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Conserved domains on  [gi|496695763|ref|WP_009337306|]
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MULTISPECIES: Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Afipia]

Protein Classification

NAD(P) transhydrogenase subunit alpha( domain architecture ID 10143114)

NAD(P) transhydrogenase subunit alpha is part of the enzyme complex that catalyzes the transhydrogenation between NADH and NADP which is coupled to respiration and ATP hydrolysis and functions as a proton pump across the membrane

CATH:  3.40.50.720
EC:  7.1.1.1
Gene Ontology:  GO:0070403|GO:0016491
PubMed:  17323922

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-364 0e+00

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


:

Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 577.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVV--SADAVKDADIVIKVKRPTAAE 78
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIvsDAEELAQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  79 AASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTA 158
Cdd:cd05304   81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAK 238
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEE--DAEGAGGYAKELSEEFLAK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 239 QAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADVNGVKIIGYTNLAGK 318
Cdd:cd05304  239 QRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPSR 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 496695763 319 VPASASGLYARNLQAFIETMFDKEtKSLAVKWDDELVKATALTKDG 364
Cdd:cd05304  319 LPTQASQLYAKNLLNFLELLVKDD-GELTLDLEDEIVRGTLVTHDG 363
 
Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-364 0e+00

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 577.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVV--SADAVKDADIVIKVKRPTAAE 78
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIvsDAEELAQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  79 AASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTA 158
Cdd:cd05304   81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAK 238
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEE--DAEGAGGYAKELSEEFLAK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 239 QAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADVNGVKIIGYTNLAGK 318
Cdd:cd05304  239 QRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPSR 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 496695763 319 VPASASGLYARNLQAFIETMFDKEtKSLAVKWDDELVKATALTKDG 364
Cdd:cd05304  319 LPTQASQLYAKNLLNFLELLVKDD-GELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-365 1.88e-180

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 504.92  E-value: 1.88e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVVSADAVKDADIVIKVKRPTAAEAA 80
Cdd:COG3288    1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDAELLGADIVLKVRPPSAEELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  81 SYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTAAG 160
Cdd:COG3288   81 ALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 161 TVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEefknAQTAGGYAKEMSKEYQAKQA 240
Cdd:COG3288  161 TIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAID----ANGAGGYAKELSEEEKAKQA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 241 ALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADVNGVKIIGYTNLAGKVP 320
Cdd:COG3288  237 ELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSRLP 316

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 496695763 321 ASASGLYARNLQAFIETMFdkETKSLAVKWDDELVKATALTKDGA 365
Cdd:COG3288  317 AHASQLYAKNLLNFLELLV--KDGALALDLEDEIVAGTLLTHDGE 359
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-369 2.58e-146

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 423.86  E-value: 2.58e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGA-VVSADAVKDADIVIKVKRPTAAEA 79
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAeIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  80 ASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTAA 159
Cdd:PRK09424  81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 160 GTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAKQ 239
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEE--EGGSGDGYAKVMSEEFIKAE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 240 AALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADV-NGVKIIGYTNLAGK 318
Cdd:PRK09424 239 MALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTdNGVTIIGYTDLPSR 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496695763 319 VPASASGLYARNLQAFIETMFDKETKSLAVKWDDELVKATALTKDGAVIHP 369
Cdd:PRK09424 319 LPTQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWP 369
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 2-375 2.97e-108

NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of alpha 2 beta 2 tetramer that couples the proton transport across the membrane to the reversible transfer of hydride ion equivalents between NAD and NADP. An alternate name is pyridine nucleotide transhydrogenase alpha subunit. The N-terminal region is homologous to alanine dehydrogenase. In some species, such as Rhodospirillum rubrum, the alpha chain is replaced by two shorter chains, both with some homology to the full-length alpha chain modeled here. These score below the trusted cutoff. [Energy metabolism, Electron transport]


