|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
11-770 |
0e+00 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 822.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 11 LAEVLPQHKFDSKSLEAYLNQHLSGFGAErEATLTIAQYRAGKSNPTFYLQKG----FQTYVLRKKPPGSLLPKAHQIDR 86
Cdd:PLN02876 9 LVPVQSAHRFDEDALLRYAAANVAGFPVP-PSTFKVSQFGHGQSNPTFLLEVGnggsVKRYVLRKKPPGKLLQSAHAVER 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 87 EFKVQKAL-FSIGFPVPKPILYCSDTSVIGTEFYVMEHVQGRIFRDLTIPGLSPAERSAIYVATVETLAQLHSLNIQSLQ 165
Cdd:PLN02876 88 EYQVLRALgEHTDVPVPKVYCLCTDASVIGTAFYIMEYLEGRIFVDPKLPGVAPERRRAIYRATAKVLAALHSADVDAIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 166 LEGYGIGAGYCKRQVSTWTKQYQAAAHQDIPA----MQQLSEWLMKNLPDNDN---EENLIHGDFRLDNIVFHPKECRVI 238
Cdd:PLN02876 168 LGKYGRRDNYCKRQVERWAKQYLASTGEGKPPrnpkMLELIDWLRENIPAEDStgaGTGIVHGDFRIDNLVFHPTEDRVI 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 239 AVLDWELSTIGHPLSDLAHFSLFYFWPRTvpmINQGSYSEN-------SGIPSMEELISIYCRCRGINSILPNWNFFLAL 311
Cdd:PLN02876 248 GILDWELSTLGNQMCDVAYSCLPYIVDIN---LDNQQVGKGfeftgipEGIPSLPEYLAEYCSASGKPWPAANWKFYVAF 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 312 SYFKMAGIAQGVYSRYLLGNNSSEDSFLFA-NIVQPLAETGLQLSKRtfSTVLP--------------QIDTTGQL-FVQ 375
Cdd:PLN02876 325 SLFRGASIYAGVYSRWLMGNASGGERARNAgKQANFLVDSALDYIAR--KNVLPehppsgqfgrepeySSLSKESGrFVP 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 376 TRKGQEVLIKVKHFMKQHILPAEKevtEFYvQNENSVDKWGKPLVIDKLKEMAKVEGLWNLFLPAVS------------- 442
Cdd:PLN02876 403 SEKVLELRKKLIKFMEDHIYPMEN---EFY-KLAQSSSRWTVHPEEERLKELAKKEGLWNLWIPLDSaararkllfednk 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 443 --------------GLSHVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTE 508
Cdd:PLN02876 479 hmvsgdsadqllgaGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIRSGFAMTE 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 509 PDVASSDATNIECSIQRDEDSYVINGKKWWSSGAGNPKCKIAIVLGRTqNTSLSRHKQHSMILVPMNTPGVKIIRPLSVF 588
Cdd:PLN02876 559 PQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKT-DFNAPKHKQQSMILVDIQTPGVQIKRPLLVF 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 589 GYTDNFHgGHFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHE 668
Cdd:PLN02876 638 GFDDAPH-GHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKLIAQHG 716
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 669 VVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITR 748
Cdd:PLN02876 717 SFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHLWATAR 796
|
810 820
....*....|....*....|..
gi 1476413373 749 VLRLADGPDEVHLSAIATMELR 770
Cdd:PLN02876 797 TLRIADGPDEVHLGTIAKLELQ 818
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
377-770 |
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: 799.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 377 RKGQEVLIKVKHFMKQHILPAEKEVTEFYVQNENSVdkWGKPLVIDKLKEMAKVEGLWNLFLPAVSGLS---HVDYALIA 453
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFLEYYAEGGDRW--WTPPPIIEKLKAKAKAEGLWNLFLPEVSGLSgltNLEYAYLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 454 EETGKCFFAPDVFNCQAPDTGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDVASSDATNIECSIQRDEDSYVIN 533
Cdd:cd01155 79 EETGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDVASSDATNIECSIERDGDDYVIN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 534 GKKWWSSGAGNPKCKIAIVLGRTQNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNfHGGHFEIHFNQVRVPATNL 613
Cdd:cd01155 159 GRKWWSSGAGDPRCKIAIVMGRTDPDGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYDDA-PHGHAEITFDNVRVPASNL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 614 ILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAH 693
Cdd:cd01155 238 ILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAHWIAKSRIEIEQARLLVLKAAH 317
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476413373 694 SMDTLGSAGAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELR 770
Cdd:cd01155 318 MIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRIADGPDEVHLRSIARMELK 394
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
380-773 |
2.92e-107 |
|
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: 332.96 E-value: 2.92e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 380 QEVLIKVKHFMKQHILPAEKEVTEfyvqnENSVDKWgkplVIDKLKEMakveGLWNLFLPAV---SGLSHVDYALIAEET 456
Cdd:COG1960 10 RALRDEVREFAEEEIAPEAREWDR-----EGEFPRE----LWRKLAEL----GLLGLTIPEEyggLGLSLVELALVLEEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 457 GKCFfAPDVFNCQAPDtGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDEDSYVINGKK 536
Cdd:COG1960 77 ARAD-ASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEPG-AGSDAAALRTTAVRDGDGYVLNGQK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 537 WWSSGAgnPKCKIAIVLGRTQNTSlsRHKQHSMILVPMNTPGVKIIRPLSVFGYTDNfhgGHFEIHFNQVRVPATNLILG 616
Cdd:COG1960 154 TFITNA--PVADVILVLARTDPAA--GHRGISLFLVPKDTPGVTVGRIEDKMGLRGS---DTGELFFDDVRVPAENLLGE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 617 EGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMD 696
Cdd:COG1960 227 EGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQHRLADMAAELEAARALVYRAAWLLD 306
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476413373 697 TLGSAGAkkEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELRDQA 773
Cdd:COG1960 307 AGEDAAL--EAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILTIYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD10_11_N-like |
cd05154 |
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
44-294 |
5.08e-99 |
|
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: 306.85 E-value: 5.08e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 44 LTIAQYRAGKSNPTFYLQKGF----QTYVLRKKPPGSLLPKAHQIDREFKVQKALFSIGFPVPKPILYCSDTSVIGTEFY 119
Cdd:cd05154 1 LAVRRLSGGASNETYLVDAGGdgggRRLVLRRPPPGGLLPSAHDLEREYRVLRALAGTGVPVPRVLALCEDPSVLGAPFY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 120 VMEHVQGRIFRD-LTIPGLSPAERSAIYVATVETLAQLHSLNIQSLQLEGYGIGAGYCKRQVSTWTKQYQAAAHQDIPAM 198
Cdd:cd05154 81 VMERVDGRVLPDpLPRPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEGYLERQVDRWRRQLEAAATDPPPAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 199 QQLSEWLMKNLPDnDNEENLIHGDFRLDNIVFHPkECRVIAVLDWELSTIGHPLSDLAHFSLFYFWPRTVPMInqGSYSE 278
Cdd:cd05154 161 EEALRWLRANLPA-DGRPVLVHGDFRLGNLLFDP-DGRVTAVLDWELATLGDPLEDLAWLLARWWRPGDPPGL--AAPTR 236
|
250
....*....|....*.
