|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
10-1064 |
0e+00 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 1947.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 10 KKLGNGVVGILAETVNKWERRTPLTPSHCARLLHGGKDrTGISRIVVQPSAKRIHHDALYEDVGCEISDDLSDCGLILGI 89
Cdd:PLN02819 1 MKLGNGVVGILAETVNKWERRAPLTPSHCARLLHSGKD-RTVSRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 90 KQPELEMILPERAYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLS 169
Cdd:PLN02819 80 KQPKLEMLLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 170 LGYSTPFLSLGASYMYSSLAAAKAAVISVGEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPHTFVEPSKLPELf 249
Cdd:PLN02819 160 LGYSTPFLSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPEL- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 250 vkdKGISQNGISTKRVYQVYGCIITSQDMVEHKDPSKSFDKADYYAHPEHYNPVFHEKISPYTSVLVNCMYWEKRFPCLL 329
Cdd:PLN02819 239 ---KGISQNKISTKRVYQVYGCVVTSQDMVEHKDPSKQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 330 STKQLQDLTKK-GLPLVGICDITCDIGGSIEFVNRATLIDSPFFRFNPSNNSYYDDMDGDGVLCMAVDILPTEFAKEASQ 408
Cdd:PLN02819 316 TTKQLQDLTRKgGCPLVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEASQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 409 HFGDILSGFVGSLASMTEISDLPAHLKRACISYRGELTSLYEYIPRMRKSNPEEAQDNIIangvsSQRTFNILVSLSGHL 488
Cdd:PLN02819 396 HFGNILSPFVGSLASMKELAELPSHLRRACIAHRGSLTPLFEYIPRMRNSNAELAQDTVS-----SQSTFNILVSLSGHL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 489 FDKFLINEALDMIEAAGGSFHLAKCELGQSADAESYSELEVGADDKRVLDQIIDSLTRLANPNEDYISPHREANKISLKI 568
Cdd:PLN02819 471 FDKFLINEALDVIEAAGGSFHLAKCQVGQSADAESYSELEVGADDKEVLDQIIDSLTRLANPNEDYISPAREANKIFLKI 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 569 GKVQQENEIKEKPEMTKKS-GVLILGAGRVCRPAADFLASVRTIssqqwykTYFGADSEEKTDVHVIVASLYLKDAKETV 647
Cdd:PLN02819 551 GKVQQENECNEKAEVTKKSqNVLILGAGRVCRPAAEYLASVKTI-------SYYGDDSEEPTDVHVIVASLYLKDAKETV 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 648 EGISDVEAVRLDVSDSESLLKYVSQVDVVLSLLPASCHAVVAKTCIELKKHLVTASYVDDETSMLHEKAKSAGITILGEM 727
Cdd:PLN02819 624 EGIENAEAVQLDVSDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEM 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 728 GLDPGIDHMMAMKMINDAHIKKGKVKSFTSYCGGLPSPAAANNPLAYKFSWNPAGAIRAGQNPAKYKSNGDIIHVDGKNL 807
Cdd:PLN02819 704 GLDPGIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGENL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 808 YDSAARFRVPNLPAFALECFPNRDSLVYGEHYGIESEATTIFRGTLRYEGFSMIMATLSKLGFFDSEANQVLSTGKRITF 887
Cdd:PLN02819 784 FASAVRFRLPNLPAFALECLPNRDSLVYGELYGIEKEAATIFRGTLRYEGFSMIMATLSKLGLFDSENHPLLSTGKRTTY 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 888 GALLSNILNKDADNESEPLAGEEEISKRIIKLGHSK--ETAAKAAKTIVFLGFNEEREVPSLCKSVFDATCYLMEEKLAY 965
Cdd:PLN02819 864 GALLDALLLQDGHNENGPLAGEEEISKRLAKLGHSKnrETAAKAAKTIVFLGLDEETEVPKSCKSIFDVTCYRMEEKLAY 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 966 SGNEQDMVLLHHEVEVEFLESKRIEKHTATLLEFGDIKNGQTTTAMAKTVGIPAAIGALLLIEDKIKTRGVLRPLEAEVY 1045
Cdd:PLN02819 944 SGNEQDMVLLHHEVEVEFPDSKRIEKHSATLLEFGEIKNGRTTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVY 1023
|
1050
....*....|....*....
