|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02876 |
PLN02876 |
acyl-CoA dehydrogenase |
1-831 |
0e+00 |
|
acyl-CoA dehydrogenase
Pssm-ID: 215473 [Multi-domain] Cd Length: 822 Bit Score: 1698.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 1 MLTSGLLRPVDDAHAIDEAALLRYAAEHVAGFPSPARGLALTQFGHGQSNPTYCIEASApGGVTARYVLRKKPPGAILQS 80
Cdd:PLN02876 3 KRTSDLLVPVQSAHRFDEDALLRYAAANVAGFPVPPSTFKVSQFGHGQSNPTFLLEVGN-GGSVKRYVLRKKPPGKLLQS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 81 AHAVEREFQVLKALGTYTDVPVPKVFCLCTDASVIGTPFYIMEHLEGLIYPDNKLTGVTPTKRKTIYLAAAETLAAIHKV 160
Cdd:PLN02876 82 AHAVEREYQVLRALGEHTDVPVPKVYCLCTDASVIGTAFYIMEYLEGRIFVDPKLPGVAPERRRAIYRATAKVLAALHSA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 161 DVTAIGLQKYGRRDNYCKRQVERWGRQYLSSTGEGKPARYQKMLDLAHWLKEHIPKEDSSaGFGTGLVHGDYRVDNLVFH 240
Cdd:PLN02876 162 DVDAIGLGKYGRRDNYCKRQVERWAKQYLASTGEGKPPRNPKMLELIDWLRENIPAEDST-GAGTGIVHGDFRIDNLVFH 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 241 PTEDRVIGVLDWELSTLGNQMCDVAYSSLPYIIDATTSTGYSYGGFEYTGIPDGIPPLEEYLAAYCSISARPWPAASWKF 320
Cdd:PLN02876 241 PTEDRVIGILDWELSTLGNQMCDVAYSCLPYIVDINLDNQQVGKGFEFTGIPEGIPSLPEYLAEYCSASGKPWPAANWKF 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 321 YVAFSLFRGASIYAGVYHRWTMGNASGGERARFSGKIANAMVDRAWDIINRENVLREQPARGMHasngpsqefQRKHEGS 400
Cdd:PLN02876 321 YVAFSLFRGASIYAGVYSRWLMGNASGGERARNAGKQANFLVDSALDYIARKNVLPEHPPSGQF---------GREPEYS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 401 ISTKDQGKFVPSEKVMQLRNKLMKFMEDYIYPMESEFYKRAHSTSRWTIHPEEEKLKALAKREGLWNLFIPLDSAARARE 480
Cdd:PLN02876 392 SLSKESGRFVPSEKVLELRKKLIKFMEDHIYPMENEFYKLAQSSSRWTVHPEEERLKELAKKEGLWNLWIPLDSAARARK 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 481 LLFEDMSHGSPGSSEELLLGAGLTNLEYGYLCEIMGRSIWAPQIFNCGPPDTGNMEVLLRYGTKEQQKQWLVPLLEGKIR 560
Cdd:PLN02876 472 LLFEDNKHMVSGDSADQLLGAGLSNLEYGYLCEIMGRSVWAPQVFNCGAPDTGNMEVLLRYGNKEQQLEWLIPLLEGKIR 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 561 SGFAMTEPQVASSDATNIECSISRQGDFYVINGTKWWTSGAMDPRCQILVLMGKTDFSAPKHKQQSMILVDVKTPGVQIR 640
Cdd:PLN02876 552 SGFAMTEPQVASSDATNIECSIRRQGDSYVINGTKWWTSGAMDPRCRVLIVMGKTDFNAPKHKQQSMILVDIQTPGVQIK 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 641 RPLLVFGFDDAPHGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKK 720
Cdd:PLN02876 632 RPLLVFGFDDAPHGHAEISFENVRVPAKNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMQLMVQRALSRKAFGKL 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 721 IAQHGSFLADLAKCRVELEQARLLVLEAADQLDRHGNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHL 800
Cdd:PLN02876 712 IAQHGSFLSDLAKCRVELEQTRLLVLEAADQLDRLGNKKARGIIAMAKVAAPNMALKVLDMAMQVHGAAGVSSDTVLAHL 791
|
810 820 830
....*....|....*....|....*....|.
gi 1002285595 801 WATARTLRIADGPDEVHLGTIAKLELQRARM 831
Cdd:PLN02876 792 WATARTLRIADGPDEVHLGTIAKLELQRAKL 822
|
|
| ACAD_FadE2 |
cd01155 |
Acyl-CoA dehydrogenases similar to fadE2; FadE2-like Acyl-CoA dehydrogenase (ACAD). Acyl-CoA ... |
413-827 |
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: 699.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 413 EKVMQLRNKLMKFMEDYIYPMESEF--YKRAHSTSRWTIHPEEEKLKALAKREGLWNLFIPLDSAararellfedmshgs 490
Cdd:cd01155 1 RKAQELRARVKAFMEEHVYPAEQEFleYYAEGGDRWWTPPPIIEKLKAKAKAEGLWNLFLPEVSG--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 491 pgsseelllGAGLTNLEYGYLCEIMGRSIWAPQIFNCGPPDTGNMEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQV 570
Cdd:cd01155 66 ---------LSGLTNLEYAYLAEETGRSFFAPEVFNCQAPDTGNMEVLHRYGSEEQKKQWLEPLLDGKIRSAFAMTEPDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 571 ASSDATNIECSISRQGDFYVINGTKWWTSGAMDPRCQILVLMGKTDF-SAPKHKQQSMILVDVKTPGVQIRRPLLVFGFD 649
Cdd:cd01155 137 ASSDATNIECSIERDGDDYVINGRKWWSSGAGDPRCKIAIVMGRTDPdGAPRHRQQSMILVPMDTPGVTIIRPLSVFGYD 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 650 DAPHGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLA 729
Cdd:cd01155 217 DAPHGHAEITFDNVRVPASNLILGEGRGFEIAQGRLGPGRIHHCMRLIGAAERALELMCQRAVSREAFGKKLAQHGVVAH 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 730 DLAKCRVELEQARLLVLEAADQLDRHGNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRI 809
Cdd:cd01155 297 WIAKSRIEIEQARLLVLKAAHMIDTVGNKAARKEIAMIKVAAPRMALKIIDRAIQVHGAAGVSQDTPLANMYAWARTLRI 376
|
410
....*....|....*...
