|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
6-769 |
0e+00 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 829.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 6 TSDTV-EVLPQHKFDLRSLEAYLNQHLPGFGSDSRAvLTVTQYRSGQSNPTFFLQKGS----QAYVLRKKPPGSLLPKAH 80
Cdd:PLN02876 5 TSDLLvPVQSAHRFDEDALLRYAAANVAGFPVPPST-FKVSQFGHGQSNPTFLLEVGNggsvKRYVLRKKPPGKLLQSAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 81 KIDREFKIQKAL-FSIGFPVAKPLLYCRDASVIGTEFYVMEHVQGRIFRDFSIPGVSSAERAAIYVSVAETLAWLHSLDI 159
Cdd:PLN02876 84 AVEREYQVLRALgEHTDVPVPKVYCLCTDASVIGTAFYIMEYLEGRIFVDPKLPGVAPERRRAIYRATAKVLAALHSADV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 160 RSLKLDKYGTGVGYCKRQVSTWTKQYQASAHQSIPA----MDQLSTWLMKNLPDSDS---EECLVHGDFKLDNIVFHPKE 232
Cdd:PLN02876 164 DAIGLGKYGRRDNYCKRQVERWAKQYLASTGEGKPPrnpkMLELIDWLRENIPAEDStgaGTGIVHGDFRIDNLVFHPTE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 233 CRVIAVLDWELSTFGHPLTDLAHLSLFYYWPRTL--PMINRG---SHIPEntGIPLMEELISIYCHRRGIDPNLPNWNFF 307
Cdd:PLN02876 244 DRVIGILDWELSTLGNQMCDVAYSCLPYIVDINLdnQQVGKGfefTGIPE--GIPSLPEYLAEYCSASGKPWPAANWKFY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 308 MALSFFKLAGISQGVYRRYLMGNNSS-EDSFLTANTVQPLAETGLQLSKR--TLRTTPP----------QADAKSQL-FA 373
Cdd:PLN02876 322 VAFSLFRGASIYAGVYSRWLMGNASGgERARNAGKQANFLVDSALDYIARknVLPEHPPsgqfgrepeySSLSKESGrFV 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 374 QSRRGQEVLTRVKQFMKQHVFPAEKEvaeyYAQSGNSAEKWG-HPLViEKLKEIAKAEGLWNLFLPAVS----------- 441
Cdd:PLN02876 402 PSEKVLELRKKLIKFMEDHIYPMENE----FYKLAQSSSRWTvHPEE-ERLKELAKKEGLWNLWIPLDSaararkllfed 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 442 ----------------GLSQVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCM 505
Cdd:PLN02876 477 nkhmvsgdsadqllgaGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAM 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 506 TEPNVSSSDATNIECTIQRDGGGYIVNGKKWWSSGAGNPKCKIAIVLGRTEsPSASRHRQHSMILVPMDTPGVELIRPLS 585
Cdd:PLN02876 557 TEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTD-FNAPKHKQQSMILVDIQTPGVQIKRPLL 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 586 VFGYMDNMHgGHWEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYE 665
Cdd:PLN02876 636 VFGFDDAPH-GHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQ 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 666 HEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTLGSASARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAI 745
Cdd:PLN02876 715 HGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWAT 794
|
810 820
....*....|....*....|....
gi 74271799 746 IRTLRLADGPDEVHLSAIAKMELQ 769
Cdd:PLN02876 795 ARTLRIADGPDEVHLGTIAKLELQ 818
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
376-769 |
0e+00 |
|
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACAD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. ACAD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173844 [Multi-domain] Cd Length: 394 Bit Score: 802.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 376 RRGQEVLTRVKQFMKQHVFPAEKEVAEYYAQSGNSAekWGHPLVIEKLKEIAKAEGLWNLFLPAVSGLS---QVDYALIA 452
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFLEYYAEGGDRW--WTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSgltNLEYAYLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 453 EETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNVSSSDATNIECTIQRDGGGYIVN 532
Cdd:cd01155 79 EETGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 533 GKKWWSSGAGNPKCKIAIVLGRTESPSASRHRQHSMILVPMDTPGVELIRPLSVFGYMDNmHGGHWEVHFNHVRVPASNL 612
Cdd:cd01155 159 GRKWWSSGAGDPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDA-PHGHAEITFDNVRVPASNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 613 ILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAH 692
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAH 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74271799 693 SIDTLGSASARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKMELQ 769
Cdd:cd01155 318 MIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
372-772 |
2.43e-108 |
|
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and metabolism]; Acyl-CoA dehydrogenase related to the alkylation response protein AidB is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 441563 [Multi-domain] Cd Length: 381 Bit Score: 335.66 E-value: 2.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 372 FAQSRRGQEVLTRVKQFMKQHVFPAEKEVAEyyaqsgnsaekwgHPLVIEKLKEIAKAEGLWNLFLPAV---SGLSQVDY 448
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDR-------------EGEFPRELWRKLAELGLLGLTIPEEyggLGLSLVEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 449 ALIAEETGKCFfAPDVFNCQAPDtGNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGG 528
Cdd:COG1960 70 ALVLEELARAD-ASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRDGDG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 529 YIVNGKKWWSSGAgnPKCKIAIVLGRTESpsASRHRQHSMILVPMDTPGVELIRPLSVFGYMDNMHGghwEVHFNHVRVP 608
Cdd:COG1960 147 YVLNGQKTFITNA--PVADVILVLARTDP--AAGHRGISLFLVPKDTPGVTVGRIEDKMGLRGSDTG---ELFFDDVRVP 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 609 ASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTL 688
Cdd:COG1960 220 AENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVY 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 689 KAAHSIDTlgSASARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKMEL 768
Cdd:COG1960 300 RAAWLLDA--GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLL 377
|
....