gi 18418158 1046 LPALDILQAYGIKLMEKAE 1064
Cdd:PLN02819 1024 VPALEILQAYGIKLMEKVE 1042
|
|
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
16-456 |
0e+00 |
|
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: 695.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 16 VVGILAETVNKWERRTPLTPSHCARLLHGGkdrtGIsRIVVQPSAKRIHHDALYEDVGCEISDDLSDCGLILGIKQPELE 95
Cdd:cd12189 1 VIGIRREDKNIWERRAPLTPSHVRELVKKP----GV-KVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 96 MILPERAYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLSLGYSTP 175
Cdd:cd12189 76 KLLPDKTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 176 FLSLGASYMYSSLAAAKAAVISVGEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPHTFVEPSKLPELfvKDKGI 255
Cdd:cd12189 156 FLHIGRAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPEL--AKSGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 256 SQNGIstkrvyqvYGCIITSQDMVEHKDPSKsFDKADYYAHPEHYNPVFHEKISPYTSVLVNCMYWEKRFPCLLSTKQLQ 335
Cdd:cd12189 234 DRNKV--------YGCVVTPEDYLERKDGGP-FDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 336 DLTKK---GLPLVGICDITCDIGGSIEFVNRATLIDSPFFRFNPSNNSYYDDMDGDGVLCMAVDILPTEFAKEASQHFGD 412
Cdd:cd12189 305 ALLRPpagPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGD 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 18418158 413 ILSGFVGSLASM-----TEISDLPAHLKRACISYRGELTSLYEYIPRMR 456
Cdd:cd12189 385 ALLPYVPDLAKSdaskpLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
|
|
| Sacchrp_dh_C |
pfam16653 |
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
728-1057 |
1.98e-88 |
|
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Pssm-ID: 465219 Cd Length: 255 Bit Score: 284.57 E-value: 1.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 728 GLDPGIDHMMAMKMINDAHIKKGKVKSFTSYCGGLPSPAAANNPLAYKFSWNPAGAIRAGQNPAKYKSNGDIIHVDGKNL 807
Cdd:pfam16653 1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 808 YDsaarfRVPNLPAFALECFPNRDSLVYGEHYGIeSEATTIFRGTLRYEGFSMIMATLSKLGFFDSeanqvlstgkritf 887
Cdd:pfam16653 81 ME-----PIYIRPGFAFEGYPNRDSLPHEELYSL-PEAKTLYRGTLRYPGFDEAIKSLVELGLLSE-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 888 gallsnilnkdadneseplagEEEISKRIIKLGhsketaakaaktivflgfneerevpslckSVFDATCYLMEEKLAYSG 967
Cdd:pfam16653 141 ---------------------EPKVSLEWLLFS-----------------------------GPLDVLAALLEDKLSLGP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 968 NEQDMVLLHHEVeveflESKRIEKHTATLLEFGDIKNGqTTTAMAKTVGIPAAIGALLLIEDKIKTRGVLRPLE-AEVYL 1046
Cdd:pfam16653 171 GERDMVVLQHEF-----DGKKGERRTYTLVDYGDHEEV-GPSAMARTVGVPAAIAALLILDGKIKNKGVVNPEEdPEIYE 244
|
330
....*....|.
gi 18418158 1047 PALDILQAYGI 1057
Cdd:pfam16653 245 PFLEELEKRGI 255
|
|
| Lys9 |
COG1748 |
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
632-1062 |
1.24e-68 |
|
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441354 [Multi-domain] Cd Length: 352 Bit Score: 233.96 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 632 HVIVASLYLKDAKETVEGISDVEAVRLDVSDSESLLKYVSQVDVVLSLLPASCHAVVAKTCIELKKHLVTASYVDDETSM 711
Cdd:COG1748 2 EVTLADRSLEKAEALAASGPKVEAAQLDASDPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 712 ---LHEKAKSAGITILGEMGLDPGIDHMMAMKMINdaHIKkgKVKSFTSYCGGLPSPaaANNPLAYKFSWNPAGAIRAGQ 788
Cdd:COG1748 82 klaLDELAKEAGVTAIPGCGLAPGLSNVLAAYAAD--RFD--EIDSIDIRVGGLPGY--PSNPLNYGTTWSPEGVIREYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 789 NPAKYKSNGDIIHVDGknlYDSAARFRVPNLPAFalECFPNRDSLVY-GEHYGiesEATTIFRGTLRYEGFSMIMATLSK 867
Cdd:COG1748 156 NPARAIEDGKWVEVPP---LSERETIDFPGVGRY--EAYNTDGELETlPETYP---GVKTVRFKTGRYPGHLNHLKVLVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 868 LGFFDseanqvlstgkritfgallsnilnkdadneseplageeeiskriiklghsketaakaaktivflgfNEEREVPSL 947
Cdd:COG1748 228 LGLTD------------------------------------------------------------------DEPVEVEGV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 948 CKSVFDATCYLMEEKLAYSGNEQDMVLLHheVEVEFLESKRIEKHTATLLEFGDikNGQTTTAMAKTVGIPAAIGALLLI 1027
Cdd:COG1748 242 EVSPRDVLKAILPDPLPLGPTDKDVVVIG--VVVKGTKDGKRETYVYNLVDHED--AETGSTAMAYTTGVPAAIAAELLL 317
|
410 420 430
....*....|....*....|....*....|....*.