gi 1002285595 810 ADGPDEVHLGTIAKLELQ 827
Cdd:cd01155 377 ADGPDEVHLRSIARMELK 394
|
|
| CaiA |
COG1960 |
Acyl-CoA dehydrogenase related to the alkylation response protein AidB [Lipid transport and ... |
409-830 |
5.82e-106 |
|
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: 331.03 E-value: 5.82e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 409 FVPSEKVMQLRNKLMKFMEDYIYPMESEFYKRAHstsrwtiHPEEekLKALAKREGLWNLFIPldsaaraREllfedmsH 488
Cdd:COG1960 3 FELTEEQRALRDEVREFAEEEIAPEAREWDREGE-------FPRE--LWRKLAELGLLGLTIP-------EE-------Y 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 489 GspgsseelllGAGLTNLEYGYLCEIMGRSiWAPQIFNCGPPDtGNMEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEP 568
Cdd:COG1960 60 G----------GLGLSLVELALVLEELARA-DASLALPVGVHN-GAAEALLRFGTEEQKERYLPRLASGEWIGAFALTEP 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 569 QvASSDATNIECSISRQGDFYVINGTKWWTSGAmdPRCQILVLMGKTDfSAPKHKQQSMILVDVKTPGVQIRRPLLVFGf 648
Cdd:COG1960 128 G-AGSDAAALRTTAVRDGDGYVLNGQKTFITNA--PVADVILVLARTD-PAAGHRGISLFLVPKDTPGVTVGRIEDKMG- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 649 dDAPHGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFL 728
Cdd:COG1960 203 -LRGSDTGELFFDDVRVPAENLLGEEGKGFKIAMSTLNAGRLGLAAQALGIAEAALELAVAYAREREQFGRPIADFQAVQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 729 ADLAKCRVELEQARLLVLEAADQLDRhgNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLR 808
Cdd:COG1960 282 HRLADMAAELEAARALVYRAAWLLDA--GEDAALEAAMAKLFATEAALEVADEALQIHGGYGYTREYPLERLYRDARILT 359
|
410 420
....*....|....*....|..
gi 1002285595 809 IADGPDEVHLGTIAKLELQRAR 830
Cdd:COG1960 360 IYEGTNEIQRLIIARRLLGRPG 381
|
|
| ACAD10_11_N-like |
cd05154 |
N-terminal domain of Acyl-CoA dehydrogenase (ACAD) 10 and 11, and similar proteins; This ... |
39-309 |
3.57e-92 |
|
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: 290.29 E-value: 3.57e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 39 LALTQFGHGQSNPTYCIEASAPGGvTARYVLRKKPPGAILQSAHAVEREFQVLKALGTyTDVPVPKVFCLCTDASVIGTP 118
Cdd:cd05154 1 LAVRRLSGGASNETYLVDAGGDGG-GRRLVLRRPPPGGLLPSAHDLEREYRVLRALAG-TGVPVPRVLALCEDPSVLGAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 119 FYIMEHLEGLIYPDNKL-TGVTPTKRKTIYLAAAETLAAIHKVDVTAIGLQKYGRRDNYCKRQVERWGRQYLSSTGEGKP 197
Cdd:cd05154 79 FYVMERVDGRVLPDPLPrPDLSPEERRALARSLVDALAALHSVDPAALGLADLGRPEGYLERQVDRWRRQLEAAATDPPP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 198 AryqkMLDLAHWLKEHIPKEDssagfGTGLVHGDYRVDNLVFHPTeDRVIGVLDWELSTLGNQMCDVAYSSLPYIIDATT 277
Cdd:cd05154 159 A----LEEALRWLRANLPADG-----RPVLVHGDFRLGNLLFDPD-GRVTAVLDWELATLGDPLEDLAWLLARWWRPGDP 228
|
250 260 270
....*....|....*....|....*....|..
gi 1002285595 278 STGYSYGGfeytgiPDGIPPLEEYLAAYCSIS 309
Cdd:cd05154 229 PGLAAPTR------LPGFPSREELLARYEEAS 254
|
|
| ACAD |
cd00567 |
Acyl-CoA dehydrogenase; Both mitochondrial acyl-CoA dehydrogenases (ACAD) and peroxisomal ... |
531-823 |
2.08e-86 |
|
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: 277.63 E-value: 2.08e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 531 DTGNMEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWWTSGAmdPRCQILV 610
Cdd:cd00567 41 LLLGAALLLAYGTEEQKERYLPPLASGEAIAAFALTEPG-AGSDLAGIRTTARKDGDGYVLNGRKIFISNG--GDADLFI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 611 LMGKTDFSAPKHKQQSMILVDVKTPGVQIRRPLLVFGFDdaPHGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRL 690
Cdd:cd00567 118 VLARTDEEGPGHRGISAFLVPADTPGVTVGRIWDKMGMR--GSGTGELVFDDVRVPEDNLLGEEGGGFELAMKGLNVGRL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 691 HHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLDRhGNKKARGILAMAKVA 770
Cdd:cd00567 196 LLAAVALGAARAALDEAVEYAKQRKQFGKPLAEFQAVQFKLADMAAELEAARLLLYRAAWLLDQ-GPDEARLEAAMAKLF 274
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1002285595 771 APNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEVHLGTIAK 823
Cdd:cd00567 275 ATEAAREVADLAMQIHGGRGYSREYPVERYLRDARAARIAEGTAEIQRLIIAR 327
|
|
| YcbJ |
COG3173 |
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction ... |
14-323 |
9.24e-68 |
|
Predicted kinase, aminoglycoside phosphotransferase (APT) family [General function prediction only];
Pssm-ID: 442406 [Multi-domain] Cd Length: 284 Bit Score: 226.15 E-value: 9.24e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 14 HAIDEAALLRYAAEHVAGFPSPARglaLTQFGHGQSNPTYCIEASApggvtaRYVLRKKPPGaiLQSAHAVEREFQVLKA 93
Cdd:COG3173 1 EELDEAALRALLAAQLPGLAGLPE---VEPLSGGWSNLTYRLDTGD------RLVLRRPPRG--LASAHDVRREARVLRA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 94 LGTYTDVPVPKVFCLCTDASVIGTPFYIMEHLEGLIYPDnKLTGVTPTKRKTIYLAAAETLAAIHKVDVTAIGLQKyGRR 173
Cdd:COG3173 70 LAPRLGVPVPRPLALGEDGEVIGAPFYVMEWVEGETLED-ALPDLSPAERRALARALGEFLAALHAVDPAAAGLAD-GRP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 174 DNyCKRQVERWGRQYlsstgEGKPARYQKMLDL----AHWLKEHIPKEDSsagfgTGLVHGDYRVDNLVFHPTEDRVIGV 249
Cdd:COG3173 148 EG-LERQLARWRAQL-----RRALARTDDLPALrerlAAWLAANLPEWGP-----PVLVHGDLRPGNLLVDPDDGRLTAV 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002285595 250 LDWELSTLGNQMCDVAYSSLPYIIDattstgysyggfeytgiPDGIPPLEEYLAAYCsisARPWPAASWKFYVA 323
Cdd:COG3173 217 IDWELATLGDPAADLAYLLLYWRLP-----------------DDLLGPRAAFLAAYE---EATGDLDDLTWWAL 270
|
|
| SCAD_SBCAD |
cd01158 |