Pssm-ID: 273140 [Multi-domain]  Cd Length: 512  Bit Score: 327.01  E-value: 2.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763    2 KIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGA-VVSADAVKDADIVIKVKRPTAAEAA 80
Cdd:TIGR00561   1 LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAeIGEGAEIWQSDIIFKVNAPLDDEIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   81 SYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTAAG 160
Cdd:TIGR00561  81 LLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  161 TVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAKQA 240
Cdd:TIGR00561 161 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKE--EAGSGDGYAKVMSDAFIKAAM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  241 ALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADV-NGVKIIGYTNLAGKV 319
Cdd:TIGR00561 239 ELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTeNGVKVIGYTDFPGRL 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496695763  320 PASASGLYARNLQAFIETMFDKETKSLAVKWDDELVKATALTKDGAVIHP------NFQPKA 375
Cdd:TIGR00561 319 PTQSSQLYGTNLVNLLKLLCKEKDGNINIDFDDVVIRGVTVIRAGEETIPaapiqvSAQPKA 380
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 140-368 3.16e-80

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 244.71  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  140 AVIEGAEAFGRAFPMMMTAAGTVP---AAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVES-LGAKFLAVed 215
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  216 eefknaqtaggyakemskeyQAKQAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEG 295
Cdd:pfam01262  79 --------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVET 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496695763  296 AKADEIAD----VNGVKIIGYTNLAGKVPASASGLYARNLQAFIETMFDKETKslAVKWDDELVKATALTKDGAVIH 368
Cdd:pfam01262 139 SRPTTHGEpvyvVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLADKGLK--AALLEDEALRAGLNTHDGKITH 213
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 145-311 6.69e-57

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 182.71  E-value: 6.69e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   145 AEAFGRAFPMMMTAAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVES-LGAKFLAVEdeefknaqt 223
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTTLY--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   224 aggyakemskeyqaKQAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIAD 303
Cdd:smart01002  72 --------------SQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTTHDD 137

                          170
                   ....*....|..
gi 496695763   304 ----VNGVKIIG 311
Cdd:smart01002 138 ptyvVDGVVHYC 149
 
Name Accession Description Interval E-value
Rubrum_tdh cd05304
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ...
 1-364 0e+00

Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matrix side. DI contains 2 domains in Rossmann-like folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than a classical Rossmann domain.


Pssm-ID: 240629 [Multi-domain]  Cd Length: 363  Bit Score: 577.82  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVV--SADAVKDADIVIKVKRPTAAE 78
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIvsDAEELAQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  79 AASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTA 158
Cdd:cd05304   81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAK 238
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEE--DAEGAGGYAKELSEEFLAK 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 239 QAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADVNGVKIIGYTNLAGK 318
Cdd:cd05304  239 QRELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGETVVTNGVTIIGPTNLPSR 318

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 496695763 319 VPASASGLYARNLQAFIETMFDKEtKSLAVKWDDELVKATALTKDG 364
Cdd:cd05304  319 LPTQASQLYAKNLLNFLELLVKDD-GELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-365 1.88e-180

NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 504.92  E-value: 1.88e-180
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVVSADAVKDADIVIKVKRPTAAEAA 80
Cdd:COG3288    1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDAELLGADIVLKVRPPSAEELA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  81 SYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTAAG 160
Cdd:COG3288   81 ALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAAG 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 161 TVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEefknAQTAGGYAKEMSKEYQAKQA 240
Cdd:COG3288  161 TIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAID----ANGAGGYAKELSEEEKAKQA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 241 ALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADVNGVKIIGYTNLAGKVP 320
Cdd:COG3288  237 ELLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGETVTKNGVTIIGPTNLPSRLP 316

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 496695763 321 ASASGLYARNLQAFIETMFdkETKSLAVKWDDELVKATALTKDGA 365
Cdd:COG3288  317 AHASQLYAKNLLNFLELLV--KDGALALDLEDEIVAGTLLTHDGE 359
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-369 2.58e-146

Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 423.86  E-value: 2.58e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGA-VVSADAVKDADIVIKVKRPTAAEA 79
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAeIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  80 ASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTAA 159
Cdd:PRK09424  81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 160 GTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAKQ 239
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEE--EGGSGDGYAKVMSEEFIKAE 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 240 AALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADV-NGVKIIGYTNLAGK 318
Cdd:PRK09424 239 MALFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTdNGVTIIGYTDLPSR 318

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496695763 319 VPASASGLYARNLQAFIETMFDKETKSLAVKWDDELVKATALTKDGAVIHP 369
Cdd:PRK09424 319 LPTQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWP 369
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 2-375 2.97e-108

NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of alpha 2 beta 2 tetramer that couples the proton transport across the membrane to the reversible transfer of hydride ion equivalents between NAD and NADP. An alternate name is pyridine nucleotide transhydrogenase alpha subunit. The N-terminal region is homologous to alanine dehydrogenase. In some species, such as Rhodospirillum rubrum, the alpha chain is replaced by two shorter chains, both with some homology to the full-length alpha chain modeled here. These score below the trusted cutoff. [Energy metabolism, Electron transport]


Pssm-ID: 273140 [Multi-domain]  Cd Length: 512  Bit Score: 327.01  E-value: 2.97e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763    2 KIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGA-VVSADAVKDADIVIKVKRPTAAEAA 80
Cdd:TIGR00561   1 LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAeIGEGAEIWQSDIIFKVNAPLDDEIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   81 SYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTAAG 160
Cdd:TIGR00561  81 LLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  161 TVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfkNAQTAGGYAKEMSKEYQAKQA 240
Cdd:TIGR00561 161 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKE--EAGSGDGYAKVMSDAFIKAAM 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  241 ALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADV-NGVKIIGYTNLAGKV 319
Cdd:TIGR00561 239 ELFAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTeNGVKVIGYTDFPGRL 318

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496695763  320 PASASGLYARNLQAFIETMFDKETKSLAVKWDDELVKATALTKDGAVIHP------NFQPKA 375
Cdd:TIGR00561 319 PTQSSQLYGTNLVNLLKLLCKEKDGNINIDFDDVVIRGVTVIRAGEETIPaapiqvSAQPKA 380
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 140-368 3.16e-80

Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 426165 [Multi-domain]  Cd Length: 213  Bit Score: 244.71  E-value: 3.16e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  140 AVIEGAEAFGRAFPMMMTAAGTVP---AAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVES-LGAKFLAVed 215
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  216 eefknaqtaggyakemskeyQAKQAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEG 295
Cdd:pfam01262  79 --------------------LYSQAELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVET 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 496695763  296 AKADEIAD----VNGVKIIGYTNLAGKVPASASGLYARNLQAFIETMFDKETKslAVKWDDELVKATALTKDGAVIH 368
Cdd:pfam01262 139 SRPTTHGEpvyvVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLADKGLK--AALLEDEALRAGLNTHDGKITH 213
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 2-336 1.87e-74

Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such as the hexameric L-alanine dehydrogenase of Phormidium lapideum, contain 2 Rossmann fold-like domains linked by an alpha helical region. Related proteins include Saccharopine Dehydrogenase (SDH), bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme, N(5)-(carboxyethyl)ornithine synthase, and Rubrum transdehydrogenase. Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyrucate to L-alanine via reductive amination. Transhydrogenases found in bacterial and inner mitochondrial membranes link NAD(P)(H)-dependent redox reactions to proton translocation. The energy of the proton electrochemical gradient (delta-p), generated by the respiratory electron transport chain, is consumed by transhydrogenase in NAD(P)+ reduction. Transhydrogenase is likely involved in the regulation of the citric acid cycle. Rubrum transhydrogenase has 3 components, dI, dII, and dIII. dII spans the membrane while dI and dIII protrude on the cytoplasmic/matirx side. DI contains 2 domains with Rossmann folds, linked by a long alpha helix, and contains a NAD binding site. Two dI polypeptides (represented in this sub-family) spontaneously form a heterotrimer with one dIII in the absence of dII. In the heterotrimer, both dI chains may bind NAD, but only one is well-ordered. dIII also binds a well-ordered NADP, but in a different orientation than classical Rossmann domains.


