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488471102  226 VLGIQVSMASAIADVAEARRDYmdesgGryVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGR 296
Cdd:pfam00478 301 VAGVGVPQLTAIYDVAEAAKKY-----G--VPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGE 364
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
 13-296 4.62e-27

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 111.60  E-value: 4.62e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  13 AYSLDDIALIPSRRTRGTEMVNLEWRI-DALTFDFPIMAAPMDSVMSPATAIEFGRLGGLGVL----------------- 74
Cdd:PTZ00314  17 GLTYDDVILLPGYIDFSRDDVDLSTRLtRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIhnncsieeqveevrkvk 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  75 --------------------------------------------NLEGLWTRYEdpTPYLEELAGLSDDVATTRRMQEIY 110
Cdd:PTZ00314  97 rfengfimdpyvlspnhtvadvleikekkgfssilitvdgkvggKLLGIVTSRD--IDFVKDKSTPVSEVMTPREKLVVG 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 111 AEPIKAELITERMAEIRAAGVPVAG---------SLSP-------KNASRFSE--------------------TVVNAGA 154
Cdd:PTZ00314 175 NTPISLEEANEVLRESRKGKLPIVNdngelvalvSRSDlkknrgyPNASLDSNgqllvgaaistrpedieraaALIEAGV 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 155 DFFVIrgttvsaeHVANGDDVL--DLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQ 230
Cdd:PTZ00314 255 DVLVV--------DSSQGNSIYqiDMIKKLKSNypHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQEVCAVG 326

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488471102 231 VSMASAIADVAEARRDYmdesggrYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGR 296
Cdd:PTZ00314 327 RPQASAVYHVARYARER-------GVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGE 385
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
 160-361 5.13e-25

IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP reductase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440282 [Multi-domain]  Cd Length: 326  Bit Score: 103.75  E-value: 5.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 160 RGTTVSAEHVANGDDVLDLRKFIYDlDVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVSMASAIAD 239
Cdd:COG0516  111 DVLVIDAAHGHSGGDAMKKIKLTFD-DVLLIPGNSATVEPARALVDAGADLTKVGIGPGSICTTRVVIGLGIPQLSAAMD 189

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 240 VAEARRDYmdesggryVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPG-------------RGWHWGAEAWH 306
Cdd:COG0516  190 TVTEARMA--------IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGevilyqgrsvkryRGMGSDAKKLV 261

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488471102 307 PDlprGARVHFEPVGTLAEVLNgpsrvpdgtmNLVGGLRQAMATTGYSEVKEFQR 361
Cdd:COG0516  262 PE---GIEGRVPYKGPLEDTLH----------QLLGGLRSGMGYCGARTIEELRE 303
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
 13-360 2.03e-23

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 100.50  E-value: 2.03e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  13 AYSLDDIALIPSRRTRGTEMVNLEWRIDA-LTFDFPIMAAPMDSVMSPATAIEFGRLGGLGV----LNLEGLWTRYEDPT 87
Cdd:PRK06843   9 ALTFDDVSLIPRKSSVLPSEVSLKTQLTKnISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIihknMSIEAQRKEIEKVK 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  88 PYLEELAGLSDDVATTRRMQ-----------EIYAEPIKAELITERMAEIRAA-GVPVAGSLSPKNASRFSEtVVNAGAD 155
Cdd:PRK06843  89 TYKFQKTINTNGDTNEQKPEiftakqhleksDAYKNAEHKEDFPNACKDLNNKlRVGAAVSIDIDTIERVEE-LVKAHVD 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 156 FFVIrgttvSAEHvANGDDVLDLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVSM 233
Cdd:PRK06843 168 ILVI-----DSAH-GHSTRIIELVKKIKTKypNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQ 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 234 ASAIADVAEARRDymdesggRYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGRGWHWGAEAWHP------ 307
Cdd:PRK06843 242 ITAICDVYEVCKN-------TNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSyvgmgs 314

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488471102 308 --DLPRGARVHF------EPVGTLAEVLNG----PSRVPDGTMNLVGGLRQAMATTGYSEVKEFQ 360
Cdd:PRK06843 315 isAMKRGSKSRYfqlennEPKKLVPEGIEGmvpySGKLKDILTQLKGGLMSGMGYLGAATISDLK 379
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
 147-295 6.65e-17

