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Conserved domains on  [gi|643668504|ref|WP_025247552|]
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Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha [Mannheimia varigena]

Protein Classification

NAD(P) transhydrogenase subunit alpha( domain architecture ID 11484142)

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

EC:  7.1.1.1
Gene Ontology:  GO:0050661|GO:0120029|GO:0005886|GO:0051287|GO:0008746|GO:0008750|GO:0006740|GO:0046983

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-511 0e+00

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


:

Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 1031.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVWNADIIFKVNAPTEAEI 80
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAA 160
Cdd:PRK09424  81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 161 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAME 240
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEMA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 241 LYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVFVTDNQVKVIGYTDFPARLP 320
Cdd:PRK09424 241 LFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTDNGVTIIGYTDLPSRLP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 321 TQSSQLYGTNLVNLLKLLAPNKDGQIDINFEDVVLRGVTVVRDGELTWPAPPIQVSAQPQKQAVAPQAVKKEEKPANPKV 400
Cdd:PRK09424 321 TQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAPAAKEEEKKPASPWR 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 401 KYGVMAGVGALFLWIASVAPAAFLSHFTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGAVLQIAQpvGNFFI 480
Cdd:PRK09424 401 KYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGS--GSGLV 478

                        490       500       510
                 ....*....|....*....|....*....|.
gi 643668504 481 DILAFIAILVASINIFGGFKVTQRMLAMFRK 511
Cdd:PRK09424 479 TFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
 
Name Accession Description Interval E-value
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-511 0e+00

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


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 1031.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVWNADIIFKVNAPTEAEI 80
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAA 160
Cdd:PRK09424  81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 161 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAME 240
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEMA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 241 LYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVFVTDNQVKVIGYTDFPARLP 320
Cdd:PRK09424 241 LFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTDNGVTIIGYTDLPSRLP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 321 TQSSQLYGTNLVNLLKLLAPNKDGQIDINFEDVVLRGVTVVRDGELTWPAPPIQVSAQPQKQAVAPQAVKKEEKPANPKV 400
Cdd:PRK09424 321 TQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAPAAKEEEKKPASPWR 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 401 KYGVMAGVGALFLWIASVAPAAFLSHFTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGAVLQIAQpvGNFFI 480
Cdd:PRK09424 401 KYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGS--GSGLV 478

                        490       500       510
                 ....*....|....*....|....*....|.
gi 643668504 481 DILAFIAILVASINIFGGFKVTQRMLAMFRK 511
Cdd:PRK09424 479 TFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 2-512 0e+00

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: 949.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504    2 LIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVWNADIIFKVNAPTEAEIA 81
Cdd:TIGR00561   1 LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   82 LIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAAG 161
Cdd:TIGR00561  81 LLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  162 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAMEL 241
Cdd:TIGR00561 161 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIKAAMEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  242 YAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVFVTDNQVKVIGYTDFPARLPT 321
Cdd:TIGR00561 241 FAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTENGVKVIGYTDFPGRLPT 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  322 QSSQLYGTNLVNLLKLLAPNKDGQIDINFEDVVLRGVTVVRDGELTWPAPPIQVSAQPQK-QAVAPQAVKKEEKPANPKV 400
Cdd:TIGR00561 321 QSSQLYGTNLVNLLKLLCKEKDGNINIDFDDVVIRGVTVIRAGEETIPAAPIQVSAQPKAaQKAAPEAEKEEKCPCDPRR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  401 KYGVMAGVGALFLWIASVAPAAFLSHFTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGAVLQIAQPVGNFFI 480
Cdd:TIGR00561 401 KYALMAGAGILFGWLASVAPAAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALLQIGQGGGNLFI 480

                         490       500       510
                  ....*....|....*....|....*....|..
gi 643668504  481 DILAFIAILVASINIFGGFKVTQRMLAMFRKG 512
Cdd:TIGR00561 481 DALAFIAILIASINIFGGFRVTQRMLAMFRKG 512
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: 595.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIG-TQQEVWNADIIFKVNAPTEAE 79
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVsDAEELAQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  80 IALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITA 159
Cdd:cd05304   81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 160 AGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAM 239
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEEFLAKQR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 240 ELYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVfVTDNQVKVIGYTDFPARL 319
Cdd:cd05304  241 ELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGET-VVTNGVTIIGPTNLPSRL 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 643668504 320 PTQSSQLYGTNLVNLLKLLAPnKDGQIDINFEDVVLRGVTVVRDG 364
Cdd:cd05304  320 PTQASQLYAKNLLNFLELLVK-DDGELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-365 1.72e-168

