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Conserved domains on  [gi|42543065|pdb|1NFB|B]
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Chain B, Inosine-5'-monophosphate dehydrogenase 2

Protein Classification

IMPDH/GMPR family protein( domain architecture ID 11488369)

IMPDH/GMPR family protein similar to inosine-5'-monophosphate dehydrogenase that catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), and GMP reductase that catalyzes the irreversible NADPH-dependent deamination of GMP to IMP

CATH:  3.20.20.70
EC:  1.-.-.-
Gene Ontology:  GO:0046872|GO:0016491
SCOP:  4003103

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
16-510 0e+00

inosine-5'-monophosphate dehydrogenase; Provisional


:

Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 783.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        16 DGLTAQQLFNCG-DGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHN 94
Cdd:PTZ00314   3 DGMSADELFNSIpTGLTYDDVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIHNN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        95 CTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDcf 174
Cdd:PTZ00314  83 CSIEEQVEEVRKVKRFENGFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGGKLLGIVTSRDIDFVKDKSTP-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       175 LEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHE 254
Cdd:PTZ00314 161 VSEVMTPREKLVVGNTPISLEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRGYPNASLDSNGQLLVGAAISTRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       255 DDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQ 334
Cdd:PTZ00314 241 EDIERAAALIEAGVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       335 EVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGM 414
Cdd:PTZ00314 321 EVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       415 GSLDAMdKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRT 494
Cdd:PTZ00314 401 GSLEAM-LSKESGERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRS 479
                        490
                 ....*....|....*.
1NFB_B       495 SSAQVEGGVHSLHSYE 510
Cdd:PTZ00314 480 GSAIKEGGVHSLHKFE 495
 
Name Accession Description Interval E-value
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
16-510 0e+00

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 783.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        16 DGLTAQQLFNCG-DGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHN 94
Cdd:PTZ00314   3 DGMSADELFNSIpTGLTYDDVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIHNN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        95 CTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDcf 174
Cdd:PTZ00314  83 CSIEEQVEEVRKVKRFENGFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGGKLLGIVTSRDIDFVKDKSTP-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       175 LEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHE 254
Cdd:PTZ00314 161 VSEVMTPREKLVVGNTPISLEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRGYPNASLDSNGQLLVGAAISTRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       255 DDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQ 334
Cdd:PTZ00314 241 EDIERAAALIEAGVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       335 EVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGM 414
Cdd:PTZ00314 321 EVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       415 GSLDAMdKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRT 494
Cdd:PTZ00314 401 GSLEAM-LSKESGERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRS 479
                        490
                 ....*....|....*.
1NFB_B       495 SSAQVEGGVHSLHSYE 510
Cdd:PTZ00314 480 GSAIKEGGVHSLHKFE 495
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
29-504 0e+00

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: 754.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B         29 GLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:pfam00478   1 GLTFDDVLLVPGYSEVLPREVDLSTRLTRNITLNIPLVSAAMDTVTEARMAIAMAREGGIGIIHKNMSIEEQAEEVRKVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        109 KYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDIDFlkEEEHDCFLEEIMTKrEDLVVA 188
Cdd:pfam00478  81 RSESGMITDPVTLSPDATVADALALMERYGISGVPVVDDGK----LVGIVTNRDLRF--ETDLSQPVSEVMTK-ENLVTA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        189 PAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGV 268
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEKAKEYPNAAKDEQGRLRVGAAVGVGDDTLERAEALVEAGV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        269 DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVY 348
Cdd:pfam00478 234 DVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVPQLTAIY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        349 KVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHlsSQN 428
Cdd:pfam00478 314 DVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLGAMKKG--SKD 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1NFB_B        429 RYFSE-ADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAmmysgELKFEKRTSSAQVEGGVH 504
Cdd:pfam00478 392 RYFQEdDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELRE-----KARFVRITAAGLRESHPH 463
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
29-481 0e+00

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 660.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B         29 GLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:TIGR01302   1 GLTFDDVLLLPGFIDVEPDDVDLSTRITRNIKLNIPILSSPMDTVTESRMAIAMAREGGIGVIHRNMSIEEQAEQVKRVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        109 KYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEehDCFLEEIMTkREDLVVA 188
Cdd:TIGR01302  81 RAENGIISDPVTISPETTVADVLELMERKGISGIPVVEDGDMTGKLVGIITKRDIRFVKDK--GKPVSEVMT-REEVITV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        189 PAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGV 268
Cdd:TIGR01302 158 PEGIDLEEALKVLHEHRIEKLPVVDKNGELVGLITMKDIVKRRKFPHASKDENGRLIVGAAVGTREFDKERAEALVKAGV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        269 DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVY 348
Cdd:TIGR01302 238 DVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        349 KVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKhlSSQN 428
Cdd:TIGR01302 318 DVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIINGRRYKQYRGMGSLGAMTK--GSSD 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
1NFB_B        429 RYFSE--ADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRA 481
Cdd:TIGR01302 396 RYLQDenKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDELRE 450
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
29-480 2.36e-169

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: 480.86  E-value: 2.36e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       29 GLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:cd00381   1 GLTFDDVLLVPGYSTVLPSEVDLSTKLTKNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVRKVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      109 Kyeqgfitdpvvlspkdrvrdvfeakarhgfcgipitdtgrmgsrlvgiissrdidflkeeehdcfleeimtkredlvva 188
Cdd:cd00381  81 G------------------------------------------------------------------------------- 81
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      189 pagitlkeaneilqrskkgklpivneddelvaiiartdlkknrdyplaskdakkQLLCGAAIGTHEDDKYRLDLLAQAGV 268
Cdd:cd00381  82 ------------------------------------------------------RLLVGAAVGTREDDKERAEALVEAGV 107
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      269 DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVY 348
Cdd:cd00381 108 DVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVA 187
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      349 KVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHlsSQN 428
Cdd:cd00381 188 DVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKG--GGD 265
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
1NFB_B      429 RYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR 480
Cdd:cd00381 266 RYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQ 317
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
162-504 7.53e-67

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: 218.54  E-value: 7.53e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      162 DIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLasKDAK 241
Cdd:COG0516   4 DALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLL--LVDD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      242 KQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDAL 321
Cdd:COG0516  82 DGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGGDAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      322 RVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFgVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYF 401
Cdd:COG0516 162 KVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      402 FSDGIRLKKYRGMGSldamdkhlssqnryfseADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRA 481
Cdd:COG0516 241 LYQGRSVKRYRGMGS-----------------DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELRE 303
                       330       340
                ....*....|....*....|...
1NFB_B      482 mmysgELKFEKRTSSAQVEGGVH 504
Cdd:COG0516 304 -----KARFVRITSAGLRESHPH 321
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
184-231 1.47e-08

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 50.59  E-value: 1.47e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
1NFB_B         184 DLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNR 231
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
 
Name Accession Description Interval E-value
PTZ00314 PTZ00314
inosine-5'-monophosphate dehydrogenase; Provisional
16-510 0e+00

inosine-5'-monophosphate dehydrogenase; Provisional


Pssm-ID: 240355 [Multi-domain]  Cd Length: 495  Bit Score: 783.00  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        16 DGLTAQQLFNCG-DGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHN 94
Cdd:PTZ00314   3 DGMSADELFNSIpTGLTYDDVILLPGYIDFSRDDVDLSTRLTRNIRLKIPIVSSPMDTVTEHKMAIAMALMGGIGVIHNN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        95 CTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDcf 174
Cdd:PTZ00314  83 CSIEEQVEEVRKVKRFENGFIMDPYVLSPNHTVADVLEIKEKKGFSSILITVDGKVGGKLLGIVTSRDIDFVKDKSTP-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       175 LEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHE 254
Cdd:PTZ00314 161 VSEVMTPREKLVVGNTPISLEEANEVLRESRKGKLPIVNDNGELVALVSRSDLKKNRGYPNASLDSNGQLLVGAAISTRP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       255 DDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQ 334
Cdd:PTZ00314 241 EDIERAAALIEAGVDVLVVDSSQGNSIYQIDMIKKLKSNYPHVDIIAGNVVTADQAKNLIDAGADGLRIGMGSGSICITQ 320
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       335 EVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGM 414
Cdd:PTZ00314 321 EVCAVGRPQASAVYHVARYARERGVPCIADGGIKNSGDICKALALGADCVMLGSLLAGTEEAPGEYFFKDGVRLKVYRGM 400
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       415 GSLDAMdKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRT 494
Cdd:PTZ00314 401 GSLEAM-LSKESGERYLDENETIKVAQGVSGSVVDKGSVAKLIPYLVKGVKHGMQYIGAHSIPELHEKLYSGQVRFERRS 479
                        490
                 ....*....|....*.
1NFB_B       495 SSAQVEGGVHSLHSYE 510
Cdd:PTZ00314 480 GSAIKEGGVHSLHKFE 495
PLN02274 PLN02274
inosine-5'-monophosphate dehydrogenase
15-514 0e+00

inosine-5'-monophosphate dehydrogenase


Pssm-ID: 215154 [Multi-domain]  Cd Length: 505  Bit Score: 782.70  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        15 DDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHN 94
Cdd:PLN02274   7 EDGFSAEKLFNQGVSYTYDDVIFHPGYIDFPADAVDLSTRLSRNIPLSIPCVSSPMDTVTESDMAIAMAALGGIGIVHYN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        95 CTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDcf 174
Cdd:PLN02274  87 NTAEEQAAIVRKAKSRRVGFVSDPVVKSPSSTISSLDELKASRGFSSVCVTETGTMGSKLLGYVTKRDWDFVNDRETK-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       175 LEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASK---DAKKQLLCGAAIG 251
Cdd:PLN02274 165 LSEVMTSDDDLVTAPAGIDLEEAEAVLKDSKKGKLPLVNEDGELVDLVTRTDVKRVKGYPKLGKpsvGKDGKLLVGAAIG 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       252 THEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSIC 331
Cdd:PLN02274 245 TRESDKERLEHLVKAGVDVVVLDSSQGDSIYQLEMIKYIKKTYPELDVIGGNVVTMYQAQNLIQAGVDGLRVGMGSGSIC 324
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       332 ITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKY 411
Cdd:PLN02274 325 TTQEVCAVGRGQATAVYKVASIAAQHGVPVIADGGISNSGHIVKALTLGASTVMMGSFLAGTTEAPGEYFYQDGVRVKKY 404
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       412 RGMGSLDAMDKhlSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFE 491
Cdd:PLN02274 405 RGMGSLEAMTK--GSDQRYLGDTAKLKIAQGVSGAVADKGSVLKFVPYTMQAVKQGFQDLGASSLQSAHELLRSGTLRLE 482
                        490       500
                 ....*....|....*....|...
1NFB_B       492 KRTSSAQVEGGVHSLHSYEKRLF 514
Cdd:PLN02274 483 VRTGAAQVEGGVHGLVSYEKKAF 505
IMPDH pfam00478
IMP dehydrogenase / GMP reductase domain; This family is involved in biosynthesis of guanosine ...
29-504 0e+00

