|
Name |
Accession |
Description |
Interval |
E-value |
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
25-466 |
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: 774.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 25 VMALRREDVNAWERRAPLAPKHIKGITKL-GYKVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEKLMSK 103
Cdd:cd12189 1 VIGIRREDKNIWERRAPLTPSHVRELVKKpGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 104 KTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHLG 183
Cdd:cd12189 81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 184 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVSKTG-DLRKVYG 262
Cdd:cd12189 161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 263 TVLSRHHHLVRKTDGVYDPVEYEKYPERYTSRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLVPvkssvvpvegc 342
Cdd:cd12189 241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 343 PELPHKLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPY 422
Cdd:cd12189 310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 31980703 423 VEEMLLSDASQPLESQNFSPVVRDAVITSNGLLTDKYKYIQKLR 466
Cdd:cd12189 390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
|
|
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
25-916 |
0e+00 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 719.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 25 VMALRREDVNAWERRAPLAPKHIKGITKLGY-----KVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEK 99
Cdd:PLN02819 7 VVGILAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGVKQPKLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 100 LMSKKTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPF 179
Cdd:PLN02819 87 LLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLSLGYSTPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 180 MHLGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVSK------ 253
Cdd:PLN02819 167 LSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPELKGisqnki 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 254 -TGDLRKVYGTVLSRHHHLVRKTDG-VYDPVEYEKYPERYTSRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLVP 331
Cdd:PLN02819 247 sTKRVYQVYGCVVTSQDMVEHKDPSkQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 332 VkssvvpveGCPelphkLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEA 411
Cdd:PLN02819 327 G--------GCP-----LVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 412 TEYFGDMLYPYVEEmlLSDASQPLEsqnFSPVVRDAVITSNGLLTDKYKYIQKLRESRERI------------------- 472
Cdd:PLN02819 394 SQHFGNILSPFVGS--LASMKELAE---LPSHLRRACIAHRGSLTPLFEYIPRMRNSNAELaqdtvssqstfnilvslsg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 473 ----QFL---------------------------SMSTKK---------------------------------------- 481
Cdd:PLN02819 469 hlfdKFLinealdvieaaggsfhlakcqvgqsadAESYSElevgaddkevldqiidsltrlanpnedyispareankifl 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 482 ----------------------KVLVLGSGYVSGPVLEYLSRDNNIEiTLGSDMTNQMQQ---LSKKY------------ 524
Cdd:PLN02819 549 kigkvqqenecnekaevtkksqNVLILGAGRVCRPAAEYLASVKTIS-YYGDDSEEPTDVhviVASLYlkdaketvegie 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 525 NINPVSLTVgKQEAKLQSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMKELEKSVDDAGITVIGELGLD 604
Cdd:PLN02819 628 NAEAVQLDV-SDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLD 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 605 PGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPASYLLNGKVVNVTGGvSFLN 684
Cdd:PLN02819 707 PGIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGE-NLFA 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 685 SVTP--MDYFPGLNLEGYPNRDSIKYAEIYGIS-SAHTLLRGTLRYKGYSKALNGFVKLGLINREAYPALRPEANPlTWK 761
Cdd:PLN02819 786 SAVRfrLPNLPAFALECLPNRDSLVYGELYGIEkEAATIFRGTLRYEGFSMIMATLSKLGLFDSENHPLLSTGKRT-TYG 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 762 QLLCDLV---GISRSSPC----EKLKEVVFTKLGGDN-TQLEAAE---WLGLLGDEQVPQA-ESIVDAFSKHLVSKLSYG 829
Cdd:PLN02819 865 ALLDALLlqdGHNENGPLageeEISKRLAKLGHSKNReTAAKAAKtivFLGLDEETEVPKScKSIFDVTCYRMEEKLAYS 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 830 PEEKDMIVMRDSFGIRHP-SGHLENKTIDLVVYGDF-NG--FSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPFTKEIYG 905
Cdd:PLN02819 945 GNEQDMVLLHHEVEVEFPdSKRIEKHSATLLEFGEIkNGrtTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVYV 1024
|
1050
....*....|.