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


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 480.27  E-value: 1.72e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQqEVWNADIIFKVNAPTEAEI 80
Cdd:COG3288    1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDA-ELLGADIVLKVRPPSAEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAA 160
Cdd:COG3288   80 AALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 161 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGgsGDGYAKVMSEEFNRRAME 240
Cdd:COG3288  160 GTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAIDANG--AGGYAKELSEEEKAKQAE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 241 LYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVfVTDNQVKVIGYTDFPARLP 320
Cdd:COG3288  238 LLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGET-VTKNGVTIIGPTNLPSRLP 316

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 643668504 321 TQSSQLYGTNLVNLLKLLApnKDGQIDINFEDVVLRGVTVVRDGE 365
Cdd:COG3288  317 AHASQLYAKNLLNFLELLV--KDGALALDLEDEIVAGTLLTHDGE 359
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 141-368 1.17e-81

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: 252.80  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  141 AVIEAANSFGSFFTGQITAAGKVP---PAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKS-MGADFLEIdf 216
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  217 eeeggsgdgyakVMSEEfnrramELYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCE--- 293
Cdd:pfam01262  79 ------------LYSQA------ELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEtsr 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643668504  294 YTKAGEVFVTDNQVKVIGYTDFPARLPTQSSQLYGTNLVNLLKLLApNKdGQIDINFEDVVLRGVTVVRDGELTW 368
Cdd:pfam01262 141 PTTHGEPVYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLA-DK-GLKAALLEDEALRAGLNTHDGKITH 213
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-135 1.03e-59

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: 193.01  E-value: 1.03e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504     4 GVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVW-NADIIFKVNAPTEAEIAL 82
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWaDADIILKVKEPSPEELAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 643668504    83 IKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMAN 135
Cdd:smart01003  81 LREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
 
Name Accession Description Interval E-value
pntA PRK09424
Re/Si-specific NAD(P)(+) transhydrogenase subunit alpha;
1-511 0e+00

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


Pssm-ID: 236507 [Multi-domain]  Cd Length: 509  Bit Score: 1031.32  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVWNADIIFKVNAPTEAEI 80
Cdd:PRK09424   1 MRIGIPRERLPGETRVAATPKTVEQLLKLGFEVVVESGAGQLASFDDAAYREAGAEIVDGAAVWQSDIILKVNAPSDDEI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAA 160
Cdd:PRK09424  81 ALLREGATLVSFIWPAQNPELLEKLAARGVTVLAMDAVPRISRAQSLDALSSMANIAGYRAVIEAAHEFGRFFTGQITAA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 161 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAME 240
Cdd:PRK09424 161 GKVPPAKVLVIGAGVAGLAAIGAAGSLGAIVRAFDTRPEVAEQVESMGAEFLELDFEEEGGSGDGYAKVMSEEFIKAEMA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 241 LYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVFVTDNQVKVIGYTDFPARLP 320
Cdd:PRK09424 241 LFAEQAKEVDIIITTALIPGKPAPKLITAEMVASMKPGSVIVDLAAENGGNCELTVPGEVVVTDNGVTIIGYTDLPSRLP 320

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 321 TQSSQLYGTNLVNLLKLLAPNKDGQIDINFEDVVLRGVTVVRDGELTWPAPPIQVSAQPQKQAVAPQAVKKEEKPANPKV 400
Cdd:PRK09424 321 TQSSQLYGTNLVNLLKLLCPEKDGNIVVDFDDVVIRGVTVVRDGEITWPPPPIQVSAAPAAAAAAPAAKEEEKKPASPWR 400

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 401 KYGVMAGVGALFLWIASVAPAAFLSHFTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGAVLQIAQpvGNFFI 480
Cdd:PRK09424 401 KYALMALAAALFGWLASVAPAEFLSHFTVFVLACVVGYYVVWNVSHALHTPLMSVTNAISGIIVVGALLQIGS--GSGLV 478

                        490       500       510
                 ....*....|....*....|....*....|.
gi 643668504 481 DILAFIAILVASINIFGGFKVTQRMLAMFRK 511
Cdd:PRK09424 479 TFLAFIAVLIASINIFGGFTVTQRMLKMFRK 509
pntA TIGR00561
NAD(P) transhydrogenase, alpha subunit; This integral membrane protein is the alpha subunit of ...
 2-512 0e+00