gi 74271799 769 QDQA 772
Cdd:COG1960 378 GRPG 381
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
471-765 |
1.71e-95 |
|
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal acyl-CoA oxidases (AXO) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. In contrast, AXO catalyzes a different oxidative half-reaction, in which the reduced FAD is reoxidized by molecular oxygen. The ACAD family includes the eukaryotic beta-oxidation enzymes, short (SCAD), medium (MCAD), long (LCAD) and very-long (VLCAD) chain acyl-CoA dehydrogenases. These enzymes all share high sequence similarity, but differ in their substrate specificities. The ACAD family also includes amino acid catabolism enzymes such as Isovaleryl-CoA dehydrogenase (IVD), short/branched chain acyl-CoA dehydrogenases(SBCAD), Isobutyryl-CoA dehydrogenase (IBDH), glutaryl-CoA deydrogenase (GCD) and Crotonobetainyl-CoA dehydrogenase. The mitochondrial ACAD's are generally homotetramers, except for VLCAD, which is a homodimer. Related enzymes include the SOS adaptive reponse proten aidB, Naphthocyclinone hydroxylase (NcnH), and and Dibenzothiophene (DBT) desulfurization enzyme C (DszC)
Pssm-ID: 173838 [Multi-domain] Cd Length: 327 Bit Score: 300.35 E-value: 1.71e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 471 DTGNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKKWWSSGAGNpkCKIAI 550
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNGGD--ADLFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 551 VLGRTEsPSASRHRQHSMILVPMDTPGVELIRPLSVFGymdnMHG-GHWEVHFNHVRVPASNLILGEGRGFEISQGRLGP 629
Cdd:cd00567 118 VLARTD-EEGPGHRGISAFLVPADTPGVTVGRIWDKMG----MRGsGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 630 GRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTlGSASARKEIAMI 709
Cdd:cd00567 193 GRLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMA 271
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 74271799 710 KVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAK 765
Cdd:cd00567 272 KLFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| ACAD10_11_N-like |
cd05154 |
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
42-292 |
1.76e-95 |
|
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This subfamily is composed of the N-terminal domains of vertebrate ACAD10 and ACAD11, and similar uncharacterized bacterial and eukaryotic proteins. ACADs are a family of flavoproteins that are involved in the beta-oxidation of fatty acyl-CoA derivatives. ACAD deficiency can cause metabolic disorders including muscle fatigue, hypoglycemia, and hepatic lipidosis. There are at least 11 distinct ACADs, some of which show distinct substrate specificities to either straight-chain or branched-chain fatty acids. ACAD10 is widely expressed in human tissues and highly expressed in liver, kidney, pancreas, and spleen. ACAD10 and ACAD11 are both significantly expressed in human brain tissues. They contain a long N-terminal domain with similarity to phosphotransferases with a Protein Kinase fold, which is absent in other ACADs. They may exhibit multiple functions in acyl-CoA oxidation pathways. ACAD11 utilizes substrates with carbon chain lengths of 20 to 26, with optimal activity towards C22CoA. ACAD10 may be associated with an increased risk in type II diabetes. The ACAD10/11-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270703 [Multi-domain] Cd Length: 254 Bit Score: 297.60 E-value: 1.76e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 42 LTVTQYRSGQSNPTFFLQ----KGSQAYVLRKKPPGSLLPKAHKIDREFKIQKALFSIGFPVAKPLLYCRDASVIGTEFY 117
Cdd:cd05154 1 LAVRRLSGGASNETYLVDaggdGGGRRLVLRRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLALCEDPSVLGAPFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 118 VMEHVQGRIFRDFSI-PGVSSAERAAIYVSVAETLAWLHSLDIRSLKLDKYGTGVGYCKRQVSTWTKQYQASAHQSIPAM 196
Cdd:cd05154 81 VMERVDGRVLPDPLPrPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEGYLERQVDRWRRQLEAAATDPPPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 197 DQLSTWLMKNLPDsDSEECLVHGDFKLDNIVFHPkECRVIAVLDWELSTFGHPLTDLAHLSLFYYWPRTLPMINRGSHIP 276
Cdd:cd05154 161 EEALRWLRANLPA-DGRPVLVHGDFRLGNLLFDP-DGRVTAVLDWELATLGDPLEDLAWLLARWWRPGDPPGLAAPTRLP 238
|
250
....*....|....*.
gi 74271799 277 entGIPLMEELISIYC 292
Cdd:cd05154 239 ---GFPSREELLARYE 251
|
|
| YcbJ |
COG3173 |
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
16-311 |
1.42e-69 |
|
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];
Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 230.39 E-value: 1.42e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 16 HKFDLRSLEAYLNQHLPGFgsdsRAVLTVTQYRSGQSNPTFFLQKGSQaYVLRKKPPGslLPKAHKIDREFKIQKALFSI 95
Cdd:COG3173 1 EELDEAALRALLAAQLPGL----AGLPEVEPLSGGWSNLTYRLDTGDR-LVLRRPPRG--LASAHDVRREARVLRALAPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 96 -GFPVAKPLLYCRDASVIGTEFYVMEHVQGRIFRDfSIPGVSSAERAAIYVSVAETLAWLHSLDIRSLKL-DKYGTGVGy 173
Cdd:COG3173 74 lGVPVPRPLALGEDGEVIGAPFYVMEWVEGETLED-ALPDLSPAERRALARALGEFLAALHAVDPAAAGLaDGRPEGLE- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 174 ckRQVSTWTKQYQA--SAHQSIPAM-DQLSTWLMKNLPDsDSEECLVHGDFKLDNIVFHPKECRVIAVLDWELSTFGHPL 250
Cdd:COG3173 152 --RQLARWRAQLRRalARTDDLPALrERLAAWLAANLPE-WGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGDPA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74271799 251 TDLAHLSLFYYWPRTLPminrgshipentgiPLMEELISIYCHRRGidpNLPNWNFFMALS 311
Cdd:COG3173 229 ADLAYLLLYWRLPDDLL--------------GPRAAFLAAYEEATG---DLDDLTWWALAD 272
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
387-766 |
2.06e-52 |
|
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA dehydrogenases; Short chain acyl-CoA dehydrogenase (SCAD). SCAD is a mitochondrial beta-oxidation enzyme. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of SCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. This subgroup also contains the eukaryotic short/branched chain acyl-CoA dehydrogenase(SBCAD), the bacterial butyryl-CoA dehydorgenase(BCAD) and 2-methylbutyryl-CoA dehydrogenase, which is involved in isoleucine catabolism. These enzymes are homotetramers.