gi 31980703 906 PILERIKAEGI 916
Cdd:PLN02819 1025 PALEILQAYGI 1035
|
|
| Sacchrp_dh_C |
pfam16653 |
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
602-916 |
3.09e-91 |
|
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: 289.58 E-value: 3.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 602 GLDPGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPASYLLNGKVVNVTGGVS 681
Cdd:pfam16653 1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 682 FlnsvTPMDYFPGLNLEGYPNRDSIKYAEIYGISSAHTLLRGTLRYKGYSKALNGFVKLGLINREAYPALrpeanpltwk 761
Cdd:pfam16653 81 M----EPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYPGFDEAIKSLVELGLLSEEPKVSL---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 762 qllcdlvgisrsspceklkevvftklggdntqleaaEWLGLlgdeqvpqaESIVDAFSKHLVSKLSYGPEEKDMIVMRDS 841
Cdd:pfam16653 147 ------------------------------------EWLLF---------SGPLDVLAALLEDKLSLGPGERDMVVLQHE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980703 842 FGIRHPsghlENKTIDLVVYGDF--NGFSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPF-TKEIYGPILERIKAEGI 916
Cdd:pfam16653 182 FDGKKG----ERRTYTLVDYGDHeeVGPSAMARTVGVPAAIAALLILDGKIKNKGVVNPEeDPEIYEPFLEELEKRGI 255
|
|
| Lys9 |
COG1748 |
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
506-921 |
1.93e-57 |
|
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: 201.22 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 506 EITLGSDMTNQMQQLSKKY-NINPVSLTVGKQEAkLQSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMK 584
Cdd:COG1748 2 EVTLADRSLEKAEALAASGpKVEAAQLDASDPEA-LAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 585 ---ELEKSVDDAGITVIGELGLDPGLDHMLAMETIDTAKElgatVESYVSYCGGLPAPEhsDNPLRYKFSWSPVGVLMNI 661
Cdd:COG1748 81 aklALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDE----IDSIDIRVGGLPGYP--SNPLNYGTTWSPEGVIREY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 662 MQPASYLLNGKVVnvtggvsflnSVTPMD-----YFPGL-NLEGYPNRDSIKY-AEIYGisSAHTLLRGTLRYKGYSKAL 734
Cdd:COG1748 155 TNPARAIEDGKWV----------EVPPLSeretiDFPGVgRYEAYNTDGELETlPETYP--GVKTVRFKTGRYPGHLNHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 735 NGFVKLGLINREAYPALRPEANPLtwkqllcdlvgisrsspceklkevvftklggdntqleaaewlgllgdeqvpqaesi 814
Cdd:COG1748 223 KVLVDLGLTDDEPVEVEGVEVSPR-------------------------------------------------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 815 vDAFSKHLVSKLSYGPEEKDMIVMRDSF-GIRHpsGHLENKTIDLVVYGDFN-GFSAMAKTVGLPTAMAAKMLLDGEIEA 892
Cdd:COG1748 247 -DVLKAILPDPLPLGPTDKDVVVIGVVVkGTKD--GKRETYVYNLVDHEDAEtGSTAMAYTTGVPAAIAAELLLEGKIPK 323
|
410 420 430
....*....|....*....|....*....|
gi 31980703 893 KGLMGPftKEIYG-PILERIKAEGIVFNTQ 921
Cdd:COG1748 324 PGVVNP--EQLDPdPFLEELAKRGIPIEEE 351
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
27-157 |
1.78e-30 |
|
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: 116.76 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 27 ALRREdVNAWERRAPLAPKHIKGITKLGYKVLIQPSN--RRAIHDKEYVRAGGILQ----EDITEACLILGVKRP--PEE 98