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: 754.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B         29 GLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:pfam00478   1 GLTFDDVLLVPGYSEVLPREVDLSTRLTRNITLNIPLVSAAMDTVTEARMAIAMAREGGIGIIHKNMSIEEQAEEVRKVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        109 KYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDIDFlkEEEHDCFLEEIMTKrEDLVVA 188
Cdd:pfam00478  81 RSESGMITDPVTLSPDATVADALALMERYGISGVPVVDDGK----LVGIVTNRDLRF--ETDLSQPVSEVMTK-ENLVTA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        189 PAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGV 268
Cdd:pfam00478 154 PEGTTLEEAKEILHKHKIEKLPVVDDNGRLVGLITIKDIEKAKEYPNAAKDEQGRLRVGAAVGVGDDTLERAEALVEAGV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        269 DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVY 348
Cdd:pfam00478 234 DVLVVDTAHGHSKGVIDTVKWIKKKYPDVQVIAGNVATAEGAKALIEAGADAVKVGIGPGSICTTRVVAGVGVPQLTAIY 313
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        349 KVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHlsSQN 428
Cdd:pfam00478 314 DVAEAAKKYGVPVIADGGIKYSGDIVKALAAGADAVMLGSLLAGTDESPGEVILYQGRRYKSYRGMGSLGAMKKG--SKD 391
                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1NFB_B        429 RYFSE-ADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAmmysgELKFEKRTSSAQVEGGVH 504
Cdd:pfam00478 392 RYFQEdDDKKLVPEGVEGRVPYKGPLSDVVYQLVGGLRSGMGYCGAKTIEELRE-----KARFVRITAAGLRESHPH 463
IMP_dehydrog TIGR01302
inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of ...
29-481 0e+00

inosine-5'-monophosphate dehydrogenase; This model describes IMP dehydrogenase, an enzyme of GMP biosynthesis. This form contains two CBS domains. This model describes a rather tightly conserved cluster of IMP dehydrogenase sequences, many of which are characterized. The model excludes two related families of proteins proposed also to be IMP dehydrogenases, but without characterized members. These are related families are the subject of separate models. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]


Pssm-ID: 273546 [Multi-domain]  Cd Length: 450  Bit Score: 660.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B         29 GLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:TIGR01302   1 GLTFDDVLLLPGFIDVEPDDVDLSTRITRNIKLNIPILSSPMDTVTESRMAIAMAREGGIGVIHRNMSIEEQAEQVKRVK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        109 KYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEehDCFLEEIMTkREDLVVA 188
Cdd:TIGR01302  81 RAENGIISDPVTISPETTVADVLELMERKGISGIPVVEDGDMTGKLVGIITKRDIRFVKDK--GKPVSEVMT-REEVITV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        189 PAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGV 268
Cdd:TIGR01302 158 PEGIDLEEALKVLHEHRIEKLPVVDKNGELVGLITMKDIVKRRKFPHASKDENGRLIVGAAVGTREFDKERAEALVKAGV 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        269 DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVY 348
Cdd:TIGR01302 238 DVIVIDSSHGHSIYVIDSIKEIKKTYPDLDIIAGNVATAEQAKALIDAGADGLRVGIGPGSICTTRIVAGVGVPQITAVY 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        349 KVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKhlSSQN 428
Cdd:TIGR01302 318 DVAEYAAQSGIPVIADGGIRYSGDIVKALAAGADAVMLGSLLAGTTESPGEYEIINGRRYKQYRGMGSLGAMTK--GSSD 395
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*
1NFB_B        429 RYFSE--ADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRA 481
Cdd:TIGR01302 396 RYLQDenKTKKFVPEGVEGAVPYKGSVLELLPQLVGGLKSGMGYVGARSIDELRE 450
IMPDH cd00381
IMPDH: The catalytic domain of the inosine monophosphate dehydrogenase. IMPDH catalyzes the ...
29-480 2.36e-169

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: 480.86  E-value: 2.36e-169
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       29 GLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:cd00381   1 GLTFDDVLLVPGYSTVLPSEVDLSTKLTKNITLNIPLVSAPMDTVTESEMAIAMARLGGIGVIHRNMSIEEQAEEVRKVK 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      109 Kyeqgfitdpvvlspkdrvrdvfeakarhgfcgipitdtgrmgsrlvgiissrdidflkeeehdcfleeimtkredlvva 188
Cdd:cd00381  81 G------------------------------------------------------------------------------- 81
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      189 pagitlkeaneilqrskkgklpivneddelvaiiartdlkknrdyplaskdakkQLLCGAAIGTHEDDKYRLDLLAQAGV 268
Cdd:cd00381  82 ------------------------------------------------------RLLVGAAVGTREDDKERAEALVEAGV 107
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      269 DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVY 348
Cdd:cd00381 108 DVIVIDSAHGHSVYVIEMIKFIKKKYPNVDVIAGNVVTAEAARDLIDAGADGVKVGIGPGSICTTRIVTGVGVPQATAVA 187
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      349 KVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHlsSQN 428
Cdd:cd00381 188 DVAAAARDYGVPVIADGGIRTSGDIVKALAAGADAVMLGSLLAGTDESPGEYIEINGKRYKEYRGMGSLGAMKKG--GGD 265
                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|..
1NFB_B      429 RYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVR 480
Cdd:cd00381 266 RYFGEEAKKLVPEGVEGIVPYKGSVKDVLPQLVGGLRSSMGYCGAKSLKELQ 317
PRK07107 PRK07107
IMP dehydrogenase;
31-504 2.15e-104

IMP dehydrogenase;


Pssm-ID: 180842 [Multi-domain]  Cd Length: 502  Bit Score: 321.65  E-value: 2.15e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        31 TYNDFLILPGY--IDFTADQVDLTSALTK-------KITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQA 101
Cdd:PRK07107  11 TFSEYLLVPGLssKECVPANVSLKTPLVKfkkgeesAITLNIPLVSAIMQSVSDDNMAIALAREGGLSFIFGSQSIESEA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       102 NEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCfLEEIMTK 181
Cdd:PRK07107  91 AMVRRVKNYKAGFVVSDSNLTPDNTLADVLDLKEKTGHSTVAVTEDGTAHGKLLGIVTSRDYRISRMSLDTK-VKDFMTP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       182 REDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHeDDKYRLD 261
Cdd:PRK07107 170 FEKLVTANEGTTLKEANDIIWDHKLNTLPIVDKNGNLVYLVFRKDYDSHKENPLELLDSSKRYVVGAGINTR-DYAERVP 248
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       262 LLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKY-PNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACG 340
Cdd:PRK07107 249 ALVEAGADVLCIDSSEGYSEWQKRTLDWIREKYgDSVKVGAGNVVDREGFRYLAEAGADFVKVGIGGGSICITREQKGIG 328
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       341 RPQATAVYKVS----EYARRFGV--PVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGM 414
Cdd:PRK07107 329 RGQATALIEVAkardEYFEETGVyiPICSDGGIVYDYHMTLALAMGADFIMLGRYFARFDESPTNKVNINGNYMKEYWGE 408
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       415 GSLDAmdkhlssQN--RYFSEADK-IKVAQGVSGavqdkgsihkFVPYliAGiqhSCQDIGAKSLTQVRAMMYS------ 485
Cdd:PRK07107 409 GSNRA-------RNwqRYDLGGDKkLSFEEGVDS----------YVPY--AG---SLKDNVAITLSKVRSTMCNcgalsi 466
                        490       500
                 ....*....|....*....|...
1NFB_B       486 GELKFEKR----TSSAQVEGGVH 504
Cdd:PRK07107 467 PELQQKAKitlvSSTSIVEGGAH 489
PRK06843 PRK06843
inosine 5-monophosphate dehydrogenase; Validated
28-508 3.66e-76

inosine 5-monophosphate dehydrogenase; Validated


Pssm-ID: 180725 [Multi-domain]  Cd Length: 404  Bit Score: 245.33  E-value: 3.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        28 DGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKV 107
Cdd:PRK06843   8 EALTFDDVSLIPRKSSVLPSEVSLKTQLTKNISLNIPFLSSAMDTVTESQMAIAIAKEGGIGIIHKNMSIEAQRKEIEKV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       108 KKYEqgfitdpvvlspkdrvrdvfeakarhgfcgipITDTgrmgsrlvgIISSRDIDflkEEEhdcflEEIMTKREDLvv 187
Cdd:PRK06843  88 KTYK--------------------------------FQKT---------INTNGDTN---EQK-----PEIFTAKQHL-- 116
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       188 apagitlkEANEILQRSKKGKlpivneddelvaiiartdlkknrDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAG 267
Cdd:PRK06843 117 --------EKSDAYKNAEHKE-----------------------DFPNACKDLNNKLRVGAAVSIDIDTIERVEELVKAH 165
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       268 VDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAV 347
Cdd:PRK06843 166 VDILVIDSAHGHSTRIIELVKKIKTKYPNLDLIAGNIVTKEAALDLISVGADCLKVGIGPGSICTTRIVAGVGVPQITAI 245
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       348 YKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKhlSSQ 427
Cdd:PRK06843 246 CDVYEVCKNTNICIIADGGIRFSGDVVKAIAAGADSVMIGNLFAGTKESPSEEIIYNGKKFKSYVGMGSISAMKR--GSK 323
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       428 NRYF----SEADKIkVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAmmysgELKFEKRTSSAQVEGGV 503
Cdd:PRK06843 324 SRYFqlenNEPKKL-VPEGIEGMVPYSGKLKDILTQLKGGLMSGMGYLGAATISDLKI-----NSKFVKISHSSLKESHP 397

                 ....*
1NFB_B       504 HSLHS 508
Cdd:PRK06843 398 HDVFN 402
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
162-504 7.53e-67