Pssm-ID: 173847 [Multi-domain] Cd Length: 373 Bit Score: 186.70 E-value: 2.06e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 387 QFMKQHV--FpAEKEVAEYYAQSGNSAEKwgHPLVIEKLKEIakaeGLWNLFLPAV---SGLSQVDYALIAEETGKCFFA 461
Cdd:cd01158 4 QMIRKTVrdF-AEKEIAPLAAEMDEKGEF--PREVIKEMAEL----GLMGIPIPEEyggAGLDFLAYAIAIEELAKVDAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 462 PDVFNCQAPDTGNMEVLhLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKKWWSSGA 541
Cdd:cd01158 77 VAVIVSVHNSLGANPII-KFGTEEQKKKYLPPLATGEKIGAFALSEPG-AGSDAAALKTTAKKDGDDYVLNGSKMWITNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 542 GnpKCKIAIVLGRTEsPSAsRHRQHSMILVPMDTPGVELIRPLSVFGymdnMHG-GHWEVHFNHVRVPASNLILGEGRGF 620
Cdd:cd01158 155 G--EADFYIVFAVTD-PSK-GYRGITAFIVERDTPGLSVGKKEDKLG----IRGsSTTELIFEDVRVPKENILGEEGEGF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 621 EISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTlgSA 700
Cdd:cd01158 227 KIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDN--GE 304
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74271799 701 SARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKM 766
Cdd:cd01158 305 PFIKEAAMAKLFASEVAMRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKH 370
|
|
| APH |
pfam01636 |
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
43-268 |
5.81e-43 |
|
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance proteins, which confer resistance to various aminoglycosides they include: aminoglycoside 3'-phosphotransferase or kanamycin kinase / neomycin-kanamycin phosphotransferase and streptomycin 3''-kinase or streptomycin 3''-phosphotransferase. The aminoglycoside phosphotransferases inactivate aminoglycoside antibiotics via phosphorylation. This family also includes homoserine kinase. This family is related to fructosamine kinase pfam03881.
Pssm-ID: 426359 [Multi-domain] Cd Length: 239 Bit Score: 155.74 E-value: 5.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 43 TVTQYRSGQSNPTFFLQKGSQAYVLRKKPPGSLLPKAHKIDREFKI-QKALFSigfPVAKPLLYCRDASVIGTEFYVMEH 121
Cdd:pfam01636 1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEELRRELALLRHlAAAGVP---PVPRVLAGCTDAELLGLPFLLMEY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 122 VQGRIFRDFSIPgvssAERAAIYVSVAETLAWLHSLDIRSLKLDKYGTGVGYCKRQVSTWTKQYQASA-HQSIPAMD-QL 199
Cdd:pfam01636 78 LPGEVLARPLLP----EERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAElLDRLEELEeRL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74271799 200 STWLMKNLPdSDSEECLVHGDFKLDNIVFHPKEcRVIAVLDWELSTFGHPLTDLAhlSLFYYWPRTLPM 268
Cdd:pfam01636 154 LAALLALLP-AELPPVLVHGDLHPGNLLVDPGG-RVSGVIDFEDAGLGDPAYDLA--ILLNSWGRELGA 218
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
397-765 |
6.93e-41 |
|
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found in the mitochondria of eukaryotes and in some prokaryotes. It catalyzes the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of LCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. LCAD acts as a homodimer.
Pssm-ID: 173849 [Multi-domain] Cd Length: 372 Bit Score: 154.20 E-value: 6.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 397 EKEVAEYYAQsgnsAEKWGHplVIEKLKEIAKAEGLWNLFLPAVSGLSQVDY---ALIAEETGKcffapdvFNCQAP--- 470
Cdd:cd01160 15 AKEVAPFHHE----WEKAGE--VPREVWRKAGEQGLLGVGFPEEYGGIGGDLlsaAVLWEELAR-------AGGSGPgls 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 471 ---DTGNMEVLHlYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKKWW-SSGAgnpKC 546
Cdd:cd01160 82 lhtDIVSPYITR-AGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNGSKTFiTNGM---LA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 547 KIAIVLGRTESPSASRHRQhSMILVPMDTPGVELIRPLSVFGYMDNMHGghwEVHFNHVRVPASNLILGEGRGFEISQGR 626
Cdd:cd01160 157 DVVIVVARTGGEARGAGGI-SLFLVERGTPGFSRGRKLKKMGWKAQDTA---ELFFDDCRVPAENLLGEENKGFYYLMQN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 627 LGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIA--KSRIAIEEIRLLTLKAAHSIDTLGSAsark 704
Cdd:cd01160 233 LPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAelATKVAVTRAFLDNCAWRHEQGRLDVA---- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74271799 705 EIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAK 765
Cdd:cd01160 309 EASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
441-769 |
8.56e-38 |
|
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- dehydrogenation of short branched chain acyl-CoA intermediates in valine catabolism. It is predicted to be a homotetramer.
Pssm-ID: 173851 [Multi-domain] Cd Length: 375 Bit Score: 145.28 E-value: 8.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 441 SGLSQVDYALIAEE--TGKCFFAPDVfncqapDTGNMEV--LHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDAT 516
Cdd:cd01162 58 SGLSRLDASIIFEAlsTGCVSTAAYI------SIHNMCAwmIDSFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 517 NIECTIQRDGGGYIVNGKKWWSSGAGNPKckIAIVLGRTESPSAsrhRQHSMILVPMDTPGVElirplsvFGYMDNMHGG 596
Cdd:cd01162 131 ALRTRAVREGDHYVLNGSKAFISGAGDSD--VYVVMARTGGEGP---KGISCFVVEKGTPGLS-------FGANEKKMGW 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 597 HWE----VHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHW 672
Cdd:cd01162 199 NAQptraVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 673 IAKSRIAIEEIRLLTLKAAHSIDTlGSASARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLA 752
Cdd:cd01162 279 LADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQIL 357
|
330
....*....|....*..
gi 74271799 753 DGPDEVHLSAIAKMELQ 769
Cdd:cd01162 358 EGTNEIMRLIIARALLT 374
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
617-765 |
1.57e-36 |
|
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an all-alpha, four helical up-and-down bundle.