Short chain acyl-CoA dehydrogenases and eukaryotic short/branched chain acyl-CoA ... |
538-823 |
5.30e-48 |
|
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: 174.76 E-value: 5.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 538 LLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPqVASSDATNIECSISRQGDFYVINGTKWWTSGAMDprCQILVLMGKTDF 617
Cdd:cd01158 92 IIKFGTEEQKKKYLPPLATGEKIGAFALSEP-GAGSDAAALKTTAKKDGDDYVLNGSKMWITNGGE--ADFYIVFAVTDP 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 618 SApKHKQQSMILVDVKTPGVQIRRPLLVFGFDDAPHghAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLI 697
Cdd:cd01158 169 SK-GYRGITAFIVERDTPGLSVGKKEDKLGIRGSST--TELIFEDVRVPKENILGEEGEGFKIAMQTLDGGRIGIAAQAL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 698 GAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLDRHGN--KKArgilAMAKVAAPNMA 775
Cdd:cd01158 246 GIAQAALDAAVDYAKERKQFGKPIADFQGIQFKLADMATEIEAARLLTYKAARLKDNGEPfiKEA----AMAKLFASEVA 321
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1002285595 776 LKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEVHLGTIAK 823
Cdd:cd01158 322 MRVTTDAVQIFGGYGYTKDYPVERYYRDAKITEIYEGTSEIQRLVIAK 369
|
|
| IBD |
cd01162 |
Isobutyryl-CoA dehydrogenase; Isobutyryl-CoA dehydrogenase (IBD) catalyzes the alpha, beta- ... |
540-828 |
4.95e-43 |
|
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: 160.69 E-value: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 540 RYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWWTSGAMDPrcQILVLMGKTDFSA 619
Cdd:cd01162 95 SFGNDEQRERFLPDLCTMEKLASYCLTEPG-SGSDAAALRTRAVREGDHYVLNGSKAFISGAGDS--DVYVVMARTGGEG 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 620 PKhkQQSMILVDVKTPGVQIRRPLLVFGFDDAPHghAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGA 699
Cdd:cd01162 172 PK--GISCFVVEKGTPGLSFGANEKKMGWNAQPT--RAVIFEDCRVPVENRLGGEGQGFGIAMAGLNGGRLNIASCSLGA 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 700 AERGMNLMVERALSRTTFGKKIA--QHGSF-LADLAkcrVELEQARLLVLEAADQLDRhGNKKARGILAMAKVAAPNMAL 776
Cdd:cd01162 248 AQAALDLARAYLEERKQFGKPLAdfQALQFkLADMA---TELVASRLMVRRAASALDR-GDPDAVKLCAMAKRFATDECF 323
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1002285595 777 KVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEVHLGTIAKLELQR 828
Cdd:cd01162 324 DVANQALQLHGGYGYLKDYPVEQYVRDLRVHQILEGTNEIMRLIIARALLTR 375
|
|
| ACAD_fadE6_17_26 |
cd01152 |
Putative acyl-CoA dehydrogenases similar to fadE6, fadE17, and fadE26; Putative acyl-CoA ... |
524-827 |
2.05e-40 |
|
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: 153.27 E-value: 2.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 524 IFNCGPpdtgnmeVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWWTSGAMd 603
Cdd:cd01152 89 IDLAGP-------TILAYGTDEQKRRFLPPILSGEEIWCQGFSEPG-AGSDLAGLRTRAVRDGDDWVVNGQKIWTSGAH- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 604 pRCQILVLMGKTDFSAPKHKQQSMILVDVKTPGVQIrRPLLVFgfdDAPHGHAEITFENVRVPATNILLGEGRGFEIAQG 683
Cdd:cd01152 160 -YADWAWLLVRTDPEAPKHRGISILLVDMDSPGVTV-RPIRSI---NGGEFFNEVFLDDVRVPDANRVGEVNDGWKVAMT 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 684 RLGPGRlhhcMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLDRHGNKKARGi 763
Cdd:cd01152 235 TLNFER----VSIGGSAATFFELLLARLLLLTRDGRPLIDDPLVRQRLARLEAEAEALRLLVFRLASALAAGKPPGAEA- 309
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002285595 764 lAMAKVAAPNMALKVLDMAMQVHGGAGL----SSDTVLSHLWA----TARTLRIADGPDEVHLGTIAKLELQ 827
Cdd:cd01152 310 -SIAKLFGSELAQELAELALELLGTAALlrdpAPGAELAGRWEadylRSRATTIYGGTSEIQRNIIAERLLG 380
|
|
| Acyl-CoA_dh_1 |
pfam00441 |
Acyl-CoA dehydrogenase, C-terminal domain; C-terminal domain of Acyl-CoA dehydrogenase is an ... |
675-823 |
3.02e-39 |
|
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: 142.39 E-value: 3.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 675 GRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLDR 754
Cdd:pfam00441 1 GRGFRVAMETLNHERLAIAAMALGLARRALDEALAYARRRKAFGRPLIDFQLVRHKLAEMAAEIEAARLLVYRAAEALDA 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1002285595 755 HGNKKARGilAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEVHLGTIAK 823
Cdd:pfam00441 81 GGPDGAEA--SMAKLYASEAAVEVADLAMQLHGGYGYLREYPVERLYRDARVLRIGEGTSEIQRNIIAR 147
|
|
| APH |
pfam01636 |
Phosphotransferase enzyme family; This family consists of bacterial antibiotic resistance ... |
41-306 |
6.63e-39 |
|
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: 144.57 E-value: 6.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 41 LTQFGHGQSNPTYCIEASApggvtARYVLRKKPPGAILQSAHAVEREFQVLKALGtytDVPVPKVFCLCTDASVIGTPFY 120
Cdd:pfam01636 2 LRPISSGASNRTYLVTTGD-----GRYVLRLPPPGRAAEELRRELALLRHLAAAG---VPPVPRVLAGCTDAELLGLPFL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 121 IMEHLEGLIYpdnkLTGVTPTKRKTIYLAAAETLAAIHKVDVTAIGLQKYGRRDNYCKRQVERWGRQYLsstgegKPARY 200
Cdd:pfam01636 74 LMEYLPGEVL----ARPLLPEERGALLEALGRALARLHAVDPAALPLAGRLARLLELLRQLEAALARLL------AAELL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 201 QKMLDLAHWLKEHIPKEDSSAGFgTGLVHGDYRVDNLVFHPtEDRVIGVLDWELSTLGNQMCDVAYSslpyiidattstg 280
Cdd:pfam01636 144 DRLEELEERLLAALLALLPAELP-PVLVHGDLHPGNLLVDP-GGRVSGVIDFEDAGLGDPAYDLAIL------------- 208
|
250 260
....*....|....*....|....*.
