|
Name |
Accession |
Description |
Interval |
E-value |
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
4-365 |
0e+00 |
|
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (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. SHD 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.
Pssm-ID: 240664 [Multi-domain] Cd Length: 351 Bit Score: 602.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 4 VTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYRQAGAIIVPAGSWKTAPRDRIIIGLKEMPEtD 83
Cdd:cd12188 1 THLWLRAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRIFPDEEYEAVGCELVPAGSWVNAPKDAIILGLKELPE-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 84 TFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSDDedL 163
Cdd:cd12188 80 TFPLPHRHIYFAHAYKGQAGWKDVLSRFARGGGTLLDLEYLVDDDGRRVAAFGYWAGFAGAALGLLAWAHQQLGPVT--L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 164 PAVSPYPNEKALVKDVTKdykeALATGARKPTVLIIGALGRCGSGAIDLLHKVGIpdaNILKWDIKETSRGGPFDEIPQA 243
Cdd:cd12188 158 PPVSPYPNEEALVADVKK----ALATGGRKPRALVIGALGRCGSGAVDLLEAAGI---EVTKWDMAETKAGGPFPEILDH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 244 DIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNKPTVLVPTTaGPKLSVISIDHLPS 323
Cdd:cd12188 231 DIFVNCIYLSKPIPPFLTPEMLQAPGRRLRVIGDVSCDPTNPYNPIPIYDVATTFDKPTLRVPTG-GPPLDVIAIDHLPS 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 766281585 324 LLPREASEFFSHDLLPSLELLPQRKTAPVWVRAKKLFDRHCA 365
Cdd:cd12188 310 LLPRESSEDFSNDLLPSLLELAERDTAGVWARAKKLFDTKVA 351
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
7-142 |
1.63e-36 |
|
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: 129.08 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 7 HLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSP--QSTFNINEYRQAGAIIVPAgSWKTAPRDRIIIGLKE--MPET 82
Cdd:pfam05222 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVDT-AAEVWAEADLILKVKEpqPEEY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 83 DTFPLVHEHIQFAHCykdqAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFA 142
Cdd:pfam05222 80 ALLREGQTLITFLHP----AANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
8-140 |
3.73e-30 |
|
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: 112.12 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 8 LRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSP--QSTFNINEYRQAGAIIVPAGS-WKTAPrdrIIIGLKEMPETDT 84
Cdd:smart01003 2 VPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTAEvWADAD---IILKVKEPSPEEL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 766281585 85 FPLVHEHIQFAhcYKDQAGWQNVLMRFIKGHGTLYDLEFLEND-QGRRVAAFGFYAG 140
Cdd:smart01003 79 ALLREGQILFG--YLHPAANPELLEALAAKGVTAIAYETVPRIsRAQSLDALSSMAE 133
|
|
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
8-349 |
4.22e-11 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 64.44 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 8 LRAETKPLEARAALTPTTVKKLIAKGF-----KIYVEDSPQSTFNINEYRQAGAIIVP----AGswktaprdrIIIGLKE 78
Cdd:PLN02819 11 LAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEdlsdCG---------LILGVKQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 79 mPETDTFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVR---DWAFKQ 155
Cdd:PLN02819 82 -PKLEMLLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRglgQRLLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 156 THSDdedlPAVS-----PYPN---EKALVKDVTKDYKEALATGARKPTVLIIGALGRCGSGAIDLL----HKVGIPDANI 223
Cdd:PLN02819 161 GYST----PFLSlgssyMYSSlaaAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFkllpHTFVEPSKLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 224 LKWDI---KETSRG------------------GP---FDE------------------IPQADIFINCIYLSKPIAPFTN 261
Cdd:PLN02819 237 ELKGIsqnKISTKRvyqvygcvvtsqdmvehkDPskqFDKadyyahpehynpvfhekiAPYASVIVNCMYWEKRFPRLLT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 262 MEKL----NNPNRRLRTVVDVSADTtnpHNPIPIYTVATVFNKPTVLV-PTT-------AGPKLSVISIDHLPSLLPREA 329
Cdd:PLN02819 317 TKQLqdltRKGGCPLVGVCDITCDI---GGSIEFLNKTTSIEKPFFRYnPSNnsyhddmDGDGILCMAVDILPTEFAKEA 393
|
410 420
....*....|....*....|
gi 766281585 330 SEFFSHDLLPSLELLPQRKT 349
Cdd:PLN02819 394 SQHFGNILSPFVGSLASMKE 413
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
10-65 |
2.59e-08 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 55.01 E-value: 2.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 766281585 10 AETKPLEARAALTPTTVKKLIAKGFKIYVED--SPQSTFNINEYRQAGAIIVPAGSWK 65
Cdd:COG3288 7 KETAPGERRVALTPETVKKLVKLGAEVLVESgaGLAAGFPDAAYEAAGAEIVDAELLG 64
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
4-365 |
0e+00 |
|
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (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. SHD 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.