Pssm-ID: 395354 [Multi-domain] Cd Length: 149 Bit Score: 134.30 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 617 GRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDT 696
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74271799 697 LGSASArkEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAK 765
Cdd:pfam00441 81 GGPDGA--EASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
377-769 |
8.49e-35 |
|
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA dehydrogenases (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha, beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173841 [Multi-domain] Cd Length: 380 Bit Score: 136.71 E-value: 8.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 377 RGQEVLTRVKQFMKQHVfPAE--KEVAEYYAQSGNSAEKWghplvieklkEIAKAEGLW-NLFLPAV---SGLSQVDYAL 450
Cdd:cd01152 2 SEEAFRAEVRAWLAAHL-PPElrEESALGYREGREDRRRW----------QRALAAAGWaAPGWPKEyggRGASLMEQLI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 451 IAEETGKcFFAPDVFNCQAPDT-GNmeVLHLYGSEQQKKQWLEPLLRGDItsVFCM--TEPNvSSSDATNIECTIQRDGG 527
Cdd:cd01152 71 FREEMAA-AGAPVPFNQIGIDLaGP--TILAYGTDEQKRRFLPPILSGEE--IWCQgfSEPG-AGSDLAGLRTRAVRDGD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 528 GYIVNGKKWWSSGAgnPKCKIAIVLGRTEsPSASRHRQHSMILVPMDTPGVElIRPLSVFgymdNMHGGHWEVHFNHVRV 607
Cdd:cd01152 145 DWVVNGQKIWTSGA--HYADWAWLLVRTD-PEAPKHRGISILLVDMDSPGVT-VRPIRSI----NGGEFFNEVFLDDVRV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 608 PASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCdrAVQREAFkkKLYEHEVVAHWIAKSRIAIEEIRLLT 687
Cdd:cd01152 217 PDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARLL--LLTRDGR--PLIDDPLVRQRLARLEAEAEALRLLV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 688 LKAAHSIDTLGSASArkEIAMIKVAAPKAVCKIADWAIQVHGGAGV-SQDYPLAN-------MYAIIRTLRLADGPDEVH 759
Cdd:cd01152 293 FRLASALAAGKPPGA--EASIAKLFGSELAQELAELALELLGTAALlRDPAPGAElagrweaDYLRSRATTIYGGTSEIQ 370
|
410
....*....|
gi 74271799 760 LSAIAKMELQ 769
Cdd:cd01152 371 RNIIAERLLG 380
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
386-768 |
8.61e-35 |
|
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which catalyze the alpha,beta dehydrogenation of the corresponding medium chain acyl-CoA by FAD, which becomes reduced. The reduced form of MCAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. MCAD is a homotetramer.
Pssm-ID: 173846 [Multi-domain] Cd Length: 378 Bit Score: 136.56 E-value: 8.61e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 386 KQFMKQHVFPaekeVAEYYAQSGnsaeKWGHPLvIEKLKEIakaeGLWNLFLPAVSG---LSQVDYALIAEETGkcffap 462
Cdd:cd01157 13 RKFAREEIIP----VAAEYDKSG----EYPWPL-IKRAWEL----GLMNTHIPEDCGglgLGTFDTCLITEELA------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 463 dvFNC-------QAPDTGNMEVLhLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKK 535
Cdd:cd01157 74 --YGCtgvqtaiEANSLGQMPVI-ISGNDEQKKKYLGRMTEEPLMCAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 536 WWSSGAGnpKCKIAIVLGRTES-PSASRHRQHSMILVPMDTPGVELIRPLSVFGYMDNMHGGhweVHFNHVRVPASNLIL 614
Cdd:cd01157 150 MWITNGG--KANWYFLLARSDPdPKCPASKAFTGFIVEADTPGIQPGRKELNMGQRCSDTRG---ITFEDVRVPKENVLI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 615 GEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSI 694
Cdd:cd01157 225 GEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEV 304
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74271799 695 DTLGSASARKEIAmiKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAKMEL 768
Cdd:cd01157 305 DSGRRNTYYASIA--KAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
368-770 |
2.40e-34 |
|
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is found in the mitochondria of eukaryotes and in some bacteria. It catalyzes the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. VLCAD acts as a homodimer.
Pssm-ID: 173850 [Multi-domain] Cd Length: 409 Bit Score: 136.06 E-value: 2.40e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 368 KSQLFAQSRRGQEVLTrvkQFMKQHVFPAEKEVAEYYAQSGNSAEKWGHPLVIEKLKEIakaeGLWNLFLPAV---SGLS 444
Cdd:cd01161 13 TKQVFPYPSVLTEEQT---EELNMLVGPVEKFFEEVNDPAKNDQLEKIPRKTLTQLKEL----GLFGLQVPEEyggLGLN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 445 QVDYALIAEETGKCFFAPDVFNCQApDTGNMEVLhLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQR 524
Cdd:cd01161 86 NTQYARLAEIVGMDLGFSVTLGAHQ-SIGFKGIL-LFGTEAQKEKYLPKLASGEWIAAFALTEPS-SGSDAASIRTTAVL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 525 --DGGGYIVNGKKWWSSGAGnpKCKIAIVLGRTE--SPSASRHRQHSMILVPMDTPGVELIRPLSVFGymdnMHGGHW-E 599
Cdd:cd01161 163 seDGKHYVLNGSKIWITNGG--IADIFTVFAKTEvkDATGSVKDKITAFIVERSFGGVTNGPPEKKMG----IKGSNTaE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 600 VHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIA 679
Cdd:cd01161 237 VYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAIL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 680 IEEIRLLTLKAAHSIDTLGSASARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVH 759
Cdd:cd01161 317 QYATESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEIL 396
|
410
....*....|.
gi 74271799 760 LSAIAKMELQD 770
Cdd:cd01161 397 RLFIALTGLQH 407
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
424-765 |
2.88e-27 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 114.44 E-value: 2.88e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 424 KEIAKA---EGLWNLFLPAVSGLSQVDYA---LIAEETGKCFFAPDVF-NCQAPDtgnmEVLHlYGSEQQKKQWLEPLL- 495
Cdd:PRK12341 40 REFMRAladNGISMLGVPEEFGGTPADYVtqmLVLEEVSKCGAPAFLItNGQCIH----SMRR-FGSAEQLRKTAESTLe 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 496 RGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKKWWSSGAGNpkCKIAIVLGRtESPSASRHRQHSMILVPMDT 575
Cdd:PRK12341 115 TGDPAYALALTEPG-AGSDNNSATTTYTRKNGKVYLNGQKTFITGAKE--YPYMLVLAR-DPQPKDPKKAFTLWWVDSSK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 576 PGVElIRPLSVFGYmdNMhGGHWEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQ 655
Cdd:PRK12341 191 PGIK-INPLHKIGW--HM-LSTCEVYLDNVEVEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 656 REAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTlgSASARKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQ 735
Cdd:PRK12341 267 RIQFGKPIGHNQLIQEKLTLMAIKIENMRNMVYKVAWQADN--GQSLRTSAALAKLYCARTAMEVIDDAIQIMGGLGYTD 344
|
330 340 350
....*....|....*....|....*....|....
gi 74271799 736 DYPLANMYAIIRTLRLADGPDE--VHLS--AIAK 765
Cdd:PRK12341 345 EARVSRFWRDVRCERIGGGTDEimIYIAgrQILK 378
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
441-745 |
1.28e-26 |
|
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA dehydrogenase, which catalyzes the third step in leucine catabolism, the conversion of isovaleryl-CoA (3-methylbutyryl-CoA) into 3-methylcrotonyl-CoA. IVD is a homotetramer and has the greatest affinity for small branched chain substrates.