gi 1002285595 281 ysyggFEYTGIPDGIPPLEEYLAAYC 306
Cdd:pfam01636 209 -----LNSWGRELGAELLAAYLAAYG 229
|
|
| VLCAD |
cd01161 |
Very long chain acyl-CoA dehydrogenase; VLCAD is an acyl-CoA dehydrogenase (ACAD), which is ... |
500-829 |
4.59e-36 |
|
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: 141.45 E-value: 4.59e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 500 GAGLTNLEYGYLCEIMGR------SIWAPQifncgppDTGNMEVLLrYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASS 573
Cdd:cd01161 81 GLGLNNTQYARLAEIVGMdlgfsvTLGAHQ-------SIGFKGILL-FGTEAQKEKYLPKLASGEWIAAFALTEPS-SGS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 574 DATNIECS--ISRQGDFYVINGTKWW-TSGAMdprCQILVLMGKTDFSAPKHKQQSMI---LVDVKTPGVQIRRPLLVFG 647
Cdd:cd01161 152 DAASIRTTavLSEDGKHYVLNGSKIWiTNGGI---ADIFTVFAKTEVKDATGSVKDKItafIVERSFGGVTNGPPEKKMG 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 648 FDDAphGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSF 727
Cdd:cd01161 229 IKGS--NTAEVYFEDVKIPVENVLGEVGDGFKVAMNILNNGRFGMGAALIGTMKRCIEKAVDYANNRKQFGKKIHEFGLI 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 728 LADLAKCRVELEQARLLVLEAADQLDRHGNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTL 807
Cdd:cd01161 307 QEKLANMAILQYATESMAYMTSGNMDRGLKAEYQIEAAISKVFASEAAWLVVDEAIQIHGGMGFMREYGVERVLRDLRIF 386
|
330 340
....*....|....*....|..
gi 1002285595 808 RIADGPDEVHLGTIAKLELQRA 829
Cdd:cd01161 387 RIFEGTNEILRLFIALTGLQHA 408
|
|
| MCAD |
cd01157 |
Medium chain acyl-CoA dehydrogenase; MCADs are mitochondrial beta-oxidation enzymes, which ... |
412-828 |
6.05e-36 |
|
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: 140.41 E-value: 6.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 412 SEKVMQLRNKLMKFMEDYIYPMESEFYKRAHSTsrWTIHPEEEKLkalakreGLWNLFIPLDsaararellfedmsHGSP 491
Cdd:cd01157 2 TEQQKEFQETARKFAREEIIPVAAEYDKSGEYP--WPLIKRAWEL-------GLMNTHIPED--------------CGGL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 492 GSSeelLLGAGLTNLEYGYLCEIMGRSIWAPQIfncgppdtGNMEVLLRyGTKEQQKQWLVPLLEGKIRSGFAMTEPQvA 571
Cdd:cd01157 59 GLG---TFDTCLITEELAYGCTGVQTAIEANSL--------GQMPVIIS-GNDEQKKKYLGRMTEEPLMCAYCVTEPG-A 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 572 SSDATNIECSISRQGDFYVINGTKWWTSGAMDPRCQILVLMGKTDFSAPKHKQQSMILVDVKTPGVQIRRPLLVFGfdDA 651
Cdd:cd01157 126 GSDVAGIKTKAEKKGDEYIINGQKMWITNGGKANWYFLLARSDPDPKCPASKAFTGFIVEADTPGIQPGRKELNMG--QR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 652 PHGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADL 731
Cdd:cd01157 204 CSDTRGITFEDVRVPKENVLIGEGAGFKIAMGAFDKTRPPVAAGAVGLAQRALDEATKYALERKTFGKLIAEHQAVSFML 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 732 AKCRVELEQARLLVLEAADQLDRhgNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIAD 811
Cdd:cd01157 284 ADMAMKVELARLAYQRAAWEVDS--GRRNTYYASIAKAFAADIANQLATDAVQIFGGNGFNSEYPVEKLMRDAKIYQIYE 361
|
410
....*....|....*..
gi 1002285595 812 GPDEVHLGTIAKLELQR 828
Cdd:cd01157 362 GTSQIQRLIISREHLGK 378
|
|
| LCAD |
cd01160 |
Long chain acyl-CoA dehydrogenase; LCAD is an acyl-CoA dehydrogenases (ACAD), which is found ... |
535-823 |
3.13e-34 |
|
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: 134.94 E-value: 3.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 535 MEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWWTSGAMdpRCQILVLMGK 614
Cdd:cd01160 88 SPYITRAGSPEQKERVLPQMVAGKKIGAIAMTEPG-AGSDLQGIRTTARKDGDHYVLNGSKTFITNGM--LADVVIVVAR 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 615 TDFSAPKHKQQSMILVDVKTPGVQIRRPLLVFGFddAPHGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCM 694
Cdd:cd01160 165 TGGEARGAGGISLFLVERGTPGFSRGRKLKKMGW--KAQDTAELFFDDCRVPAENLLGEENKGFYYLMQNLPQERLLIAA 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 695 RLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLvLEAADQLDRHGNKKARGIlAMAKVAAPNM 774
Cdd:cd01160 243 GALAAAEFMLEETRNYVKQRKAFGKTLAQLQVVRHKIAELATKVAVTRAF-LDNCAWRHEQGRLDVAEA-SMAKYWATEL 320
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1002285595 775 ALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEVHLGTIAK 823
Cdd:cd01160 321 QNRVAYECVQLHGGWGYMREYPIARAYRDARVQPIYGGTTEIMKELISR 369
|
|
| IVD |
cd01156 |
Isovaleryl-CoA dehydrogenase; Isovaleryl-CoA dehydrogenase (IVD) is an is an acyl-CoA ... |
538-816 |
1.44e-31 |
|
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: 127.14 E-value: 1.44e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 538 LLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWWTSGAmdPRCQILVLMGKTDF 617
Cdd:cd01156 95 IYRNGSAAQKEKYLPKLISGEHIGALAMSEPN-AGSDVVSMKLRAEKKGDRYVLNGSKMWITNG--PDADTLVVYAKTDP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 618 SAPKHKQQSMIlVDVKTPGVQIRRPLLVFGFDDAPHGhaEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLI 697
Cdd:cd01156 172 SAGAHGITAFI-VEKGMPGFSRAQKLDKLGMRGSNTC--ELVFEDCEVPEENILGGENKGVYVLMSGLDYERLVLAGGPI 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 698 GAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLDRHG--NKKARGILAMAKVAAPNMA 775
Cdd:cd01156 249 GIMQAALDVAIPYAHQRKQFGQPIGEFQLVQGKLADMYTRLNASRSYLYTVAKACDRGNmdPKDAAGVILYAAEKATQVA 328
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1002285595 776 LKvldmAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEV 816
Cdd:cd01156 329 LD----AIQILGGNGYINDYPTGRLLRDAKLYEIGAGTSEI 365