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: 949.49  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504    2 LIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVWNADIIFKVNAPTEAEIA 81
Cdd:TIGR00561   1 LIGIPRELLENESRVAATPKTVEQILKLGFDVAVEHDAGFKASFDDKAFLEAGAEIGEGAEIWQSDIIFKVNAPLDDEIA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   82 LIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAAG 161
Cdd:TIGR00561  81 LLKEGAALVSFIWPAQNPELMKKLAAKKINVLAMDAVPRISRAQALDALSSMANIAGYRAIIEAAHEFGRFFTGQITAAG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  162 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAMEL 241
Cdd:TIGR00561 161 KVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVQSMGAEFLEIDFKEEAGSGDGYAKVMSDAFIKAAMEL 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  242 YAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVFVTDNQVKVIGYTDFPARLPT 321
Cdd:TIGR00561 241 FAAQAKEVDIIITTAAIPGKPAPKLITKEMVDSMKAGSVIVDLAAANGGNCEYTQAGEIFTTENGVKVIGYTDFPGRLPT 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  322 QSSQLYGTNLVNLLKLLAPNKDGQIDINFEDVVLRGVTVVRDGELTWPAPPIQVSAQPQK-QAVAPQAVKKEEKPANPKV 400
Cdd:TIGR00561 321 QSSQLYGTNLVNLLKLLCKEKDGNINIDFDDVVIRGVTVIRAGEETIPAAPIQVSAQPKAaQKAAPEAEKEEKCPCDPRR 400

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  401 KYGVMAGVGALFLWIASVAPAAFLSHFTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGAVLQIAQPVGNFFI 480
Cdd:TIGR00561 401 KYALMAGAGILFGWLASVAPAAFLGHFTVFALACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGALLQIGQGGGNLFI 480

                         490       500       510
                  ....*....|....*....|....*....|..
gi 643668504  481 DILAFIAILVASINIFGGFKVTQRMLAMFRKG 512
Cdd:TIGR00561 481 DALAFIAILIASINIFGGFRVTQRMLAMFRKG 512
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: 595.54  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIG-TQQEVWNADIIFKVNAPTEAE 79
Cdd:cd05304    1 MTIGVPKETAPGERRVALTPETVKKLVKLGFEVLVESGAGEAAGFSDEAYEEAGAEIVsDAEELAQADIVLKVRPPSEEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  80 IALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITA 159
Cdd:cd05304   81 VALLKEGAVLIGFLDPAQNPELVEALAKKGVTAFAMELVPRISRAQSMDALSSQANIAGYKAVLEAANHLPRFFPMLMTA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 160 AGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGGSGDGYAKVMSEEFNRRAM 239
Cdd:cd05304  161 AGTIPPAKVLVIGAGVAGLQAIATAKRLGAVVEAFDVRPAAKEQVESLGAKFVEVDVEEDAEGAGGYAKELSEEFLAKQR 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 240 ELYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVfVTDNQVKVIGYTDFPARL 319
Cdd:cd05304  241 ELLAKHIAEADIVITTALIPGRKAPKLITKEMVESMKPGSVIVDLAAEQGGNCELTVPGET-VVTNGVTIIGPTNLPSRL 319

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 643668504 320 PTQSSQLYGTNLVNLLKLLAPnKDGQIDINFEDVVLRGVTVVRDG 364
Cdd:cd05304  320 PTQASQLYAKNLLNFLELLVK-DDGELTLDLEDEIVRGTLVTHDG 363
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
1-365 1.72e-168

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


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 480.27  E-value: 1.72e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQqEVWNADIIFKVNAPTEAEI 80
Cdd:COG3288    1 MKIGVPKETAPGERRVALTPETVKKLVKLGAEVLVESGAGLAAGFPDAAYEAAGAEIVDA-ELLGADIVLKVRPPSAEEL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQITAA 160
Cdd:COG3288   80 AALKPGAVLIGFLDPLGNPELVKALAAAGLTVFALELIPRISRAQSMDALSSQANFAGYKAVLLAAPALHTFFPLMSTAA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 161 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEGgsGDGYAKVMSEEFNRRAME 240
Cdd:COG3288  160 GTIRPAGVLVVGAGVAGLQAIATAKRLGAVVEAYDVRPAVKEQVESLGAKFVELAIDANG--AGGYAKELSEEEKAKQAE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 241 LYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVfVTDNQVKVIGYTDFPARLP 320
Cdd:COG3288  238 LLAEHIAKADIVITTALIPGRPAPFLVTERMLAMMKPGSVIVDLAAEQGGNCELTVPGET-VTKNGVTIIGPTNLPSRLP 316

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 643668504 321 TQSSQLYGTNLVNLLKLLApnKDGQIDINFEDVVLRGVTVVRDGE 365
Cdd:COG3288  317 AHASQLYAKNLLNFLELLV--KDGALALDLEDEIVAGTLLTHDGE 359
AlaDh_PNT_C pfam01262
Alanine dehydrogenase/PNT, C-terminal domain; This family now also contains the lysine ...
 141-368 1.17e-81