Pssm-ID: 240664 [Multi-domain] Cd Length: 351 Bit Score: 602.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 4 VTLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQSTFNINEYRQAGAIIVPAGSWKTAPRDRIIIGLKEMPEtD 83
Cdd:cd12188 1 THLWLRAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRIFPDEEYEAVGCELVPAGSWVNAPKDAIILGLKELPE-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 84 TFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSDDedL 163
Cdd:cd12188 80 TFPLPHRHIYFAHAYKGQAGWKDVLSRFARGGGTLLDLEYLVDDDGRRVAAFGYWAGFAGAALGLLAWAHQQLGPVT--L 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 164 PAVSPYPNEKALVKDVTKdykeALATGARKPTVLIIGALGRCGSGAIDLLHKVGIpdaNILKWDIKETSRGGPFDEIPQA 243
Cdd:cd12188 158 PPVSPYPNEEALVADVKK----ALATGGRKPRALVIGALGRCGSGAVDLLEAAGI---EVTKWDMAETKAGGPFPEILDH 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 244 DIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIYTVATVFNKPTVLVPTTaGPKLSVISIDHLPS 323
Cdd:cd12188 231 DIFVNCIYLSKPIPPFLTPEMLQAPGRRLRVIGDVSCDPTNPYNPIPIYDVATTFDKPTLRVPTG-GPPLDVIAIDHLPS 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 766281585 324 LLPREASEFFSHDLLPSLELLPQRKTAPVWVRAKKLFDRHCA 365
Cdd:cd12188 310 LLPRESSEDFSNDLLPSLLELAERDTAGVWARAKKLFDTKVA 351
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
5-345 |
3.80e-123 |
|
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: 357.70 E-value: 3.80e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 5 TLHLRAETK-PLEARAALTPTTVKKLIAK--GFKIYVEDSPQSTFNINEYRQAGAIIVpagswKTAPRDRIIIGLKEMPE 81
Cdd:cd05199 1 KIGIIREGKtPPDRRVPLTPEQCKELQAKypGVEIFVQPSPVRCFKDEEYRAAGIEVV-----EDLSDCDILLGVKEVPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 82 tDTFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSDDE 161
Cdd:cd05199 76 -EQLIPNKTYFFFSHTIKKQPYNRKLLQTILEKNITLIDYEVLVDEQGKRVIAFGRYAGIVGAYNGLRAYGKKTGLFDLK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 162 DLPAVSpypnekalvkDVTKDYKEALATGARKPTVLIIGAlGRCGSGAIDLLHKVGIpdaNILKWDIKETsrggpfdeip 241
Cdd:cd05199 155 RAHECS----------DLEELIAELKKVGLPPPKIVITGS-GRVGSGAAEVLKALGI---KEVSPEDFLT---------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 242 QADIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTtnpHNPIPIYTVATVFNKPTVLVPTTAG--------PKL 313
Cdd:cd05199 211 VADILINGHYWDKRAPRLFTKEDLKKPDFKIRVIADVTCDI---HGSIPSTLRASTIADPVYDYDPTTNkevafsspDSI 287
|
330 340 350
....*....|....*....|....*....|..