Pssm-ID: 240621 [Multi-domain]  Cd Length: 317  Bit Score: 233.45  E-value: 1.87e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   2 KIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVV---SADAVKDADIVIKVKRPTAAE 78
Cdd:cd01620    1 TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIvpaASKEAYSADIIVKLKEPEFAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  79 AASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRItraqVMDVLSSQANLAGYRAVIEGAEAFGRAFPMMMTA 158
Cdd:cd01620   81 YDLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLEND----FRPRLAPNSNIAGYAGVQLGAYELARIQGGRMGG 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfknaqtaggyakEMSKEyqak 238
Cdd:cd01620  157 AGGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRYSQKE------------ELEKE---- 220

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 239 qaaltaehIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKAD----EIADVNGVKIIGYTN 314
Cdd:cd01620  221 --------LKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETSIPTtegvPTYEVDGVVIYGVDN 292

                        330       340
                 ....*....|....*....|..
gi 496695763 315 LAGKVPASASGLYARNLQAFIE 336
Cdd:cd01620  293 MPSLVPREASELLSKNLLPYLV 314
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 145-311 6.69e-57

Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214966 [Multi-domain]  Cd Length: 149  Bit Score: 182.71  E-value: 6.69e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   145 AEAFGRAFPMMMTAAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVES-LGAKFLAVEdeefknaqt 223
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTTLY--------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   224 aggyakemskeyqaKQAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIAD 303
Cdd:smart01002  72 --------------SQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTTHDD 137

                          170
                   ....*....|..
gi 496695763   304 ----VNGVKIIG 311
Cdd:smart01002 138 ptyvVDGVVHYC 149
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 3-336 1.36e-51

Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related dehydrogenases; The formate/glycerate dehydrogenase like family contains a diverse group of enzymes such as formate dehydrogenase (FDH), glycerate dehydrogenase (GDH), D-lactate dehydrogenase, L-alanine dehydrogenase, and S-Adenosylhomocysteine hydrolase, that share a common 2-domain structure. Despite often low sequence identity, these proteins typically have a characteristic arrangement of 2 similar domains of the alpha/beta Rossmann fold NAD+ binding form. The NAD(P) binding domain is inserted within the linear sequence of the mostly N-terminal catalytic domain. Structurally, these domains are connected by extended alpha helices and create a cleft in which NAD(P) is bound, primarily to the C-terminal portion of the 2nd (internal) domain. While many members of this family are dimeric, alanine DH is hexameric and phosphoglycerate DH is tetrameric. 2-hydroxyacid dehydrogenases are enzymes that catalyze the conversion of a wide variety of D-2-hydroxy acids to their corresponding keto acids. The general mechanism is (R)-lactate + acceptor to pyruvate + reduced acceptor. Formate dehydrogenase (FDH) catalyzes the NAD+-dependent oxidation of formate ion to carbon dioxide with the concomitant reduction of NAD+ to NADH. FDHs of this family contain no metal ions or prosthetic groups. Catalysis occurs though direct transfer of a hydride ion to NAD+ without the stages of acid-base catalysis typically found in related dehydrogenases.