gi 18418158 1028 EDKIKTRGVLRPLeaEVYL-PALDILQAYGIKLMEK 1062
Cdd:COG1748 318 EGKIPKPGVVNPE--QLDPdPFLEELAKRGIPIEEE 351
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
18-152 |
1.44e-23 |
|
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: 97.10 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 18 GILAETVNkWERRTPLTPSHCARLLHGGkdrtgiSRIVVQPSA--KRIHHDALYEDVGCEISDD---LSDCGLILGIKQP 92
Cdd:smart01003 1 GVPKEIKP-GERRVALTPAGVKKLVKLG------HEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18418158 93 EL-EMILPERAYAFFSHTHKAQkeNMPLLDKILSERVTLCDYELIVGDH-GKRLLAFGKYAG 152
Cdd:smart01003 74 SPeELALLREGQILFGYLHPAA--NPELLEALAAKGVTAIAYETVPRISrAQSLDALSSMAE 133
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
10-1064 |
0e+00 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 1947.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 10 KKLGNGVVGILAETVNKWERRTPLTPSHCARLLHGGKDrTGISRIVVQPSAKRIHHDALYEDVGCEISDDLSDCGLILGI 89
Cdd:PLN02819 1 MKLGNGVVGILAETVNKWERRAPLTPSHCARLLHSGKD-RTVSRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 90 KQPELEMILPERAYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLS 169
Cdd:PLN02819 80 KQPKLEMLLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 170 LGYSTPFLSLGASYMYSSLAAAKAAVISVGEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPHTFVEPSKLPELf 249
Cdd:PLN02819 160 LGYSTPFLSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPEL- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 250 vkdKGISQNGISTKRVYQVYGCIITSQDMVEHKDPSKSFDKADYYAHPEHYNPVFHEKISPYTSVLVNCMYWEKRFPCLL 329
Cdd:PLN02819 239 ---KGISQNKISTKRVYQVYGCVVTSQDMVEHKDPSKQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 330 STKQLQDLTKK-GLPLVGICDITCDIGGSIEFVNRATLIDSPFFRFNPSNNSYYDDMDGDGVLCMAVDILPTEFAKEASQ 408
Cdd:PLN02819 316 TTKQLQDLTRKgGCPLVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEASQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 409 HFGDILSGFVGSLASMTEISDLPAHLKRACISYRGELTSLYEYIPRMRKSNPEEAQDNIIangvsSQRTFNILVSLSGHL 488
Cdd:PLN02819 396 HFGNILSPFVGSLASMKELAELPSHLRRACIAHRGSLTPLFEYIPRMRNSNAELAQDTVS-----SQSTFNILVSLSGHL 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 489 FDKFLINEALDMIEAAGGSFHLAKCELGQSADAESYSELEVGADDKRVLDQIIDSLTRLANPNEDYISPHREANKISLKI 568
Cdd:PLN02819 471 FDKFLINEALDVIEAAGGSFHLAKCQVGQSADAESYSELEVGADDKEVLDQIIDSLTRLANPNEDYISPAREANKIFLKI 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 569 GKVQQENEIKEKPEMTKKS-GVLILGAGRVCRPAADFLASVRTIssqqwykTYFGADSEEKTDVHVIVASLYLKDAKETV 647
Cdd:PLN02819 551 GKVQQENECNEKAEVTKKSqNVLILGAGRVCRPAAEYLASVKTI-------SYYGDDSEEPTDVHVIVASLYLKDAKETV 623
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 648 EGISDVEAVRLDVSDSESLLKYVSQVDVVLSLLPASCHAVVAKTCIELKKHLVTASYVDDETSMLHEKAKSAGITILGEM 727
Cdd:PLN02819 624 EGIENAEAVQLDVSDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEM 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 728 GLDPGIDHMMAMKMINDAHIKKGKVKSFTSYCGGLPSPAAANNPLAYKFSWNPAGAIRAGQNPAKYKSNGDIIHVDGKNL 807
Cdd:PLN02819 704 GLDPGIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGENL 783
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 808 YDSAARFRVPNLPAFALECFPNRDSLVYGEHYGIESEATTIFRGTLRYEGFSMIMATLSKLGFFDSEANQVLSTGKRITF 887
Cdd:PLN02819 784 FASAVRFRLPNLPAFALECLPNRDSLVYGELYGIEKEAATIFRGTLRYEGFSMIMATLSKLGLFDSENHPLLSTGKRTTY 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 888 GALLSNILNKDADNESEPLAGEEEISKRIIKLGHSK--ETAAKAAKTIVFLGFNEEREVPSLCKSVFDATCYLMEEKLAY 965