Cdd:pfam05222 1 GVPKE-IKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVdtaaEVWAEADLILKVKEPqpEEY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 99 KLMSK-KTYAFFSHTIkaqeANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVA 157
Cdd:pfam05222 80 ALLREgQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
27-155 |
2.39e-24 |
|
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: 99.41 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 27 ALRREDVNaWERRAPLAPKHIKGITKLGYKVLIQPSN--RRAIHDKEYVRAGGILQED---ITEACLILGVKRP-PEEKL 100
Cdd:smart01003 1 GVPKEIKP-GERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEPsPEELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 31980703 101 MSKKTYAFFSHtiKAQEANMNLLDEVLKQEIRLIDYEKMV-DHRGSRIVAFGQWAG 155
Cdd:smart01003 80 LLREGQILFGY--LHPAANPELLEALAAKGVTAIAYETVPrISRAQSLDALSSMAE 133
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
37-100 |
8.47e-05 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 8.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980703 37 ERRAPLAPKHIKGITKLGYKVLIQP--SNRRAIHDKEYVRAGG-ILQEDITEACLILGVKRPPEEKL 100
Cdd:COG3288 13 ERRVALTPETVKKLVKLGAEVLVESgaGLAAGFPDAAYEAAGAeIVDAELLGADIVLKVRPPSAEEL 79
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| LKR_SDH_like |
cd12189 |
bifunctional lysine ketoglutarate reductase /saccharopine dehydrogenase enzyme; Bifunctional ... |
25-466 |
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: 774.43 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 25 VMALRREDVNAWERRAPLAPKHIKGITKL-GYKVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEKLMSK 103
Cdd:cd12189 1 VIGIRREDKNIWERRAPLTPSHVRELVKKpGVKVLVQPSNRRAFPDQEYEAAGAIIQEDLSDADLILGVKEPPIDKLLPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 104 KTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPFMHLG 183
Cdd:cd12189 81 KTYAFFSHTIKAQPYNMPLLDAILEKNIRLIDYELIVDESGKRLVAFGWFAGVAGMIDILHGLGLRLLALGYSTPFLHIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 184 MAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVSKTG-DLRKVYG 262
Cdd:cd12189 161 RAYNYPSLEEAKQAVRDAGYEIALGGLPKSLGPLVFVFTGSGNVSQGAQEIFEELPHEYVEPSDLPELAKSGaDRNKVYG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 263 TVLSRHHHLVRKTDGVYDPVEYEKYPERYTSRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLVPvkssvvpvegc 342
Cdd:cd12189 241 CVVTPEDYLERKDGGPFDRADYYANPELYESVFHEKIAPYLSVLINGIYWDPRFPRLLTNEQLQALLRP----------- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 343 PELPHKLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPY 422
Cdd:cd12189 310 PAGPHRLLAIADISCDIGGSIEFLTKATTIDSPFYVYDPDTDKIHDSVSGDGILVMSVDNLPAELPREASEHFGDALLPY 389
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 31980703 423 VEEMLLSDASQPLESQNFSPVVRDAVITSNGLLTDKYKYIQKLR 466
Cdd:cd12189 390 VPDLAKSDASKPLEESELPPVLRRATIASNGKLTPKYEYIQELR 433
|
|
| PLN02819 |
PLN02819 |
lysine-ketoglutarate reductase/saccharopine dehydrogenase |
25-916 |
0e+00 |
|
lysine-ketoglutarate reductase/saccharopine dehydrogenase
Pssm-ID: 215439 [Multi-domain] Cd Length: 1042 Bit Score: 719.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 25 VMALRREDVNAWERRAPLAPKHIKGITKLGY-----KVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEK 99