|
|
| PRK12341 |
PRK12341 |
acyl-CoA dehydrogenase; |
526-816 |
1.35e-29 |
|
acyl-CoA dehydrogenase;
Pssm-ID: 183454 [Multi-domain] Cd Length: 381 Bit Score: 121.76 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 526 NCGPP----DTGNMEVLLRYGTKEQQKQWLVPLLE-GKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWWTSG 600
Cdd:PRK12341 80 CGAPAflitNGQCIHSMRRFGSAEQLRKTAESTLEtGDPAYALALTEPG-AGSDNNSATTTYTRKNGKVYLNGQKTFITG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 601 AMD-PRCqilVLMGKTDFSAPKHKQQSMILVDVKTPGVQIRrPLLVFGFDDAPHghAEITFENVRVPATNILLGEGRGFE 679
Cdd:PRK12341 159 AKEyPYM---LVLARDPQPKDPKKAFTLWWVDSSKPGIKIN-PLHKIGWHMLST--CEVYLDNVEVEESDLVGEEGMGFL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 680 IAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIaqhGSF------LADLAkcrVELEQARLLVLEAADQLD 753
Cdd:PRK12341 233 NVMYNFEMERLINAARSLGFAECAFEDAARYANQRIQFGKPI---GHNqliqekLTLMA---IKIENMRNMVYKVAWQAD 306
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1002285595 754 RHGNKKARGilAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEV 816
Cdd:PRK12341 307 NGQSLRTSA--ALAKLYCARTAMEVIDDAIQIMGGLGYTDEARVSRFWRDVRCERIGGGTDEI 367
|
|
| PRK03354 |
PRK03354 |
crotonobetainyl-CoA dehydrogenase; Validated |
499-830 |
2.19e-25 |
|
crotonobetainyl-CoA dehydrogenase; Validated
Pssm-ID: 179566 [Multi-domain] Cd Length: 380 Bit Score: 109.15 E-value: 2.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 499 LGAGLTNLEYGYlcEIMGRsIWAPQIFNCGPPdtGNMEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNI 578
Cdd:PRK03354 63 LDAGFVTLAAVW--MELGR-LGAPTYVLYQLP--GGFNTFLREGTQEQIDKIMAFRGTGKQMWNSAITEPG-AGSDVGSL 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 579 ECSISRQGDFYVINGTKWW-TSGAMDPrcqILVLMGKtDFSAPKHKQQSMILVDVKTPGVQIRR-PLLVFGFDDAphghA 656
Cdd:PRK03354 137 KTTYTRRNGKVYLNGSKCFiTSSAYTP---YIVVMAR-DGASPDKPVYTEWFVDMSKPGIKVTKlEKLGLRMDSC----C 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 657 EITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRV 736
Cdd:PRK03354 209 EITFDDVELDEKDMFGREGNGFNRVKEEFDHERFLVALTNYGTAMCAFEDAARYANQRVQFGEAIGRFQLIQEKFAHMAI 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 737 ELEQARLLVLEAADQLDRhgNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEV 816
Cdd:PRK03354 289 KLNSMKNMLYEAAWKADN--GTITSGDAAMCKYFCANAAFEVVDSAMQVLGGVGIAGNHRISRFWRDLRVDRVSGGSDEM 366
|
330
....*....|....
gi 1002285595 817 HLGTIAKLELQRAR 830
Cdd:PRK03354 367 QILTLGRAVLKQYR 380
|
|
| PTZ00461 |
PTZ00461 |
isovaleryl-CoA dehydrogenase; Provisional |
543-823 |
2.73e-24 |
|
isovaleryl-CoA dehydrogenase; Provisional
Pssm-ID: 185640 [Multi-domain] Cd Length: 410 Bit Score: 106.18 E-value: 2.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 543 TKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGD-FYVINGTKWW-TSGAMdprCQILVLMGKTDfsap 620
Cdd:PTZ00461 135 SPAQRARWLPKVLTGEHVGAMGMSEPG-AGTDVLGMRTTAKKDSNgNYVLNGSKIWiTNGTV---ADVFLIYAKVD---- 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 621 khKQQSMILVDVKTPGVQIRRPLLVFGFDdAPHgHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRLIGAA 700
Cdd:PTZ00461 207 --GKITAFVVERGTKGFTQGPKIDKCGMR-ASH-MCQLFFEDVVVPAENLLGEEGKGMVGMMRNLELERVTLAAMAVGIA 282
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 701 ERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLdRHGNKKARGILAMAKVAAPnMALKVLD 780
Cdd:PTZ00461 283 ERSVELMTSYASERKAFGKPISNFGQIQRYIAEGYADTEAAKALVYSVSHNV-HPGNKNRLGSDAAKLFATP-IAKKVAD 360
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1002285595 781 MAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEVHLGTIAK 823
Cdd:PTZ00461 361 SAIQVMGGMGYSRDMPVERLWRDAKLLEIGGGTIEAHHKNITK 403
|
|
| AidB |
cd01154 |
Proteins involved in DNA damage response, similar to the AidB gene product; AidB is one of ... |
532-816 |
5.05e-23 |
|
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: 102.45 E-value: 5.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 532 TGNMEVLLRYGTKEQQKQWLVPLLEGKIR----SGFAMTEPQVASSDATNIECSISRQGDFYVINGTKWWTSGAMdprCQ 607
Cdd:cd01154 116 TDAAVYALRKYGPEELKQYLPGLLSDRYKtgllGGTWMTEKQGGSDLGANETTAERSGGGVYRLNGHKWFASAPL---AD 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 608 ILVLMGKTDFSAPKHKQQSMILVDVKTP-----GVQIRRPLLVFGFDDAPHGhaEITFENvrvpATNILLG-EGRGFEIA 681
Cdd:cd01154 193 AALVLARPEGAPAGARGLSLFLVPRLLEdgtrnGYRIRRLKDKLGTRSVATG--EVEFDD----AEAYLIGdEGKGIYYI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 682 QGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLDRHGNKK-- 759
Cdd:cd01154 267 LEMLNISRLDNAVAALGIMRRALSEAYHYARHRRAFGKPLIDHPLMRRDLAEMEVDVEAATALTFRAARAFDRAAADKpv 346
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1002285595 760 ----ARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEV 816
Cdd:cd01154 347 eahmARLATPVAKLIACKRAAPVTSEAMEVFGGNGYLEEWPVARLHREAQVTPIWEGTGNI 407
|
|
| Acyl-CoA_dh_M |
pfam02770 |
Acyl-CoA dehydrogenase, middle domain; Central domain of Acyl-CoA dehydrogenase has a ... |
562-661 |
9.18e-21 |
|
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: 87.72 E-value: 9.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 562 GFAMTEPQvASSDATNIE-CSISRQGDFYVINGTKWWTSGAmdPRCQILVLMGKTDfSAPKHKQQSMILVDVKTPGVQIR 640
Cdd:pfam02770 1 AFALTEPG-AGSDVASLKtTAADGDGGGWVLNGTKWWITNA--GIADLFLVLARTG-GDDRHGGISLFLVPKDAPGVSVR 76
|
90 100
....*....|....*....|.