gi 1476413373 279 NSGIPSMEELISIYCR 294
Cdd:cd05154 237 LPGFPSREELLARYEE 252
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
472-765 |
2.67e-90 |
|
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: 286.87 E-value: 2.67e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 472 DTGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDEDSYVINGKKWWSSGAGNpkCKIAI 551
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNGGD--ADLFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 552 VLGRTQNtSLSRHKQHSMILVPMNTPGVKIIRPLSVFGYTdnfHGGHFEIHFNQVRVPATNLILGEGRGFEISQGRLGPG 631
Cdd:cd00567 118 VLARTDE-EGPGHRGISAFLVPADTPGVTVGRIWDKMGMR---GSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 632 RIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTlGSAGAKKEIAMIK 711
Cdd:cd00567 194 RLLLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAK 272
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1476413373 712 VAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIA 765
Cdd:cd00567 273 LFATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIA 326
|
|
| YcbJ |
COG3173 |
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
18-312 |
1.64e-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: 1.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 18 HKFDSKSLEAYLNQHLSGFGAEREATltiaQYRAGKSNPTFYLQKGfQTYVLRKKPPGslLPKAHQIDREFKVQKALFSI 97
Cdd:COG3173 1 EELDEAALRALLAAQLPGLAGLPEVE----PLSGGWSNLTYRLDTG-DRLVLRRPPRG--LASAHDVRREARVLRALAPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 98 -GFPVPKPILYCSDTSVIGTEFYVMEHVQGRIFRDlTIPGLSPAERSAIYVATVETLAQLHSLNIQSLQLEGYGIGAGyc 176
Cdd:COG3173 74 lGVPVPRPLALGEDGEVIGAPFYVMEWVEGETLED-ALPDLSPAERRALARALGEFLAALHAVDPAAAGLADGRPEGL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 177 KRQVSTWTKQYQAAAHQ--DIPAMQ-QLSEWLMKNLPDnDNEENLIHGDFRLDNIVFHPKECRVIAVLDWELSTIGHPLS 253
Cdd:COG3173 151 ERQLARWRAQLRRALARtdDLPALReRLAAWLAANLPE-WGPPVLVHGDLRPGNLLVDPDDGRLTAVIDWELATLGDPAA 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1476413373 254 DLAHFSLFYFWPRTVPminqgsysensgiPSMEELISIYCRCRGinsILPNWNFFLALS 312
Cdd:COG3173 230 DLAYLLLYWRLPDDLL-------------GPRAAFLAAYEEATG---DLDDLTWWALAD 272
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
420-770 |
4.85e-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: 185.55 E-value: 4.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 420 VIDKLKEMakveGLWNLFLPAV---SGLSHVDYALIAEETGKCFFAPDVFNCQAPDTGNMEVLhLYGSEEQKKQWLEPLL 496
Cdd:cd01158 35 VIKEMAEL----GLMGIPIPEEyggAGLDFLAYAIAIEELAKVDASVAVIVSVHNSLGANPII-KFGTEEQKKKYLPPLA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 497 QGNITSCFCMTEPdVASSDATNIECSIQRDEDSYVINGKKWWSSGAGnpKCKIAIVLGRTQNTSlsRHKQHSMILVPMNT 576
Cdd:cd01158 110 TGEKIGAFALSEP-GAGSDAAALKTTAKKDGDDYVLNGSKMWITNGG--EADFYIVFAVTDPSK--GYRGITAFIVERDT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 577 PGVKIIRPLSVFGytdnFHG-GHFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERAT 655
Cdd:cd01158 185 PGLSVGKKEDKLG----IRGsSTTELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQALGIAQAALDAAVDYAK 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 656 QRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHsmdtLGSAGAK--KEIAMIKVAAPRAVSKIVDWAIQVCGGAG 733
Cdd:cd01158 261 ERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAAR----LKDNGEPfiKEAAMAKLFASEVAMRVTTDAVQIFGGYG 336
|
330 340 350
....*....|....*....|....*....|....*..
gi 1476413373 734 VSQDYPLANMYAITRVLRLADGPDEVHLSAIATMELR 770
Cdd:cd01158 337 YTKDYPVERYYRDAKITEIYEGTSEIQRLVIAKHLLK 373
|
|
| APH |
pfam01636 |
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
45-288 |
4.22e-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: 156.12 E-value: 4.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 45 TIAQYRAGKSNPTFYLQKGFQTYVLRKKPPGSLLPKAHqidREFKVQKALFSIGF-PVPKPILYCSDTSVIGTEFYVMEH 123
Cdd:pfam01636 1 TLRPISSGASNRTYLVTTGDGRYVLRLPPPGRAAEELR---RELALLRHLAAAGVpPVPRVLAGCTDAELLGLPFLLMEY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 124 VQGRIFRDltipGLSPAERSAIYVATVETLAQLHSLNIQSLQLEGYGIGAGYCKRQVSTWTKQYQAAAHQD--IPAMQQL 201
Cdd:pfam01636 78 LPGEVLAR----PLLPEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLLAAELLDrlEELEERL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 202 SEWLMKNLPDNDNEEnLIHGDFRLDNIVFHPKEcRVIAVLDWELSTIGHPLSDLA-HFSLFYFWPRTVPMINQGSYSENS 280
Cdd:pfam01636 154 LAALLALLPAELPPV-LVHGDLHPGNLLVDPGG-RVSGVIDFEDAGLGDPAYDLAiLLNSWGRELGAELLAAYLAAYGAF 231
|
....*...