Pssm-ID: 240631 [Multi-domain]  Cd Length: 310  Bit Score: 174.34  E-value: 1.36e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   3 IAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVVS--ADAVKDADIVIKVKRP-TAAEA 79
Cdd:cd12154    1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVtlAKALWSLDVVLKVKEPlTNAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  80 ASYKKGALAIAIMDPYNNDAAL--KSLADAGVSAFAMELMPRItraqvmdVLSSQANLAGYRAVIEGAEAFGRAFPMMMT 157
Cdd:cd12154   81 ALIQKLGDRLLFTYTIGADHRDltEALARAGLTAIAVEGVELP-------LLTSNSIGAGELSVQFIARFLEVQQPGRLG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 158 AAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFLAVEDEEfknaqtaggyakemskeyqa 237
Cdd:cd12154  154 GAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVEELEEA-------------------- 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 238 kqaaltaehIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKADEIADVNGVKIIGYTNL-- 315
Cdd:cd12154  214 ---------LAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEGHGVVHYGDVNMpg 284

                        330       340
                 ....*....|....*....|....
gi 496695763 316 ---AGKVPASASGLYARNLQAFIE 336
Cdd:cd12154  285 pgcAMGVPWDATLRLAANTLPALV 308
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-134 7.97e-49

Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the NAD-dependent reversible reductive amination of pyruvate into alanine.


Pssm-ID: 214967 [Multi-domain]  Cd Length: 133  Bit Score: 161.04  E-value: 7.97e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763     4 AIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVV--SADAVKDADIVIKVKRPTAAEAAS 81
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIvdTAEVWADADIILKVKEPSPEELAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 496695763    82 YKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRITRAQVMDVLSSQAN 134
Cdd:smart01003  81 LREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 1-324 1.47e-47

Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) catalyzes the NAD-dependent conversion of pyruvate to L-alanine via reductive amination. Like formate dehydrogenase and related enzymes, L-AlaDH is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. Ligand binding and active site residues are found in the cleft between the subdomains. L-AlaDH is typically hexameric and is critical in carbon and nitrogen metabolism in micro-organisms.


Pssm-ID: 240630 [Multi-domain]  Cd Length: 359  Bit Score: 164.89  E-value: 1.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGA--VVSADAV-KDADIVIKVKRPTAA 77
Cdd:cd05305    1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAeiVPTAEEVwAKADLIVKVKEPLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  78 EAASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMprITRAQVMDVLSSQANLAGYRAVIEGAEAFGRAFP---M 154
Cdd:cd05305   81 EYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETI--EDEDGSLPLLAPMSEIAGRLAVQIGAEYLEKPNGgrgV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 155 MMTAAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAkflavedeefKNAQTAggyakeMSKE 234
Cdd:cd05305  159 LLGGVPGVPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFG----------GRVTTL------YSNP 222

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 235 YqakqaaLTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKA----DEIADVNGVkiI 310
Cdd:cd05305  223 A------NLEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETSRPtthdNPTYVVHGV--I 294

                        330
                 ....*....|....*.
gi 496695763 311 GY--TNLAGKVPASAS 324
Cdd:cd05305  295 HYcvPNMPGAVPRTST 310
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 4-136 8.72e-43

Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine 2-oxoglutarate reductases.


Pssm-ID: 461595 [Multi-domain]  Cd Length: 135  Bit Score: 145.65  E-value: 8.72e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763    4 AIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGAVV---SADAVKDADIVIKVKRPTAAEAA 80
Cdd:pfam05222   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIvdtAAEVWAEADLILKVKEPQPEEYA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 496695763   81 SYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMPRiTRAQVMDVLSSQANLA 136
Cdd:pfam05222  81 LLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANIA 135
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 1-324 2.77e-42

Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and metabolism]; Alanine dehydrogenase (includes sporulation protein SpoVN) is part of the Pathway/BioSystem: Urea cycle


Pssm-ID: 440450 [Multi-domain]  Cd Length: 372  Bit Score: 151.32  E-value: 2.77e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKSLGIDVAIEPGAGIKSGLLDADYEAMGA--VVSADAV-KDADIVIKVKRPTAA 77
Cdd:COG0686    1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAeiVDTAEEVfAQADLIVKVKEPQPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  78 EAASYKKG-----ALAIAIMDPYnndaaLKSLADAGVSAFAMELmprITRAQ-VMDVLSSQANLAGYRAVIEGAEafgra 151
Cdd:COG0686   81 EYALLRPGqilftYLHLAADPEL-----TEALLEKGVTAIAYET---VEDPDgSLPLLAPMSEIAGRMAIQIGAE----- 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 152 fpMMMTAAGT----------VPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVeslgakflaveDEEF-KN 220
Cdd:COG0686  148 --YLEKPNGGrgvllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRL-----------DDIFgGR 214