Cdd:PLN02819 864 GALLDALLLQDGHNENGPLAGEEEISKRLAKLGHSKnrETAAKAAKTIVFLGLDEETEVPKSCKSIFDVTCYRMEEKLAY 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 966 SGNEQDMVLLHHEVEVEFLESKRIEKHTATLLEFGDIKNGQTTTAMAKTVGIPAAIGALLLIEDKIKTRGVLRPLEAEVY 1045
Cdd:PLN02819 944 SGNEQDMVLLHHEVEVEFPDSKRIEKHSATLLEFGEIKNGRTTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVY 1023
|
1050
....*....|....*....
gi 18418158 1046 LPALDILQAYGIKLMEKAE 1064
Cdd:PLN02819 1024 VPALEILQAYGIKLMEKVE 1042
|
|
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
16-456 |
0e+00 |
|
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: 695.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 16 VVGILAETVNKWERRTPLTPSHCARLLHGGkdrtGIsRIVVQPSAKRIHHDALYEDVGCEISDDLSDCGLILGIKQPELE 95
Cdd:cd12189 1 VIGIRREDKNIWERRAPLTPSHVRELVKKP----GV-KVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPID 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 96 MILPERAYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLSLGYSTP 175
Cdd:cd12189 76 KLLPDKTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 176 FLSLGASYMYSSLAAAKAAVISVGEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPHTFVEPSKLPELfvKDKGI 255
Cdd:cd12189 156 FLHIGRAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPEL--AKSGA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 256 SQNGIstkrvyqvYGCIITSQDMVEHKDPSKsFDKADYYAHPEHYNPVFHEKISPYTSVLVNCMYWEKRFPCLLSTKQLQ 335
Cdd:cd12189 234 DRNKV--------YGCVVTPEDYLERKDGGP-FDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 336 DLTKK---GLPLVGICDITCDIGGSIEFVNRATLIDSPFFRFNPSNNSYYDDMDGDGVLCMAVDILPTEFAKEASQHFGD 412
Cdd:cd12189 305 ALLRPpagPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGD 384
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 18418158 413 ILSGFVGSLASM-----TEISDLPAHLKRACISYRGELTSLYEYIPRMR 456
Cdd:cd12189 385 ALLPYVPDLAKSdaskpLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
16-421 |
6.95e-134 |
|
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: 407.39 E-value: 6.95e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 16 VVGILAETVNKWERRTPLTPSHCARLLHGGKDrtgiSRIVVQPSAKRIHHDALYEDVGCEISDDLSDCGLILGIKQPELE 95
Cdd:cd05199 1 KIGIIREGKTPPDRRVPLTPEQCKELQAKYPG----VEIFVQPSPVRCFKDEEYRAAGIEVVEDLSDCDILLGVKEVPIE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 96 MILPERAYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLSLGYSTP 175
Cdd:cd05199 77 QLIPNKTYFFFSHTIKKQPYNRKLLQTILEKNITLIDYEVLVDEQGKRVIAFGRYAGIVGAYNGLRAYGKKTGLFDLKRA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 176 FLSLGAsymysslaaakaavisvgEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPHTFVEPSKLPElfvkdkgi 255
Cdd:cd05199 157 HECSDL------------------EELIAELKKVGLPPPKIVITGSGRVGSGAAEVLKALGIKEVSPEDFLT-------- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 256 sqngistkrvyqvygciitsqdmvehkdpsksfdkadyyahpehynpvfhekispYTSVLVNCMYWEKRFPCLLStkqLQ 335
Cdd:cd05199 211 -------------------------------------------------------VADILINGHYWDKRAPRLFT---KE 232
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 336 DLTKKGLPLVGICDITCDIGGSIEFVNRATLIDSPFFRFNPSNNSYYDDMDGDGVLCMAVDILPTEFAKEASQHFGDILS 415
Cdd:cd05199 233 DLKKPDFKIRVIADVTCDIHGSIPSTLRASTIADPVYDYDPTTNKEVAFSSPDSITVMAVDNLPCELPRDASEDFGEQLI 312
|
....*.