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: 218.54  E-value: 7.53e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      162 DIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLasKDAK 241
Cdd:COG0516   4 DALRRRLISRSGVVVVVVVGKLTIITTRRRRRDEAVKALVVTTVIEKLLLVTVAGETALLALALLLLKKKKFLL--LVDD 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      242 KQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDAL 321
Cdd:COG0516  82 DGLLLLVLVGVKDDDKEKARALAAADAGVDVLVIDAAHGHSGGDAMKKIKLTFDDVLLIPGNSATVEPARALVDAGADLT 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      322 RVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFgVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYF 401
Cdd:COG0516 162 KVGIGPGSICTTRVVIGLGIPQLSAAMDTVTEARMA-IAIAADGGIGYIHDNAKALAAGADAVMLGSLFAGTEEQPGEVI 240
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      402 FSDGIRLKKYRGMGSldamdkhlssqnryfseADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRA 481
Cdd:COG0516 241 LYQGRSVKRYRGMGS-----------------DAKKLVPEGIEGRVPYKGPLEDTLHQLLGGLRSGMGYCGARTIEELRE 303
                       330       340
                ....*....|....*....|...
1NFB_B      482 mmysgELKFEKRTSSAQVEGGVH 504
Cdd:COG0516 304 -----KARFVRITSAGLRESHPH 321
PRK07807 PRK07807
GuaB1 family IMP dehydrogenase-related protein;
30-478 8.93e-61

GuaB1 family IMP dehydrogenase-related protein;


Pssm-ID: 181127 [Multi-domain]  Cd Length: 479  Bit Score: 207.06  E-value: 8.93e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        30 LTYNDFLILPGYIDFTADQ-VDLTSALTKKITLktPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVK 108
Cdd:PRK07807  13 LTYDDVFLVPSRSDVGSRFdVDLSTADGTGTTI--PLVVANMTAVAGRRMAETVARRGGLVVLPQDIPIDVVAEVVAWVK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       109 KYEQGFITdPVVLSPKDRVRDVFE--AKARHGfCGIPITDTGRMgsrlVGIISSRDIdflkeEEHDCF--LEEIMTkrED 184
Cdd:PRK07807  91 SRDLVFDT-PVTLSPDDTVGDALAllPKRAHG-AVVVVDEEGRP----VGVVTEADC-----AGVDRFtqVRDVMS--TD 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       185 LVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASkDAKKQLLCGAAIGTHEDDKYRLDLLA 264
Cdd:PRK07807 158 LVTLPAGTDPREAFDLLEAARVKLAPVVDADGRLVGVLTRTGALRATIYTPAV-DAAGRLRVAAAVGINGDVAAKARALL 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       265 QAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQA 344
Cdd:PRK07807 237 EAGVDVLVVDTAHGHQEKMLEALRAVRALDPGVPIVAGNVVTAEGTRDLVEAGADIVKVGVGPGAMCTTRMMTGVGRPQF 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       345 TAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGE-YFFSDGIRLKKYRGMGSLDAMdKH 423
Cdd:PRK07807 317 SAVLECAAAARELGAHVWADGGVRHPRDVALALAAGASNVMIGSWFAGTYESPGDlMRDRDGRPYKESFGMASARAV-AA 395
                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*....
1NFB_B       424 LSSQNRYFSEADKIKVAQGVSGAV----QDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQ 478
Cdd:PRK07807 396 RTAGDSAFDRARKALFEEGISTSRmyldPGRPGVEDLLDHITSGVRSSCTYAGARTLAE 454
CBS_pair_IMPDH cd04601
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' ...
115-229 2.21e-50

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341376 [Multi-domain]  Cd Length: 110  Bit Score: 167.98  E-value: 2.21e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGrmgSRLVGIISSRDIDFLKEEEHdcFLEEIMTKREDLVVAPAGITL 194
Cdd:cd04601   1 ITDPVTLSPDATVADVLELKAEYGISGVPVTEDG---GKLVGIVTSRDIRFETDLST--PVSEVMTPDERLVTAPEGITL 75
                        90       100       110
                ....*....|....*....|....*....|....*
1NFB_B      195 KEANEILQRSKKGKLPIVNEDDELVAIIARTDLKK 229
Cdd:cd04601  76 EEAKEILHKHKIEKLPIVDDNGELVGLITRKDIEK 110
PRK05458 PRK05458
guanosine 5'-monophosphate oxidoreductase; Provisional
241-416 2.04e-34

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235479 [Multi-domain]  Cd Length: 326  Bit Score: 132.00  E-value: 2.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       241 KKQLLCGAAIGTHEDDKYRLDLLAQAGV--DVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGV 318
Cdd:PRK05458  83 EQGLIASISVGVKDDEYDFVDQLAAEGLtpEYITIDIAHGHSDSVINMIQHIKKHLPETFVIAGNVGTPEAVRELENAGA 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       319 DALRVGMGSGSICITQEVLACGRP--QATAVYKVSEYARRfgvPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEA 396
Cdd:PRK05458 163 DATKVGIGPGKVCITKIKTGFGTGgwQLAALRWCAKAARK---PIIADGGIRTHGDIAKSIRFGATMVMIGSLFAGHEES 239
                        170       180
                 ....*....|....*....|
1NFB_B       397 PGEYFFSDGIRLKKYRGMGS 416
Cdd:PRK05458 240 PGKTVEIDGKLYKEYFGSAS 259
PRK05096 PRK05096
guanosine 5'-monophosphate oxidoreductase; Provisional
250-476 8.25e-32

guanosine 5'-monophosphate oxidoreductase; Provisional


Pssm-ID: 235343 [Multi-domain]  Cd Length: 346  Bit Score: 125.05  E-value: 8.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       250 IGTHEDD--KYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGS 327
Cdd:PRK05096 103 TGTSDADfeKTKQILALSPALNFICIDVANGYSEHFVQFVAKAREAWPDKTICAGNVVTGEMVEELILSGADIVKVGIGP 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       328 GSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIR 407
Cdd:PRK05096 183 GSVCTTRVKTGVGYPQLSAVIECADAAHGLGGQIVSDGGCTVPGDVAKAFGGGADFVMLGGMLAGHEESGGEIVEENGEK 262
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
1NFB_B       408 LKKYRGMGSLDAMDKHLSSQNRYfseadkiKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSL 476
Cdd:PRK05096 263 FMLFYGMSSESAMKRHVGGVAEY-------RAAEGKTVKLPLRGPVENTARDILGGLRSACTYVGASRL 324
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
33-227 2.03e-23

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 98.03  E-value: 2.03e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       33 NDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQ 112
Cdd:COG2524   1 LLVLLLLALSLLLPLLAVVLAALLLLAALVLALTAAAAATVLLLAAAAAAAGAGGLGLLLLLLLIVLQAAAVRVVAEKEL 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      113 GFI----------TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDIDFLKEEEHDCF---LEEIM 179
Cdd:COG2524  81 GLVlkmkvkdimtKDVITVSPDTTLEEALELMLEKGISGLPVVDDGK----LVGIITERDLLKALAEGRDLLdapVSDIM 156
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
1NFB_B      180 TKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:COG2524 157 TR--DVVTVSEDDSLEEALRLMLEHGIGRLPVVDDDGKLVGIITRTDI 202
CBS COG0517
CBS domain [Signal transduction mechanisms];
109-236 8.47e-23

CBS domain [Signal transduction mechanisms];


Pssm-ID: 440283 [Multi-domain]  Cd Length: 128  Bit Score: 93.78  E-value: 8.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      109 KYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDIDFLKEEEHDCFLE----EIMTKreD 184
Cdd:COG0517   2 KVKDIMTTDVVTVSPDATVREALELMSEKRIGGLPVVDEDG---KLVGIVTDRDLRRALAAEGKDLLDtpvsEVMTR--P 76
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
1NFB_B      185 LVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLA 236
Cdd:COG0517  77 PVTVSPDTSLEEAAELMEEHKIRRLPVVDDDGRLVGIITIKDLLKALLEPLA 128
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
116-227 7.56e-19

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 81.91  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGrmgSRLVGIISSRDIDFLKEEEHDCF---LEEIMTKreDLVVAPAGI 192
Cdd:cd02205   2 RDVVTVDPDTTVREALELMAENGIGALPVVDDD---GKLVGIVTERDILRALVEGGLALdtpVAEVMTP--DVITVSPDT 76
                        90       100       110
                ....*....|....*....|....*....|....*
1NFB_B      193 TLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd02205  77 DLEEALELMLEHGIRRLPVVDDDGKLVGIVTRRDI 111
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
115-227 3.40e-17

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 77.98  E-value: 3.40e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDI---------DFLKEEEHDCFLEEIMTKreDL 185
Cdd:COG3448   9 TRDVVTVSPDTTLREALELMREHGIRGLPVVDEDG---RLVGIVTERDLlrallpdrlDELEERLLDLPVEDVMTR--PV 83
                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
1NFB_B      186 VVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:COG3448  84 VTVTPDTPLEEAAELMLEHGIHRLPVVDDDGRLVGIVTRTDL 125
GuaB COG0516
IMP dehydrogenase/GMP reductase [Nucleotide transport and metabolism]; IMP dehydrogenase/GMP ...
30-160 5.34e-16

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: 79.10  E-value: 5.34e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       30 LTYNDFLILPGYI---DFTADQVDLTSALTK-------------KITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHH 93
Cdd:COG0516 132 LTFDDVLLIPGNSatvEPARALVDAGADLTKvgigpgsicttrvVIGLGIPQLSAAMDTVTEARMAIAIAADGGIGYIHD 211
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       94 NC-----------------TPEFQANEV-----RKVKKYE-----------QGFIT-DPVVLSPKDRVRDVFEA-KARHG 138
Cdd:COG0516 212 NAkalaagadavmlgslfaGTEEQPGEVilyqgRSVKRYRgmgsdakklvpEGIEGrVPYKGPLEDTLHQLLGGlRSGMG 291
                       170       180
                ....*....|....*....|..
1NFB_B      139 FCGIPITDTGRMGSRLVGIISS 160
Cdd:COG0516 292 YCGARTIEELREKARFVRITSA 313
YtoI COG4109
Predicted transcriptional regulator containing CBS domains [Transcription];
115-227 1.32e-15

Predicted transcriptional regulator containing CBS domains [Transcription];


Pssm-ID: 443285 [Multi-domain]  Cd Length: 135  Bit Score: 73.41  E-value: 1.32e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFE--AKARHGfcGIPITDTGRmgsRLVGIISSRDIdflKEEEHDCFLEEIMTKreDLVVAPAGI 192
Cdd:COG4109  24 LEDVATLSEDDTVEDALEllEKTGHS--RFPVVDENG---RLVGIVTSKDI---LGKDDDTPIEDVMTK--NPITVTPDT 93
                        90       100       110
                ....*....|....*....|....*....|....*
1NFB_B      193 TLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:COG4109  94 SLASAAHKMIWEGIELLPVVDDDGRLLGIISRQDV 128
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
116-227 8.67e-15