gi 766281585 314 SVISIDHLPSLLPREASEFFSHDLLPSLELLP 345
Cdd:cd05199 288 TVMAVDNLPCELPRDASEDFGEQLIKSVLPEL 319
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
5-345 |
2.66e-116 |
|
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: 340.54 E-value: 2.66e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 5 TLHLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSPQS--TFNINEYRQAGAIIVPAGSwKTAPRDRIIIGLKEMPET 82
Cdd:cd01620 1 TLGFPKETKNNEFRVALTPSFVKKLVANGFKVYIETGAGSgaGFSDEDYLQAGAQIVPAAS-KEAYSADIIVKLKEPEFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 83 DTFPLV--HEHIQFAHCYKdQAGWQNVLMRfikGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVRDWAFKQTHSdd 160
Cdd:cd01620 80 EYDLIKkgQLLVTFLHAAT-NRGVVEVLMR---KKLTAYALEDLENDFRPRLAPNSNIAGYAGVQLGAYELARIQGGR-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 161 edlpavspypnekalvkdvtkdykEALATGARKPTVLIIGAlGRCGSGAIDLLHKVGipdANILKWDIKETSRGG----- 235
Cdd:cd01620 154 ------------------------MGGAGGVPPAKVLIIGA-GVVGLGAAKIAKKLG---ANVLVYDIKEEKLKGvetlg 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 236 -----------PFDEIPQADIFINCIYLSKPIAPFTNMEKLNNPNRRLRTVVDVSADTTNPHNPIPIytvatvfnkPTVL 304
Cdd:cd01620 206 gsrlrysqkeeLEKELKQTDILINAILVDGPRAPILIMEELVGPMKRGAVIVDLAADQGGNDETSIP---------TTEG 276
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 766281585 305 VPTTAGPKLSVISIDHLPSLLPREASEFFSHDLLPSLELLP 345
Cdd:cd01620 277 VPTYEVDGVVIYGVDNMPSLVPREASELLSKNLLPYLVKLA 317
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
7-142 |
1.63e-36 |
|
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: 129.08 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 7 HLRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSP--QSTFNINEYRQAGAIIVPAgSWKTAPRDRIIIGLKE--MPET 82
Cdd:pfam05222 1 GVPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVDT-AAEVWAEADLILKVKEpqPEEY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 83 DTFPLVHEHIQFAHCykdqAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFA 142
Cdd:pfam05222 80 ALLREGQTLITFLHP----AANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
5-342 |
2.16e-34 |
|
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: 131.53 E-value: 2.16e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 5 TLHLRAETKPL-EARAALTPTTVKKLIAK-GFKIYVEDSPQSTFNINEYRQAGAIIVPAGSwktaPRDrIIIGLKEMPET 82
Cdd:cd12189 1 VIGIRREDKNIwERRAPLTPSHVRELVKKpGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLS----DAD-LILGVKEPPID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 83 DtfpLVHE--HIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGA-----ALGVRDWA--- 152
Cdd:cd12189 76 K---LLPDktYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMidilhGLGLRLLAlgy 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 153 ---F---KQTHSddedlpavspYPNEKALVKDVtKDYKEALATG----ARKP-TVLIIGAlGRCGSGAIDLLHKVGIP-- 219
Cdd:cd12189 153 stpFlhiGRAYN----------YPSLEEAKQAV-RDAGYEIALGglpkSLGPlVFVFTGS-GNVSQGAQEIFEELPHEyv 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 220 -------------DAN------ILKWDIKETSRGGPFDE------------------IPQADIFINCIYLSK---PIAPF 259
Cdd:cd12189 221 epsdlpelaksgaDRNkvygcvVTPEDYLERKDGGPFDRadyyanpelyesvfhekiAPYLSVLINGIYWDPrfpRLLTN 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 260 TNMEKL---NNPNRRLRTVVDVSAD----------TTNPHNPIPIYTVATVFNKPTVlvpttAGPKLSVISIDHLPSLLP 326
Cdd:cd12189 301 EQLQALlrpPAGPHRLLAIADISCDiggsiefltkATTIDSPFYVYDPDTDKIHDSV-----SGDGILVMSVDNLPAELP 375
|
410
....*....|....*.