Cdd:PLN02819 7 VVGILAETVNKWERRAPLTPSHCARLLHSGKdrtvsRIIVQPSSKRIHHDAQYEDVGCEISEDLSDCGLILGVKQPKLEM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 100 LMSKKTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRLLALGHHTPF 179
Cdd:PLN02819 87 LLPDRAYAFFSHTHKAQPENMPLLDKILEERVSLFDYELIVGDHGKRLVAFGKYAGRAGMIDFFRGLGQRLLSLGYSTPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 180 MHLGMAHNYRNSSQAVQAVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVSK------ 253
Cdd:PLN02819 167 LSLGSSYMYSSLAAAKAAVISVGEEIASSGLPLGICPLVFVFTGSGNVSQGAQEIFKLLPHTFVEPSKLPELKGisqnki 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 254 -TGDLRKVYGTVLSRHHHLVRKTDG-VYDPVEYEKYPERYTSRFNTDIAPYTTCLINGIYWEQNTPRLLTRQDAQSLLVP 331
Cdd:PLN02819 247 sTKRVYQVYGCVVTSQDMVEHKDPSkQFDKADYYAHPEHYNPVFHEKIAPYASVIVNCMYWEKRFPRLLTTKQLQDLTRK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 332 VkssvvpveGCPelphkLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEA 411
Cdd:PLN02819 327 G--------GCP-----LVGVCDITCDIGGSIEFLNKTTSIEKPFFRYNPSNNSYHDDMDGDGILCMAVDILPTEFAKEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 412 TEYFGDMLYPYVEEmlLSDASQPLEsqnFSPVVRDAVITSNGLLTDKYKYIQKLRESRERI------------------- 472
Cdd:PLN02819 394 SQHFGNILSPFVGS--LASMKELAE---LPSHLRRACIAHRGSLTPLFEYIPRMRNSNAELaqdtvssqstfnilvslsg 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 473 ----QFL---------------------------SMSTKK---------------------------------------- 481
Cdd:PLN02819 469 hlfdKFLinealdvieaaggsfhlakcqvgqsadAESYSElevgaddkevldqiidsltrlanpnedyispareankifl 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 482 ----------------------KVLVLGSGYVSGPVLEYLSRDNNIEiTLGSDMTNQMQQ---LSKKY------------ 524
Cdd:PLN02819 549 kigkvqqenecnekaevtkksqNVLILGAGRVCRPAAEYLASVKTIS-YYGDDSEEPTDVhviVASLYlkdaketvegie 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 525 NINPVSLTVgKQEAKLQSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMKELEKSVDDAGITVIGELGLD 604
Cdd:PLN02819 628 NAEAVQLDV-SDSESLLKYVSQVDVVISLLPASCHAVVAKACIELKKHLVTASYVSEEMSALDSKAKEAGITILCEMGLD 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 605 PGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPASYLLNGKVVNVTGGvSFLN 684
Cdd:PLN02819 707 PGIDHMMAMKMIDDAHERGGKVKSFTSYCGGLPSPEAANNPLAYKFSWNPAGAIKAGQNPAVYKSNGQIIHVDGE-NLFA 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 685 SVTP--MDYFPGLNLEGYPNRDSIKYAEIYGIS-SAHTLLRGTLRYKGYSKALNGFVKLGLINREAYPALRPEANPlTWK 761
Cdd:PLN02819 786 SAVRfrLPNLPAFALECLPNRDSLVYGELYGIEkEAATIFRGTLRYEGFSMIMATLSKLGLFDSENHPLLSTGKRT-TYG 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 762 QLLCDLV---GISRSSPC----EKLKEVVFTKLGGDN-TQLEAAE---WLGLLGDEQVPQA-ESIVDAFSKHLVSKLSYG 829
Cdd:PLN02819 865 ALLDALLlqdGHNENGPLageeEISKRLAKLGHSKNReTAAKAAKtivFLGLDEETEVPKScKSIFDVTCYRMEEKLAYS 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 830 PEEKDMIVMRDSFGIRHP-SGHLENKTIDLVVYGDF-NG--FSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPFTKEIYG 905
Cdd:PLN02819 945 GNEQDMVLLHHEVEVEFPdSKRIEKHSATLLEFGEIkNGrtTTAMAKTVGIPAAIGALLLLEGKIKTRGVLRPLEPEVYV 1024
|
1050
....*....|.