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 81.64  E-value: 6.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 147 ETVVNAGADFFVIRGTtvsaehvaNGDDV--LDLRKFIYDL--DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHT 222
Cdd:PLN02274 254 EHLVKAGVDVVVLDSS--------QGDSIyqLEMIKYIKKTypELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSICT 325

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488471102 223 TRQVLGIQVSMASAIADVAEarrdYMDESGgryVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPG 295
Cdd:PLN02274 326 TQEVCAVGRGQATAVYKVAS----IAAQHG---VPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPG 391
PRK07107 PRK07107
IMP dehydrogenase;
141-296 1.80e-14

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 74.35  E-value: 1.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 141 NASRFSETV---VNAGADFFVIRGTTVSAEHVAngdDVLDLRKFIYDLDVPVIVGGCATYQAALHLMRTGAAGVLVGFGG 217
Cdd:PRK07107 239 NTRDYAERVpalVEAGADVLCIDSSEGYSEWQK---RTLDWIREKYGDSVKVGAGNVVDREGFRYLAEAGADFVKVGIGG 315

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488471102 218 GATHTTRQVLGIQVSMASAIADVAEARRDYMDESgGRYVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPGR 296
Cdd:PRK07107 316 GSICITREQKGIGRGQATALIEVAKARDEYFEET-GVYIPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTN 393
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
184-295 3.21e-11

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 64.54  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 184 DLDVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVSMASAIADVAEARRDYmdesgGRyvHVIADGS 263
Cdd:PRK07807 266 DPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQFSAVLECAAAAREL-----GA--HVWADGG 338

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488471102 264 VGRSGDIAKAIACGADAVMVGSPLARATEAPG 295
Cdd:PRK07807 339 VRHPRDVALALAAGASNVMIGSWFAGTYESPG 370
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
 173-290 7.91e-11

FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase [Energy production and conversion, Lipid transport and metabolism, General function prediction only]; FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl diphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440915 [Multi-domain]  Cd Length: 357  Bit Score: 62.84  E-value: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 173 DDVLDLRKFiydLDVPVIVGGCATYQAALHLMRTGAAGVLV-GFGGgathttRQVLGiQVSMASAIADVAEArrdymdeS 251
Cdd:COG1304  215 DDIAWLRER---WPGPLIVKGVLSPEDARRAVDAGVDGIDVsNHGG------RQLDG-GPPTIDALPEIRAA-------V 277

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488471102 252 GGRyVHVIADGSVgRSG-DIAKAIACGADAVMVGSPLARA 290
Cdd:COG1304  278 GGR-IPVIADGGI-RRGlDVAKALALGADAVGLGRPFLYG 315
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
 189-295 1.06e-08

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 56.12  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 189 VIVGGCATYQAALHLMRTGAAGVLVGFGGGATHTTRQVLGIQVS--MASAIADVAEARRDymdesggryvHVIADGSVGR 266
Cdd:PRK05458 143 VIAGNVGTPEAVRELENAGADATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAARK----------PIIADGGIRT 212

                         90       100
                 ....*....|....*....|....*....
gi 488471102 267 SGDIAKAIACGADAVMVGSPLARATEAPG 295
Cdd:PRK05458 213 HGDIAKSIRFGATMVMIGSLFAGHEESPG 241
FMN_dh pfam01070
FMN-dependent dehydrogenase;
3-302 2.53e-08

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 54.84  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102    3 DIGRSKRATRAySLDDIALIPsRRTRGTEMVNLEWRIDALTFDFPIMAAPM--DSVMSP----ATAIEFGRLGglgvlnl 76
Cdd:pfam01070  18 GDEVTLRRNRA-AFDRIRLRP-RVLRDVSNRDLSTTLLGQRLSLPFGIAPVgmQGLAHPdgelALARAAAAAG------- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102   77 eglwtryedpTPY---------LEELAglsdDVATTRRMQEIYaePIKAELITERM-AEIRAAG---------VPVAG-- 135
Cdd:pfam01070  89 ----------IPFvlstvsstsLEEVA----AAAGGPLWFQLY--VPRDRELTEDLlERAEAAGykalvltvdTPVLGrr 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  136 ------------SLSPKNAS------RFSETVVNAGADFFVIRGTTVSAEHVANGDDVLDLRKfiyDLDVPVIVGGCATY 197
Cdd:pfam01070 153 erdlrngftlppRLTPRNLLdlalhpRWALGVLRRGGAGGAAAFVGSQFDPALTWDDLAWLRE---RWKGPLVVKGILSP 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  198 QAALHLMRTGAAGVLVGFGGGathttRQVLGiQVSMASAIADVAEARRDYMDesggryvhVIADGSVGRSGDIAKAIACG 277
Cdd:pfam01070 230 EDAKRAVEAGVDGIVVSNHGG-----RQLDG-APATIDALPEIVAAVGGRIP--------VLVDGGIRRGTDVLKALALG 295