Pssm-ID: 173845 [Multi-domain] Cd Length: 376 Bit Score: 112.50 E-value: 1.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 441 SGLSQVDYALIAEETGKCffAPDVfncqAPDTG---NMEVLHLY--GSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDA 515
Cdd:cd01156 59 SGMGYLAHVIIMEEISRA--SGSV----ALSYGahsNLCINQIYrnGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 516 TNIECTIQRDGGGYIVNGKKWWSSGAgnPKCKIAIVLGRTEsPSASRHRQHSMIlVPMDTPGVELIRPLSVFGymdnMHG 595
Cdd:cd01156 132 VSMKLRAEKKGDRYVLNGSKMWITNG--PDADTLVVYAKTD-PSAGAHGITAFI-VEKGMPGFSRAQKLDKLG----MRG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 596 GH-WEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIA 674
Cdd:cd01156 204 SNtCELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLA 283
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74271799 675 KSRIAIEEIRLLTLKAAHSIDTlGSASARKEIAMIKVAAPKAVcKIADWAIQVHGGAGVSQDYPL------ANMYAI 745
Cdd:cd01156 284 DMYTRLNASRSYLYTVAKACDR-GNMDPKDAAGVILYAAEKAT-QVALDAIQILGGNGYINDYPTgrllrdAKLYEI 358
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
380-759 |
9.51e-24 |
|
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, which catalyzes the oxidative decarboxylation of glutaryl-CoA to crotonyl-CoA and carbon dioxide in the catabolism of lysine, hydroxylysine, and tryptophan. It uses electron transfer flavoprotein (ETF) as an electron acceptor. GCD is a homotetramer. GCD deficiency leads to a severe neurological disorder in humans.
Pssm-ID: 173840 [Multi-domain] Cd Length: 386 Bit Score: 103.98 E-value: 9.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 380 EVLTR--VKQFMKQHVFPaekEVAEYYAQsgnsaEKWGHPLvIEKLKEI----AKAEGLwnlflpAVSGLSQVDYALIAE 453
Cdd:cd01151 17 ERAIRdtAREFCQEELAP---RVLEAYRE-----EKFDRKI-IEEMGELgllgATIKGY------GCAGLSSVAYGLIAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 454 ETGKCffapdvfncqapDTG-----------NMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNVsSSDATNIECTI 522
Cdd:cd01151 82 EVERV------------DSGyrsfmsvqsslVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPNH-GSDPGGMETRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 523 QRDGGGYIVNGKKWWSSGAgnPKCKIAIVLGRTESPSASRHrqhsmILVPMDTPGVELIRPLSVFGYMDNMHGghwEVHF 602
Cdd:cd01151 149 RKDGGGYKLNGSKTWITNS--PIADVFVVWARNDETGKIRG-----FILERGMKGLSAPKIQGKFSLRASITG---EIVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 603 NHVRVPASNLiLGEGRGFEISQGRLGPGRIHHCMRTVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEE 682
Cdd:cd01151 219 DNVFVPEENL-LPGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIAL 297
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74271799 683 IRLLTLKAAHSIDTLGSASarKEIAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVH 759
Cdd:cd01151 298 GLLACLRVGRLKDQGKATP--EQISLLKRNNCGKALEIARTAREMLGGNGISDEYHIIRHMVNLESVNTYEGTHDIH 372
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
503-603 |
2.96e-23 |
|
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a beta-barrel fold.
Pssm-ID: 460685 [Multi-domain] Cd Length: 95 Bit Score: 94.65 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 503 FCMTEPNVSSsDATNIE-CTIQRDGGGYIVNGKKWWSSGAgnPKCKIAIVLGRTESPsaSRHRQHSMILVPMDTPGVELI 581
Cdd:pfam02770 2 FALTEPGAGS-DVASLKtTAADGDGGGWVLNGTKWWITNA--GIADLFLVLARTGGD--DRHGGISLFLVPKDAPGVSVR 76
|
90 100
....*....|....*....|..
gi 74271799 582 RPLSVFGYMDNMHGghwEVHFN 603
Cdd:pfam02770 77 RIETKLGVRGLPTG---ELVFD 95
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
483-765 |
4.39e-22 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 99.63 E-value: 4.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 483 SEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDG-GGYIVNGKKWWSSGAgnPKCKIAIVLGRTESpsas 561
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSnGNYVLNGSKIWITNG--TVADVFLIYAKVDG---- 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 562 rhrQHSMILVPMDTPGVELIRPLSVFGymdnMHGGHW-EVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVG 640
Cdd:PTZ00461 208 ---KITAFVVERGTKGFTQGPKIDKCG----MRASHMcQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVG 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 641 LAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSI-----DTLGSASARKeiamikVAAPK 715
Cdd:PTZ00461 281 IAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVhpgnkNRLGSDAAKL------FATPI 354
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 74271799 716 AVcKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADGPDEVHLSAIAK 765
Cdd:PTZ00461 355 AK-KVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
482-738 |
1.83e-18 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 88.40 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 482 GSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKKWWSSGAgnPKCKIAIVLGRTESPSAS 561
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWCTNG--PVAQTLVVYAKTDVAAGS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 562 RHRQHSMILVPMdtPGVELIRPLSVFGymdnMHGGH-WEVHFNHVRVPASNLILGEGRGFEISQGRLGPGRIHHCMRTVG 640
Cdd:PLN02519 202 KGITAFIIEKGM--PGFSTAQKLDKLG----MRGSDtCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPLG 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 641 LAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSIDTlGSASaRKEIAMIKVAAPKAVCKI 720
Cdd:PLN02519 276 LMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN-GKVD-RKDCAGVILCAAERATQV 353
|
250
....*....|....*...
gi 74271799 721 ADWAIQVHGGAGVSQDYP 738
Cdd:PLN02519 354 ALQAIQCLGGNGYINEYP 371
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
488-743 |
4.80e-18 |
|
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of several genes involved in the SOS adaptive response to DNA alkylation damage, whose expression is activated by the Ada protein. Its function has not been entirely elucidated; however, it is similar in sequence and function to acyl-CoA dehydrogenases. It has been proposed that aidB directly destroys DNA alkylating agents such as nitrosoguanidines (nitrosated amides) or their reaction intermediates.