gi 1002285595 641 RPLLVFGFDDAPHGhaEITFE 661
Cdd:pfam02770 77 RIETKLGVRGLPTG--ELVFD 95
|
|
| PLN02519 |
PLN02519 |
isovaleryl-CoA dehydrogenase |
538-816 |
2.77e-20 |
|
isovaleryl-CoA dehydrogenase
Pssm-ID: 215284 [Multi-domain] Cd Length: 404 Bit Score: 94.17 E-value: 2.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 538 LLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGDFYVINGTKWW-TSGamdPRCQILVLMGKTD 616
Cdd:PLN02519 121 LVRNGTPAQKEKYLPKLISGEHVGALAMSEPN-SGSDVVSMKCKAERVDGGYVLNGNKMWcTNG---PVAQTLVVYAKTD 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 617 FSAPKHKQQSMIlVDVKTPGVQIRRPLLVFGFDDAphGHAEITFENVRVPATNILLGEGRGFEIAQGRLGPGRLHHCMRL 696
Cdd:PLN02519 197 VAAGSKGITAFI-IEKGMPGFSTAQKLDKLGMRGS--DTCELVFENCFVPEENVLGQEGKGVYVMMSGLDLERLVLAAGP 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 697 IGAAERGMNLMVERALSRTTFGKKIAQHGSFLADLAKCRVELEQARLLVLEAADQLD--RHGNKKARGILAMAKVAAPNM 774
Cdd:PLN02519 274 LGLMQACLDVVLPYVRQREQFGRPIGEFQFIQGKLADMYTSLQSSRSYVYSVARDCDngKVDRKDCAGVILCAAERATQV 353
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1002285595 775 ALKvldmAMQVHGGAGLSSDTVLSHLWATARTLRIADGPDEV 816
Cdd:PLN02519 354 ALQ----AIQCLGGNGYINEYPTGRLLRDAKLYEIGAGTSEI 391
|
|
| ACAD_fadE5 |
cd01153 |
Putative acyl-CoA dehydrogenases similar to fadE5; Putative acyl-CoA dehydrogenase (ACAD). ... |
532-812 |
1.63e-19 |
|
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: 91.68 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 532 TGNMEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGD-FYVINGTKWWTS---GAMDPRCQ 607
Cdd:cd01153 90 QGAAATLLAHGTEAQREKWIPRLAEGEWTGTMCLTEPD-AGSDLGALRTKAVYQADgSWRINGVKRFISageHDMSENIV 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 608 ILVLmGKTDFSAPKHKQQSMILV-----DVKTPGVQIRRPLLVFGFDDAPhgHAEITFENVRVPatniLLGE-GRG---- 677
Cdd:cd01153 169 HLVL-ARSEGAPPGVKGLSLFLVpkfldDGERNGVTVARIEEKMGLHGSP--TCELVFDNAKGE----LIGEeGMGlaqm 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 678 FEIAQG-RLGPGrlhhcMRLIGAAERGMNLMVERALSRTTFGK--------KIAQHGSFLADLAKCRVELEQARLLVLEA 748
Cdd:cd01153 242 FAMMNGaRLGVG-----TQGTGLAEAAYLNALAYAKERKQGGDlikaapavTIIHHPDVRRSLMTQKAYAEGSRALDLYT 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002285595 749 ADQLD------------RHGNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRIADG 812
Cdd:cd01153 317 ATVQDlaerkategedrKALSALADLLTPVVKGFGSEAALEAVSDAIQVHGGSGYTREYPIEQYYRDARITTIYEG 392
|
|
| GCD |
cd01151 |
Glutaryl-CoA dehydrogenase; Glutaryl-CoA dehydrogenase (GCD). GCD is an acyl-CoA dehydrogenase, ... |
500-794 |
2.91e-19 |
|
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: 90.88 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 500 GAGLTNLEYGYLCEIMGRSiwapqifncgppDTG---NMEVLL--------RYGTKEQQKQWLVPLLEGKIRSGFAMTEP 568
Cdd:cd01151 68 CAGLSSVAYGLIAREVERV------------DSGyrsFMSVQSslvmlpiyDFGSEEQKQKYLPKLASGELIGCFGLTEP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 569 QvASSDATNIECSISRQGDFYVINGTKWWTSGAmdPRCQILVLMGKTDFSAPKHKqqsmILVDVKTPGVQIRRPLLVFGF 648
Cdd:cd01151 136 N-HGSDPGGMETRARKDGGGYKLNGSKTWITNS--PIADVFVVWARNDETGKIRG----FILERGMKGLSAPKIQGKFSL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 649 DDAPHGHaeITFENVRVPATNiLLGEGRGFEIAQGRLGPGRLHHCMRLIGAAERGMNLMVERALSRTTFGKKIAQHGSFL 728
Cdd:cd01151 209 RASITGE--IVMDNVFVPEEN-LLPGAEGLRGPFKCLNNARYGIAWGALGAAEDCYHTARQYVLDRKQFGRPLAAFQLVQ 285
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1002285595 729 ADLAKCRVELEQARLLVLEAADQLDRhgNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAGLSSD 794
Cdd:cd01151 286 KKLADMLTEIALGLLACLRVGRLKDQ--GKATPEQISLLKRNNCGKALEIARTAREMLGGNGISDE 349
|
|
| APH_ChoK_like |
cd05120 |
Aminoglycoside 3'-phosphotransferase and Choline Kinase family; This family is composed of APH, ... |
43-266 |
3.22e-17 |
|
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: 79.65 E-value: 3.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 43 QFGHGQSNPTYCIeasapgGVTARYVLRKKPPgailQSAHAVEREFQVLKALGTYTDVPVPKVFCLCTDAsviGTPFYIM 122
Cdd:cd05120 5 LIKEGGDNKVYLL------GDPREYVLKIGPP----RLKKDLEKEAAMLQLLAGKLSLPVPKVYGFGESD---GWEYLLM 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 123 EHLEGLIYpDNKLTGVTPTKRKTIYLAAAETLAAIHKVDVTAiglqkygrrdnyckrqverwgrqylsstgegkparyqk 202