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: 252.80  E-value: 1.17e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  141 AVIEAANSFGSFFTGQITAAGKVP---PAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKS-MGADFLEIdf 216
Cdd:pfam01262   1 AVQEGANYLEKFFGGRGTLAGGVPgvaPAKVLVIGGGVAGLNAAATAKGLGAIVTILDVRPARLEQLESiLGAKFVET-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  217 eeeggsgdgyakVMSEEfnrramELYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCE--- 293
Cdd:pfam01262  79 ------------LYSQA------ELIAEAVKEADLVIGTALIPGAKAPKLVTREMVKSMKPGSVIVDVAIDQGGNVEtsr 140

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643668504  294 YTKAGEVFVTDNQVKVIGYTDFPARLPTQSSQLYGTNLVNLLKLLApNKdGQIDINFEDVVLRGVTVVRDGELTW 368
Cdd:pfam01262 141 PTTHGEPVYVVDGVVHYGVANMPGAVPRTSSQALTNNTLPYLLLLA-DK-GLKAALLEDEALRAGLNTHDGKITH 213
Ala_dh_like cd01620
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ...
 3-339 1.33e-78

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: 248.86  E-value: 1.33e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   3 IGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQ--QEVWNADIIFKVNAPTEAEI 80
Cdd:cd01620    2 LGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSGAGFSDEDYLQAGAQIVPAasKEAYSADIIVKLKEPEFAEY 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRaqalDALSSMANISGYRAVIEAANSFGSFFTGQITAA 160
Cdd:cd01620   82 DLIKKGQLLVTFLHAATNRGVVEVLMRKKLTAYALEDLENDFR----PRLAPNSNIAGYAGVQLGAYELARIQGGRMGGA 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 161 GKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEggsgdgyakvMSEEFnrrame 240
Cdd:cd01620  158 GGVPPAKVLIIGAGVVGLGAAKIAKKLGANVLVYDIKEEKLKGVETLGGSRLRYSQKEE----------LEKEL------ 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 241 lyaaqaKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCE----YTKAGEVFVTDNqVKVIGYTDFP 316
Cdd:cd01620  222 ------KQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDEtsipTTEGVPTYEVDG-VVIYGVDNMP 294

                        330       340
                 ....*....|....*....|...
gi 643668504 317 ARLPTQSSQLYGTNLVNLLKLLA 339
Cdd:cd01620  295 SLVPREASELLSKNLLPYLVKLA 317
L-AlaDH cd05305
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ...
 1-370 7.82e-61

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: 203.79  E-value: 7.82e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANI-GTQQEVWN-ADIIFKVNAPTEA 78
Cdd:cd05305    1 MKIGIPKEIKNQENRVALTPAGVAELVAAGHEVLVEKGAGLGSGFSDEEYSEAGAEIvPTAEEVWAkADLIVKVKEPLPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  79 EIALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVprISRAQALDALSSMANISGYRAVIEAANSFGSFFTGQ-- 156
Cdd:cd05305   81 EYDLLREGQILFTYLHLAADKELTEALLEKKVTAIAYETI--EDEDGSLPLLAPMSEIAGRLAVQIGAEYLEKPNGGRgv 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 157 ----ITAagkVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIdfeeeggsgdgyakVMSE 232
Cdd:cd05305  159 llggVPG---VPPAKVVILGAGVVGENAARVALGLGAEVTVLDINLERLRYLDDIFGGRVTT--------------LYSN 221

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 233 EFNrramelYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKA----GEVFVTDNqvk 308
Cdd:cd05305  222 PAN------LEEALKEADLVIGAVLIPGAKAPKLVTEEMVKTMKPGSVIVDVAIDQGGCFETSRPtthdNPTYVVHG--- 292

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643668504 309 VIGY--TDFPARLPTQSSQLYGTNLVNLLKLLApNKDGQIDINFEDVVLRGVTVVrDGELTWPA 370
Cdd:cd05305  293 VIHYcvPNMPGAVPRTSTLALTNATLPYLLKLA-NKGLEEALLEDPGLAKGLNTY-KGKLTNKA 354
AlaDh_PNT_N smart01003
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ...
 4-135 1.03e-59

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: 193.01  E-value: 1.03e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504     4 GVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGTQQEVW-NADIIFKVNAPTEAEIAL 82
Cdd:smart01003   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGEGAGFSDEAYEAAGAEIVDTAEVWaDADIILKVKEPSPEELAL 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 643668504    83 IKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISRAQALDALSSMAN 135
Cdd:smart01003  81 LREGQILFGYLHPAANPELLEALAAKGVTAIAYETVPRISRAQSLDALSSMAE 133
AlaDh_PNT_N pfam05222
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ...
 4-136 1.05e-54