gi 18418158 416 GFVGSL 421
Cdd:cd05199 313 KSVLPE 318
|
|
| Sacchrp_dh_C |
pfam16653 |
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
728-1057 |
1.98e-88 |
|
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Pssm-ID: 465219 Cd Length: 255 Bit Score: 284.57 E-value: 1.98e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 728 GLDPGIDHMMAMKMINDAHIKKGKVKSFTSYCGGLPSPAAANNPLAYKFSWNPAGAIRAGQNPAKYKSNGDIIHVDGKNL 807
Cdd:pfam16653 1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 808 YDsaarfRVPNLPAFALECFPNRDSLVYGEHYGIeSEATTIFRGTLRYEGFSMIMATLSKLGFFDSeanqvlstgkritf 887
Cdd:pfam16653 81 ME-----PIYIRPGFAFEGYPNRDSLPHEELYSL-PEAKTLYRGTLRYPGFDEAIKSLVELGLLSE-------------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 888 gallsnilnkdadneseplagEEEISKRIIKLGhsketaakaaktivflgfneerevpslckSVFDATCYLMEEKLAYSG 967
Cdd:pfam16653 141 ---------------------EPKVSLEWLLFS-----------------------------GPLDVLAALLEDKLSLGP 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 968 NEQDMVLLHHEVeveflESKRIEKHTATLLEFGDIKNGqTTTAMAKTVGIPAAIGALLLIEDKIKTRGVLRPLE-AEVYL 1046
Cdd:pfam16653 171 GERDMVVLQHEF-----DGKKGERRTYTLVDYGDHEEV-GPSAMARTVGVPAAIAALLILDGKIKNKGVVNPEEdPEIYE 244
|
330
....*....|.
gi 18418158 1047 PALDILQAYGI 1057
Cdd:pfam16653 245 PFLEELEKRGI 255
|
|
| Lys9 |
COG1748 |
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
632-1062 |
1.24e-68 |
|
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine dehydrogenase, NADP-dependent is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 441354 [Multi-domain] Cd Length: 352 Bit Score: 233.96 E-value: 1.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 632 HVIVASLYLKDAKETVEGISDVEAVRLDVSDSESLLKYVSQVDVVLSLLPASCHAVVAKTCIELKKHLVTASYVDDETSM 711
Cdd:COG1748 2 EVTLADRSLEKAEALAASGPKVEAAQLDASDPEALAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 712 ---LHEKAKSAGITILGEMGLDPGIDHMMAMKMINdaHIKkgKVKSFTSYCGGLPSPaaANNPLAYKFSWNPAGAIRAGQ 788
Cdd:COG1748 82 klaLDELAKEAGVTAIPGCGLAPGLSNVLAAYAAD--RFD--EIDSIDIRVGGLPGY--PSNPLNYGTTWSPEGVIREYT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 789 NPAKYKSNGDIIHVDGknlYDSAARFRVPNLPAFalECFPNRDSLVY-GEHYGiesEATTIFRGTLRYEGFSMIMATLSK 867
Cdd:COG1748 156 NPARAIEDGKWVEVPP---LSERETIDFPGVGRY--EAYNTDGELETlPETYP---GVKTVRFKTGRYPGHLNHLKVLVD 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 868 LGFFDseanqvlstgkritfgallsnilnkdadneseplageeeiskriiklghsketaakaaktivflgfNEEREVPSL 947
Cdd:COG1748 228 LGLTD------------------------------------------------------------------DEPVEVEGV 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 948 CKSVFDATCYLMEEKLAYSGNEQDMVLLHheVEVEFLESKRIEKHTATLLEFGDikNGQTTTAMAKTVGIPAAIGALLLI 1027
Cdd:COG1748 242 EVSPRDVLKAILPDPLPLGPTDKDVVVIG--VVVKGTKDGKRETYVYNLVDHED--AETGSTAMAYTTGVPAAIAAELLL 317
|
410 420 430
....*....|....*....|....*....|....*.
gi 18418158 1028 EDKIKTRGVLRPLeaEVYL-PALDILQAYGIKLMEK 1062
Cdd:COG1748 318 EGKIPKPGVVNPE--QLDPdPFLEELAKRGIPIEEE 351
|
|
| SDH_N_domain |
cd12144 |
Saccharopine dehydrogenase N-terminal domain; SDH N-terminal domain is named due to its ... |
480-600 |
1.58e-35 |
|
Saccharopine dehydrogenase N-terminal domain; SDH N-terminal domain is named due to its appearance at the N-terminal of SDH in eukaryotes, but can be found C-terminal of the SDH-like domain in other enzymes, such as the bifunctional lysine ketoglutarate reductase/saccharopine dehydrogenase enzyme. 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 a related structure.