gi 1476413373 281 GIPSMEEL 288
Cdd:pfam01636 232 GYARLREL 239
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
398-765 |
3.08e-36 |
|
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: 140.71 E-value: 3.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 398 EKEVTEFYvqnensvDKWGKPLVIDK-LKEMAKVEGLWNLFLPAVSGLSHVDY---ALIAEETGKcffapdvFNCQAP-- 471
Cdd:cd01160 15 AKEVAPFH-------HEWEKAGEVPReVWRKAGEQGLLGVGFPEEYGGIGGDLlsaAVLWEELAR-------AGGSGPgl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 472 ----DTGNMEVLHlYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDEDSYVINGKKWW-SSGAgnpK 546
Cdd:cd01160 81 slhtDIVSPYITR-AGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNGSKTFiTNGM---L 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 547 CKIAIVLGRTQNTSLSRHKQhSMILVPMNTPGVKIIRPLSVFGY--TDNFhgghfEIHFNQVRVPATNLILGEGRGFEIS 624
Cdd:cd01160 156 ADVVIVVARTGGEARGAGGI-SLFLVERGTPGFSRGRKLKKMGWkaQDTA-----ELFFDDCRVPAENLLGEENKGFYYL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 625 QGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAE--SRIAIEKIRLLTLKAAHSMDTLGSAg 702
Cdd:cd01160 230 MQNLPQERLLIAAGALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAElaTKVAVTRAFLDNCAWRHEQGRLDVA- 308
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1476413373 703 akkEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIA 765
Cdd:cd01160 309 ---EASMAKYWATELQNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELIS 368
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
618-765 |
3.90e-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: 133.15 E-value: 3.90e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 618 GRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDT 697
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476413373 698 LGSAGAkkEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIA 765
Cdd:pfam00441 81 GGPDGA--EASMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIA 146
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
442-770 |
7.25e-34 |
|
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: 133.72 E-value: 7.25e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 442 SGLSHVDYALIAEE--TGKCFFAPDVfncqapDTGNMEV--LHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDAT 517
Cdd:cd01162 58 SGLSRLDASIIFEAlsTGCVSTAAYI------SIHNMCAwmIDSFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 518 NIECSIQRDEDSYVINGKKWWSSGAGNPKckIAIVLGRTQNTSlsrHKQHSMILVPMNTPGVKiirplsvFGYTDNFHGG 597
Cdd:cd01162 131 ALRTRAVREGDHYVLNGSKAFISGAGDSD--VYVVMARTGGEG---PKGISCFVVEKGTPGLS-------FGANEKKMGW 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 598 HFE----IHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHW 673
Cdd:cd01162 199 NAQptraVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGAAQAALDLARAYLEERKQFGKPLADFQALQFK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 674 IAESRIAIEKIRLLTLKAAHSMDTlGSAGAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLA 753
Cdd:cd01162 279 LADMATELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECFDVANQALQLHGGYGYLKDYPVEQYVRDLRVHQIL 357
|
330
....*....|....*..
gi 1476413373 754 DGPDEVHLSAIATMELR 770
Cdd:cd01162 358 EGTNEIMRLIIARALLT 374
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
432-769 |
7.61e-33 |
|
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: 131.17 E-value: 7.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 432 GLWNLFLPAVSG---LSHVDYALIAEETGkcffapdvFNC-------QAPDTGNMEVLhLYGSEEQKKQWLEPLLQGNIT 501
Cdd:cd01157 45 GLMNTHIPEDCGglgLGTFDTCLITEELA--------YGCtgvqtaiEANSLGQMPVI-ISGNDEQKKKYLGRMTEEPLM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 502 SCFCMTEPDvASSDATNIECSIQRDEDSYVINGKKWWSSGAGnpKCKIAIVLGRTQ-NTSLSRHKQHSMILVPMNTPGVK 580
Cdd:cd01157 116 CAYCVTEPG-AGSDVAGIKTKAEKKGDEYIINGQKMWITNGG--KANWYFLLARSDpDPKCPASKAFTGFIVEADTPGIQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 581 IIRPLSVFGYTDNFHGGhfeIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAF 660
Cdd:cd01157 193 PGRKELNMGQRCSDTRG---ITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTF 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 661 KKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGAKKEIAmiKVAAPRAVSKIVDWAIQVCGGAGVSQDYPL 740
Cdd:cd01157 270 GKLIAEHQAVSFMLADMAMKVELARLAYQRAAWEVDSGRRNTYYASIA--KAFAADIANQLATDAVQIFGGNGFNSEYPV 347
|
330 340
....*....|....*....|....*....