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 70.91  E-value: 8.67e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGrmgsRLVGIISSRDI------DFLKEEEHDCF-------LEEIMTKr 182
Cdd:cd04584   8 KNVVTVTPDTSLAEARELMKEHKIRHLPVVDDG----KLVGIVTDRDLlraspsKATSLSIYELNyllskipVKDIMTK- 82
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
1NFB_B      183 eDLVVAPAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04584  83 -DVITVSPDDTVEEAALLMLENKIGCLPVV-DGGKLVGIITETDI 125
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
116-227 1.30e-14

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 70.24  E-value: 1.30e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDI-DFLKEEEHDCF---LEEIMTKreDLVVAPAG 191
Cdd:COG2905   7 RDVVTVSPDATVREAARLMTEKGVGSLVVVDDDG---RLVGIITDRDLrRRVLAEGLDPLdtpVSEVMTR--PPITVSPD 81
                        90       100       110
                ....*....|....*....|....*....|....*.
1NFB_B      192 ITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:COG2905  82 DSLAEALELMEEHRIRHLPVV-DDGKLVGIVSITDL 116
NPD_like cd04730
2-Nitropropane dioxygenase (NPD), one of the nitroalkane oxidizing enzyme families, catalyzes ...
252-397 5.43e-14

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: 71.36  E-value: 5.43e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      252 THEDDKYRLDLLAQAGVDVVVLdsSQGNSIfqiNMIKYIKDKypNLQVIGgNVVTAAQAKNLIDAGVDALRV-GMGSG-- 328
Cdd:cd04730  65 SNPDFEALLEVALEEGVPVVSF--SFGPPA---EVVERLKAA--GIKVIP-TVTSVEEARKAEAAGADALVAqGAEAGgh 136
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
1NFB_B      329 --SICITQEVLacgrpqatavykVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAP 397
Cdd:cd04730 137 rgTFDIGTFAL------------VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESG 195
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
118-227 2.30e-13

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 66.37  E-value: 2.30e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      118 PV-VLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDID-FLKEEEHDCFLEEIMTKreDLVVAPAGITLK 195
Cdd:cd04595   3 PVkTVSPDTTIEEARKIMLRYGHTGLPVVEDGK----LVGIISRRDVDkAKHHGLGHAPVKGYMST--NVITIDPDTSLE 76
                        90       100       110
                ....*....|....*....|....*....|..
1NFB_B      196 EANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04595  77 EAQELMVEHDIGRLPVV-EEGKLVGIVTRSDV 107
CBS_pair_ParBc_assoc cd04610
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ...
116-226 1.07e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a ParBc (ParB-like nuclease) domain downstream. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341383 [Multi-domain]  Cd Length: 108  Bit Score: 64.26  E-value: 1.07e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDIdfLKEEEHDcFLEEIMTKreDLVVAPAGITLK 195
Cdd:cd04610   3 RDVITVSPDDTVKDVIKLIKETGHDGFPVVDDGK----VVGYVTAKDL--LGKDDDE-KVSEIMSR--DTVVADPDMDIT 73
                        90       100       110
                ....*....|....*....|....*....|.
1NFB_B      196 EANEILQRSKKGKLPIVNEDDELVAIIARTD 226
Cdd:cd04610  74 DAARVIFRSGISKLPVVDDEGNLVGIITNMD 104
CBS_pair_peptidase_M50 cd04801
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the ...
116-227 5.79e-12

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in the metalloprotease peptidase M50; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in peptidase M50. Members of the M50 metallopeptidase family include mammalian sterol-regulatory element binding protein (SREBP) site 2 proteases and various hypothetical bacterial homologues. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341401 [Multi-domain]  Cd Length: 113  Bit Score: 62.59  E-value: 5.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDIDFLKEEEHDCFL-EEIMTKreDLVVAPAGITL 194
Cdd:cd04801   5 PEVVTVTPEMTVSELLDRMFEEKHLGYPVVENGR----LVGIVTLEDIRKVPEVEREATRvRDVMTK--DVITVSPDADA 78
                        90       100       110
                ....*....|....*....|....*....|...
1NFB_B      195 KEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04801  79 MEALKLMSQNNIGRLPVV-EDGELVGIISRTDL 110
YrpB COG2070
NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General ...
260-397 4.17e-11

NAD(P)H-dependent flavin oxidoreductase YrpB, nitropropane dioxygenase family [General function prediction only];


Pssm-ID: 441673 [Multi-domain]  Cd Length: 302  Bit Score: 63.98  E-value: 4.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      260 LDLLAQAGVDVVVldSSQGNSIfqiNMIKYIKDKypNLQVIGgNVVTAAQAKNLIDAGVDALRV-GMGSG----SICITQ 334
Cdd:COG2070  75 LEVVLEEGVPVVS--TSAGLPA---DLIERLKEA--GIKVIP-IVTSVREARKAEKAGADAVVAeGAEAGghrgADEVST 146
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
1NFB_B      335 EVLacgrpqatavykVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAP 397
Cdd:COG2070 147 FAL------------VPEVRDAVDIPVIAAGGIADGRGIAAALALGADGVQMGTRFLATEESP 197
CBS_pair_GGDEF_assoc cd04599
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
117-227 8.34e-11

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the GGDEF (DiGuanylate-Cyclase (DGC)) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in association with the GGDEF (DiGuanylate-Cyclase (DGC)) domain. The GGDEF domain has been suggested to be homologous to the adenylyl cyclase catalytic domain and is thought to be involved in regulating cell surface adhesiveness in bacteria. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341374 [Multi-domain]  Cd Length: 107  Bit Score: 58.89  E-value: 8.34e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      117 DPVVLSPKDRVRDVFEAKARHGFCGIPITDTGrmgsRLVGIISSRDIDFLKEEEhdcFLEEIMTKreDLVVAPAGITLKE 196
Cdd:cd04599   4 NPITISPLDSVARAAALMERQRIGGLPVVENG----KLVGIITSRDVRRAHPNR---LVADAMSR--NVVTISPEASLWE 74
                        90       100       110
                ....*....|....*....|....*....|.
1NFB_B      197 ANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04599  75 AKELMEEHGIERLVVV-EEGRLVGIITKSTL 104
CBS_archAMPK_gamma-repeat1 cd17779
signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated ...
117-229 1.51e-10

signal transduction protein with CBS domains; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341415 [Multi-domain]  Cd Length: 136  Bit Score: 59.17  E-value: 1.51e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      117 DPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgSRLVGIISSRDI-DFLK--------EEEHDCFL--------EEIM 179
Cdd:cd17779   9 DVITIPPTTTIIGAIKTMTEKGFRRLPVADAGT--KRLEGIVTSMDIvDFLGggskynlvEKKHNGNLlaainepvREIM 86
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
1NFB_B      180 TkrEDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKK 229
Cdd:cd17779  87 T--RDVISVKENASIDDAIELMLEKNVGGLPIVDKDGKVIGIVTERDFLK 134
LldD COG1304
FMN-dependent dehydrogenase, includes L-lactate dehydrogenase and type II isopentenyl ...
304-387 3.06e-09

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: 58.61  E-value: 3.06e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      304 VVTAAQAKNLIDAGVDALRV-GMGsGsiciTQevLACGRPQATAVYKVSEyARRFGVPVIADGGIQNVGHIAKALALGAS 382
Cdd:COG1304 233 VLSPEDARRAVDAGVDGIDVsNHG-G----RQ--LDGGPPTIDALPEIRA-AVGGRIPVIADGGIRRGLDVAKALALGAD 304

                ....*
1NFB_B      383 TVMMG 387
Cdd:COG1304 305 AVGLG 309
CBS_pair_archHTH_assoc cd04588
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and ...
116-227 4.99e-09

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in archaea and associated with helix turn helix domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the inosine 5' monophosphate dehydrogenase (IMPDH) protein. IMPDH is an essential enzyme that catalyzes the first step unique to GTP synthesis, playing a key role in the regulation of cell proliferation and differentiation. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341364 [Multi-domain]  Cd Length: 111  Bit Score: 54.08  E-value: 4.99e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDI-DFLKEEEHDCFLEEIMTKreDLVVAPAGITL 194
Cdd:cd04588   2 KDLITLKPDATIKDAAKLLSENNIHGAPVVDDGK----LVGIVTLTDIaKALAEGKENAKVKDIMTK--DVITIDKDEKI 75
                        90       100       110
                ....*....|....*....|....*....|...
1NFB_B      195 KEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd04588  76 YDAIRLMNKHNIGRLIVVDDNGKPVGIITRTDI 108
CBS_pair_HRP1_like cd04622
CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium ...
116-227 8.58e-09

CBS pair domain found in Hypoxic Response Protein 1 (HRP1) -like proteinds; Mycobacterium tuberculosis adapts to cellular stresses by upregulation of the dormancy survival regulon. Hypoxic response protein 1 (HRP1) is encoded by one of the most strongly upregulated genes in the dormancy survival regulon. HRP1 is a 'CBS-domain-only protein; however unlike other CBS containing proteins it does not appear to bind AMP. The biological function of the protein remains unclear, but is thought to contribute to the modulation of the host immune response. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341390 [Multi-domain]  Cd Length: 115  Bit Score: 53.58  E-value: 8.58e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDtgrmGSRLVGIISSRDI---------DflkeeEHDCFLEEIMTKreDLV 186
Cdd:cd04622   3 RDVVTVSPDTTLREAARLMRDLDIGALPVCE----GDRLVGMVTDRDIvvravaegkD-----PNTTTVREVMTG--DVV 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1NFB_B      187 VAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd04622  72 TCSPDDDVEEAARLMAEHQVRRLPVVDDDGRLVGIVSLGDL 112
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
184-231 1.47e-08