Pssm-ID: 173843 [Multi-domain] Cd Length: 418 Bit Score: 87.43 E-value: 4.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 488 KQWLEPLL----RGDITSVFCMTEPNvSSSDATNIECTIQRDGGG-YIVNGKKWWSSgagNPKCKIAIVLGRTESPSASR 562
Cdd:cd01154 132 KQYLPGLLsdryKTGLLGGTWMTEKQ-GGSDLGANETTAERSGGGvYRLNGHKWFAS---APLADAALVLARPEGAPAGA 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 563 hRQHSMILVPMDTP-----GVELIRPLSVFGYMDNMHGghwEVHFNHVrvpASNLILGEGRGFEISQGRLGPGRIHHCMR 637
Cdd:cd01154 208 -RGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATG---EVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVA 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 638 TVGLAERILQIMCDRAVQREAFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAhsiDTLGSASARK--EIAMIKVAAPK 715
Cdd:cd01154 281 ALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAA---RAFDRAAADKpvEAHMARLATPV 357
|
250 260 270
....*....|....*....|....*....|....*
gi 74271799 716 A---VCKIAD----WAIQVHGGAGVSQDYPLANMY 743
Cdd:cd01154 358 AkliACKRAApvtsEAMEVFGGNGYLEEWPVARLH 392
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
472-754 |
5.80e-15 |
|
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). Mitochondrial acyl-CoA dehydrogenases (ACAD) catalyze the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. The reduced form of ACAD is reoxidized in the oxidative half-reaction by electron-transferring flavoprotein (ETF), from which the electrons are transferred to the mitochondrial respiratory chain coupled with ATP synthesis. The ACD family includes the eukaryotic beta-oxidation, as well as amino acid catabolism enzymes. These enzymes share high sequence similarity, but differ in their substrate specificities. The mitochondrial ACD's are generally homotetramers and have an active site glutamate at a conserved position.
Pssm-ID: 173842 [Multi-domain] Cd Length: 407 Bit Score: 77.82 E-value: 5.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 472 TGNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNI--ECTIQRDGGGYIVNGKKWWSSGAGNPKCKIA 549
Cdd:cd01153 90 QGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPD-AGSDLGALrtKAVYQADGSWRINGVKRFISAGEHDMSENIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 550 -IVLGRTESPSASRhRQHSMILVPMDTPGVELiRPLSVFGYMDNM--HGG-HWEVHFNHVRVPasnLILGEGRG----FE 621
Cdd:cd01153 169 hLVLARSEGAPPGV-KGLSLFLVPKFLDDGER-NGVTVARIEEKMglHGSpTCELVFDNAKGE---LIGEEGMGlaqmFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 622 -ISQGRLGPGrihhcMRTVGLAERILQIMCDRAVQREAFKKKLYE--------HEVVAHWIAKSRIAIEEIRLLTLKAAH 692
Cdd:cd01153 244 mMNGARLGVG-----TQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDLYTAT 318
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74271799 693 SIDTLGSASARKEIA------------MIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLRLADG 754
Cdd:cd01153 319 VQDLAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| APH_ChoK_like |
cd05120 |
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ... |
48-260 |
1.35e-12 |
|
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ChoK, ethanolamine kinase (ETNK), macrolide 2'-phosphotransferase (MPH2'), an unusual homoserine kinase, and uncharacterized proteins with similarity to the N-terminal domain of acyl-CoA dehydrogenase 10 (ACAD10). The members of this family catalyze the transfer of the gamma-phosphoryl group from ATP (or CTP) to small molecule substrates such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine. Phosphorylation of the antibiotics, aminoglycosides and macrolides, leads to their inactivation and to bacterial antibiotic resistance. Phosphorylation of choline, ethanolamine, and homoserine serves as precursors to the synthesis of important biological compounds, such as the major phospholipids, phosphatidylcholine and phosphatidylethanolamine and the amino acids, threonine, methionine, and isoleucine. The APH/ChoK family is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270690 [Multi-domain] Cd Length: 158 Bit Score: 66.17 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 48 RSGQSNPTFFLqKGSQAYVLRKKPPgsllPKAHKIDREFKIQKALFS-IGFPVAKPLLYCRDAsviGTEFYVMEHVQGRI 126
Cdd:cd05120 7 KEGGDNKVYLL-GDPREYVLKIGPP----RLKKDLEKEAAMLQLLAGkLSLPVPKVYGFGESD---GWEYLLMERIEGET 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 127 FRDfSIPGVSSAERAAIYVSVAETLAWLHSLDIRslkldkygtgvgyckrqvstwtkqyqasahqsipamdqlstwlmkn 206
Cdd:cd05120 79 LSE-VWPRLSEEEKEKIADQLAEILAALHRIDSS---------------------------------------------- 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74271799 207 lpdsdseeCLVHGDFKLDNIVFHPKEcRVIAVLDWELSTFGHPLTDLAHLSLFY 260
Cdd:cd05120 112 --------VLTHGDLHPGNILVKPDG-KLSGIIDWEFAGYGPPAFDYAAALRDW 156
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
379-498 |
9.38e-11 |
|
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is an all-alpha domain.
Pssm-ID: 460686 [Multi-domain] Cd Length: 113 Bit Score: 59.40 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 379 QEVLTRVKQFMKQHVFPAekeVAEYYAQSGNSAEkwghplVIEKLKEIakaeGLWNLFLPAV---SGLSQVDYALIAEET 455
Cdd:pfam02771 5 EALRDTVREFAEEEIAPH---AAEWDEEGEFPRE------LWKKLGEL----GLLGITIPEEyggAGLDYLAYALVAEEL 71
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 74271799 456 GKCFFAPDVFnCQAPDTGNMEVLHLYGSEQQKKQWLEPLLRGD 498
Cdd:pfam02771 72 ARADASVALA-LSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
634-750 |
1.95e-09 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 56.20 E-value: 1.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 634 HCMRTVGLAERILQIMCDRAVQRE--AFKKKLYEHEVVAHWIAKSRIAIEEIRLLTLKAAHSI------DTLGSASARKE 705
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIeaaaaaGKPVTPALRAE 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 74271799 706 IAMIKVAAPKAVCKIADWAIQVHGGAGVSQDYPLANMYAIIRTLR 750
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAA 126
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
379-577 |
4.68e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 59.10 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 379 QEVLTRVKQFMKQHVFPAekeVAEYYaqsgnsaEKWGHPL-VIEKLKEIAKAEGLWNLFlpAVSGLSQVDYALIAEETGK 457
Cdd:PLN02526 34 QALRKRVRECMEKEVAPI---MTEYW-------EKAEFPFhIIPKLGSLGIAGGTIKGY--GCPGLSITASAIATAEVAR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 458 CFFAPDVFnCQAPDTGNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDGGGYIVNGKKWW 537
Cdd:PLN02526 102 VDASCSTF-ILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPD-YGSDASSLNTTATKVEGGWILNGQKRW 179
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 74271799 538 ssgAGNPK-CKIAIVLGRTESPSasrhrQHSMILVPMDTPG 577
Cdd:PLN02526 180 ---IGNSTfADVLVIFARNTTTN-----QINGFIVKKGAPG 212
|
|
| CotS |
COG0510 |
Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; |
183-265 |
7.06e-09 |
|
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
Pssm-ID: 440276 [Multi-domain] Cd Length: 156 Bit Score: 55.56 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 183 KQYQASAHQSIPAMDQLSTWLMKNLPDSDSEECLVHGDFKLDNIVFHPK-ECRVIavlDWELSTFGHPLTDLAHLSLFYY 261
Cdd:COG0510 18 ERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDgRLYLI---DWEYAGLGDPAFDLAALLVEYG 94
|
....