gi 1476413373 741 ANMYAITRVLRLADGPDEVHLSAIATMEL 769
Cdd:cd01157 348 EKLMRDAKIYQIYEGTSQIQRLIISREHL 376
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
387-759 |
2.29e-32 |
|
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: 130.28 E-value: 2.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 387 KHFMKQHILPAEKEVTEFYV-----QNENSVDKwgkplVIDKLKEMakveGLWNLFLPAV---SGLSHVDYALIAEETGK 458
Cdd:cd01161 28 TEELNMLVGPVEKFFEEVNDpakndQLEKIPRK-----TLTQLKEL----GLFGLQVPEEyggLGLNNTQYARLAEIVGM 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 459 CFFAPDVFNCQApDTGNMEVLhLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDEDS--YVINGKK 536
Cdd:cd01161 99 DLGFSVTLGAHQ-SIGFKGIL-LFGTEAQKEKYLPKLASGEWIAAFALTEPS-SGSDAASIRTTAVLSEDGkhYVLNGSK 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 537 WWSSGAGnpKCKIAIVLGRT-QNTSLSRHKQH-SMILVPMNTPGVKIIRPLSVFGYTDNfhgGHFEIHFNQVRVPATNLI 614
Cdd:cd01161 176 IWITNGG--IADIFTVFAKTeVKDATGSVKDKiTAFIVERSFGGVTNGPPEKKMGIKGS---NTAEVYFEDVKIPVENVL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 615 LGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHS 694
Cdd:cd01161 251 GEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLIQEKLANMAILQYATESMAYMTSGN 330
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1476413373 695 MDTLGSAGAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEV 759
Cdd:cd01161 331 MDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIFRIFEGTNEI 395
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
443-765 |
2.61e-32 |
|
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: 129.39 E-value: 2.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 443 GLSHVDYALIAEETGKcFFAPDVFNCQAPDT-GNmeVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIEC 521
Cdd:cd01152 62 GASLMEQLIFREEMAA-AGAPVPFNQIGIDLaGP--TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRT 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 522 SIQRDEDSYVINGKKWWSSGAgnPKCKIAIVLGRTqNTSLSRHKQHSMILVPMNTPGVKiIRPLSvfgYTDnfhGGHF-- 599
Cdd:cd01152 138 RAVRDGDDWVVNGQKIWTSGA--HYADWAWLLVRT-DPEAPKHRGISILLVDMDSPGVT-VRPIR---SIN---GGEFfn 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 600 EIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRiafkKKLYAHEVVAHWIAESRI 679
Cdd:cd01152 208 EVFLDDVRVPDANRVGEVNDGWKVAMTTLNFERVSIGGSAATFFELLLARLLLLTRDG----RPLIDDPLVRQRLARLEA 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 680 AIEKIRLLTLKAAHSMDTLGSAGAkkEIAMIKVAAPRAVSKIVDWAIQVCGGAGV-SQDYPLAN-------MYAITRVLR 751
Cdd:cd01152 284 EAEALRLLVFRLASALAAGKPPGA--EASIAKLFGSELAQELAELALELLGTAALlRDPAPGAElagrweaDYLRSRATT 361
|
330
....*....|....
gi 1476413373 752 LADGPDEVHLSAIA 765
Cdd:cd01152 362 IYGGTSEIQRNIIA 375
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
451-763 |
6.13e-30 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 122.53 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 451 LIAEETGKCFFAPDVF-NCQAPDtgnmEVLHlYGSEEQKKQWLEPLLQ-GNITSCFCMTEPDvASSDATNIECSIQRDED 528
Cdd:PRK12341 72 LVLEEVSKCGAPAFLItNGQCIH----SMRR-FGSAEQLRKTAESTLEtGDPAYALALTEPG-AGSDNNSATTTYTRKNG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 529 SYVINGKKWWSSGAGNpkCKIAIVLGRTQNTSLSrHKQHSMILVPMNTPGVKIiRPLSVFGytdnFHGGHF-EIHFNQVR 607
Cdd:PRK12341 146 KVYLNGQKTFITGAKE--YPYMLVLARDPQPKDP-KKAFTLWWVDSSKPGIKI-NPLHKIG----WHMLSTcEVYLDNVE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 608 VPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLL 687
Cdd:PRK12341 218 VEESDLVGEEGMGFLNVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPIGHNQLIQEKLTLMAIKIENMRNM 297
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476413373 688 TLKAAHSMDTLGSAgaKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDE--VHLSA 763
Cdd:PRK12341 298 VYKVAWQADNGQSL--RTSAALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEimIYIAG 373
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
386-753 |
9.74e-25 |
|
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: 107.11 E-value: 9.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 386 VKHFMKQHILPAEKEVTEfyvQNENSVDKWgkplvidklKEMAKvEGLWNLFLPAV---SGLSHVDYALIAEETGKCffA 462
Cdd:cd01156 13 VREFAQKEIAPLAAKIDR---DNEFPRDLW---------RKMGK-LGLLGITAPEEyggSGMGYLAHVIIMEEISRA--S 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 463 PDVfncqAPDTG---NMEVLHLY--GSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDEDSYVINGKKW 537
Cdd:cd01156 78 GSV----ALSYGahsNLCINQIYrnGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKKGDRYVLNGSKM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 538 WSSGAgnPKCKIAIVLGRTqNTSLSRHKQHSMIlVPMNTPGVKIIRPLSVFGYTDNFHGghfEIHFNQVRVPATNLILGE 617
Cdd:cd01156 153 WITNG--PDADTLVVYAKT-DPSAGAHGITAFI-VEKGMPGFSRAQKLDKLGMRGSNTC---ELVFEDCEVPEENILGGE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 618 GRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDT 697
Cdd:cd01156 226 NKGVYVLMSGLDYERLVLAGGPIGIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDR 305
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1476413373 698 lGSAGAKKEIAMIKVAAPRAVSKIVDwAIQVCGGAGVSQDYPlanmyaITRVLRLA 753
Cdd:cd01156 306 -GNMDPKDAAGVILYAAEKATQVALD-AIQILGGNGYINDYP------TGRLLRDA 353
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
381-746 |
1.23e-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: 106.67 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 381 EVLI--KVKHFMKQHILPaekevtefYVQNENSVDKWGKPLvIDKLKEM----AKVEGLwnlflpAVSGLSHVDYALIAE 454
Cdd:cd01151 17 ERAIrdTAREFCQEELAP--------RVLEAYREEKFDRKI-IEEMGELgllgATIKGY------GCAGLSSVAYGLIAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 455 ETGKCffapdvfncqapDTG-----------NMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSI 523