                         330       340
                  ....*....|....*....|....*
gi 488471102  278 ADAVMVgsplarateapGRGWHWGA 302
Cdd:pfam01070 296 ADAVLL-----------GRPFLYGL 309
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
 3-361 2.96e-08

Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO). In green plants, glycolate oxidase is one of the key enzymes in photorespiration where it oxidizes glycolate to glyoxylate. LMO catalyzes the oxidation of L-lactate to acetate and carbon dioxide. MDH oxidizes (S)-mandelate to phenylglyoxalate. It is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate.


Pssm-ID: 239203 [Multi-domain]  Cd Length: 299  Bit Score: 54.38  E-value: 2.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102   3 DIGRSKRATRAySLDDIALIPsRRTRGTEMVNLEWRIDALTFDFPIMAAP--MDSVMSP----ATAIEFGRLGGLGVLnl 76
Cdd:cd02809   24 GDEVTLRRNRA-AFDRIRLRP-RVLRDVSKRDTSTTLLGQKLAMPFGIAPtgLQGLAHPdgelATARAAAAAGIPFTL-- 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  77 eglWTryeDPTPYLEELAglsdDVATTRRMQEIYAePIKAELITERMAEIRAAG---------VPVAGSlspknasRFSE 147
Cdd:cd02809  100 ---ST---VSTTSLEEVA----AAAPGPRWFQLYV-PRDREITEDLLRRAEAAGykalvltvdTPVLGR-------RLTW 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 148 tvvnagadffvirgttvsaehvangDDVLDLRKFIydlDVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGathttRQVL 227
Cdd:cd02809  162 -------------------------DDLAWLRSQW---KGPLILKGILTPEDALRAVDAGADGIVVSNHGG-----RQLD 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 228 GIqVSMASAIADVAEARRDYMDesggryvhVIADGSVGRSGDIAKAIACGADAVMVgsplarateapGRGWHWGAEAwhp 307
Cdd:cd02809  209 GA-PATIDALPEIVAAVGGRIE--------VLLDGGIRRGTDVLKALALGADAVLI-----------GRPFLYGLAA--- 265

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488471102 308 DLPRGArvhfepvgtlAEVLNgpsrvpdgtmNLVGGLRQAMATTGYSEVKEFQR 361
Cdd:cd02809  266 GGEAGV----------AHVLE----------ILRDELERAMALLGCASLADLDP 299
PRK05096 PRK05096
guanosine 5'-monophosphate oxidoreductase; Provisional
 203-296 1.42e-07

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235343 [Multi-domain]  Cd Length: 346  Bit Score: 52.64  E-value: 1.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 203 LMRTGAAGVLVGFGGGATHTTRQVLGIQVSMASAIADVAEARRDYmdesGGryvHVIADGSVGRSGDIAKAIACGADAVM 282
Cdd:PRK05096 168 LILSGADIVKVGIGPGSVCTTRVKTGVGYPQLSAVIECADAAHGL----GG---QIVSDGGCTVPGDVAKAFGGGADFVM 240

                         90
                 ....*....|....
gi 488471102 283 VGSPLARATEAPGR 296
Cdd:PRK05096 241 LGGMLAGHEESGGE 254
PLN02535 PLN02535
glycolate oxidase
 186-295 2.94e-07

glycolate oxidase


Pssm-ID: 215294  Cd Length: 364  Bit Score: 51.76  E-value: 2.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 186 DVPVIVGGCATYQAALHLMRTGAAGVLVgfgggATHTTRQvLGIQVSMASAIADVAEArrdymdeSGGRyVHVIADGSVG 265
Cdd:PLN02535 223 NLPILIKGVLTREDAIKAVEVGVAGIIV-----SNHGARQ-LDYSPATISVLEEVVQA-------VGGR-VPVLLDGGVR 288