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: 179.93  E-value: 1.05e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504    4 GVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIG-TQQEVWN-ADIIFKVNAPTEAEIA 81
Cdd:pfam05222   1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAGLGAGFSDEAYEAAGAEIVdTAAEVWAeADLILKVKEPQPEEYA 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 643668504   82 LIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRiSRAQALDALSSMANI 136
Cdd:pfam05222  81 LLREGQTLITFLHPAANPELLEALAAKGVTAIAYETVPR-SRGQSLDALSSMANI 134
Ald COG0686
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ...
 1-297 1.44e-54

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: 187.53  E-value: 1.44e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANI-GTQQEVW-NADIIFKVNAPTEA 78
Cdd:COG0686    1 MIIGVPKEIKNNENRVALTPAGVRELVAAGHEVLVETGAGLGSGFSDEDYSAAGAEIvDTAEEVFaQADLIVKVKEPQPE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  79 EIALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDAVprISRAQALDALSSMANISGYRAVIEAA----NSFGsfft 154
Cdd:COG0686   81 EYALLRPGQILFTYLHLAADPELTEALLEKGVTAIAYETV--EDPDGSLPLLAPMSEIAGRMAIQIGAeyleKPNG---- 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 155 gqitaaGK---------VPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKsmgadfleidfeeeggsgdg 225
Cdd:COG0686  155 ------GRgvllggvpgVPPAKVVILGGGVVGTNAARMALGLGADVTVLDINLDRLRRLD-------------------- 208

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 643668504 226 yakvmsEEFNRRAMELY------AAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKA 297
Cdd:COG0686  209 ------DIFGGRVTTLYsnpaniEEALKEADLVIGAVLIPGARAPKLVTREMVKRMKPGSVIVDVAIDQGGCFETSRP 280
AlaDh_PNT_C smart01002
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ...
 146-311 7.18e-53

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: 175.77  E-value: 7.18e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   146 ANSFGSFFTGQITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKS-MGADFLEIdfeeeggsgd 224
Cdd:smart01002   1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEVTVLDVRPARLRQLESlLGARFTTL---------- 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   225 gyakvmseefnRRAMELYAAQAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEV---F 301
Cdd:smart01002  71 -----------YSQAELLEEAVKEADLVIGAVLIPGAKAPKLVTREMVKSMKPGSVIVDVAADQGGCIETSRPTTHddpT 139

                          170
                   ....*....|
gi 643668504   302 VTDNQVKVIG 311
Cdd:smart01002 140 YVVDGVVHYC 149
PNTB_4TM pfam12769
4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of ...
 427-511 9.74e-45

4TM region of pyridine nucleotide transhydrogenase, mitoch; PNTB_4TM is the region upstream of family PNTB, pfam02233, that carries four of this transporters transmembrane regions. PNTB is the beta-subunit of pyridine nucleotide transhydrogenase. This family forms part of the Proton-translocating Transhydrogenase (PTH) Family.


Pssm-ID: 463694 [Multi-domain]  Cd Length: 84  Bit Score: 151.83  E-value: 9.74e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  427 FTVFVLACVVGYYVVWNVSHALHTPLMAVTNAISGIIIVGAVLQIAQPVGNFFiDILAFIAILVASINIFGGFKVTQRML 506
Cdd:pfam12769   1 LTVFVLALFVGYEVIWKVPPALHTPLMSVTNAISGIIIVGALLAAGGGDTTLA-TVLGFIAVVLATINVVGGFLVTDRML 79


                  ....*
gi 643668504  507 AMFRK 511
Cdd:pfam12769  80 DMFKK 84
FDH_GDH_like cd12154
Formate/glycerate dehydrogenases, D-specific 2-hydroxy acid dehydrogenases and related ...
 3-335 2.92e-40

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: 147.76  E-value: 2.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   3 IGVPRELLDGETRVAATPKTVEQIKKLGFDVLIESEAGFKASFEDNAFLNAGANIGT-QQEVWNADIIFKVNAP-TEAEI 80
Cdd:cd12154    1 IAGPKEIKNEEFRVGLSPSVVATLVEAGHEVRVETGAGIGAGFADQAYVQAGAIVVTlAKALWSLDVVLKVKEPlTNAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  81 ALIKE--GATLVSFIWPAQNPELMEKLQSKKINVLAMDAVPRISraqaldaLSSMANISGYRAVIEAANSFGSFFTGQIT 158
Cdd:cd12154   81 ALIQKlgDRLLFTYTIGADHRDLTEALARAGLTAIAVEGVELPL-------LTSNSIGAGELSVQFIARFLEVQQPGRLG 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 159 AAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEiDFEEEggsgdgyakvmseefnrra 238
Cdd:cd12154  154 GAPDVAGKTVVVVGAGVVGKEAAQMLRGLGAQVLITDINVEALEQLEELGGKNVE-ELEEA------------------- 213