Cdd:cd01151 82 EVERV------------DSGyrsfmsvqsslVMLPIYDFGSEEQKQKYLPKLASGELIGCFGLTEPN-HGSDPGGMETRA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 524 QRDEDSYVINGKKWWSSGAgnPKCKIAIVLGRTQNTSlsrhKQHSMIlVPMNTPGVKIIRPLSVFGYTDNFHGghfEIHF 603
Cdd:cd01151 149 RKDGGGYKLNGSKTWITNS--PIADVFVVWARNDETG----KIRGFI-LERGMKGLSAPKIQGKFSLRASITG---EIVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 604 NQVRVPATNLiLGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEK 683
Cdd:cd01151 219 DNVFVPEENL-LPGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQKKLADMLTEIAL 297
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1476413373 684 IRLLTLKAAHSMDTlGSAgAKKEIAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYP----LANMYAI 746
Cdd:cd01151 298 GLLACLRVGRLKDQ-GKA-TPEQISLLKRNNCGKALEIARTAREMLGGNGISDEYHiirhMVNLESV 362
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
484-765 |
2.28e-22 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 100.40 E-value: 2.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 484 SEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDED-SYVINGKKWWssgagnpkckiaIVLGRTQNTSLS 562
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSNgNYVLNGSKIW------------ITNGTVADVFLI 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 563 RHKQHSMI---LVPMNTPGVKIIRPLSVFGytdnFHGGHF-EIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMR 638
Cdd:PTZ00461 202 YAKVDGKItafVVERGTKGFTQGPKIDKCG----MRASHMcQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAM 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 639 TVGLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSM-----DTLGSAGAKkeiamiKVA 713
Cdd:PTZ00461 278 AVGIAERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNVhpgnkNRLGSDAAK------LFA 351
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1476413373 714 APRAvSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEVHLSAIA 765
Cdd:PTZ00461 352 TPIA-KKVADSAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNIT 402
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
503-604 |
4.17e-22 |
|
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: 91.19 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 503 CFCMTEPDvASSDATNIE-CSIQRDEDSYVINGKKWWSSGAgnPKCKIAIVLGRTQntSLSRHKQHSMILVPMNTPGVKI 581
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKtTAADGDGGGWVLNGTKWWITNA--GIADLFLVLARTG--GDDRHGGISLFLVPKDAPGVSV 75
|
90 100
....*....|....*....|...
gi 1476413373 582 IRPLSVFGYTDNFHGghfEIHFN 604
Cdd:pfam02770 76 RRIETKLGVRGLPTG---ELVFD 95
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
424-771 |
5.03e-18 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 86.81 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 424 LKEMAKVeGLWNLFLPAVSG---LSHVDYALIAEETGKcFFAPDVFNCQAPdtGNMEVLHLYGSEEQKKQWLEPLLQGNI 500
Cdd:PRK03354 43 VKALADM-GIDSLLIPEEHGgldAGFVTLAAVWMELGR-LGAPTYVLYQLP--GGFNTFLREGTQEQIDKIMAFRGTGKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 501 TSCFCMTEPDvASSDATNIECSIQRDEDSYVINGKKWW-SSGAGNPkckIAIVLGRtqNTSLSRHKQHSMILVPMNTPGV 579
Cdd:PRK03354 119 MWNSAITEPG-AGSDVGSLKTTYTRRNGKVYLNGSKCFiTSSAYTP---YIVVMAR--DGASPDKPVYTEWFVDMSKPGI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 580 KiIRPLSVFGY-TDNFhgghFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRI 658
Cdd:PRK03354 193 K-VTKLEKLGLrMDSC----CEITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 659 AFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMD--TLGSAGAkkeiAMIKVAAPRAVSKIVDWAIQVCGGAGVSQ 736
Cdd:PRK03354 268 QFGEAIGRFQLIQEKFAHMAIKLNSMKNMLYEAAWKADngTITSGDA----AMCKYFCANAAFEVVDSAMQVLGGVGIAG 343
|
330 340 350
....*....|....*....|....*....|....*
gi 1476413373 737 DYPLANMYAITRVLRLADGPDEVHLSAIATMELRD 771
Cdd:PRK03354 344 NHRISRFWRDLRVDRVSGGSDEMQILTLGRAVLKQ 378
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
473-755 |
1.03e-16 |
|
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: 83.21 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 473 TGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDED-SYVING-KKWWSSGAGNPKCKIA 550
Cdd:cd01153 90 QGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPD-AGSDLGALRTKAVYQADgSWRINGvKRFISAGEHDMSENIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 551 -IVLGRTQNTSlSRHKQHSMILVP-----MNTPGVKIIRPLSVFGYtdnfHGG-HFEIHFNQvrvpATNLILGE-GRG-- 620
Cdd:cd01153 169 hLVLARSEGAP-PGVKGLSLFLVPkflddGERNGVTVARIEEKMGL----HGSpTCELVFDN----AKGELIGEeGMGla 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 621 --FE-ISQGRLGPGrihhcMRTVGLAERALQIMCERATQRIAFKKKLYA--------HEVVAHWIAESRIAIEKIRLLTL 689
Cdd:cd01153 240 qmFAmMNGARLGVG-----TQGTGLAEAAYLNALAYAKERKQGGDLIKAapavtiihHPDVRRSLMTQKAYAEGSRALDL 314
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1476413373 690 KAAHSMDTLGSAGAKKEIA------------MIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPLANMYAITRVLRLADG 755
Cdd:cd01153 315 YTATVQDLAERKATEGEDRkalsaladlltpVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
483-759 |
1.37e-15 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 79.54 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 483 GSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDEDSYVINGKKWWSSGAgnPKCKIAIVLGRTQNTSLS 562
Cdd:PLN02519 125 GTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWCTNG--PVAQTLVVYAKTDVAAGS 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 563 RHKQHSMILVPMntPGVKIIRPLSVFGY--TDNfhgghFEIHFNQVRVPATNLILGEGRGFEISQGRLGPGRIHHCMRTV 640
Cdd:PLN02519 202 KGITAFIIEKGM--PGFSTAQKLDKLGMrgSDT-----CELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGPL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 641 GLAERALQIMCERATQRIAFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTlGSAGAKKEIAMIKVAAPRAVSK 720
Cdd:PLN02519 275 GLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDN-GKVDRKDCAGVILCAAERATQV 353
|
250 260 270
....*....|....*....|....*....|....*....