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 50.59  E-value: 1.47e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
1NFB_B         184 DLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNR 231
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDEEGRLVGIVTRRDIIKAL 48
CBS_pair_arch2_repeat1 cd04638
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, ...
129-227 1.31e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea, repeat 1; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341396 [Multi-domain]  Cd Length: 109  Bit Score: 50.03  E-value: 1.31e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      129 DVFEAKARHGFCGIPITDtgRMGSRLVGIISSRDIDFLKEEEHDCFLeeiMTkrEDLVVAPAGITLKEANEILQRSKKGK 208
Cdd:cd04638  16 DVLEILKKKAISGVPVVK--KETGKLVGIVTRKDLLRNPDEEQIALL---MS--RDPITISPDDTLSEAAELMLEHNIRR 88
                        90
                ....*....|....*....
1NFB_B      209 LPIVnEDDELVAIIARTDL 227
Cdd:cd04638  89 VPVV-DDDKLVGIVTVADL 106
CBS_arch_repeat1 cd17777
CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal ...
118-227 1.37e-07

CBS pair domains found in archeal proteins, repeat 1; CBS pair domains found in archeal proteins that contain 2 repeats. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341413 [Multi-domain]  Cd Length: 137  Bit Score: 50.42  E-value: 1.37e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      118 PVVLSPKDRVRDVFEAKARHGFCGIPITDtgrmGSRLVGIISSRD-IDFL--------KEEEH--DCF-------LEEIM 179
Cdd:cd17777  12 VLSISPSAPILSAFEKMNRRGIRRLVVVD----ENKLEGILSARDlVSYLgggclfkiVESRHqgDLYsalnrevVETIM 87
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1NFB_B      180 TKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd17777  88 TP--NPVYVYEDSDLIEALTIMVTRGIGSLPVVDRDGRPVGIVTERDL 133
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
175-229 1.53e-07

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 47.98  E-value: 1.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
1NFB_B        175 LEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKK 229
Cdd:pfam00571   1 VKDIMTK--DVVTVSPDTTLEEALELMREHGISRLPVVDEDGKLVGIVTLKDLLR 53
CBS_pair_BON_assoc cd04586
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
116-227 1.83e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the BON (bacterial OsmY and nodulation domain) domain. BON is a putative phospholipid-binding domain found in a family of osmotic shock protection proteins. It is also found in some secretins and a group of potential haemolysins. Its likely function is attachment to phospholipid membranes. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341362 [Multi-domain]  Cd Length: 137  Bit Score: 50.12  E-value: 1.83e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDI----------------DFLKE----------E 169
Cdd:cd04586   3 TDVVTVTPDTSVREAARLLLEHRISGLPVVDDDG---KLVGIVSEGDLlrreepgteprrvwwlDALLEsperlaeeyvK 79
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
1NFB_B      170 EHDCFLEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04586  80 AHGRTVGDVMTR--PVVTVSPDTPLEEAARLMERHRIKRLPVV-DDGKLVGIVSRADL 134
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
117-227 3.46e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 49.48  E-value: 3.46e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      117 DPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSrdIDFLKEEEHDCF--------------------LE 176
Cdd:cd04600   4 DVVTVTPDTSLEEAWRLLRRHRIKALPVVDRAR---RLVGIVTL--ADLLKHADLDPPrglrgrlrrtlglrrdrpetVG 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
1NFB_B      177 EIMTKRedLVVAPAGITLKEANEILqrSKKGK--LPIVNEDDELVAIIARTDL 227
Cdd:cd04600  79 DIMTRP--VVTVRPDTPIAELVPLF--SDGGLhhIPVVDADGRLVGIVTQSDL 127
CBS_pair_arch cd09836
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, ...
116-227 3.77e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341405 [Multi-domain]  Cd Length: 116  Bit Score: 48.67  E-value: 3.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDI------DFLKEEEhdcfLEEIMTKreDLVVAP 189
Cdd:cd09836   3 KPVVTVPPETTIREAAKLMAENNIGSVVVVDDDG---KPVGIVTERDIvravaeGIDLDTP----VEEIMTK--NLVTVS 73
                        90       100       110
                ....*....|....*....|....*....|....*...
1NFB_B      190 AGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd09836  74 PDESIYEAAELMREHNIRHLPVVDGGGKLVGVISIRDL 111
CBS_pair_DRTGG_assoc cd04596
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
115-230 7.75e-07

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DRTGG domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a DRTGG domain upstream. The function of the DRTGG domain, named after its conserved residues, is unknown. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341371 [Multi-domain]  Cd Length: 108  Bit Score: 47.46  E-value: 7.75e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFEAKARHGFCGIPITDtGRMgsRLVGIISSRDIDflkEEEHDCFLEEIMTKrEDLVVAP----- 189
Cdd:cd04596   1 LEETGYLRETDTVRDYKQLSEETGHSRFPVVD-EEN--RVVGIVTAKDVI---GKEDDTPIEKVMTK-NPITVKPktsva 73
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1NFB_B      190 --AGITLKEANEILqrskkgklPIVNEDDELVAIIARTDLKKN 230
Cdd:cd04596  74 saAHMMIWEGIELL--------PVVDENRKLLGVISRQDVLKA 108
CBS_archAMPK_gamma-repeat2 cd04631
CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; ...
106-227 1.41e-06

CBS pair domains found in archeal 5'-AMP-activated protein kinase gamma subunit-like proteins; Archeal gamma-subunit of 5'-AMP-activated protein kinase (AMPK) contains four CBS domains in tandem repeats, similar to eukaryotic homologs. AMPK is an important regulator of metabolism and of energy homeostasis. It is a heterotrimeric protein composed of a catalytic serine/threonine kinase subunit (alpha) and two regulatory subunits (beta and gamma). The gamma subunit senses the intracellular energy status by competitively binding AMP and ATP and is believed to be responsible for allosteric regulation of the whole complex. In humans mutations in gamma- subunit of AMPK are associated with hypertrophic cardiomiopathy, Wolff-Parkinson-White syndrome and glycogen storage in the skeletal muscle. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341394 [Multi-domain]  Cd Length: 130  Bit Score: 47.61  E-value: 1.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      106 KVKKYeqgFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDtgrmGSRLVGIISSRDI-DFLKEEE----------HDCF 174
Cdd:cd04631   1 VVEDY---MTKNVITATPGTPIEDVAKIMVRNGFRRLPVVS----DGKLVGIVTSTDImRYLGSGEafeklktgniHEVL 73
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
1NFB_B      175 ---LEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04631  74 nvpISSIMKR--DIITTTPDTDLGEAAELMLEKNIGALPVV-DDGKLVGIITERDI 126
alpha_hydroxyacid_oxid_FMN cd02809
Family of homologous FMN-dependent alpha-hydroxyacid oxidizing enzymes. This family occurs in ...
255-387 1.78e-06

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: 49.75  E-value: 1.78e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      255 DDKYRLDLL---AQAGVDVVVLDSSQGNSIFQINM--IKYIKDKYPnLQVIGGNVVTAAQAKNLIDAGVDALRV------ 323
Cdd:cd02809 127 DREITEDLLrraEAAGYKALVLTVDTPVLGRRLTWddLAWLRSQWK-GPLILKGILTPEDALRAVDAGADGIVVsnhggr 205
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
1NFB_B      324 ---GMGSgsiciTQEVLAcgrpqatAVykVSEYARRfgVPVIADGGIQNVGHIAKALALGASTVMMG 387
Cdd:cd02809 206 qldGAPA-----TIDALP-------EI--VAAVGGR--IEVLLDGGIRRGTDVLKALALGADAVLIG 256
TIM_phosphate_binding cd04722
TIM barrel proteins share a structurally conserved phosphate binding motif and in general ...
234-388 1.90e-06

TIM barrel proteins share a structurally conserved phosphate binding motif and in general share an eight beta/alpha closed barrel structure. Specific for this family is the conserved phosphate binding site at the edges of strands 7 and 8. The phosphate comes either from the substrate, as in the case of inosine monophosphate dehydrogenase (IMPDH), or from ribulose-5-phosphate 3-epimerase (RPE) or from cofactors, like FMN.


Pssm-ID: 240073 [Multi-domain]  Cd Length: 200  Bit Score: 48.74  E-value: 1.90e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      234 PLASKDAKKQLLCGAAI-GTHEDDKYRLDLLAQAGVDVVVLDSSQGNSI-FQINMIKYIKDKYPNLQVIGGNVVTAAQ-A 310
Cdd:cd04722  50 KEVAAETDLPLGVQLAInDAAAAVDIAAAAARAAGADGVEIHGAVGYLArEDLELIRELREAVPDVKVVVKLSPTGELaA 129
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
1NFB_B      311 KNLIDAGVDALRVGMGSGSICITQEVlacgrpqATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGS 388
Cdd:cd04722 130 AAAEEAGVDEVGLGNGGGGGGGRDAV-------PIADLLLILAKRGSKVPVIAGGGINDPEDAAEALALGADGVIVGS 200
CBS_pair_MUG70_2 cd17782
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 ...
116-222 2.18e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains similar to MUG70 repeat2; Two tandem repeats of the cystathionine beta-synthase (CBS pair) domain, present in MUG70. The MUG70 protein, encoded by the Meiotically Up-regulated Gene 70, plays a role in meiosis and contains, beside the two CBS pairs, a PB1 domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341418 [Multi-domain]  Cd Length: 118  Bit Score: 46.47  E-value: 2.18e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDIDF--LKE--EEHDCFLEEIMTKREDlvVAPAG 191
Cdd:cd17782   2 TPPPLVSPKTTVREAARLMKENRTTAVLVMDNSG---KVIGIFTSKDVVLrvLAAglDPATTSVVRVMTPNPE--TAPPS 76
                        90       100       110
                ....*....|....*....|....*....|.
1NFB_B      192 ITLKEANEILQRSKKGKLPIVNEDDELVAII 222
Cdd:cd17782  77 TTILDALHKMHEGKFLNLPVVDDEGEIVGLV 107
FMN_dh pfam01070
FMN-dependent dehydrogenase;
287-387 2.47e-06

FMN-dependent dehydrogenase;


Pssm-ID: 426029 [Multi-domain]  Cd Length: 350  Bit Score: 49.45  E-value: 2.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        287 IKYIKDKYPnLQVI--GgnVVTAAQAKNLIDAGVDAL-------RVgmgsgsicitqevLACGRPQATAVYKVSEYARRf 357
Cdd:pfam01070 210 LAWLRERWK-GPLVvkG--ILSPEDAKRAVEAGVDGIvvsnhggRQ-------------LDGAPATIDALPEIVAAVGG- 272
                          90       100       110
                  ....*....|....*....|....*....|
1NFB_B        358 GVPVIADGGIQNVGHIAKALALGASTVMMG 387
Cdd:pfam01070 273 RIPVLVDGGIRRGTDVLKALALGADAVLLG 302
COG3448 COG3448
CBS-domain-containing membrane protein [Signal transduction mechanisms];
176-229 2.89e-06