gi 766281585 327 REASEFFSHDLLPSLE 342
Cdd:cd12189 376 REASEHFGDALLPYVP 391
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
8-140 |
3.73e-30 |
|
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: 112.12 E-value: 3.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 8 LRAETKPLEARAALTPTTVKKLIAKGFKIYVEDSP--QSTFNINEYRQAGAIIVPAGS-WKTAPrdrIIIGLKEMPETDT 84
Cdd:smart01003 2 VPKEIKPGERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTAEvWADAD---IILKVKEPSPEEL 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 766281585 85 FPLVHEHIQFAhcYKDQAGWQNVLMRFIKGHGTLYDLEFLEND-QGRRVAAFGFYAG 140
Cdd:smart01003 79 ALLREGQILFG--YLHPAANPELLEALAAKGVTAIAYETVPRIsRAQSLDALSSMAE 133
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
175-308 |
7.30e-17 |
|
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: 76.78 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 175 LVKDVTKDYKEALATGARKP-TVLIIGAlGRCGSGAIDLLHKVGipdANILKWDIKETSR-------GGPF--------- 237
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPaKVVVIGA-GVVGLGAAATAKGLG---AEVTVLDVRPARLrqlesllGARFttlysqael 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 766281585 238 --DEIPQADIFINCIYLS-KPIAPFTNMEKLNNPnRRLRTVVDVSADTtnpHNPIPIyTVATVFNKPTVLVPTT 308
Cdd:smart01002 77 leEAVKEADLVIGAVLIPgAKAPKLVTREMVKSM-KPGSVIVDVAADQ---GGCIET-SRPTTHDDPTYVVDGV 145
|
|
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
8-349 |
4.22e-11 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 64.44 E-value: 4.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 8 LRAETKPLEARAALTPTTVKKLIAKGF-----KIYVEDSPQSTFNINEYRQAGAIIVP----AGswktaprdrIIIGLKE 78
Cdd:PLN02819 11 LAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEdlsdCG---------LILGVKQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 79 mPETDTFPLVHEHIQFAHCYKDQAGWQNVLMRFIKGHGTLYDLEFLENDQGRRVAAFGFYAGFAGAALGVR---DWAFKQ 155
Cdd:PLN02819 82 -PKLEMLLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRglgQRLLSL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 156 THSDdedlPAVS-----PYPN---EKALVKDVTKDYKEALATGARKPTVLIIGALGRCGSGAIDLL----HKVGIPDANI 223
Cdd:PLN02819 161 GYST----PFLSlgssyMYSSlaaAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFkllpHTFVEPSKLP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 224 LKWDI---KETSRG------------------GP---FDE------------------IPQADIFINCIYLSKPIAPFTN 261
Cdd:PLN02819 237 ELKGIsqnKISTKRvyqvygcvvtsqdmvehkDPskqFDKadyyahpehynpvfhekiAPYASVIVNCMYWEKRFPRLLT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 262 MEKL----NNPNRRLRTVVDVSADTtnpHNPIPIYTVATVFNKPTVLV-PTT-------AGPKLSVISIDHLPSLLPREA 329
Cdd:PLN02819 317 TKQLqdltRKGGCPLVGVCDITCDI---GGSIEFLNKTTSIEKPFFRYnPSNnsyhddmDGDGILCMAVDILPTEFAKEA 393
|
410 420
....*....|....*....|
gi 766281585 330 SEFFSHDLLPSLELLPQRKT 349
Cdd:PLN02819 394 SQHFGNILSPFVGSLASMKE 413
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