gi 31980703 906 PILERIKAEGI 916
Cdd:PLN02819 1025 PALEILQAYGI 1035
|
|
| Sacchrp_dh_C |
pfam16653 |
Saccharopine dehydrogenase C-terminal domain; This family comprises the C-terminal domain of ... |
602-916 |
3.09e-91 |
|
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: 289.58 E-value: 3.09e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 602 GLDPGLDHMLAMETIDTAKELGATVESYVSYCGGLPAPEHSDNPLRYKFSWSPVGVLMNIMQPASYLLNGKVVNVTGGVS 681
Cdd:pfam16653 1 GLDPGIDHMFAIKAIDDVNAKGGKIESFLSYCGGLPAPETSDNPLGYKFSWSPEGVLREGTNPARYWEDGKEVEVPGSEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 682 FlnsvTPMDYFPGLNLEGYPNRDSIKYAEIYGISSAHTLLRGTLRYKGYSKALNGFVKLGLINREAYPALrpeanpltwk 761
Cdd:pfam16653 81 M----EPIYIRPGFAFEGYPNRDSLPHEELYSLPEAKTLYRGTLRYPGFDEAIKSLVELGLLSEEPKVSL---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 762 qllcdlvgisrsspceklkevvftklggdntqleaaEWLGLlgdeqvpqaESIVDAFSKHLVSKLSYGPEEKDMIVMRDS 841
Cdd:pfam16653 147 ------------------------------------EWLLF---------SGPLDVLAALLEDKLSLGPGERDMVVLQHE 181
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 31980703 842 FGIRHPsghlENKTIDLVVYGDF--NGFSAMAKTVGLPTAMAAKMLLDGEIEAKGLMGPF-TKEIYGPILERIKAEGI 916
Cdd:pfam16653 182 FDGKKG----ERRTYTLVDYGDHeeVGPSAMARTVGVPAAIAALLILDGKIKNKGVVNPEeDPEIYEPFLEELEKRGI 255
|
|
| SDH_like |
cd05199 |
Saccharopine Dehydrogenase like proteins; Saccharopine Dehydrogenase (SDH) and related ... |
25-424 |
1.75e-90 |
|
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: 290.29 E-value: 1.75e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 25 VMALRREDVNAWERRAPLAPKHIKGITKLGY--KVLIQPSNRRAIHDKEYVRAGGILQEDITEACLILGVKRPPEEKLMS 102
Cdd:cd05199 1 KIGIIREGKTPPDRRVPLTPEQCKELQAKYPgvEIFVQPSPVRCFKDEEYRAAGIEVVEDLSDCDILLGVKEVPIEQLIP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 103 KKTYAFFSHTIKAQEANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMINILHGMGLRllalghhTPFMHL 182
Cdd:cd05199 81 NKTYFFFSHTIKKQPYNRKLLQTILEKNITLIDYEVLVDEQGKRVIAFGRYAGIVGAYNGLRAYGKK-------TGLFDL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 183 GMAHnyrnssqavqAVRDAGYEISLGLmPKSIGPLTFVFTGTGNVSKGAQEVFNELPCEYVEPHELREVsktgdlrkvyg 262
Cdd:cd05199 154 KRAH----------ECSDLEELIAELK-KVGLPPPKIVITGSGRVGSGAAEVLKALGIKEVSPEDFLTV----------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 263 tvlsrhhhlvrktdgvydpveyekyperytsrfnTDIapyttcLINGIYWEQNTPRLLTRQDAQSllvpvkssvvpvegc 342
Cdd:cd05199 212 ----------------------------------ADI------LINGHYWDKRAPRLFTKEDLKK--------------- 236
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 343 PELphKLVAICDISADTGGSIDFMTECTTIERPFCMYDADQQIIHDSVEGSGILMCSIDNLPAQLPIEATEYFGDMLYPY 422
Cdd:cd05199 237 PDF--KIRVIADVTCDIHGSIPSTLRASTIADPVYDYDPTTNKEVAFSSPDSITVMAVDNLPCELPRDASEDFGEQLIKS 314
|
..