                         90       100       110
                 ....*....|....*....|....*....|
gi 488471102 266 RSGDIAKAIACGADAVMVGSPLARATEAPG 295
Cdd:PLN02535 289 RGTDVFKALALGAQAVLVGRPVIYGLAAKG 318
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
 188-287 2.27e-06

L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing alpha-hydroxyacid oxidases and catalyzes the oxidation of l-lactate using molecular oxygen to generate pyruvate and H2O2. This family occurs in both prokaryotes and eukaryotes. Members of this family include flavocytochrome b2 (FCB2), glycolate oxidase (GOX), lactate monooxygenase (LMO), mandelate dehydrogenase (MDH), and long chain hydroxyacid oxidase (LCHAO).


Pssm-ID: 240088 [Multi-domain]  Cd Length: 351  Bit Score: 48.98  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 188 PVIVGGCATYQAALHLMRTGAAGVLVGFGGGathttRQVLGIQVSMASaIADVAEARrdymdesgGRYVHVIADGSVGRS 267
Cdd:cd04737  223 PVIVKGIQSPEDADVAINAGADGIWVSNHGG-----RQLDGGPASFDS-LPEIAEAV--------NHRVPIIFDSGVRRG 288

                         90       100
                 ....*....|....*....|
gi 488471102 268 GDIAKAIACGADAVMVGSPL 287
Cdd:cd04737  289 EHVFKALASGADAVAVGRPV 308
PLN02493 PLN02493
probable peroxisomal (S)-2-hydroxy-acid oxidase
 186-297 4.88e-06

probable peroxisomal (S)-2-hydroxy-acid oxidase


Pssm-ID: 166134 [Multi-domain]  Cd Length: 367  Bit Score: 48.19  E-value: 4.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 186 DVPVIVGGCATYQAALHLMRTGAAGVLVgfgggATHTTRQVLGIQVSMaSAIADVAEARRdymdesgGRyVHVIADGSVG 265
Cdd:PLN02493 224 KLPILVKGVLTGEDARIAIQAGAAGIIV-----SNHGARQLDYVPATI-SALEEVVKATQ-------GR-IPVFLDGGVR 289

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488471102 266 RSGDIAKAIACGADAVMVGSPLARATEAPGRG 297
Cdd:PLN02493 290 RGTDVFKALALGASGIFIGRPVVFSLAAEGEA 321
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
 177-361 6.89e-06

Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that catalyzes the reductive synthesis of L-glutamate from 2-oxoglutarate and L-glutamine via intramolecular channelling of ammonia, a reaction in the plant, yeast and bacterial pathway for ammonia assimilation. It is a multifunctional enzyme that functions through three distinct active centers, carrying out L-glutamine hydrolysis, conversion of 2-oxoglutarate into L-glutamate, and electron uptake from an electron donor.


Pssm-ID: 239202 [Multi-domain]  Cd Length: 392  Bit Score: 47.54  E-value: 6.89e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 177 DLRKFIYDL-----DVPVIVGGCATyqaalHLMRTGAAGV---------LVGFGGGaTHTTRQVLGIQVSMASAIAdVAE 242
Cdd:cd02808  200 DLAQLIEDLreatgGKPIGVKLVAG-----HGEGDIAAGVaaagadfitIDGAEGG-TGAAPLTFIDHVGLPTELG-LAR 272

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 243 ARRdYMDESGGRY-VHVIADGSVGRSGDIAKAIACGADAVMVGSpLARATEAPGrgwhwGAEAWHPDLPrgarvhfePVG 321
Cdd:cd02808  273 AHQ-ALVKNGLRDrVSLIASGGLRTGADVAKALALGADAVGIGT-AALIALGCI-----QARKCHTNTC--------PVG 337

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 488471102 322 --TLAEVLNGPSRVPDGT-------MNLVGGLRQAMATTGYSEVKEFQR 361
Cdd:cd02808  338 vaTQDPELRRRLDVEGKAervanylKSLAEELRELAAALGKRSLELLGR 386
lldD PRK11197
L-lactate dehydrogenase; Provisional
 186-296 1.83e-05