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 239 melyaaqAKEVDIIITTAAIPGKPAPRLITKEMVNSMKPGSVIVDLAAATGGNCEYTKAGEVFVTdNQVKVIGYTDFPAR 318
Cdd:cd12154  214 -------LAEADVIVTTTLLPGKRAGILVPEELVEQMKPGSVIVNVAVGAVGCVQALHTQLLEEG-HGVVHYGDVNMPGP 285

                        330       340
                 ....*....|....*....|..
gi 643668504 319 LPTQ-----SSQLYGTNLVNLL 335
Cdd:cd12154  286 GCAMgvpwdATLRLAANTLPAL 307
ceo_syn cd12181
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ...
 1-296 1.70e-14

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: 74.19  E-value: 1.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504   1 MLIGVPRELLDGETRVAATPKTVEQIK---KLGFdvliesEAGFKASF--EDNAFLNAGANIGTQQEVW-NADIIFKVnA 74
Cdd:cd12181    1 KTGGFGISNKENEKRVPLLPADLERIPlreQLYF------EEGYGERLgiSDEEYAALGAGIVSREEILaKCDVICDP-K 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  75 PTEAEIALIKEGATLVSFIWPAQNPELMEKLQSKKINVLAMDA--VPRISRAQALDALSSMAnisGYRAVIEAANSFGSF 152
Cdd:cd12181   74 PGDADYLEILEGQILWGWVHCVQDKEITQLAIDKKLTLIAWEDmfEWSKIGRHVFYKNNELA---GYAAVLHALQLYGIT 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 153 FTGQItaagkvppaKVLVIGAGvaglaaigaANSLGAIvRAFdsrpevkeqvKSMGADfleIDFeeeggsgdgyakvmse 232
Cdd:cd12181  151 PYRQT---------KVAVLGFG---------NTARGAI-RAL----------KLGGAD---VTV---------------- 182

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 643668504 233 eFNRRAMELYAAQAKEVDIIITtaAI---PGKPAPrLITKEMVNSMKPGSVIVDLAAATGGNCEYTK 296
Cdd:cd12181  183 -YTRRTEALFKEELSEYDIIVN--CIlqdTDRPDH-IIYEEDLKRLKPGALIIDVSCDEGMGIEFAK 245
PntA COG3288
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
426-473 2.60e-07

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


Pssm-ID: 442518 [Multi-domain]  Cd Length: 359  Bit Score: 52.70  E-value: 2.60e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 643668504 426 HFTVFVL------------------ACVVGYYVVWNVSHALHT--PLMAVTNAI---SGIIIVGAVLQIAQ 473
Cdd:COG3288  108 GLTVFALeliprisraqsmdalssqANFAGYKAVLLAAPALHTffPLMSTAAGTirpAGVLVVGAGVAGLQ 178
MDR cd05188
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 158-313 1.01e-05

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: 47.32  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 158 TAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLeIDfeeeggsgdgYAKVMSEEfnrr 237
Cdd:cd05188  128 RAGVLKPGDTVLVLGAGGVGLLAAQLAKAAGARVIVTDRSDEKLELAKELGADHV-ID----------YKEEDLEE---- 192

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 643668504 238 amELYAAQAKEVDIIITTAAIPGkpaprlITKEMVNSMKPGSVIVDLAAATGGNceyTKAGEVFVTDNQVKVIGYT 313
Cdd:cd05188  193 --ELRLTGGGGADVVIDAVGGPE------TLAQALRLLRPGGRIVVVGGTSGGP---PLDDLRRLLFKELTIIGST 257
hydroxyacyl_CoA_DH cd08254
6-hydroxycyclohex-1-ene-1-carboxyl-CoA dehydrogenase, N-benzyl-3-pyrrolidinol dehydrogenase, ...
 157-220 2.52e-05

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: 46.47  E-value: 2.52e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 643668504 157 ITAAGKVPPA-KVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLEIDFEEEG 220
Cdd:cd08254  157 VVRAGEVKPGeTVLVIGLGGLGLNAVQIAKAMGAAVIAVDIKEEKLELAKELGADEVLNSLDDSP 221
MurD COG0771
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ...
 167-219 2.69e-05

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


Pssm-ID: 440534 [Multi-domain]  Cd Length: 445  Bit Score: 46.61  E-value: 2.69e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 643668504 167 KVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPE---VKEQVKSMGADFLEIDFEEE 219
Cdd:COG0771    6 KVLVLGLGKSGLAAARLLAKLGAEVTVSDDRPApelAAAELEAPGVEVVLGEHPEE 61
AdhP COG1064
D-arabinose 1-dehydrogenase, Zn-dependent alcohol dehydrogenase family [Carbohydrate transport ...
 161-210 3.63e-05