CBS-domain-containing membrane protein [Signal transduction mechanisms];


Pssm-ID: 442671 [Multi-domain]  Cd Length: 136  Bit Score: 46.78  E-value: 2.89e-06
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
1NFB_B      176 EEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKK 229
Cdd:COG3448   5 RDIMTR--DVVTVSPDTTLREALELMREHGIRGLPVVDEDGRLVGIVTERDLLR 56
CBS_pair_bac cd04629
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; ...
115-227 3.19e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341392 [Multi-domain]  Cd Length: 116  Bit Score: 46.28  E-value: 3.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISsrdidflkeeEHDCF---------------LEEIM 179
Cdd:cd04629   2 TRNPVTLTPDTSILEAVELLLEHKISGAPVVDEQG---RLVGFLS----------EQDCLkalleasyhcepggtVADYM 68
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
1NFB_B      180 TKreDLVVAPAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd04629  69 ST--EVLTVSPDTSIVDLAQLFLKNKPRRYPVV-EDGKLVGQISRRDV 113
CBS_pair_DHH_polyA_Pol_assoc cd17772
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
116-227 3.86e-06

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341408 [Multi-domain]  Cd Length: 112  Bit Score: 45.64  E-value: 3.86e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDR-VRDVFEAKARHGFCGIPITDTGrmGSRLVGIISSRDIDflKEEEHDcfLE-----EIMTkREDLVVAP 189
Cdd:cd17772   1 SSPVISVEPDTtIAEAAELMTRYNINALPVVDGG--TGRLVGIITRQVAE--KAIYHG--LGdlpvsEYMT-TEFATVTP 73
                        90       100       110
                ....*....|....*....|....*....|....*...
1NFB_B      190 AGiTLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:cd17772  74 DA-PLSEIQEIIVEQRQRLVPVV-EDGRLVGVITRTDL 109
COG2524 COG2524
Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];
148-241 7.28e-06

Predicted transcriptional regulator, contains C-terminal CBS domains [Transcription];


Pssm-ID: 442013 [Multi-domain]  Cd Length: 206  Bit Score: 46.80  E-value: 7.28e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      148 GRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDL 227
Cdd:COG2524  61 LLLLIVLQAAAVRVVAEKELGLVLKMKVKDIMTK--DVITVSPDTTLEEALELMLEKGISGLPVV-DDGKLVGIITERDL 137
                        90
                ....*....|....
1NFB_B      228 KKNRDYPLASKDAK 241
Cdd:COG2524 138 LKALAEGRDLLDAP 151
NanE cd04729
N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to ...
261-388 8.49e-06

N-acetylmannosamine-6-phosphate epimerase (NanE) converts N-acetylmannosamine-6-phosphate to N-acetylglucosamine-6-phosphate. This reaction is part of the pathway that allows the usage of sialic acid as a carbohydrate source. Sialic acids are a family of related sugars that are found as a component of glycoproteins, gangliosides, and other sialoglycoconjugates.


Pssm-ID: 240080 [Multi-domain]  Cd Length: 219  Bit Score: 46.80  E-value: 8.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      261 DLLAQAGVDVVVLDSSQ-----GNSIFQinMIKYIKDKYPnlQVIGGNVVTAAQAKNLIDAGVDalrvgmgsgsiCI--T 333
Cdd:cd04729  86 DALAAAGADIIALDATDrprpdGETLAE--LIKRIHEEYN--CLLMADISTLEEALNAAKLGFD-----------IIgtT 150
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
1NFB_B      334 qevlACGRPQATAVYK------VSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGS 388
Cdd:cd04729 151 ----LSGYTEETAKTEdpdfelLKELRKALGIPVIAEGRINSPEQAAKALELGADAVVVGS 207
MDH_FMN cd04736
Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of ...
261-410 1.36e-05

Mandelate dehydrogenase (MDH)-like FMN-binding domain. MDH is part of a widespread family of homologous FMN-dependent a-hydroxy acid oxidizing enzymes that oxidizes (S)-mandelate to phenylglyoxalate. MDH is an enzyme in the mandelate pathway that occurs in several strains of Pseudomonas which converts (R)-mandelate to benzoate. 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: 240087  Cd Length: 361  Bit Score: 47.13  E-value: 1.36e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      261 DLLAQAGVDVVVLDSSqgnsiFQINMIKYIKDKYPNLQVIGGnVVTAAQAKNLIDAGVDALRVGMGSGsicitqEVLACG 340
Cdd:cd04736 207 DVEVQAALMSRQMDAS-----FNWQDLRWLRDLWPHKLLVKG-IVTAEDAKRCIELGADGVILSNHGG------RQLDDA 274
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      341 RPQATAVykvSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKK 410
Cdd:cd04736 275 IAPIEAL---AEIVAATYKPVLIDSGIRRGSDIVKALALGANAVLLGRATLYGLAARGEAGVSEVLRLLK 341
CBS smart00116
Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of ...
117-164 1.80e-05

Domain in cystathionine beta-synthase and other proteins; Domain present in all 3 forms of cellular life. Present in two copies in inosine monophosphate dehydrogenase, of which one is disordered in the crystal structure. A number of disease states are associated with CBS-containing proteins including homocystinuria, Becker's and Thomsen disease.


Pssm-ID: 214522 [Multi-domain]  Cd Length: 49  Bit Score: 42.11  E-value: 1.80e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
1NFB_B         117 DPVVLSPKDRVRDVFEAKARHGFCGIPITDTgrmGSRLVGIISSRDID 164
Cdd:smart00116   1 DVVTVSPDTTLEEALELLRENGIRRLPVVDE---EGRLVGIVTRRDII 45
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
115-227 2.47e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 43.56  E-value: 2.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTgrmGSRLVGIISSRDIDF---LKEEEHDCFLEEIMTKreDLVVAPAG 191
Cdd:cd17784   1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDD---EGKLIGIVTATDLGHnliLDKYELGTTVEEVMVK--DVATVHPD 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1NFB_B      192 ITLKEANEILQRSKKG-----KLPIVnEDDELVAIIARTDL 227
Cdd:cd17784  76 ETLLEAIKKMDSNAPDeeiinQLPVV-DDGKLVGIISDGDI 115
LOX_like_FMN cd04737
L-Lactate oxidase (LOX) FMN-binding domain. LOX is a member of the family of FMN-containing ...
287-387 2.69e-05

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: 46.28  E-value: 2.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      287 IKYIKdKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVG--------MGSGSICITQEVlacgrpqATAVYKvseyarrfG 358
Cdd:cd04737 213 IEFIA-KISGLPVIVKGIQSPEDADVAINAGADGIWVSnhggrqldGGPASFDSLPEI-------AEAVNH--------R 276
                        90       100
                ....*....|....*....|....*....
1NFB_B      359 VPVIADGGIQNVGHIAKALALGASTVMMG 387
Cdd:cd04737 277 VPIIFDSGVRRGEHVFKALASGADAVAVG 305
NMO pfam03060
Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane ...
304-397 2.78e-05

Nitronate monooxygenase; Nitronate monooxygenase (NMO), formerly referred to as 2-nitropropane dioxygenase (NPD) (EC:1.13.11.32), is an FMN-dependent enzyme that uses molecular oxygen to oxidize (anionic) alkyl nitronates and, in the case of the enzyme from Neurospora crassa, (neutral) nitroalkanes to the corresponding carbonyl compounds and nitrite. Previously classified as 2-nitropropane dioxygenase, but it is now recognized that this was the result of the slow ionization of nitroalkanes to their nitronate (anionic) forms. The enzymes from the fungus Neurospora crassa and the yeast Williopsis saturnus var. mrakii (formerly classified as Hansenula mrakii) contain non-covalently bound FMN as the cofactor. Active towards linear alkyl nitronates of lengths between 2 and 6 carbon atoms and, with lower activity, towards propyl-2-nitronate. The enzyme from N. crassa can also utilize neutral nitroalkanes, but with lower activity. One atom of oxygen is incorporated into the carbonyl group of the aldehyde product. The reaction appears to involve the formation of an enzyme-bound nitronate radical and an a-peroxynitroethane species, which then decomposes, either in the active site of the enzyme or after release, to acetaldehyde and nitrite.


Pssm-ID: 367316 [Multi-domain]  Cd Length: 331  Bit Score: 46.35  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        304 VVTAAQAKNLIDAGVDALRV-GMGSGSICITQEVLACG--RPQATAVYKVSeyarrfgVPVIADGGIQNVGHIAKALALG 380
Cdd:pfam03060 143 ISSAKEARIAEARGADALIVqGPEAGGHQGTPEYGDKGlfRLVPQVPDAVD-------IPVIAAGGIWDRRGVAAALALG 215
                          90
                  ....*....|....*..
1NFB_B        381 ASTVMMGSLLAATTEAP 397
Cdd:pfam03060 216 ASGVQMGTRFLLTKESG 232
IDI-2_FMN cd02811
Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. ...
302-399 4.63e-05

Isopentenyl-diphosphate:dimethylallyl diphosphate isomerase type 2 (IDI-2) FMN-binding domain. Two types of IDIs have been characterized at present. The long known IDI-1 is only dependent on divalent metals for activity, whereas IDI-2 requires a metal, FMN and NADPH. IDI-2 catalyzes the interconversion of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP) in the mevalonate pathway.