gi 1476413373 721 IVDwAIQVCGGAGVSQDYPLANMYAITRVLRLADGPDEV 759
Cdd:PLN02519 354 ALQ-AIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEI 391
|
|
| SrkA |
COG2334 |
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
25-256 |
3.80e-13 |
|
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: 70.72 E-value: 3.80e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 25 LEAYlnqhlsGFGAEREATLtIAQYRagksNPTFYLQ--KGfQTYVLRKKPPGSLlpKAHQIDREFKVQKALFSIGFPVP 102
Cdd:COG2334 7 LERY------GLGPLSSLKP-LNSGE----NRNYRVEteDG-RRYVLKLYRPGRW--SPEEIPFELALLAHLAAAGLPVP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 103 KPILYCSDTSVigtefyvmEHVQGRIFRDLT-IPGLSPAERSAIYVATV-ETLAQLHslniqsLQLEGYGIGAGyckRQV 180
Cdd:COG2334 73 APVPTRDGETL--------LELEGRPAALFPfLPGRSPEEPSPEQLEELgRLLARLH------RALADFPRPNA---RDL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 181 STWTKQYQAAAHQDIP------AMQQLSEWLMKNLPDNDNEEN--LIHGDFRLDNIVFHPKecRVIAVLDWELSTIGHPL 252
Cdd:COG2334 136 AWWDELLERLLGPLLPdpedraLLEELLDRLEARLAPLLGALPrgVIHGDLHPDNVLFDGD--GVSGLIDFDDAGYGPRL 213
|
....
gi 1476413373 253 SDLA 256
Cdd:COG2334 214 YDLA 217
|
|
| APH_ChoK_like |
cd05120 |
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ... |
44-265 |
6.08e-13 |
|
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: 67.33 E-value: 6.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 44 LTIAQYRAGKSNPTFYLqKGFQTYVLRKKPPgsllPKAHQIDREFKVQKALFS-IGFPVPKPI-LYCSDtsviGTEFYVM 121
Cdd:cd05120 1 ISVKLIKEGGDNKVYLL-GDPREYVLKIGPP----RLKKDLEKEAAMLQLLAGkLSLPVPKVYgFGESD----GWEYLLM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 122 EHVQGRIFRDLtIPGLSPAERSAIYVATVETLAQLHSLNIqslqlegygigagYCkrqvstwtkqyqaaahqdipamqql 201
Cdd:cd05120 72 ERIEGETLSEV-WPRLSEEEKEKIADQLAEILAALHRIDS-------------SV------------------------- 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1476413373 202 sewlmknlpdndneenLIHGDFRLDNIVFHPKEcRVIAVLDWELSTIGHPLSDLAHFslFYFWP 265
Cdd:cd05120 113 ----------------LTHGDLHPGNILVKPDG-KLSGIIDWEFAGYGPPAFDYAAA--LRDWT 157
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
506-759 |
6.51e-13 |
|
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: 71.25 E-value: 6.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 506 MTEPDVASSDATNIECSIQRDEDSYVINGKKWWSSgagNPKCKIAIVLGRTQNtSLSRHKQHSMILVPMNTP-----GVK 580
Cdd:cd01154 153 MTEKQGGSDLGANETTAERSGGGVYRLNGHKWFAS---APLADAALVLARPEG-APAGARGLSLFLVPRLLEdgtrnGYR 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 581 IIRPLSVFGYTDNFHGghfEIHFNQVrvpATNLILGEGRGFEISQGRLGPGRIHHCMRTVGLAERALQIMCERATQRIAF 660
Cdd:cd01154 229 IRRLKDKLGTRSVATG---EVEFDDA---EAYLIGDEGKGIYYILEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAF 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 661 KKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDtLGSAGAKKEIAMIKVAAP-------RAVSKIVDWAIQVCGGAG 733
Cdd:cd01154 303 GKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFD-RAAADKPVEAHMARLATPvakliacKRAAPVTSEAMEVFGGNG 381
|
250 260
....*....|....*....|....*.
gi 1476413373 734 VSQDYPLANMYAITRVLRLADGPDEV 759
Cdd:cd01154 382 YLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
635-740 |
1.85e-12 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 65.06 E-value: 1.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 635 HCMRTVGLAERALQIMCERATQRI--AFKKKLYAHEVVAHWIAESRIAIEKIRLLTLKAAHSMDTLGSAGA------KKE 706
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVraYFGVPLAEDPATQLALAEAAARIDAARLLLERAAARIEAAAAAGKpvtpalRAE 81
|
90 100 110
....*....|....*....|....*....|....
gi 1476413373 707 IAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPL 740
Cdd:pfam08028 82 ARRAAAFATELAVAAVDALFRAAGGSALFQDSPL 115
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
386-498 |
1.21e-10 |
|
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: 59.01 E-value: 1.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 386 VKHFMKQHILPAEKEVtefyvqnensvDKWGK--PLVIDKLKEMakveGLWNLFLPAV---SGLSHVDYALIAEETGKCF 460
Cdd:pfam02771 11 VREFAEEEIAPHAAEW-----------DEEGEfpRELWKKLGEL----GLLGITIPEEyggAGLDYLAYALVAEELARAD 75
|
90 100 110
....*....|....*....|....*....|....*...