gi 31980703 423 VE 424
Cdd:cd05199 315 VL 316
|
|
| Lys9 |
COG1748 |
Saccharopine dehydrogenase, NADP-dependent [Amino acid transport and metabolism]; Saccharopine ... |
506-921 |
1.93e-57 |
|
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: 201.22 E-value: 1.93e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 506 EITLGSDMTNQMQQLSKKY-NINPVSLTVGKQEAkLQSLVESQDLVISLLPYVLHPVVAKACIESRVNMVTASYITPAMK 584
Cdd:COG1748 2 EVTLADRSLEKAEALAASGpKVEAAQLDASDPEA-LAALIAGADLVINALPPYLNLTVAEACIEAGVHYVDLSEDEPETE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 585 ---ELEKSVDDAGITVIGELGLDPGLDHMLAMETIDTAKElgatVESYVSYCGGLPAPEhsDNPLRYKFSWSPVGVLMNI 661
Cdd:COG1748 81 aklALDELAKEAGVTAIPGCGLAPGLSNVLAAYAADRFDE----IDSIDIRVGGLPGYP--SNPLNYGTTWSPEGVIREY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 662 MQPASYLLNGKVVnvtggvsflnSVTPMD-----YFPGL-NLEGYPNRDSIKY-AEIYGisSAHTLLRGTLRYKGYSKAL 734
Cdd:COG1748 155 TNPARAIEDGKWV----------EVPPLSeretiDFPGVgRYEAYNTDGELETlPETYP--GVKTVRFKTGRYPGHLNHL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 735 NGFVKLGLINREAYPALRPEANPLtwkqllcdlvgisrsspceklkevvftklggdntqleaaewlgllgdeqvpqaesi 814
Cdd:COG1748 223 KVLVDLGLTDDEPVEVEGVEVSPR-------------------------------------------------------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 815 vDAFSKHLVSKLSYGPEEKDMIVMRDSF-GIRHpsGHLENKTIDLVVYGDFN-GFSAMAKTVGLPTAMAAKMLLDGEIEA 892
Cdd:COG1748 247 -DVLKAILPDPLPLGPTDKDVVVIGVVVkGTKD--GKRETYVYNLVDHEDAEtGSTAMAYTTGVPAAIAAELLLEGKIPK 323
|
410 420 430
....*....|....*....|....*....|
gi 31980703 893 KGLMGPftKEIYG-PILERIKAEGIVFNTQ 921
Cdd:COG1748 324 PGVVNP--EQLDPdPFLEELAKRGIPIEEE 351
|
|
| AlaDh_PNT_N |
pfam05222 |
Alanine dehydrogenase/PNT, N-terminal domain; This family now also contains the lysine ... |
27-157 |
1.78e-30 |
|
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: 116.76 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 27 ALRREdVNAWERRAPLAPKHIKGITKLGYKVLIQPSN--RRAIHDKEYVRAGGILQ----EDITEACLILGVKRP--PEE 98
Cdd:pfam05222 1 GVPKE-IKPGERRVALTPAGVKKLVKLGHEVLVESGAglGAGFSDEAYEAAGAEIVdtaaEVWAEADLILKVKEPqpEEY 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 99 KLMSK-KTYAFFSHTIkaqeANMNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVA 157
Cdd:pfam05222 80 ALLREgQTLITFLHPA----ANPELLEALAAKGVTAIAYETVPRSRGQSLDALSSMANIA 135
|
|
| Sacchrp_dh_NADP |
pfam03435 |
Saccharopine dehydrogenase NADP binding domain; This family contains the NADP binding domain ... |
483-598 |
3.69e-28 |
|
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: 109.60 E-value: 3.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 483 VLVLGSGYVSGPVLEYLSRDNNI-EITLGSDMTNQMQQLSKK---YNINPVSLTVGKQEAKLQSLVESQDLVISLLPYVL 558
Cdd:pfam03435 1 VLIIGAGSVGQGVAPLLARHFDVdRITVADRTLEKAQALAAKlggVRFIAVAVDADNYEAVLAALLKEGDLVVNLSPPTL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 31980703 559 HPVVAKACIESRVNMVTASYITPAMKELEKSVDDAGITVI 598
Cdd:pfam03435 81 SLDVLKACIETGVHYVDTSYLREAVLALHEKAKDAGVTAV 120