Pssm-ID: 213387 [Multi-domain] Cd Length: 114 Bit Score: 130.73 E-value: 1.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 480 ILVSLSGHLFDKFLINEALDMIEAAGGSFHLAKCELGQSADAESYSELEVGADDKRVLDQIIDSLTRLANPNEDyiSPHR 559
Cdd:cd12144 1 REVELEGHLIDSGLLNKVLDLIEDAGGDFEILECDVGKSKDDPSYARLEVSADDEEHLDRILDELTSLGAVLVD--SADA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 18418158 560 EANKISLKigKVQQENEIKEKPEMTKksgVLILGAGRVCRP 600
Cdd:cd12144 79 ELEPAPKD--GVLPDGFYSTTNHPTQ---VRLDGEWIVVEN 114
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
18-154 |
1.07e-27 |
|
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: 109.05 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 18 GILAETVNkWERRTPLTPSHCARLLHGGkdrtgiSRIVVQPSA--KRIHHDALYEDVGCEISD----DLSDCGLILGIKQ 91
Cdd:pfam05222 1 GVPKEIKP-GERRVALTPAGVKKLVKLG------HEVLVESGAglGAGFSDEAYEAAGAEIVDtaaeVWAEADLILKVKE 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18418158 92 P---ELEMILPERAYAFFSHTHkaqkENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRA 154
Cdd:pfam05222 74 PqpeEYALLREGQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| Saccharop_dh_N |
pfam04455 |
LOR/SDH bifunctional enzyme conserved region; Lysine-oxoglutarate reductase/Saccharopine ... |
479-552 |
1.41e-25 |
|
LOR/SDH bifunctional enzyme conserved region; Lysine-oxoglutarate reductase/Saccharopine dehydrogenase (LOR/SDH) is a bifunctional enzyme. This conserved region is commonly found immediately N-terminal to Saccharop_dh (pfam03435) in eukaryotes.
Pssm-ID: 427960 [Multi-domain] Cd Length: 93 Bit Score: 101.37 E-value: 1.41e-25
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18418158 479 NILVSLSGHLFDKFLINEALDMIEAAGGSFHLAKCELGQSADAESYSELEVGADDKRVLDQIIDSLTRL-ANPNE 552
Cdd:pfam04455 1 SREVELEGHLIDSGILNRVLDLIMDMGGSFEILEFDVGKRKDDPSYARLEVSAPDEEVLDRILDELIDLgANLPE 75
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
18-152 |
1.44e-23 |
|
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: 97.10 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 18 GILAETVNkWERRTPLTPSHCARLLHGGkdrtgiSRIVVQPSA--KRIHHDALYEDVGCEISDD---LSDCGLILGIKQP 92
Cdd:smart01003 1 GVPKEIKP-GERRVALTPAGVKKLVKLG------HEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEP 73
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18418158 93 EL-EMILPERAYAFFSHTHKAQkeNMPLLDKILSERVTLCDYELIVGDH-GKRLLAFGKYAG 152
Cdd:smart01003 74 SPeELALLREGQILFGYLHPAA--NPELLEALAAKGVTAIAYETVPRISrAQSLDALSSMAE 133
|
|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
28-410 |
1.13e-22 |
|
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: 100.77 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 28 ERRTPLTPSHCARLLHGGkdrtgiSRIVVQPSAKRIHHDALYEDVGCEISDDLS------DCgLILGIKQ-PELEMILPE 100
Cdd:cd12188 13 ERRTALTPTTAKKLLDAG------FKVTVERSPQRIFPDEEYEAVGCELVPAGSwvnapkDA-IILGLKElPEDTFPLPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 101 RaYAFFSHTHKAQKENMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDFLHGLGQRYLSlgySTPFLSLg 180
Cdd:cd12188 86 R-HIYFAHAYKGQAGWKDVLSRFARGGGTLLDLEYLVDDDGRRVAAFGYWAGFAGAALGLLAWAHQQLG---PVTLPPV- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 181 asymySSLAAAKAAVISVGEEIASQGLPlgicPLVFVFTGTGNVSLGAQEIFKLLphtfvepsklpelfvkdkgisqngi 260
Cdd:cd12188 161 -----SPYPNEEALVADVKKALATGGRK----PRALVIGALGRCGSGAVDLLEAA------------------------- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 261 stkrvyqvyGCIITSQDMVEHKdpsKSFDKADYYAHpehynpvfhekispytSVLVNCMYWEKRFPCLLSTKQLQDLTKK 340