gi 1476413373 461 FAPDVFnCQAPDTGNMEVLHLYGSEEQKKQWLEPLLQG 498
Cdd:pfam02771 76 ASVALA-LSVHSSLGAPPILRFGTEEQKERYLPKLASG 112
|
|
| PLN02526 |
PLN02526 |
acyl-coenzyme A oxidase |
376-583 |
2.21e-09 |
|
acyl-coenzyme A oxidase
Pssm-ID: 178141 [Multi-domain] Cd Length: 412 Bit Score: 60.25 E-value: 2.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 376 TRKGQEVLIKVKHFMKQHILPAekeVTEFYVQNENSVDkwgkplVIDKLKEMAKVEGLWNLFlpAVSGLSHVDYALIAEE 455
Cdd:PLN02526 30 TPEEQALRKRVRECMEKEVAPI---MTEYWEKAEFPFH------IIPKLGSLGIAGGTIKGY--GCPGLSITASAIATAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 456 TGKCFFAPDVFnCQAPDTGNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDVAsSDATNIECSIQRDEDSYVINGK 535
Cdd:PLN02526 99 VARVDASCSTF-ILVHSSLAMLTIALCGSEAQKQKYLPSLAQLDTVACWALTEPDYG-SDASSLNTTATKVEGGWILNGQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1476413373 536 KWWssgAGNPK-CKIAIVLGRTQNTslsrhKQHSMILVPMNTPGVKIIR 583
Cdd:PLN02526 177 KRW---IGNSTfADVLVIFARNTTT-----NQINGFIVKKGAPGLKATK 217
|
|
| CotS |
COG0510 |
Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; |
185-267 |
2.71e-09 |
|
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
Pssm-ID: 440276 [Multi-domain] Cd Length: 156 Bit Score: 56.71 E-value: 2.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 185 KQYQAAAHQDIPAMQQLSEWLMKNLPDNDNEENLIHGDFRLDNIVFHPK-ECRVIavlDWELSTIGHPLSDLAHFSLFYF 263
Cdd:COG0510 18 ERYLALGPRDLPELLRRLEELERALAARPLPLVLCHGDLHPGNFLVTDDgRLYLI---DWEYAGLGDPAFDLAALLVEYG 94
|
....
gi 1476413373 264 WPRT 267
Cdd:COG0510 95 LSPE 98
|
|
| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
55-256 |
3.02e-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: 56.11 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 55 NPTFYLQKGFQTYVLRkkppgsLLPKAH---QIDREFKVQKALFSIGFPVPKPILYcSDTSVIGTefyvmehVQGRIFRD 131
Cdd:cd05153 28 NTNYFVTTTDGRYVLT------LFEKRRsaaELPFELELLDHLAQAGLPVPRPLAD-KDGELLGE-------LNGKPAAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 132 LT-IPGLSPAERSAIYVATV-ETLAQLHSLniqslqLEGYGIGAGYCkRQVSTWTKQYQAAAHQDIPAMQQLSEWL---- 205
Cdd:cd05153 94 FPfLPGESLTTPTPEQCRAIgAALARLHLA------LAGFPPPRPNP-RGLAWWKPLAERLKARLDLLAADDRALLedel 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1476413373 206 -------MKNLPdndneENLIHGDFRLDNIVFhpKECRVIAVLDWELSTIGHPLSDLA 256
Cdd:cd05153 167 arlqalaPSDLP-----RGVIHADLFRDNVLF--DGDRLSGIIDFYDACYDPLLYDLA 217
|
|
| Bud32 |
COG3642 |
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ... |
86-256 |
3.90e-07 |
|
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: 50.34 E-value: 3.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 86 REFKVQKALFSIGFPVPKPILYCSDTSVIgtefyVMEHVQGRIFRDLTIPGLSPAErsaIYVATVETLAQLHSLNIqslq 165
Cdd:COG3642 5 REARLLRELREAGVPVPKVLDVDPDDADL-----VMEYIEGETLADLLEEGELPPE---LLRELGRLLARLHRAGI---- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 166 legygigagyckrqvstwtkqyqaaahqdipamqqlsewlmknlpdndneenlIHGDFRLDNIVFHPKEcrvIAVLDWEL 245
Cdd:COG3642 73 -----------------------------------------------------VHGDLTTSNILVDDGG---VYLIDFGL 96
|
170
....*....|.
gi 1476413373 246 STIGHPLSDLA 256
Cdd:COG3642 97 ARYSDPLEDKA 107
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
474-577 |
1.14e-06 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 52.18 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 474 GNMEVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNIECSIQRDED-SYVINGKK-WWSSGAGNPKCKIA- 550
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ-CGTDLGQVKTKAEPSADgSYKITGTKiFISAGDHDLTENIVh 233
|
90 100
....*....|....*....|....*..
gi 1476413373 551 IVLGRTQNtSLSRHKQHSMILVPMNTP 577
Cdd:PTZ00456 234 IVLARLPN-SLPTTKGLSLFLVPRHVV 259
|
|
| AXO |
cd01150 |
Peroxisomal acyl-CoA oxidase; Peroxisomal acyl-CoA oxidases (AXO) catalyze the first set in ... |
483-613 |
4.32e-06 |
|
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: 50.02 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 483 GSEEQKKQWLEPLLQGNITSCFCMTEpdvaSSDATN---IECSIQRDE--DSYVIN-----GKKWWSSGAGNpKCKIAIV 552
Cdd:cd01150 117 GTDEHQDYWLQGANNLEIIGCFAQTE----LGHGSNlqgLETTATYDPltQEFVINtpdftATKWWPGNLGK-TATHAVV 191
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 553 LGRTQnTSLSRHKQHSMIlVP---MNT----PGVKIIRPLSVFGYT--DNfhgGHfeIHFNQVRVPATNL 613
Cdd:cd01150 192 FAQLI-TPGKNHGLHAFI-VPirdPKThqplPGVTVGDIGPKMGLNgvDN---GF--LQFRNVRIPRENL 254
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
477-740 |
2.15e-05 |
|
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: 47.70 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 477 EVLHLYGSEEQKKQWLEPLLQGNITSCfCMTEPDVASSDATNIEcsIQRDEDSYVINGKKWWSSGagnpkckiAIVLGRT 556
Cdd:cd01163 81 EALLLAGPEQFRKRWFGRVLNGWIFGN-AVSERGSVRPGTFLTA--TVRDGGGYVLNGKKFYSTG--------ALFSDWV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 557 QNTSLSRHKQHSMILVPMNTPGVKIIRPLSVFG--YTDNfhGghfEIHFNQVRVPATNLIlgeGRGFEISQGRLGPG--R 632
Cdd:cd01163 150 TVSALDEEGKLVFAAVPTDRPGITVVDDWDGFGqrLTAS--G---TVTFDNVRVEPDEVL---PRPNAPDRGTLLTAiyQ 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 633 IHHCMRTVGLAERALqimcERATQRIAFKKKLYAHEVVAH---------WIAESRIAIEKIRLLTLKAAHSMDTLGSAGA 703
Cdd:cd01163 222 LVLAAVLAGIARAAL----DDAVAYVRSRTRPWIHSGAESarddpyvqqVVGDLAARLHAAEALVLQAARALDAAAAAGT 297
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1476413373 704 KKE----------IAMIKVAAPRAVSKIVDWAIQVCGGAGVSQDYPL 740
Cdd:cd01163 298 ALTaeargeaalaVAAAKVVVTRLALDATSRLFEVGGASATAREHNL 344
|
|
| Kdo |
pfam06293 |
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ... |
84-162 |
1.00e-04 |
|
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in E. coli and that it is required for virulence in invasive strains of S. enterica.