|
|
| SDH |
cd12188 |
Saccharopine Dehydrogenase NAD-binding and catalytic domains; Saccharopine Dehydrogenase (SDH) ... |
30-425 |
4.14e-27 |
|
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: 113.87 E-value: 4.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 30 REDVNAWERRAPLAPKHIKGITKLGYKVLIQPSNRRAIHDKEYVRAGGILQEDIT-----EACLILGVKRPPEEKLMSKK 104
Cdd:cd12188 6 RAETKPLERRTALTPTTAKKLLDAGFKVTVERSPQRIFPDEEYEAVGCELVPAGSwvnapKDAIILGLKELPEDTFPLPH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 105 TYAFFSHTIKAQEAnmnlLDEVLKQEIR----LIDYEKMVDHRGSRIVAFGQWAGVAgminilhGMGLRLLALGHHTPFM 180
Cdd:cd12188 86 RHIYFAHAYKGQAG----WKDVLSRFARgggtLLDLEYLVDDDGRRVAAFGYWAGFA-------GAALGLLAWAHQQLGP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 181 H-LGMAHNYRNSSQAVQAVRDAgyEISLGLMPKS--IGPLtfvftgtGNVSKGAQEVFNELPCEyVEPHELREVSKTGDl 257
Cdd:cd12188 155 VtLPPVSPYPNEEALVADVKKA--LATGGRKPRAlvIGAL-------GRCGSGAVDLLEAAGIE-VTKWDMAETKAGGP- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 258 rkvygtvlsrhhhlvrktdgvydpveyekYPErytsRFNTDIapyttcLINGIYWEQNTPRLLTRQDAQSllvpvkssvv 337
Cdd:cd12188 224 -----------------------------FPE----ILDHDI------FVNCIYLSKPIPPFLTPEMLQA---------- 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 338 pvegcPElpHKLVAICDISADTGGS---IDFMTECTTIERPfcmydadqqIIHDSVEGSGILMCSIDNLPAQLPIEATEY 414
Cdd:cd12188 255 -----PG--RRLRVIGDVSCDPTNPynpIPIYDVATTFDKP---------TLRVPTGGPPLDVIAIDHLPSLLPRESSED 318
|
410
....*....|.
gi 31980703 415 FGDMLYPYVEE 425
Cdd:cd12188 319 FSNDLLPSLLE 329
|
|
| AlaDh_PNT_N |
smart01003 |
Alanine dehydrogenase/PNT, N-terminal domain; Alanine dehydrogenase catalyzes the ... |
27-155 |
2.39e-24 |
|
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: 99.41 E-value: 2.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 27 ALRREDVNaWERRAPLAPKHIKGITKLGYKVLIQPSN--RRAIHDKEYVRAGGILQED---ITEACLILGVKRP-PEEKL 100
Cdd:smart01003 1 GVPKEIKP-GERRVALTPAGVKKLVKLGHEVLVESGAgeGAGFSDEAYEAAGAEIVDTaevWADADIILKVKEPsPEELA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 31980703 101 MSKKTYAFFSHtiKAQEANMNLLDEVLKQEIRLIDYEKMV-DHRGSRIVAFGQWAG 155
Cdd:smart01003 80 LLREGQILFGY--LHPAANPELLEALAAKGVTAIAYETVPrISRAQSLDALSSMAE 133
|
|
| AlaDh_PNT_C |
smart01002 |
Alanine dehydrogenase/PNT, C-terminal domain; Alanine dehydrogenase catalyzes the ... |
197-380 |
1.75e-20 |
|
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: 88.72 E-value: 1.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 197 AVRDAGYEISLGLMPKSIGPLTFVFTGTGNVSKGAQEVFNELPCE----YVEPHELREVsktgdlRKVYGTVLsrhhhlv 272
Cdd:smart01002 1 LEKFGGGFGMLLTGAGGVPPAKVVVIGAGVVGLGAAATAKGLGAEvtvlDVRPARLRQL------ESLLGARF------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 273 rktdgvydpveyekYPERYTSRFNTDIAPYTTCLINGIYWE-QNTPRLLTRQDAQSLLvpvkssvvpvEGCpelphklvA 351
Cdd:smart01002 68 --------------TTLYSQAELLEEAVKEADLVIGAVLIPgAKAPKLVTREMVKSMK----------PGS--------V 115
|
170 180
....*....|....*....|....*....