Cdd:cd05120 72 ERIEGETL-SEVWPRLSEEEKEKIADQLAEILAALHRIDSSV-------------------------------------- 112
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002285595 203 mldlahwlkehipkedssagfgtgLVHGDYRVDNLVFHPtEDRVIGVLDWELSTLGNQMCDVAY 266
Cdd:cd05120 113 ------------------------LTHGDLHPGNILVKP-DGKLSGIIDWEFAGYGPPAFDYAA 151
|
|
| Acyl-CoA_dh_2 |
pfam08028 |
Acyl-CoA dehydrogenase, C-terminal domain; |
692-809 |
1.01e-11 |
|
Acyl-CoA dehydrogenase, C-terminal domain;
Pssm-ID: 429790 [Multi-domain] Cd Length: 133 Bit Score: 63.13 E-value: 1.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 692 HCMRLIGAAERGMNLMVERALSRTT--FGKKIAQHGSFLADLAKCRVELEQARLLVLEAAdqlDRHGNKKARGI------ 763
Cdd:pfam08028 2 IAAAALGAARAALAEFTERARGRVRayFGVPLAEDPATQLALAEAAARIDAARLLLERAA---ARIEAAAAAGKpvtpal 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 1002285595 764 ---LAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATARTLRI 809
Cdd:pfam08028 79 raeARRAAAFATELAVAAVDALFRAAGGSALFQDSPLQRIWRDIHAAAQ 127
|
|
| DszC |
cd01163 |
Dibenzothiophene (DBT) desulfurization enzyme C; DszC is a flavin reductase dependent enzyme, ... |
536-806 |
3.34e-09 |
|
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: 59.64 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 536 EVLLRYGTKEQQKQWLVPLLEGKIRSGfAMTEpqVASSDATNIECSISRQGDFYVINGTKWWTSGAMDprCQILVLMGKT 615
Cdd:cd01163 81 EALLLAGPEQFRKRWFGRVLNGWIFGN-AVSE--RGSVRPGTFLTATVRDGGGYVLNGKKFYSTGALF--SDWVTVSALD 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 616 DFSAPKHkqqsmILVDVKTPGVQIRRPLLVFGFDDAPHGHAeiTFENVRVPATNILLGEGRGFeiaQGRLGPG--RLHHC 693
Cdd:cd01163 156 EEGKLVF-----AAVPTDRPGITVVDDWDGFGQRLTASGTV--TFDNVRVEPDEVLPRPNAPD---RGTLLTAiyQLVLA 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 694 MRLIGAAERGMNLMVERALSRTtfgkKIAQHGS---------FLADLAKCRVELEQARLLVLEAADQLDRHGNK------ 758
Cdd:cd01163 226 AVLAGIARAALDDAVAYVRSRT----RPWIHSGaesarddpyVQQVVGDLAARLHAAEALVLQAARALDAAAAAgtalta 301
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1002285595 759 KARG----ILAMAKVAAPNMALKVLDMAMQVHGGAGLSSDTVLSHLWATART 806
Cdd:cd01163 302 EARGeaalAVAAAKVVVTRLALDATSRLFEVGGASATAREHNLDRHWRNART 353
|
|
| SrkA |
COG2334 |
Ser/Thr protein kinase RdoA involved in Cpx stress response, MazF antagonist [Signal ... |
39-265 |
6.70e-07 |
|
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: 51.85 E-value: 6.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 39 LALTQFGHGQsNPTYCIEAsaPGGvtARYVLRKKPPGAIlqSAHAVEREFQVLKALGTyTDVPVPKVFCL---CTDASVI 115
Cdd:COG2334 16 SSLKPLNSGE-NRNYRVET--EDG--RRYVLKLYRPGRW--SPEEIPFELALLAHLAA-AGLPVPAPVPTrdgETLLELE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 116 GTPFYIMEHLEGLIYPDnkltgVTPTkrktIYLAAAETLAAIHKVdvtaigLQKYGRRDNyckRQVERWGRQYLSSTGE- 194
Cdd:COG2334 88 GRPAALFPFLPGRSPEE-----PSPE----QLEELGRLLARLHRA------LADFPRPNA---RDLAWWDELLERLLGPl 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1002285595 195 -GKPARYQKMLDLAHWLKEHIPKEDssAGFGTGLVHGDYRVDNLVFHPteDRVIGVLDWELSTLGNQMCDVA 265
Cdd:COG2334 150 lPDPEDRALLEELLDRLEARLAPLL--GALPRGVIHGDLHPDNVLFDG--DGVSGLIDFDDAGYGPRLYDLA 217
|
|
| PRK13026 |
PRK13026 |
acyl-CoA dehydrogenase; Reviewed |
536-790 |
3.74e-06 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 237277 [Multi-domain] Cd Length: 774 Bit Score: 50.73 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 536 EVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNI-ECSISRQGDF-------YVINGTKWWTSGAmdPRCQ 607
Cdd:PRK13026 169 ELLTHYGTQEQKDYWLPRLADGTEIPCFALTGPE-AGSDAGAIpDTGIVCRGEFegeevlgLRLTWDKRYITLA--PVAT 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 608 ILVLMGKtdFSAPKH----KQQSMI---LVDVKTPGVQI-RR--PLlvfgfdDAPHGHAEITFENVRVPATNILLGE--- 674
Cdd:PRK13026 246 VLGLAFK--LRDPDGllgdKKELGItcaLIPTDHPGVEIgRRhnPL------GMAFMNGTTRGKDVFIPLDWIIGGPdya 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 675 GRGFE-----IAQGR------LGPGRLHHCMRLIGAAERgmnlmveralSRTTFGKKIaqhGSF------LADLAKCRVE 737
Cdd:PRK13026 318 GRGWRmlvecLSAGRgislpaLGTASGHMATRTTGAYAY----------VRRQFGMPI---GQFegvqeaLARIAGNTYL 384
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1002285595 738 LEQARLLVLEAADQldrhgNKKARGILAMAKVAAPNMALKVLDMAMQVHGGAG 790