Pssm-ID: 239205 [Multi-domain]  Cd Length: 326  Bit Score: 45.57  E-value: 4.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      302 GNVVTAAQAKNLIDAGVDALRVGmGSG---------------SICITQEVLACGRPQATAVYKVSEYARrfGVPVIADGG 366
Cdd:cd02811 187 GFGISRETAKRLADAGVKAIDVA-GAGgtswarvenyrakdsDQRLAEYFADWGIPTAASLLEVRSALP--DLPLIASGG 263
                        90       100       110
                ....*....|....*....|....*....|....
1NFB_B      367 IQNVGHIAKALALGASTV-MMGSLLAATTEAPGE 399
Cdd:cd02811 264 IRNGLDIAKALALGADLVgMAGPFLKAALEGEEA 297
CBS_pair_bact_arch cd17775
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria ...
155-227 5.28e-05

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in bacteria and archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341411 [Multi-domain]  Cd Length: 117  Bit Score: 42.53  E-value: 5.28e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1NFB_B      155 VGIISSRDI--DFLKEEE--HDCFLEEIMTkrEDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd17775  39 VGIVTDRDIvvEVVAKGLdpKDVTVGDIMS--ADLITAREDDGLFEALERMREKGVRRLPVVDDDGELVGIVTLDDI 113
CBS_pair_AcuB_like cd04584
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
174-239 1.15e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ACT domain; The putative Acetoin Utilization Protein (Acub) from Vibrio Cholerae contains a CBS pair domain. The acetoin utilization protein plays a role in growth and sporulation on acetoin or butanediol for use as a carbon source. Acetoin is an important physiological metabolite excreted by many microorganisms. It is used as an external energy store by a number of fermentive bacteria. Acetoin is produced by the decarboxylation of alpha-acetolactate. Once superior carbon sources are exhausted, and the culture enters stationary phase, acetoin can be utilised in order to maintain the culture density. The conversion of acetoin into acetyl-CoA or 2,3-butanediol is catalysed by the acetoin dehydrogenase complex and acetoin reductase/2,3-butanediol dehydrogenase, respectively. Acetoin utilization proteins, acetylpolyamine amidohydrolases, and histone deacetylases are members of an ancient protein superfamily.This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the acetoin utilization proteins in bacteria. Acetoin is a product of fermentative metabolism in many prokaryotic and eukaryotic microorganisms. They produce acetoin as an external carbon storage compound and then later reuse it as a carbon and energy source during their stationary phase and sporulation. In addition these CBS domains are associated with a downstream ACT (aspartate kinase/chorismate mutase/TyrA) domain, which is linked to a wide range of metabolic enzymes that are regulated by amino acid concentration. Pairs of ACT domains bind specifically to a particular amino acid leading to regulation of the linked enzyme. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341361 [Multi-domain]  Cd Length: 130  Bit Score: 42.02  E-value: 1.15e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
1NFB_B      174 FLEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDLKKNRDYPLASKD 239
Cdd:cd04584   1 LVKDIMTK--NVVTVTPDTSLAEARELMKEHKIRHLPVV-DDGKLVGIVTDRDLLRASPSKATSLS 63
CBS_pair_inorgPPase cd04597
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with ...
115-227 2.32e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with family II inorganic pyrophosphatase; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with a subgroup of family II inorganic pyrophosphatases (PPases) that also contain a DRTGG domain. The homolog from Clostridium has been shown to be inhibited by AMP and activated by a novel effector, diadenosine 5',5-P1,P4-tetraphosphate (AP(4)A), which has been shown to bind to the CBS domain. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here.


Pssm-ID: 341372 [Multi-domain]  Cd Length: 106  Bit Score: 40.41  E-value: 2.32e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      115 ITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGrmgSRLVGIISSRDIDFLkeeehdcfLEEIMTKrEDLVVAPAGITL 194
Cdd:cd04597   4 YDKVEPLSPETSIKDAWNLMDENNLKTLPVTDDN---GKLIGLLSISDIART--------VDYIMTK-DNLIVFKEDDYL 71
                        90       100       110
                ....*....|....*....|....*....|...
1NFB_B      195 KEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd04597  72 DEVKEIMLNTNFRNYPVVDENNKFLGTISRKHL 104
PRK01130 PRK01130
putative N-acetylmannosamine-6-phosphate 2-epimerase;
261-388 3.07e-04

putative N-acetylmannosamine-6-phosphate 2-epimerase;


Pssm-ID: 234907  Cd Length: 221  Bit Score: 42.06  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B       261 DLLAQAGVDVVVLDSS-----QGNSIFQInmIKYIKDKyPNlQVIGGNVVTAAQAKNLIDAGVD----ALRvGMGSGSIC 331
Cdd:PRK01130  82 DALAAAGADIIALDATlrprpDGETLAEL--VKRIKEY-PG-QLLMADCSTLEEGLAAQKLGFDfigtTLS-GYTEETKK 156
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
1NFB_B       332 ITQEVLACgrpqatavykVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGS 388
Cdd:PRK01130 157 PEEPDFAL----------LKELLKAVGCPVIAEGRINTPEQAKKALELGAHAVVVGG 203
COG2905 COG2905
Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains ...
175-227 3.14e-04

Signal-transduction protein containing cAMP-binding, CBS, and nucleotidyltransferase domains [Signal transduction mechanisms];


Pssm-ID: 442149 [Multi-domain]  Cd Length: 124  Bit Score: 40.58  E-value: 3.14e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
1NFB_B      175 LEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:COG2905   1 VKDIMSR--DVVTVSPDATVREAARLMTEKGVGSLVVVDDDGRLVGIITDRDL 51
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd04587
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
116-227 3.17e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT (Nucleotidyltransferase) Pol-beta-like domain, and the DUF294 dom; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341363 [Multi-domain]  Cd Length: 114  Bit Score: 40.49  E-value: 3.17e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsrLVGIISSRDI---------DFlkeeehDCFLEEIMTkrEDLV 186
Cdd:cd04587   4 RPPVTVPPDATIQEAAQLMSEERVSSLLVVDDGR----LVGIVTDRDLrnrvvaeglDP------DTPVSEIMT--PPPV 71
                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
1NFB_B      187 VAPAGITLKEAneILQRSKKG--KLPIVnEDDELVAIIARTDL 227
Cdd:cd04587  72 TIDADALVFEA--LLLMLERNihHLPVV-DDGRVVGVVTATDL 111
CBS_pair_arch cd17776
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; ...
116-231 3.23e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in archaea; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341412 [Multi-domain]  Cd Length: 115  Bit Score: 40.47  E-value: 3.23e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      116 TDPVVLSPKD-RVRDVFEAKARHGFCGIPITDTGRMgsrlVGIISSRDIDFLKEEEHDCFLE----EIMTKreDLVVAPA 190
Cdd:cd17776   2 TTDVVTVDADaSLEDAAERMLRNRVGSVVVTDDGTP----AGILTETDALHAGYATDDPFSEipvrAVASR--PLVTISP 75
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
1NFB_B      191 GITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDLKKNR 231
Cdd:cd17776  76 TATLREAAERMVDEGVKKLPVV-DGLDLVGILTATDIIRAY 115
CBS_pair_SF cd02205
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS ...
182-229 3.24e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains superfamily; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341358 [Multi-domain]  Cd Length: 113  Bit Score: 40.31  E-value: 3.24e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
1NFB_B      182 REDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKK 229
Cdd:cd02205   1 TRDVVTVDPDTTVREALELMAENGIGALPVVDDDGKLVGIVTERDILR 48
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
136-229 3.66e-04

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 40.30  E-value: 3.66e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      136 RHGFCGIPITDTGrmgSRLVGIISSRDIDFLKEEEHDCfLEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNED 215
Cdd:cd04605  28 DKNVTHLPVVSED---GKLIGIVTSWDISKAVALKKDS-LEEIMTR--NVITARPDEPIELAARKMEKHNISALPVVDDD 101
                        90
                ....*....|....
1NFB_B      216 DELVAIIARTDLKK 229
Cdd:cd04605 102 RRVIGIITSDDISR 115
CBS pfam00571
CBS domain; CBS domains are small intracellular modules that pair together to form a stable ...
116-163 7.33e-04

CBS domain; CBS domains are small intracellular modules that pair together to form a stable globular domain. This family represents a single CBS domain. Pairs of these domains have been termed a Bateman domain. CBS domains have been shown to bind ligands with an adenosyl group such as AMP, ATP and S-AdoMet. CBS domains are found attached to a wide range of other protein domains suggesting that CBS domains may play a regulatory role making proteins sensitive to adenosyl carrying ligands. The region containing the CBS domains in Cystathionine-beta synthase is involved in regulation by S-AdoMet. CBS domain pairs from AMPK bind AMP or ATP. The CBS domains from IMPDH and the chloride channel CLC2 bind ATP.


Pssm-ID: 425756 [Multi-domain]  Cd Length: 57  Bit Score: 37.58  E-value: 7.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
1NFB_B        116 TDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRmgsRLVGIISSRDI 163
Cdd:pfam00571   7 KDVVTVSPDTTLEEALELMREHGISRLPVVDEDG---KLVGIVTLKDL 51
KDPG_aldolase cd00452
KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases ...
261-385 9.88e-04

KDPG and KHG aldolase; KDPG and KHG aldolase. This family belongs to the class I adolases whose reaction mechanism involves Schiff base formation between a substrate carbonyl and lysine residue in the active site. 2-keto-3-deoxy-6-phosphogluconate (KDPG) aldolase, is best known for its role in the Entner-Doudoroff pathway of bacteria, where it catalyzes the reversible cleavage of KDPG to pyruvate and glyceraldehyde-3-phosphate. 2-keto-4-hydroxyglutarate (KHG) aldolase, which has enzymatic specificity toward glyoxylate, forming KHG in the presence of pyruvate, and is capable of regulating glyoxylate levels in the glyoxylate bypass, an alternate pathway when bacteria are grown on acetate carbon sources.


Pssm-ID: 188632  Cd Length: 190  Bit Score: 40.19  E-value: 9.88e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      261 DLLAQAGVDV--VVLDSSQGnsifqINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALrVgmgsgSICITQEVLa 338
Cdd:cd00452  23 EALIEGGIRAieITLRTPGA-----LEAIRALRKEFPEALIGAGTVLTPEQADAAIAAGAQFI-V-----SPGLDPEVV- 90
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
1NFB_B      339 cgrpqatavykvsEYARRFGVPVIAdgGIQNVGHIAKALALGASTVM 385
Cdd:cd00452  91 -------------KAANRAGIPLLP--GVATPTEIMQALELGADIVK 122
CBS_pair_DHH_polyA_Pol_assoc cd04595
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
189-229 1.20e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the DHH and nucleotidyltransferase (NT) domains; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with an upstream DHH domain which performs a phosphoesterase function and a downstream nucleotidyltransferase (NT) domain of family X DNA polymerases. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341370 [Multi-domain]  Cd Length: 110  Bit Score: 38.63  E-value: 1.20e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
1NFB_B      189 PAGITLKEANEILQRSKKGKLPIVnEDDELVAIIARTDLKK 229
Cdd:cd04595   8 SPDTTIEEARKIMLRYGHTGLPVV-EDGKLVGIISRRDVDK 47
CBS_pair_arch_MET2_assoc cd04605
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
174-229 1.80e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the MET2 domain. Met2 is a key enzyme in the biosynthesis of methionine. It encodes a homoserine transacetylase involved in converting homoserine to O-acetyl homoserine. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341379 [Multi-domain]  Cd Length: 116  Bit Score: 38.37  E-value: 1.80e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
1NFB_B      174 FLEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKK 229
Cdd:cd04605   1 LVEDIMSK--DVATIREDISIEEAAKIMIDKNVTHLPVVSEDGKLIGIVTSWDISK 54
CBS_pair_CorC_HlyC_assoc cd04590
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which ...
176-227 2.13e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains the majority of which are associated with the CorC_HlyC domain. CorC_HlyC is a transporter associated domain. This small domain is found in Na+/H+ antiporters, in proteins involved in magnesium and cobalt efflux, and in association with some proteins of unknown function. The function of the CorC_HlyC domain is uncertain but it might be involved in modulating transport of ion substrates. These CBS domains are found in highly conserved proteins that either have unknown function or are puported to be hemolysins, exotoxins involved in lysis of red blood cells in vitro. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341366 [Multi-domain]  Cd Length: 119  Bit Score: 38.25  E-value: 2.13e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
1NFB_B      176 EEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNED-DELVAIIARTDL 227
Cdd:cd04590   3 REVMTPRTDVVALDADATLEELLELILESGYSRFPVYEGDlDNIIGVLHVKDL 55
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
265-390 2.36e-03