gi 74271799 262 WPRT 265
Cdd:COG0510 95 LSPE 98
|
|
| SrkA |
COG2334 |
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
23-254 |
7.13e-09 |
|
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal transduction mechanisms]; Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 441905 [Multi-domain] Cd Length: 297 Bit Score: 58.01 E-value: 7.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 23 LEAYlnqhlpGFGSDSRavltVTQYRSGQsNPTFFLQ-KGSQAYVLRKKPPGSLLPKAhkIDREFKIQKALFSIGFPVAK 101
Cdd:COG2334 7 LERY------GLGPLSS----LKPLNSGE-NRNYRVEtEDGRRYVLKLYRPGRWSPEE--IPFELALLAHLAAAGLPVPA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 102 PLLyCRDASVIGTefyvmehVQGRIFRDFS-IPGVS-SAERAAIYVSVAETLAWLHSLdIRSLKLDKygtgvgycKRQVS 179
Cdd:COG2334 74 PVP-TRDGETLLE-------LEGRPAALFPfLPGRSpEEPSPEQLEELGRLLARLHRA-LADFPRPN--------ARDLA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 180 TWTKQYQASAHQSIP----------AMDQLSTWLMKNLPDSDSeeCLVHGDFKLDNIVFHPKecRVIAVLDWELSTFGHP 249
Cdd:COG2334 137 WWDELLERLLGPLLPdpedralleeLLDRLEARLAPLLGALPR--GVIHGDLHPDNVLFDGD--GVSGLIDFDDAGYGPR 212
|
....*
gi 74271799 250 LTDLA 254
Cdd:COG2334 213 LYDLA 217
|
|
| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
53-254 |
3.91e-08 |
|
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a subset of bacteria, which have a Protein Kinase fold. These proteins do not bear any similarity to the GHMP family homoserine kinases present in most bacteria and eukaryotes. Homoserine kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to L-homoserine producing L-homoserine phosphate, an intermediate in the production of the amino acids threonine, methionine, and isoleucine. The Type II homoserine kinase subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270702 [Multi-domain] Cd Length: 300 Bit Score: 55.73 E-value: 3.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 53 NPTFFLQKGSQAYVLRkkppgsLLPKAHK---IDREFKIQKALFSIGFPVAKPLLYcRDASVIGTefyvmehVQGRIFRD 129
Cdd:cd05153 28 NTNYFVTTTDGRYVLT------LFEKRRSaaeLPFELELLDHLAQAGLPVPRPLAD-KDGELLGE-------LNGKPAAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 130 FS-IPGVS----SAERAAiyvSVAETLAWLHSLdirslkLDKYgtgVGYCK--RQVSTWTKQYQASAHQSIPAM------ 196
Cdd:cd05153 94 FPfLPGESlttpTPEQCR---AIGAALARLHLA------LAGF---PPPRPnpRGLAWWKPLAERLKARLDLLAaddral 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74271799 197 -----DQLSTWLMKNLPDSdseecLVHGDFKLDNIVFhpKECRVIAVLDWELSTFGHPLTDLA 254
Cdd:cd05153 162 ledelARLQALAPSDLPRG-----VIHADLFRDNVLF--DGDRLSGIIDFYDACYDPLLYDLA 217
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
476-717 |
3.80e-06 |
|
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, which catalyzes the first two steps of DBT desulfurization in mesophilic bacteria. DszC converts DBT to DBT-sulfoxide, which is then converted to DBT-sulfone. Bacteria with this enzyme are candidates for the removal of organic sulfur compounds from fossil fuels, which pollute the environment. An equivalent enzyme tdsC, is found in thermophilic bacteria. This alignment also contains a closely related uncharacterized subgroup.
Pssm-ID: 173852 [Multi-domain] Cd Length: 377 Bit Score: 50.01 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 476 EVLHLYGSEQQKKQWLEPLLRGDITSVfCMTEpnVSSSDATNIECTIQRDGGGYIVNGKKWWSSGAGNPKCKIAIVLGRT 555
Cdd:cd01163 81 EALLLAGPEQFRKRWFGRVLNGWIFGN-AVSE--RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALFSDWVTVSALDEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 556 EspsasrhrQHSMILVPMDTPGVELIRPLSVFGYMDNMHGghwEVHFNHVRVPASNLIlgeGRGFEISQGRLGPG--RIH 633
Cdd:cd01163 158 G--------KLVFAAVPTDRPGITVVDDWDGFGQRLTASG---TVTFDNVRVEPDEVL---PRPNAPDRGTLLTAiyQLV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 634 HCMRTVGLAERILqimcDRAVQREAFKKKLYEHEVVAH---------WIAKSRIAIEEIRLLTLKAAHSIDTL------G 698
Cdd:cd01163 224 LAAVLAGIARAAL----DDAVAYVRSRTRPWIHSGAESarddpyvqqVVGDLAARLHAAEALVLQAARALDAAaaagtaL 299
|
250
....*....|....*....
gi 74271799 699 SASARKEIAmIKVAAPKAV 717
Cdd:cd01163 300 TAEARGEAA-LAVAAAKVV 317
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
473-572 |
2.03e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 47.94 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 473 GNMEVLHLYGSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRDG-GGYIVNGKK-WWSSGAGNPKCKIA- 549
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ-CGTDLGQVKTKAEPSAdGSYKITGTKiFISAGDHDLTENIVh 233
|
90 100
....*....|....*....|...