Cdd:cd12188 207 ---------GIEVTKWDMAETK---AGGPFPEILDH----------------DIFVNCIYLSKPIPPFLTPEMLQAPGRR 258
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18418158 341 glpLVGICDITCDIGGS---IEFVNRATLIDSPFFRFNPSNNSyyddmdgdgVLCMAVDILPTEFAKEASQHF 410
Cdd:cd12188 259 ---LRVIGDVSCDPTNPynpIPIYDVATTFDKPTLRVPTGGPP---------LDVIAIDHLPSLLPRESSEDF 319
|
|
| Sacchrp_dh_NADP |
pfam03435 |
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
589-724 |
4.28e-21 |
|
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain of saccharopine dehydrogenase. In some organizms this enzyme is found as a bifunctional polypeptide with lysine ketoglutarate reductase. The saccharopine dehydrogenase can also function as a saccharopine reductase.
Pssm-ID: 397480 [Multi-domain] Cd Length: 120 Bit Score: 89.57 E-value: 4.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 589 VLILGAGRVCRPAADFLASVRTISsqqwyktyfgadseektdvHVIVASLYLKDAKETVEGISD--VEAVRLDVSDSESL 666
Cdd:pfam03435 1 VLIIGAGSVGQGVAPLLARHFDVD-------------------RITVADRTLEKAQALAAKLGGvrFIAVAVDADNYEAV 61
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 18418158 667 L-KYVSQVDVVLSLLPASCHAVVAKTCIELKKHLVTASYVDDETSMLHEKAKSAGITIL 724
Cdd:pfam03435 62 LaALLKEGDLVVNLSPPTLSLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
194-372 |
3.53e-18 |
|
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: 82.17 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 194 AVISVGEEIASQGLPLGICPLVFVFTGTGNVSLGAQEIFKLLPH----TFVEPSKLpelfvkdkgisqngistKRVYQVY 269
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAevtvLDVRPARL-----------------RQLESLL 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 270 GCIITSQdmvehkdpsksfdkadyyahpeHYNPVFHEKISPYTSVLVNCMYWE-KRFPCLLSTKQLQDLtKKGlplVGIC 348
Cdd:smart01002 64 GARFTTL----------------------YSQAELLEEAVKEADLVIGAVLIPgAKAPKLVTREMVKSM-KPG---SVIV 117
|
170 180
....*....|....*....|....
gi 18418158 349 DITCDIGGSIEFvNRATLIDSPFF 372
Cdd:smart01002 118 DVAADQGGCIET-SRPTTHDDPTY 140
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
17-411 |
3.12e-10 |
|
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: 62.81 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 17 VGILAETVNKwERRTPLTPSHCARLLHGGKDrtgisrIVVQPSA--KRIHHDALYEDVGCEI----SDDLSDCGLILGIK 90
Cdd:cd01620 2 LGFPKETKNN-EFRVALTPSFVKKLVANGFK------VYIETGAgsGAGFSDEDYLQAGAQIvpaaSKEAYSADIIVKLK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 91 QPELEMILPERAYA-FFSHTHKAQkeNMPLLDKILSERVTLCDYELIVGDHGKRLLAFGKYAGRAGLVDflhglgqryls 169
Cdd:cd01620 75 EPEFAEYDLIKKGQlLVTFLHAAT--NRGVVEVLMRKKLTAYALEDLENDFRPRLAPNSNIAGYAGVQL----------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 170 lGYStpFLSLGASYMYSSLAAAKAAVISVgeeiasqglplgicplvfvfTGTGNVSLGAQEIFKLlphtfvepsklpelf 249
Cdd:cd01620 142 -GAY--ELARIQGGRMGGAGGVPPAKVLI--------------------IGAGVVGLGAAKIAKK--------------- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 250 vkdkgisqngistkrvyqvYGCIITSQDMvehKDPSKSFDKADYYAHPEHYNPVFHEKISPYTSVLVNCMYWEKRFPCLL 329
Cdd:cd01620 184 -------------------LGANVLVYDI---KEEKLKGVETLGGSRLRYSQKEELEKELKQTDILINAILVDGPRAPIL 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 330 STKQLQDLTKKGLPLVgicDITCDIGGSIEfVNRATLIDSPFFrfnpsnnsyyddmDGDGVLCMAVDILPTEFAKEASQH 409
Cdd:cd01620 242 IMEELVGPMKRGAVIV---DLAADQGGNDE-TSIPTTEGVPTY-------------EVDGVVIYGVDNMPSLVPREASEL 304
|
..