gi 31980703 352 ICDISADTGGSIDFmTECTTIERPFCMYD 380
Cdd:smart01002 116 IVDVAADQGGCIET-SRPTTHDDPTYVVD 143
|
|
| Ala_dh_like |
cd01620 |
Alanine dehydrogenase and related dehydrogenases; Alanine dehydrogenase/Transhydrogenase, such ... |
37-427 |
3.03e-08 |
|
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: 56.26 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 37 ERRAPLAPKHIKGITKLGYKVLIQ--PSNRRAIHDKEYVRAGGIL----QEDITEACLILGVKRPPE-EKLMSKKTYAFF 109
Cdd:cd01620 12 EFRVALTPSFVKKLVANGFKVYIEtgAGSGAGFSDEDYLQAGAQIvpaaSKEAYSADIIVKLKEPEFaEYDLIKKGQLLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 110 SHTIKAQEAnmNLLDEVLKQEIRLIDYEKMVDHRGSRIVAFGQWAGVAGMInilhgMGLRLLAlghhtpfMHLGMAHNYR 189
Cdd:cd01620 92 TFLHAATNR--GVVEVLMRKKLTAYALEDLENDFRPRLAPNSNIAGYAGVQ-----LGAYELA-------RIQGGRMGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 190 NSSqavqavrdagyeislglmpksiGPLTFVFTGTGNVSKGAqevfnelpceyvephelrevsktGDLRKVYGTVlsrhh 269
Cdd:cd01620 158 GGV----------------------PPAKVLIIGAGVVGLGA-----------------------AKIAKKLGAN----- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 270 hlVRKTD---GVYDPVEYEKYPERYTSRFNT--DIAPYTTCLINGIYWE-QNTPRLLTRQDAQSLlvpvkssvvpvegcp 343
Cdd:cd01620 188 --VLVYDikeEKLKGVETLGGSRLRYSQKEEleKELKQTDILINAILVDgPRAPILIMEELVGPM--------------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 344 elpHKLVAICDISADTGGsidfmtectTIERPfcmydadQQIIHD--SVEGSGILMCSIDNLPAQLPIEATEYFGDMLYP 421
Cdd:cd01620 251 ---KRGAVIVDLAADQGG---------NDETS-------IPTTEGvpTYEVDGVVIYGVDNMPSLVPREASELLSKNLLP 311
|
....*.
gi 31980703 422 YVEEML 427
Cdd:cd01620 312 YLVKLA 317
|
|
| Rubrum_tdh |
cd05304 |
Rubrum transdehydrogenase NAD-binding and catalytic domains; Transhydrogenases found in ... |
37-98 |
6.30e-05 |
|
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: 46.24 E-value: 6.30e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980703 37 ERRAPLAPKHIKGITKLGYKVLIQP-SNRRA-IHDKEYVRAGGIL---QEDITEACLILGVKRPPEE 98
Cdd:cd05304 13 ERRVALTPETVKKLVKLGFEVLVESgAGEAAgFSDEAYEEAGAEIvsdAEELAQADIVLKVRPPSEE 79
|
|
| PntA |
COG3288 |
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion]; |
37-100 |
8.47e-05 |
|
NAD/NADP transhydrogenase alpha subunit [Energy production and conversion];
Pssm-ID: 442518 [Multi-domain] Cd Length: 359 Bit Score: 45.76 E-value: 8.47e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 31980703 37 ERRAPLAPKHIKGITKLGYKVLIQP--SNRRAIHDKEYVRAGG-ILQEDITEACLILGVKRPPEEKL 100
Cdd:COG3288 13 ERRVALTPETVKKLVKLGAEVLVESgaGLAAGFPDAAYEAAGAeIVDAELLGADIVLKVRPPSAEEL 79
|
|
| L-AlaDH |
cd05305 |
Alanine dehydrogenase NAD-binding and catalytic domains; Alanine dehydrogenase (L-AlaDH) ... |
37-145 |
5.09e-03 |
|
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: 40.08 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 31980703 37 ERRAPLAPKHIKGITKLGYKVLIQ-----PSNrraIHDKEYVRAGGIL---QEDITEAC-LILGVKRP-PEE-KLMSKKT 105
Cdd:cd05305 13 ENRVALTPAGVAELVAAGHEVLVEkgaglGSG---FSDEEYSEAGAEIvptAEEVWAKAdLIVKVKEPlPEEyDLLREGQ 89
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 31980703 106 --YAFFsHtIKAQEAnmnLLDEVLKQEIRLIDYEKMVDHRGS 145
Cdd:cd05305 90 ilFTYL-H-LAADKE---LTEALLEKKVTAIAYETIEDEDGS 126
|
|
| |