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


Pssm-ID: 440684 [Multi-domain]  Cd Length: 332  Bit Score: 45.87  E-value: 3.63e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 643668504 161 GKVPPA-KVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGAD 210
Cdd:COG1064  158 AGVGPGdRVAVIGAGGLGHLAVQIAKALGAEVIAVDRSPEKLELARELGAD 208
MDR_TM0436_like cd08231
Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This ...
 159-210 1.66e-04

Hypothetical enzyme TM0436 resembles the zinc-dependent alcohol dehydrogenases (ADH); This group contains the hypothetical TM0436 alcohol dehydrogenase from Thermotoga maritima, proteins annotated as 5-exo-alcohol dehydrogenase, and other members of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family. MDR, 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.


Pssm-ID: 176193 [Multi-domain]  Cd Length: 361  Bit Score: 43.79  E-value: 1.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 643668504 159 AAGKVPPAK-VLVIGAGVAGLAAIGAANSLGAI-VRAFDSRPEVKEQVKSMGAD 210
Cdd:cd08231  171 RAGPVGAGDtVVVQGAGPLGLYAVAAAKLAGARrVIVIDGSPERLELAREFGAD 224
Tdh COG1063
Threonine dehydrogenase or related Zn-dependent dehydrogenase [Amino acid transport and ...
 160-230 2.86e-04

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: 43.20  E-value: 2.86e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643668504 160 AGKVPPAKVLVIGAGVAGLAAIGAANSLGAI-VRAFDSRPEVKEQVKSMGADFLeIDFEEEggsgDGYAKVM 230
Cdd:COG1063  157 AGVKPGDTVLVIGAGPIGLLAALAARLAGAArVIVVDRNPERLELARELGADAV-VNPREE----DLVEAVR 223
Zn_ADH7 cd08261
Alcohol dehydrogenases of the MDR family; This group contains members identified as related to ...
 167-210 3.41e-04

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: 42.95  E-value: 3.41e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 643668504 167 KVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGAD 210
Cdd:cd08261  162 TVLVVGAGPIGLGVIQVAKARGARVIVVDIDDERLEFARELGAD 205
MDR2 cd08268
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 144-231 3.54e-04

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. 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: 176229 [Multi-domain]  Cd Length: 328  Bit Score: 42.59  E-value: 3.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 144 EAANSFGSFFTGQ---ITAAGKVPPAKVLVIGA-GVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLeIDFEEE 219
Cdd:cd08268  121 EAAALWMQYLTAYgalVELAGLRPGDSVLITAAsSSVGLAAIQIANAAGATVIATTRTSEKRDALLALGAAHV-IVTDEE 199

                         90
                 ....*....|..
gi 643668504 220 ggsgDGYAKVMS 231
Cdd:cd08268  200 ----DLVAEVLR 207
Zn_ADH3 cd08265
Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol ...
 157-287 1.39e-03

Alcohol dehydrogenases of the MDR family; This group resembles the zinc-dependent alcohol dehydrogenase and has the catalytic and structural zinc-binding sites characteristic of this group. 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. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.


Pssm-ID: 176226 [Multi-domain]  Cd Length: 384  Bit Score: 40.96  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504 157 ITAAGKVPPAKVLVIGAGVAGLAAIGAANSLGAI-VRAFDSRPEVKEQVKSMGADFLeIDFEEEGGsgdgyakvmsEEFN 235
Cdd:cd08265  196 IRGGGFRPGAYVVVYGAGPIGLAAIALAKAAGASkVIAFEISEERRNLAKEMGADYV-FNPTKMRD----------CLSG 264

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 643668504 236 RRAMELYAAQAkeVDIIITTAAipgkpAPRLITKEMVNSMKPGSVIVDLAAA 287
Cdd:cd08265  265 EKVMEVTKGWG--ADIQVEAAG-----APPATIPQMEKSIAINGKIVYIGRA 309
TDH cd05281
Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent ...
 160-219 1.94e-03

Threonine dehydrogenase; L-threonine dehydrogenase (TDH) catalyzes the zinc-dependent formation of 2-amino-3-ketobutyrate from L-threonine via NAD(H)- dependent oxidation. THD is a member of the zinc-requiring, medium chain NAD(H)-dependent alcohol dehydrogenase family (MDR). MDRs have a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria) and have 2 tightly bound zinc atoms per subunit. Sorbitol and aldose reductase are NAD(+) binding proteins of the polyol pathway, which interconverts glucose and fructose.