11-61 |
6.72e-09 |
|
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: 57.03 E-value: 6.72e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 766281585 11 ETKPLEARAALTPTTVKKLIAKGFKIYVE----------DSpqstfninEYRQAGAIIVPA 61
Cdd:cd05304 8 ETAPGERRVALTPETVKKLVKLGFEVLVEsgageaagfsDE--------AYEEAGAEIVSD 60
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
10-65 |
2.59e-08 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 55.01 E-value: 2.59e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 766281585 10 AETKPLEARAALTPTTVKKLIAKGFKIYVED--SPQSTFNINEYRQAGAIIVPAGSWK 65
Cdd:COG3288 7 KETAPGERRVALTPETVKKLVKLGAEVLVESgaGLAAGFPDAAYEAAGAEIVDAELLG 64
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
11-91 |
1.97e-07 |
|
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: 52.41 E-value: 1.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 11 ETKPLEARAALTPTTVKKLIAKGFKIYVEDSP--QSTFNINEYRQAGAIIV--PAGSWKTAPrdrIIIGLKEmPETDTFP 86
Cdd:cd05305 8 EIKNQENRVALTPAGVAELVAAGHEVLVEKGAglGSGFSDEEYSEAGAEIVptAEEVWAKAD---LIVKVKE-PLPEEYD 83
|
....*
gi 766281585 87 LVHEH 91
Cdd:cd05305 84 LLREG 88
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
12-345 |
5.04e-06 |
|
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: 47.61 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 12 TKPLEARAALTPTTVKKlIAKGFKIYVEDSPQSTFNIN--EYRQAGAIIVPAGSwKTAPRDrIIIGLKeMPETDTFPLVH 89
Cdd:cd12181 9 NKENEKRVPLLPADLER-IPLREQLYFEEGYGERLGISdeEYAALGAGIVSREE-ILAKCD-VICDPK-PGDADYLEILE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 90 EHIQF--AHCYKDQagwqNVLMRFIKGHGTLYDLE--FLENDQGRRVaafgFY-----AGFAGaalgVRDwAFKQTHSDd 160
Cdd:cd12181 85 GQILWgwVHCVQDK----EITQLAIDKKLTLIAWEdmFEWSKIGRHV----FYknnelAGYAA----VLH-ALQLYGIT- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 161 edlpavsPYPNEKALVkdvtkdykealatgarkptvLIIGALGRcgsGAIDLLHKvGIPDANILkwdikeTSRGGPF--D 238
Cdd:cd12181 151 -------PYRQTKVAV--------------------LGFGNTAR---GAIRALKL-GGADVTVY------TRRTEALfkE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 766281585 239 EIPQADIFINCIY--LSKPIaPFTNMEKLnnpnRRLRT---VVDVSADTTNphnpipiytvATVFNKPTvlvpTTAGPKL 313
Cdd:cd12181 194 ELSEYDIIVNCILqdTDRPD-HIIYEEDL----KRLKPgalIIDVSCDEGM----------GIEFAKPT----TFDDPIY 254
|
330 340 350
....*....|....*....|....*....|....*..
gi 766281585 314 SVISI-----DHLPSLLPREASEFFSHDLLPSLELLP 345
Cdd:cd12181 255 KVDGIdyyavDHTPSLFYRSASRSISKALAPYLDTVI 291
|
|
| Ald |
COG0686 |
Alanine dehydrogenase (includes sporulation protein SpoVN) [Amino acid transport and ... |
11-78 |
8.54e-06 |
|
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: 47.31 E-value: 8.54e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 766281585 11 ETKPLEARAALTPTTVKKLIAKGFKIYVEDSP--QSTFNINEYRQAGAIIVPAGS--WKTAPrdrIIIGLKE 78
Cdd:COG0686 8 EIKNNENRVALTPAGVRELVAAGHEVLVETGAglGSGFSDEDYSAAGAEIVDTAEevFAQAD---LIVKVKE 76
|
|
| |