gi 18418158 410 FG 411
Cdd:cd01620 305 LS 306
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
16-136 |
1.86e-06 |
|
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: 51.25 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 16 VVGILAETVNKwERRTPLTPSHCARLLHGGKDrtgisrIVVQPSA-KRIH-HDALYEDVGCEISDD---LSDCGLILGIK 90
Cdd:cd05304 2 TIGVPKETAPG-ERRVALTPETVKKLVKLGFE------VLVESGAgEAAGfSDEAYEEAGAEIVSDaeeLAQADIVLKVR 74
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 18418158 91 QPELEMI--LPERAYaFFSHTHKAQkeNMPLLDKILSERVTLCDYELI 136
Cdd:cd05304 75 PPSEEEValLKEGAV-LIGFLDPAQ--NPELVEALAKKGVTAFAMELV 119
|
|
| ceo_syn |
cd12181 |
N(5)-(carboxyethyl)ornithine synthase; N(5)-(carboxyethyl)ornithine synthase (ceo_syn) ... |
28-421 |
1.22e-05 |
|
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: 48.38 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 28 ERRTPLTPSHCARLLH--------GGKDRTGISrivvqpsakrihhDALYEDVGCEI---SDDLSDCGLILGIK--QPEL 94
Cdd:cd12181 13 EKRVPLLPADLERIPLreqlyfeeGYGERLGIS-------------DEEYAALGAGIvsrEEILAKCDVICDPKpgDADY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 95 EMILPERAyaFFSHTHKAQKENMplLDKILSERVTLCDYELIVGDHGKRLLAFGK---YAGRAGLvdfLHGLgQRYLSLG 171
Cdd:cd12181 80 LEILEGQI--LWGWVHCVQDKEI--TQLAIDKKLTLIAWEDMFEWSKIGRHVFYKnneLAGYAAV---LHAL-QLYGITP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 172 YSTpflslgasymysslaaAKAAVIsvgeeiasqglplgicplvfvftGTGNVSLGAQEIFKLlphtfvepsklpelfvk 251
Cdd:cd12181 152 YRQ----------------TKVAVL-----------------------GFGNTARGAIRALKL----------------- 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 252 dkgisqnGISTKRVYqvygciitsqdmvehkdpsksfdkadyYAHPEHynpVFHEKISPYtSVLVNCMYWEKRFPCLLST 331
Cdd:cd12181 176 -------GGADVTVY---------------------------TRRTEA---LFKEELSEY-DIIVNCILQDTDRPDHIIY 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 332 KQLQDLTKKGLPLVgicDITCDIGGSIEFvNRATLIDSPFFRFnpsnnsyyddmdgDGVLCMAVDILPTEFAKEASQHFG 411
Cdd:cd12181 218 EEDLKRLKPGALII---DVSCDEGMGIEF-AKPTTFDDPIYKV-------------DGIDYYAVDHTPSLFYRSASRSIS 280
|
410
....*....|
gi 18418158 412 DILSGFVGSL 421
Cdd:cd12181 281 KALAPYLDTV 290
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
17-142 |
7.62e-04 |
|
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: 43.16 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18418158 17 VGILAETVNKwERRTPLTPSHCARLLHGGKdrtgisRIVVQPSA-KRIH-HDALYEDVGCEISDDL----SDCGLILGIK 90
Cdd:cd05305 3 IGIPKEIKNQ-ENRVALTPAGVAELVAAGH------EVLVEKGAgLGSGfSDEEYSEAGAEIVPTAeevwAKADLIVKVK 75
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 18418158 91 QPelemILPERAY-----AFFSHTH-KAQKEnmpLLDKILSERVTLCDYELIVGDHGK 142
Cdd:cd05305 76 EP----LPEEYDLlregqILFTYLHlAADKE---LTEALLEKKVTAIAYETIEDEDGS 126
|
|
| |