gi 74271799 550 IVLGRTESPSASRhRQHSMILVP 572
Cdd:PTZ00456 234 IVLARLPNSLPTT-KGLSLFLVP 255
|
|
| Bud32 |
COG3642 |
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ... |
84-254 |
2.99e-05 |
|
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification
Pssm-ID: 442859 [Multi-domain] Cd Length: 159 Bit Score: 44.95 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 84 REFKIQKALFSIGFPVAKPLLYCRDASVIgtefyVMEHVQGRIFRDFSipgVSSAERAAIYVSVAETLAWLHSLDIrslk 163
Cdd:COG3642 5 REARLLRELREAGVPVPKVLDVDPDDADL-----VMEYIEGETLADLL---EEGELPPELLRELGRLLARLHRAGI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 164 ldkygtgvgyckrqvstwtkqyqasahqsipamdqlstwlmknlpdsdseeclVHGDFKLDNIVFHPKEcrvIAVLDWEL 243
Cdd:COG3642 73 -----------------------------------------------------VHGDLTTSNILVDDGG---VYLIDFGL 96
|
170
....*....|.
gi 74271799 244 STFGHPLTDLA 254
Cdd:COG3642 97 ARYSDPLEDKA 107
|
|
| ChoK-like |
cd05151 |
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic ... |
49-258 |
5.09e-05 |
|
Choline Kinase and similar proteins; This subfamily is composed of bacterial and eukaryotic choline kinases, as well as eukaryotic ethanolamine kinase. ChoK catalyzes the transfer of the gamma-phosphoryl group from ATP (or CTP) to its substrate, choline, producing phosphorylcholine (PCho), a precursor to the biosynthesis of two major membrane phospholipids, phosphatidylcholine (PC), and sphingomyelin (SM). Although choline is the preferred substrate, ChoK also shows substantial activity towards ethanolamine and its N-methylated derivatives. Bacterial ChoK is also referred to as licA protein. ETNK catalyzes the transfer of the gamma-phosphoryl group from CTP to ethanolamine (Etn), the first step in the CDP-Etn pathway for the formation of the major phospholipid, phosphatidylethanolamine (PtdEtn). Unlike ChoK, ETNK shows specific activity for its substrate and displays negligible activity towards N-methylated derivatives of Etn. ChoK plays an important role in cell signaling pathways and the regulation of cell growth. The ChoK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases, such as the typical serine/threonine/tyrosine protein kinases (PKs), RIO kinases, actin-fragmin kinase (AFK), and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270700 [Multi-domain] Cd Length: 152 Bit Score: 44.08 E-value: 5.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 49 SGQSNPTFFLQKGSQAYVLRKkpPGSLLpkAHKIDR--EFKIQKALFSIGfpVAKPLLYCRDAsvigTEFYVMEHVQGRI 126
Cdd:cd05151 8 GGLTNKNYLVEVAGKKYVLRI--PGAGT--ELLIDRenEKANSKAAAELG--IAPEVIYFDPE----TGVKITEFIEGAT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 127 F--RDFSIPGVSSAeraaiyvsVAETLAWLHSLDIRSLkldkygtgvgyckrqvstwtkqyqasahqsipamdqlstwlm 204
Cdd:cd05151 78 LltNDFSDPENLER--------IAALLRKLHSSPLEDL------------------------------------------ 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 74271799 205 knlpdsdseeCLVHGDFKLDNIVFHPKECRVIavlDWELSTFGHPLTDLAHLSL 258
Cdd:cd05151 108 ----------VLCHNDLVPGNFLLDDDRLYLI---DWEYAGMNDPLFDLAALFS 148
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
482-612 |
1.23e-03 |
|
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in the peroxisomal fatty acid beta-oxidation, the alpha,beta dehydrogenation of the corresponding trans-enoyl-CoA by FAD, which becomes reduced. In a second oxidative half-reaction, the reduced FAD is reoxidized by molecular oxygen. AXO is generally a homodimer, but it has been reported to form a different type of oligomer in yeast. There are several subtypes of AXO's, based on substrate specificity. Palmitoyl-CoA oxidase acts on straight-chain fatty acids and prostanoids; whereas, the closely related Trihydroxycoprostanoly-CoA oxidase has the greatest activity for 2-methyl branched side chains of bile precursors. Pristanoyl-CoA oxidase, acts on 2-methyl branched fatty acids. AXO has an additional domain, C-terminal to the region with similarity to acyl-CoA dehydrogenases, which is included in this alignment.
Pssm-ID: 173839 [Multi-domain] Cd Length: 610 Bit Score: 42.32 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74271799 482 GSEQQKKQWLEPLLRGDITSVFCMTEPNvSSSDATNIECTIQRD--GGGYIVN-----GKKWWSSGAGNpKCKIAIVLGR 554
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTELG-HGSNLQGLETTATYDplTQEFVINtpdftATKWWPGNLGK-TATHAVVFAQ 194
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74271799 555 TESPsASRHRQHSMIlVP---MDT----PGVELIRPLSVFGY--MDNmhGGHWevhFNHVRVPASNL 612
Cdd:cd01150 195 LITP-GKNHGLHAFI-VPirdPKThqplPGVTVGDIGPKMGLngVDN--GFLQ---FRNVRIPRENL 254
|
|
| RIO2_C |
cd05144 |
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ... |
84-124 |
4.63e-03 |
|
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is present in archaea and eukaryotes. It contains an N-terminal winged helix (wHTH) domain and a C-terminal RIO kinase catalytic domain. The wHTH domain is primarily seen in DNA-binding proteins, although some wHTH domains may be involved in RNA recognition. RIO2 is essential for survival and is necessary for rRNA cleavage during 40S ribosomal subunit maturation. RIO kinases are atypical protein serine kinases containing a kinase catalytic signature, but otherwise show very little sequence similarity to typical PKs. Serine kinases catalyze the transfer of the gamma-phosphoryl group from ATP to serine residues in protein substrates. The RIO catalytic domain is truncated compared to the catalytic domains of typical PKs, with deletions of the loops responsible for substrate binding. The RIO2 kinase catalytic domain family is part of a larger superfamily, that includes the catalytic domains of other kinases such as the typical serine/threonine/tyrosine protein kinases (PKs), aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).
Pssm-ID: 270695 [Multi-domain] Cd Length: 183 Bit Score: 39.02 E-value: 4.63e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 74271799 84 REFKIQKALFSIGFPVAKPLLYCRDAsvigtefYVMEHVQG 124
Cdd:cd05144 67 KEFAALKALYEEGFPVPKPIDWNRHA-------VVMELIDG 100
|
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