Cdd:PRK13026 385 LEAARRLTTTGLDL-----GVKPSVVTAIAKYHMTELARDVVNDAMDIHAGKG 432
|
|
| Acyl-CoA_dh_N |
pfam02771 |
Acyl-CoA dehydrogenase, N-terminal domain; The N-terminal domain of Acyl-CoA dehydrogenase is ... |
417-558 |
5.42e-06 |
|
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: 45.92 E-value: 5.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 417 QLRNKLMKFMEDYIYPMESEFYKRAHstsrwtiHPEE--EKLKALakreGLWNLFIPldsaararellfEDmsHGspgss 494
Cdd:pfam02771 6 ALRDTVREFAEEEIAPHAAEWDEEGE-------FPRElwKKLGEL----GLLGITIP------------EE--YG----- 55
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1002285595 495 eelllGAGLTNLEYGYLCEIMGRsIWAPQIFNCGPPDTGNMEVLLRYGTKEQQKQWLVPLLEGK 558
Cdd:pfam02771 56 -----GAGLDYLAYALVAEELAR-ADASVALALSVHSSLGAPPILRFGTEEQKERYLPKLASGE 113
|
|
| HomoserineK_II |
cd05153 |
Type II Homoserine Kinase; This subfamily is composed of unusual homoserine kinases, from a ... |
18-275 |
2.22e-05 |
|
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: 47.25 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 18 EAALLRYAAEHVAGFpspaRGLAltqfgHGQSNPTYCIEASapggvTARYVLR---KKPPGAILQSahaverEFQVLKAL 94
Cdd:cd05153 5 AEFLAHYDLGELLSF----EGIA-----AGIENTNYFVTTT-----DGRYVLTlfeKRRSAAELPF------ELELLDHL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 95 GTyTDVPVPKVfcLCT-DASVIGT----PFYIMEHLEGliypdNKLTGVTPTKRKTIylaaAETLAAIHKVdvtaigLQK 169
Cdd:cd05153 65 AQ-AGLPVPRP--LADkDGELLGElngkPAALFPFLPG-----ESLTTPTPEQCRAI----GAALARLHLA------LAG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 170 Y-GRRDNYckRQVERWgrqyLSSTGEGKPARYQKMLDLAHWLKE---HIPKEDSSAGfGTGLVHGDYRVDNLVFhpTEDR 245
Cdd:cd05153 127 FpPPRPNP--RGLAWW----KPLAERLKARLDLLAADDRALLEDelaRLQALAPSDL-PRGVIHADLFRDNVLF--DGDR 197
|
250 260 270
....*....|....*....|....*....|
gi 1002285595 246 VIGVLDWELSTLGNQMCDVAYSSLPYIIDA 275
Cdd:cd05153 198 LSGIIDFYDACYDPLLYDLAIALNDWCFDD 227
|
|
| PTZ00456 |
PTZ00456 |
acyl-CoA dehydrogenase; Provisional |
533-759 |
3.44e-05 |
|
acyl-CoA dehydrogenase; Provisional
Pssm-ID: 185635 [Multi-domain] Cd Length: 622 Bit Score: 47.56 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 533 GNMEVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNIECSISRQGD-FYVINGTKWWTS-GAMDPRCQIL- 609
Cdd:PTZ00456 155 GAANTLMAWGSEEQKEQYLTKLVSGEWSGTMCLTEPQ-CGTDLGQVKTKAEPSADgSYKITGTKIFISaGDHDLTENIVh 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 610 VLMGKTDFSAPKHKQQSMILVD---VKTPG-VQIRRPLLVFGFDD--APHGHA--EITFENvrvpATNILLGE-GRGFEI 680
Cdd:PTZ00456 234 IVLARLPNSLPTTKGLSLFLVPrhvVKPDGsLETAKNVKCIGLEKkmGIKGSStcQLSFEN----SVGYLIGEpNAGMKQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 681 AQGRLGPGRLHHCMRLIGAAE----------RGMNLMveRALSRTT----FGKKIAQHGSFLADLAKCRVELEQARLLVL 746
Cdd:PTZ00456 310 MFTFMNTARVGTALEGVCHAElafqnalryaRERRSM--RALSGTKepekPADRIICHANVRQNILFAKAVAEGGRALLL 387
|
250
....*....|...
gi 1002285595 747 EAADQLDRHGNKK 759
Cdd:PTZ00456 388 DVGRLLDIHAAAK 400
|
|
| fadE |
PRK09463 |
acyl-CoA dehydrogenase; Reviewed |
536-578 |
1.54e-04 |
|
acyl-CoA dehydrogenase; Reviewed
Pssm-ID: 236528 [Multi-domain] Cd Length: 777 Bit Score: 45.58 E-value: 1.54e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 1002285595 536 EVLLRYGTKEQQKQWLVPLLEGKIRSGFAMTEPQvASSDATNI 578
Cdd:PRK09463 170 ELLLHYGTDEQKDHYLPRLARGEEIPCFALTSPE-AGSDAGSI 211
|
|
| CotS |
COG0510 |
Thiamine kinase or a related kinase [Coenzyme transport and metabolism]; |
177-353 |
2.50e-04 |
|
Thiamine kinase or a related kinase [Coenzyme transport and metabolism];
Pssm-ID: 440276 [Multi-domain] Cd Length: 156 Bit Score: 42.46 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 177 CKRQVERWGRQYLSSTGEGKPARYQKMLDLAHWLKEHIPkedsSAGFGTGLVHGDYRVDNLVFhpTEDRVIGVLDWELST 256
Cdd:COG0510 5 SPALLRFDLFARLERYLALGPRDLPELLRRLEELERALA----ARPLPLVLCHGDLHPGNFLV--TDDGRLYLIDWEYAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1002285595 257 LGNQMCDVAYSSLPYIIDATTstgysyggfeytgipdgippLEEYLAAYCSISARPWPAASWKFYVAFSLFRGASIYAGV 336
Cdd:COG0510 79 LGDPAFDLAALLVEYGLSPEQ--------------------AEELLEAYGFGRPTEELLRRLRAYRALADLLWALWALVR 138
|
170
....*....|....*..
gi 1002285595 337 YHRWTMGNASGGERARF 353
Cdd:COG0510 139 AAQEANGDLLKYLLRRL 155
|
|
| |