L-lactate dehydrogenase; Provisional


Pssm-ID: 183033  Cd Length: 381  Bit Score: 46.17  E-value: 1.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 186 DVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGathttRQVLGIqVSMASAIADVAEARRDYMDesggryvhVIADGSVg 265
Cdd:PRK11197 245 DGPMVIKGILDPEDARDAVRFGADGIVVSNHGG-----RQLDGV-LSSARALPAIADAVKGDIT--------ILADSGI- 309

                         90       100       110
                 ....*....|....*....|....*....|..
gi 488471102 266 RSG-DIAKAIACGADAVMVGSPLARATEAPGR 296
Cdd:PRK11197 310 RNGlDVVRMIALGADTVLLGRAFVYALAAAGQ 341
Glu_synthase pfam01645
Conserved region in glutamate synthase; This family represents a region of the glutamate ...
 177-286 3.11e-05

Conserved region in glutamate synthase; This family represents a region of the glutamate synthase protein. This region is expressed as a separate subunit in the glutamate synthase alpha subunit from archaebacteria, or part of a large multidomain enzyme in other organizms. The aligned region of these proteins contains a putative FMN binding site and Fe-S cluster.


Pssm-ID: 396287 [Multi-domain]  Cd Length: 367  Bit Score: 45.40  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  177 DLRKFIYDL-----DVPV---IVGGCATYQAALHLMRTGAAGVLV-GFGGG---ATHTTRQVLGIQVSMAsaiadVAEAR 244
Cdd:pfam01645 188 DLAQLIYDLkeinpKAPIsvkLVSGHGVGTIAAGVAKAGADIILIdGYDGGtgaSPKTSIKHAGLPWELA-----LAEAH 262

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 488471102  245 RDYMDESGGRYVHVIADGSVGRSGDIAKAIACGADAVMVGSP 286
Cdd:pfam01645 263 QTLKENGLRDRVSLIADGGLRTGADVAKAAALGADAVYIGTA 304
LMO_FMN cd03332
L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that ...
 186-288 4.41e-05

L-Lactate 2-monooxygenase (LMO) FMN-binding domain. LMO is a FMN-containing enzyme that catalyzes the conversion of L-lactate and oxygen to acetate, carbon dioxide, and water. LMO is a member of the family of alpha-hydroxy acid oxidases. It is thought to be a homooctamer with two- and four- fold axes in the center of the octamer.


Pssm-ID: 239448 [Multi-domain]  Cd Length: 383  Bit Score: 44.97  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 186 DVPVIVGGCATYQAALHLMRTGAAGVLVgfgggATHTTRQVLGiQVSMASAIADVAEARRDYMDesggryvhVIADGSVG 265
Cdd:cd03332  253 DLPIVLKGILHPDDARRAVEAGVDGVVV-----SNHGGRQVDG-SIAALDALPEIVEAVGDRLT--------VLFDSGVR 318

                         90       100
                 ....*....|....*....|...
gi 488471102 266 RSGDIAKAIACGADAVMVGSPLA 288
Cdd:cd03332  319 TGADIMKALALGAKAVLIGRPYA 341
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
 45-294 1.21e-04

2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes oxidative denitrification of nitroalkanes to their corresponding carbonyl compounds and nitrites. NDP is a member of the NAD(P)H-dependent flavin oxidoreductase family that reduce a range of alternative electron acceptors. Most use FAD/FMN as a cofactor and NAD(P)H as electron donor. Some contain 4Fe-4S cluster to transfer electron from FAD to FMN.