Pssm-ID: 428872 Cd Length: 206 Bit Score: 44.30 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 84 IDREFKVQKALFSIGFPVPKPILYCSDTSVIG-TEFYVMEHVQGriFRDLTI-----PGLSPAERSAIYVATVETLAQLH 157
Cdd:pfam06293 57 AFREFRLIRRLREAGLPVPKPVAAGEVKVGGGyRADLLTERLEG--AQSLADwladwAVPSGELRRAIWEAVGRLIRQMH 134
|
....*
gi 1476413373 158 SLNIQ 162
Cdd:pfam06293 135 RAGVQ 139
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
477-519 |
3.48e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 44.04 E-value: 3.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1476413373 477 EVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNI 519
Cdd:PRK09463 170 ELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPE-AGSDAGSI 211
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
477-519 |
6.51e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 43.41 E-value: 6.51e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1476413373 477 EVLHLYGSEEQKKQWLEPLLQGNITSCFCMTEPDvASSDATNI 519
Cdd:PRK13026 169 ELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPE-AGSDAGAI 210
|
|
| RIO2 |
COG0478 |
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction ... |
86-161 |
8.61e-04 |
|
RIO-like serine/threonine protein kinase fused to N-terminal HTH domain [Signal transduction mechanisms];
Pssm-ID: 440246 [Multi-domain] Cd Length: 183 Bit Score: 41.04 E-value: 8.61e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1476413373 86 REFKVQKALFSIGFPVPKPILYCsdTSVIgtefyVMEHVQGRIFRDLTipgLSPAErsAIYVATVETLAQLHSLNI 161
Cdd:COG0478 48 REFRALERLYPAGLPVPRPIAAN--RHAI-----VMERIEGVELARLK---LEDPE--EVLDKILEEIRRAHDAGI 111
|
|
| DarT |
pfam14487 |
ssDNA thymidine ADP-ribosyltransferase, DarT; This family of proteins is found in bacteria, ... |
243-414 |
1.22e-03 |
|
ssDNA thymidine ADP-ribosyltransferase, DarT; This family of proteins is found in bacteria, archaea and eukaryotes. Proteins in this family are typically between 201 and 230 amino acids in length. There is a single completely conserved residue E that may be functionally important. This family is distantly similar to pfam01885. Studies in search for novel ADP-ribosylation systems in bacterial genomes have identified an operon that encodes a conserved protein containing a distinct type of macrodomain associated with this family. This led to the identification of a toxin-antitoxin (TA) system, with DarT acting as the toxin. It is an enzyme that specifically modifies thymidines on single-stranded DNA in a sequence-specific manner by a nucleotide-type modification called ADP-ribosylation. This modification in turn can be removed by DarG, the antitoxin macrodomain protein. In addition, it was illustrated that substitution of the single completely conserved glutamate residue resulted in attenuation of function where DarT was non-toxic.
Pssm-ID: 433984 Cd Length: 201 Bit Score: 40.80 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 243 WELSTIGHPLSDLAHFSLFYFWPRTvPM---INQGsyseNSGIPSMEELISIYCRCRGINSILPNWNFFLalsyfkmaGI 319
Cdd:pfam14487 44 LNLTVPCPPGGTLGDYVPFYFCPRS-PMlyrIHGG----NHPEYQGDDIVVLVIDLEILVESGRGWVFTD--------GN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1476413373 320 AQGVYSRYLLGNNSSEdsFLFANIVQplaetglqlSKRTFSTVLPQidttgqlFVQTRKGQEVLIKvkhfmkqHILPAEK 399
Cdd:pfam14487 111 AAASYTRFYNGLEDLK--EIDWDLVY---------ARYWFPTDDDS-------DRKERKQAEFLVP-------DRIPWEL 165
|
170
....*....|....*
gi 1476413373 400 eVTEFYVQNENSVDK 414
Cdd:pfam14487 166 -ITGIGVRNQEVKDR 179
|
|
| RIO2_C |
cd05144 |
C-terminal catalytic domain of the atypical protein serine kinase, RIO2 kinase; RIO2 is ... |
86-126 |
1.31e-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: 40.57 E-value: 1.31e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1476413373 86 REFKVQKALFSIGFPVPKPILYcsDTSVIgtefyVMEHVQG 126
Cdd:cd05144 67 KEFAALKALYEEGFPVPKPIDW--NRHAV-----VMELIDG 100
|
|
| APH_ChoK_like_1 |
cd05155 |
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and ... |
219-256 |
9.05e-03 |
|
Uncharacterized bacterial proteins with similarity to Aminoglycoside 3'-phosphotransferase and Choline kinase; This subfamily is composed of uncharacterized bacterial proteins with similarity to APH and ChoK. Other APH/ChoK-like proteins include 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). These proteins 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-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: 270704 [Multi-domain] Cd Length: 234 Bit Score: 38.37 E-value: 9.05e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1476413373 219 IHGDFRLDNIVFhpKECRVIAVLDWELSTIGHPLSDLA 256
Cdd:cd05155 166 LHGDLHPGNLLV--RDGRLSAVIDFGDLGVGDPACDLA 201
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|
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