Pssm-ID: 176184 [Multi-domain]  Cd Length: 341  Bit Score: 40.30  E-value: 1.94e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 643668504 160 AGKVPPAKVLVIGAGVAGLAAIGAANSLGA-IVRAFDSRPEVKEQVKSMGADFLeIDFEEE 219
Cdd:cd05281  159 AGDVSGKSVLITGCGPIGLMAIAVAKAAGAsLVIASDPNPYRLELAKKMGADVV-INPREE 218
murD PRK14106
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional
 167-214 3.34e-03

UDP-N-acetylmuramoyl-L-alanyl-D-glutamate synthetase; Provisional


Pssm-ID: 184511 [Multi-domain]  Cd Length: 450  Bit Score: 39.95  E-value: 3.34e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 643668504 167 KVLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEV--KEQVKSMGADFLEI 214
Cdd:PRK14106   7 KVLVVGAGVSGLALAKFLKKLGAKVILTDEKEEDqlKEALEELGELGIEL 56
Zn_ADH6 cd08260
Alcohol dehydrogenases of the MDR family; NAD(P)(H)-dependent oxidoreductases are the major ...
 157-210 5.57e-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: 39.12  E-value: 5.57e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 643668504 157 ITAAGKVPPAK-VLVIGAGVAGLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGAD 210
Cdd:cd08260  157 LVHQARVKPGEwVAVHGCGGVGLSAVMIASALGARVIAVDIDDDKLELARELGAV 211
Zn_ADH8 cd08262
Alcohol dehydrogenases of the MDR family; The medium chain dehydrogenases/reductase (MDR) ...
 160-219 5.66e-03

Alcohol dehydrogenases 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 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: 176223 [Multi-domain]  Cd Length: 341  Bit Score: 38.83  E-value: 5.66e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 643668504 160 AGKVPPAKVLVIGAGVAGLAAIGAANSLGA--IVrAFDSRPEVKEQVKSMGADFLeIDFEEE 219
Cdd:cd08262  157 ARLTPGEVALVIGCGPIGLAVIAALKARGVgpIV-ASDFSPERRALALAMGADIV-VDPAAD 216
MDR1 cd08267
Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ...
 157-210 6.28e-03

Medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family; This group is a member of the medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, but lacks the zinc-binding sites of the zinc-dependent alcohol dehydrogenases. 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: 176228 [Multi-domain]  Cd Length: 319  Bit Score: 38.74  E-value: 6.28e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 643668504 157 ITAAGKVPP-AKVLVIGA--GVaGLAAIGAANSLGAIVRAFDSRPEVkEQVKSMGAD 210
Cdd:cd08267  135 LRDAGKVKPgQRVLINGAsgGV-GTFAVQIAKALGAHVTGVCSTRNA-ELVRSLGAD 189
NADP_ADH cd08285
NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol ...
 168-230 6.90e-03

NADP(H)-dependent alcohol dehydrogenases; This group is predominated by atypical alcohol dehydrogenases; they exist as tetramers and exhibit specificity for NADP(H) as a cofactor in the interconversion of alcohols and aldehydes, or ketones. Like other zinc-dependent alcohol dehydrogenases (ADH) of the medium chain alcohol dehydrogenase/reductase family (MDR), tetrameric ADHs have a catalytic zinc that resides between the catalytic and NAD(H)binding domains; however, they do not have and a structural zinc in a lobe of the catalytic domain. The medium chain alcohol dehydrogenase family (MDR) has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The N-terminal region typically has an all-beta catalytic domain. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit.


Pssm-ID: 176245 [Multi-domain]  Cd Length: 351  Bit Score: 38.76  E-value: 6.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 643668504 168 VLVIGAGVAGLAAIGAANSLGA-IVRAFDSRPEVKEQVKSMGADFLeIDFEEeggsGDGYAKVM 230
Cdd:cd08285  170 VAVFGIGPVGLMAVAGARLRGAgRIIAVGSRPNRVELAKEYGATDI-VDYKN----GDVVEQIL 228
ADH_zinc_N pfam00107
Zinc-binding dehydrogenase;
177-259 7.54e-03

Zinc-binding dehydrogenase;


Pssm-ID: 395057 [Multi-domain]  Cd Length: 129  Bit Score: 36.82  E-value: 7.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 643668504  177 GLAAIGAANSLGAIVRAFDSRPEVKEQVKSMGADFLeIDFEEeggsgDGYAKVMSEEFNrramelyaaqAKEVDIIITTA 256
Cdd:pfam00107   3 GLAAIQLAKAAGAKVIAVDGSEEKLELAKELGADHV-INPKE-----TDLVEEIKELTG----------GKGVDVVFDCV 66


                  ...
gi 643668504  257 AIP 259
Cdd:pfam00107  67 GSP 69
 
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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