Pssm-ID: 240081 [Multi-domain]  Cd Length: 236  Bit Score: 42.86  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102  45 DFPIMAAPMDSVMSPATAIEFGRLGGLGVLnleglwtryedPTPYLEelaglsddvattrrmqeiyAEPIKAELITERMA 124
Cdd:cd04730    2 RYPIIQAPMAGVSTPELAAAVSNAGGLGFI-----------GAGYLT-------------------PEALRAEIRKIRAL 51

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 125 EIRAAGVPVAGSLSPKNASRFSETVVNAGADFFVIrgttvsaehvaNGDDVLDLRKFIYDLDVPVIVGgCATYQAALHLM 204
Cdd:cd04730   52 TDKPFGVNLLVPSSNPDFEALLEVALEEGVPVVSF-----------SFGPPAEVVERLKAAGIKVIPT-VTSVEEARKAE 119

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 205 RTGAAG-VLVGFGGGAtHTTRQVLGIQVSMAsAIADVAEarrdymdesggryVHVIADGSVGRSGDIAKAIACGADAVMV 283
Cdd:cd04730  120 AAGADAlVAQGAEAGG-HRGTFDIGTFALVP-EVRDAVD-------------IPVIAAGGIADGRGIAAALALGADGVQM 184

                        250
                 ....*....|.
gi 488471102 284 GSPLARATEAP 294
Cdd:cd04730  185 GTRFLATEESG 195
DUS_like_FMN cd02801
Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze ...
 112-216 5.61e-03

Dihydrouridine synthase-like (DUS-like) FMN-binding domain. Members of this family catalyze the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. 1VHN, a putative flavin oxidoreductase, has high sequence similarity to DUS. The enzymatic mechanism of 1VHN is not known at the present.


Pssm-ID: 239200 [Multi-domain]  Cd Length: 231  Bit Score: 37.86  E-value: 5.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 112 EPIKAELITERMAEirAAGVPV-----AGSLSPKNASRFSETVVNAGADFFVIRGTTVS--AEHVANGDDVLDLRKFiyd 184
Cdd:cd02801  107 DPELVAEIVRAVRE--AVPIPVtvkirLGWDDEEETLELAKALEDAGASALTVHGRTREqrYSGPADWDYIAEIKEA--- 181

                         90       100       110
                 ....*....|....*....|....*....|....
gi 488471102 185 LDVPVIV-GGCATYQAALHLM-RTGAAGVLVGFG 216
Cdd:cd02801  182 VSIPVIAnGDIFSLEDALRCLeQTGVDGVMIGRG 215
PRK13585 PRK13585
1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide ...
 142-214 7.39e-03

1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase;


Pssm-ID: 184165  Cd Length: 241  Bit Score: 37.58  E-value: 7.39e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488471102 142 ASRFSEtvVNAGADFFvirgTTVSAEHVANGDDVLDLRKFIYDLDVPVIV-GGCATYQAALHLMRTGAAGVLVG 214
Cdd:PRK13585 155 AKRFEE--LGAGSILF----TNVDVEGLLEGVNTEPVKELVDSVDIPVIAsGGVTTLDDLRALKEAGAAGVVVG 222
FCB2_FMN cd02922
Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) ...
 173-295 7.51e-03

Flavocytochrome b2 (FCB2) FMN-binding domain. FCB2 (AKA L-lactate:cytochrome c oxidoreductase) is a respiratory enzyme located in the intermembrane space of fungal mitochondria which catalyzes the oxidation of L-lactate to pyruvate. FCB2 also participates in a short electron-transport chain involving cytochrome c and cytochrome oxidase which ultimately directs the reducing equivalents gained from L-lactate oxidation to oxygen, yielding one molecule of ATP for every L-lactate molecule consumed. FCB2 is composed of 2 domains: a C-terminal flavin-binding domain, which includes the active site for lacate oxidation, and an N-terminal b2-cytochrome domain, required for efficient cytochrome c reduction. FCB2 is a homotetramer and contains two noncovalently bound cofactors, FMN and heme per subunit.


Pssm-ID: 239238 [Multi-domain]  Cd Length: 344  Bit Score: 37.96  E-value: 7.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488471102 173 DDVLDLRKFiydLDVPVIVGGCATYQAALHLMRTGAAGVLVGFGGGathttRQVLGIQvsmaSAIADVAEARRdYMDESG 252
Cdd:cd02922  203 DDIKWLRKH---TKLPIVLKGVQTVEDAVLAAEYGVDGIVLSNHGG-----RQLDTAP----APIEVLLEIRK-HCPEVF 269

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488471102 253 GRyVHVIADGSVGRSGDIAKAIACGADAVMVGSPLARATEAPG 295
Cdd:cd02922  270 DK-IEVYVDGGVRRGTDVLKALCLGAKAVGLGRPFLYALSAYG 311
 
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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