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 221 AQTAggyakeMSkeyqakQAALTAEHIKKQDIIITTALIPGRPAPKLVTLEMVKSMKPGSVLVDLAVERGGNVEGAKA-- 298
Cdd:COG0686  215 VTTL------YS------NPANIEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETSRPtt 282

                        330       340       350
                 ....*....|....*....|....*....|
gi 496695763 299 --DEIADVNGVkiIGY--TNLAGKVPASAS 324
Cdd:COG0686  283 hdDPTYVVHGV--VHYcvANMPGAVPRTST 310
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 1-307 2.44e-11

N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) catalyzes the NADP-dependent conversion of N5-(L-1-carboxyethyl)-L-ornithine to L-ornithine + pyruvate. Ornithine plays a key role in the urea cycle, which in mammals is used in arginine biosynthesis, and is a precursor in polyamine synthesis. ceo_syn is related to the NAD-dependent L-alanine dehydrogenases. Like formate dehydrogenase and related enzymes, ceo_syn is comprised of 2 domains connected by a long alpha helical stretch, each resembling a Rossmann fold NAD-binding domain. The NAD-binding domain is inserted within the linear sequence of the more divergent catalytic domain. These ceo_syn proteins have a partially conserved NAD-binding motif and active site residues that are characteristic of related enzymes such as Saccharopine Dehydrogenase.


Pssm-ID: 240658 [Multi-domain]  Cd Length: 295  Bit Score: 63.79  E-value: 2.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763   1 MKIAIAKEQDAAEPRVAATPDTVKKFKsLGIDVAIEPGAGIKSGLLDADYEAMGA-VVS-ADAVKDADIVIKVKrPTAAE 78
Cdd:cd12181    1 KTGGFGISNKENEKRVPLLPADLERIP-LREQLYFEEGYGERLGISDEEYAALGAgIVSrEEILAKCDVICDPK-PGDAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763  79 AASYKKGALAIAIMDPYNNDAALKSLADAGVSAFAMELMpRITRAQVMDVLSSQANLAGYRAVIEGAEAFGRaFPMMMTa 158
Cdd:cd12181   79 YLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAWEDM-FEWSKIGRHVFYKNNELAGYAAVLHALQLYGI-TPYRQT- 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 159 agtvpaaKVFVMGVGvaglqaiATARrlGAVvsatdvrpatkeqveslgakflavedeefkNAQTAGGYAKEMskeYQAK 238
Cdd:cd12181  156 -------KVAVLGFG-------NTAR--GAI------------------------------RALKLGGADVTV---YTRR 186

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496695763 239 QAALTAEHIKKQDIIITTALI-PGRPAPkLVTLEMVKSMKPGSVLVDLAVERGGNVEGAK----ADEIADVNGV 307
Cdd:cd12181  187 TEALFKEELSEYDIIVNCILQdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGMGIEFAKpttfDDPIYKVDGI 259
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 155-225 3.76e-07

6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, and other MDR family members; This group contains enzymes of the zinc-dependent alcohol dehydrogenase family, including members (aka MDR) identified as 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase and N-benzyl-3-pyrrolidinol dehydrogenase. 6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase catalyzes the conversion of 6-Hydroxycyclohex-1-enecarbonyl-CoA and NAD+ to 6-Ketoxycyclohex-1-ene-1-carboxyl-CoA,NADH, and H+. This group displays the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176216 [Multi-domain]  Cd Length: 338  Bit Score: 51.48  E-value: 3.76e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 496695763 155 MMTAAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGA-KFLAVEDEEFKNAQTAG 225
Cdd:cd08254  157 VVRAGEVKPGETVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGAdEVLNSLDDSPKDKKAAG 228
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 146-228 1.15e-04