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 39.77  E-value: 2.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        265 QAGVDVVVLDSSqgnSIFQINMIKYIKDKYPNLQVI-------------GGNVVTAAQ----AKNLIDAGV------DAL 321
Cdd:pfam00977  93 SAGADRVIIGTA---AVKNPELIKEAAEKFGSQCIVvaidarrgkvainGWREDTGIDavewAKELEELGAgeilltDID 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        322 RVGMGSGS-ICITQEVlacgrpqatavykvseyARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLL 390
Cdd:pfam00977 170 RDGTLSGPdLELTREL-----------------AEAVNIPVIASGGVGSLEDLKELFTEGVDGVIAGSAL 222
CBS_pair_HPP_assoc cd04600
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the ...
179-234 2.83e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the HPP motif domain. These proteins are integral membrane proteins with four transmembrane spanning helices. The function of these proteins is uncertain, but they are thought to be transporters. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341375 [Multi-domain]  Cd Length: 133  Bit Score: 37.93  E-value: 2.83e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
1NFB_B      179 MTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYP 234
Cdd:cd04600   1 MSR--DVVTVTPDTSLEEAWRLLRRHRIKALPVVDRARRLVGIVTLADLLKHADLD 54
GltS_FMN cd02808
Glutamate synthase (GltS) FMN-binding domain. GltS is a complex iron-sulfur flavoprotein that ...
340-387 3.17e-03

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: 39.83  E-value: 3.17e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|..
1NFB_B      340 GRPQATAVYKVSEYARRFG----VPVIADGGIQNVGHIAKALALGASTVMMG 387
Cdd:cd02808 263 GLPTELGLARAHQALVKNGlrdrVSLIASGGLRTGADVAKALALGADAVGIG 314
CBS_pair_CAP-ED_NT_Pol-beta-like_DUF294_assoc cd17771
CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase ...
117-163 3.39e-03

CBS domain protein; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains associated with the bacterial CAP_ED (cAMP receptor protein effector domain) family of transcription factors, the NT_Pol-beta-like domain, and the DUF294 domain. Members of CAP_ED, include CAP which binds cAMP, FNR (fumarate and nitrate reductase) which uses an iron-sulfur cluster to sense oxygen, and CooA a heme containing CO sensor. In all cases binding of the effector leads to conformational changes and the ability to activate transcription. The NT_Pol-beta-like domain includes the Nucleotidyltransferase (NT) domains of DNA polymerase beta and other family X DNA polymerases, as well as the NT domains of class I and class II CCA-adding enzymes, RelA- and SpoT-like ppGpp synthetases and hydrolases, 2'5'-oligoadenylate (2-5A)synthetases, Escherichia coli adenylyltransferase (GlnE), Escherichia coli uridylyl transferase (GlnD), poly (A) polymerases, terminal uridylyl transferases, Staphylococcus aureus kanamycin nucleotidyltransferase, and similar proteins. DUF294 is a putative nucleotidyltransferase with a conserved DxD motif. CBS is a small domain originally identified in cystathionine beta-synthase and subsequently found in a wide range of different proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341407 [Multi-domain]  Cd Length: 115  Bit Score: 37.30  E-value: 3.39e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
1NFB_B      117 DPVVLSPKDRVRDVFEAKARHGFCGIPITDTGrmgsRLVGIISSRDI 163
Cdd:cd17771  70 DPVRLPPSASAFEAALLMAEHGFRHVCVVDNG----RLVGVVSERDL 112
CBS_pair_ABC_OpuCA_assoc cd04583
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with ...
153-227 3.61e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found associated with the ABC transporter OpuCA; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domains found in association with the ABC transporter OpuCA. OpuCA is the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment but the function of the CBS domains in OpuCA remains unknown. In the related ABC transporter, OpuA, the tandem CBS domains have been shown to function as sensors for ionic strength, whereby they control the transport activity through an electronic switching mechanism. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. They are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341360 [Multi-domain]  Cd Length: 110  Bit Score: 37.11  E-value: 3.61e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
1NFB_B      153 RLVGIISSRDIDFLKEEEHDcfLEEIMTKreDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDL 227
Cdd:cd04583  36 VLLGIVDIEDINRNYRKAKK--VGEIMER--DVFTVKEDSLLRDTVDRILKRGLKYVPVVDEQGRLVGLVTRASL 106
His_biosynth pfam00977
Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine ...
298-388 3.65e-03

Histidine biosynthesis protein; Proteins involved in steps 4 and 6 of the histidine biosynthesis pathway are contained in this family. Histidine is formed by several complex and distinct biochemical reactions catalyzed by eight enzymes. The enzymes in this Pfam entry are called His6 and His7 in eukaryotes and HisA and HisF in prokaryotes. The structure of HisA is known to be a TIM barrel fold. In some archaeal HisA proteins the TIM barrel is composed of two tandem repeats of a half barrel. This family belong to the common phosphate binding site TIM barrel family.


Pssm-ID: 425971  Cd Length: 228  Bit Score: 39.00  E-value: 3.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B        298 QVIGGNVVtaAQAKNLIDAGVDALRVGMGSGSICitqevlacGRPQATAVykVSEYARRFGVPVIADGGIQNVGHIAKAL 377
Cdd:pfam00977  25 TVYAGDPV--ELAKRYEEEGADELHFVDLDAAKE--------GRPVNLDV--VEEIAEEVFIPVQVGGGIRSLEDVERLL 92
                          90
                  ....*....|.
1NFB_B        378 ALGASTVMMGS 388
Cdd:pfam00977  93 SAGADRVIIGT 103
CBS_pair_Mg_transporter cd04606
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium ...
142-222 4.44e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains in the magnesium transporter, MgtE; This cd contains two tandem repeats of the cystathionine beta-synthase (CBS pair) domain in the magnesium transporter, MgtE. MgtE and its homologs are found in eubacteria, archaebacteria, and eukaryota. Members of this family transport Mg2+ or other divalent cations into the cell via two highly conserved aspartates. The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341380 [Multi-domain]  Cd Length: 121  Bit Score: 37.31  E-value: 4.44e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      142 IPITDTGRmgsRLVGIISSRDIDFLKEEEHdcfLEEIMTkrEDLVVAPAGITLKEANEILQR----SkkgkLPIVNEDDE 217
Cdd:cd04606  40 IYVVDEDR---RLLGVVSLRDLLLADPDTK---VSDIMD--TDVISVSADDDQEEVARLFAKydllA----LPVVDEEGR 107

                ....*
1NFB_B      218 LVAII 222
Cdd:cd04606 108 LVGII 112
CBS_pair_Euryarchaeota cd17784
Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in ...
182-230 4.80e-03

Two tandem repeats of the cystathionine beta-synthase (CBS pair) domains present in Euryarchaeota; The CBS domain, named after human CBS, is a small domain originally identified in cystathionine beta-synthase and is subsequently found in a wide range of different proteins. CBS domains usually occur in tandem repeats. They associate to form a so-called Bateman domain or a CBS pair based on crystallographic studies in bacteria. The CBS pair was used as a basis for this cd hierarchy since the human CBS proteins can adopt the typical core structure and form an intramolecular CBS pair. The interface between the two CBS domains forms a cleft that is a potential ligand binding site. The CBS pair coexists with a variety of other functional domains and this has been used to help in its classification here. It has been proposed that the CBS domain may play a regulatory role, although its exact function is unknown. Mutations of conserved residues within this domain are associated with a variety of human hereditary diseases, including congenital myotonia, idiopathic generalized epilepsy, hypercalciuric nephrolithiasis, and classic Bartter syndrome (CLC chloride channel family members), Wolff-Parkinson-White syndrome (gamma 2 subunit of AMP-activated protein kinase), retinitis pigmentosa (IMP dehydrogenase-1), and homocystinuria (cystathionine beta-synthase).


Pssm-ID: 341420 [Multi-domain]  Cd Length: 120  Bit Score: 37.02  E-value: 4.80e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
1NFB_B      182 REDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKN 230
Cdd:cd17784   1 TKNVITAKPNEGVVEAFEKMLKHKISALPVVDDEGKLIGIVTATDLGHN 49
OYE_like_FMN_family cd02803
Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme ...
310-391 9.75e-03

Old yellow enzyme (OYE)-like FMN binding domain. OYE was the first flavin-dependent enzyme identified, however its true physiological role remains elusive to this day. Each monomer of OYE contains FMN as a non-covalently bound cofactor, uses NADPH as a reducing agent with oxygens, quinones, and alpha,beta-unsaturated aldehydes and ketones, and can act as electron acceptors in the catalytic reaction. Members of OYE family include trimethylamine dehydrogenase, 2,4-dienoyl-CoA reductase, enoate reductase, pentaerythriol tetranitrate reductase, xenobiotic reductase, and morphinone reductase.


Pssm-ID: 239201 [Multi-domain]  Cd Length: 327  Bit Score: 38.32  E-value: 9.75e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1NFB_B      310 AKNLIDAGVDALRVgmgSGSICITQEVLACGR--PQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALG-ASTVMM 386
Cdd:cd02803 234 AKALEEAGVDALHV---SGGSYESPPPIIPPPyvPEGYFLELAEKIKKAVKIPVIAVGGIRDPEVAEEILAEGkADLVAL 310

                ....*.
1NFB_B      387 G-SLLA 391
Cdd:cd02803 311 GrALLA 316
 
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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