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


Pssm-ID: 176178 [Multi-domain]  Cd Length: 271  Bit Score: 43.46  E-value: 1.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 146 EAFGRAFPMMMTAAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGAKFL---AVEDEEFKNAQ 222
Cdd:cd05188  117 EPLATAYHALRRAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHVidyKEEDLEEELRL 196


                 ....*.
gi 496695763 223 TAGGYA 228
Cdd:cd05188  197 TGGGGA 202
LKR_SDH_like cd12189
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ...
 3-74 2.94e-04

bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases. Along with formate dehydrogenase and similar enzymes, SDH consists paired domains resembling Rossmann folds in which the NAD-binding domain is inserted within the linear sequence of the catalytic domain. In this bifunctional enzyme, the LKR domain is N-terminal of the SDH domain. These proteins have a close match to the active site motif of SDHs, and an NAD-binding site motif that is a partial match to that found in SDH and other FDH-related proteins.


Pssm-ID: 240665 [Multi-domain]  Cd Length: 433  Bit Score: 42.55  E-value: 2.94e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496695763   3 IAIAKEQDAA-EPRVAATPDTVKK-FKSLGIDVAIEPGAgiKSGLLDADYEAMGAVVSADaVKDADIVIKVKRP 74
Cdd:cd12189    2 IGIRREDKNIwERRAPLTPSHVRElVKKPGVKVLVQPSN--RRAFPDQEYEAAGAIIQED-LSDADLILGVKEP 72
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 159-208 3.69e-04

D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport and metabolism];


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 42.02  E-value: 3.69e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGA 208
Cdd:COG1064  158 AGVGPGDRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGA 207
CAD1 cd05283
Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the ...
 151-221 8.15e-04

Cinnamyl alcohol dehydrogenases (CAD); Cinnamyl alcohol dehydrogenases (CAD), members of the medium chain dehydrogenase/reductase family, reduce cinnamaldehydes to cinnamyl alcohols in the last step of monolignal metabolism in plant cells walls. CAD binds 2 zinc ions and is NADPH- dependent. CAD family members are also found in non-plant species, e.g. in yeast where they have an aldehyde reductase activity. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176186 [Multi-domain]  Cd Length: 337  Bit Score: 40.94  E-value: 8.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 496695763 151 AFPMM---------MTAAGTVPAAKVFVMGVGvaGL--QAIATARRLGAVVSATDVRPATKEQVESLGAK-FLAVEDEEF 218
Cdd:cd05283  148 AAPLLcagitvyspLKRNGVGPGKRVGVVGIG--GLghLAVKFAKALGAEVTAFSRSPSKKEDALKLGADeFIATKDPEA 225


                 ...
gi 496695763 219 KNA 221
Cdd:cd05283  226 MKK 228
SDH_like cd05199
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ...
 2-72 1.70e-03

Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related proteins, including bifunctional lysine ketoglutarate reductase/SDH enzymes and N(5)-(carboxyethyl)ornithine synthases. SDH catalyzes the final step in the reversible NAD-dependent oxidative deamination of saccharopine to alpha-ketoglutarate and lysine, in the alpha-aminoadipate pathway of L-lysine biosynthesis. SDH is structurally related to formate dehydrogenase and similar enzymes, having a 2-domain structure in which a Rossmann-fold NAD(P)-binding domain is inserted within the linear sequence of a catalytic domain of related structure. Bifunctional lysine ketoglutarate reductase/SDH protein is a pair of enzymes linked on a single polypeptide chain that catalyze the initial, consecutive steps of lysine degradation. These proteins are related to the 2-domain saccharopine dehydrogenases.


Pssm-ID: 240623 [Multi-domain]  Cd Length: 319  Bit Score: 39.91  E-value: 1.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 496695763   2 KIAIAKE-QDAAEPRVAATPDTVKKF--KSLGIDVAIEPGAgiKSGLLDADYEAMGAVVSADAVkDADIVIKVK 72
Cdd:cd05199    1 KIGIIREgKTPPDRRVPLTPEQCKELqaKYPGVEIFVQPSP--VRCFKDEEYRAAGIEVVEDLS-DCDILLGVK 71
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 148-208 1.72e-03

Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. This group has the characteristic catalytic and structural zinc sites of the zinc-dependent alcohol dehydrogenases. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. A GxGxxG motif after the first mononucleotide contact half allows the close contact of the coenzyme with the ADH backbone. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. NAD(H)-binding occurs in the cleft between the catalytic and coenzyme-binding domains at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. In human ADH catalysis, the zinc ion helps coordinate the alcohol, followed by deprotonation of a histidine, the ribose of NAD, a serine, then the alcohol, which allows the transfer of a hydride to NAD+, creating NADH and a zinc-bound aldehyde or ketone. In yeast and some bacteria, the active site zinc binds an aldehyde, polarizing it, and leading to the reverse reaction.


Pssm-ID: 176221 [Multi-domain]  Cd Length: 345  Bit Score: 39.89  E-value: 1.72e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496695763 148 FGRAFPMMMTAAGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGA 208
Cdd:cd08260  150 FATAFRALVHQARVKPGEWVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGA 210
PRK14193 PRK14193
bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate ...
 244-306 1.78e-03

bifunctional 5,10-methylene-tetrahydrofolate dehydrogenase/ 5,10-methylene-tetrahydrofolate cyclohydrolase; Provisional


Pssm-ID: 237637 [Multi-domain]  Cd Length: 284  Bit Score: 39.61  E-value: 1.78e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 496695763 244 AEHIKKQDIIITTALIPGrpapkLVTLEMVKsmkPGSVLVDLAVERGGN--VEGAKADEIADVNG 306
Cdd:PRK14193 198 AAHTRRADIIVAAAGVAH-----LVTADMVK---PGAAVLDVGVSRAGDgkLVGDVHPDVWEVAG 254
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 159-208 1.96e-03

Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and metabolism, General function prediction only]; Threonine dehydrogenase or related Zn-dependent dehydrogenase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway


Pssm-ID: 440683 [Multi-domain]  Cd Length: 341  Bit Score: 39.74  E-value: 1.96e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGA-VVSATDVRPATKEQVESLGA 208
Cdd:COG1063  157 AGVKPGDTVLVIGAGPIGLLAALAARLAGAaRVIVVDRNPERLELARELGA 207
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 140-208 3.10e-03

Alcohol dehydrogenases of the MDR family; This group contains members identified as related to zinc-dependent alcohol dehydrogenase and other members of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group includes various activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.


Pssm-ID: 176222 [Multi-domain]  Cd Length: 337  Bit Score: 39.09  E-value: 3.10e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 496695763 140 AVIE----GAEAFGRAfpmmmtaaGTVPAAKVFVMGVGVAGLQAIATARRLGAVVSATDVRPATKEQVESLGA 208
Cdd:cd08261  140 ALVEplaiGAHAVRRA--------GVTAGDTVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGA 204
PRK09880 PRK09880
L-idonate 5-dehydrogenase; Provisional
 159-227 5.73e-03

L-idonate 5-dehydrogenase; Provisional


Pssm-ID: 182130 [Multi-domain]  Cd Length: 343  Bit Score: 38.51  E-value: 5.73e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 496695763 159 AGTVPAAKVFVMGVGVAGLQAIATARRLGAV-VSATDVRPATKEQVESLGA-KFLAVEDEEFKNAQTAGGY 227
Cdd:PRK09880 165 AGDLQGKRVFVSGVGPIGCLIVAAVKTLGAAeIVCADVSPRSLSLAREMGAdKLVNPQNDDLDHYKAEKGY 235
 
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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