|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02980 |
PLN02980 |
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate ... |
1-1367 |
0e+00 |
|
2-oxoglutarate decarboxylase/ hydro-lyase/ magnesium ion binding / thiamin pyrophosphate binding
Pssm-ID: 215530 [Multi-domain] Cd Length: 1655 Bit Score: 2619.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1 MLNRETEVSNFLRDEANINAVWASAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKG 80
Cdd:PLN02980 282 MLDHEGEVSNFLKDYANINAVWASLIIEECTRLGLTYFCVAPGSRSSPLAIAASNHPLTTCIACFDERSLAFHALGYARG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 81 SLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIPVRMV 160
Cdd:PLN02980 362 SLKPAVVITSSGTAVSNLLPAVVEASQDFVPLLLLTADRPPELQDAGANQAINQVNHFGSFVRFFFNLPPPTDLIPARMV 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 161 LTTVDSALHWATGSACGPVHLNCPFRDPLDGSPTNWSSNCLNGLDMWMSNAEPFTKYFQVQSHKSDGVTTGQITEILQVI 240
Cdd:PLN02980 442 LTTLDSAVHWATSSPCGPVHINCPFREPLDGSPTNWMSSCLKGLDMWMSNAEPFTKYIQMQSSKADGDTTGQITEVLEVI 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 241 KEAKKGLLLIGAIHTEDEIWASLLLAKELMWPVVADVLSGVRLRKLFKPFVE-KLTHVFVDHLDHALFSDSVRNLIEFDV 319
Cdd:PLN02980 522 QEAKRGLLLIGAIHTEDDIWAALLLAKHLMWPVVADILSGLRLRKLFKSFPEfELNILFVDHLDHALLSDSVRNWIQFDV 601
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 320 VIQVGSRITSKRVSQMLEKCFPFAYILVDKHPCRHDPSHLVTHRVQSNIVQFANCVLKSRFPWRRSKLHGHLQALDGAIA 399
Cdd:PLN02980 602 VIQIGSRITSKRVSQMLEKCFPFSYILVDKHPCRHDPSHLVTHRVQSNIVQFADCLLKAQFPRRRSKWHGHLQALDGMVA 681
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 400 REMSFQISAESSLTEPYVAHMLSKALTSKSALFIGNSMPIRDVDMYGCSSEN-SSHVVDMMLSAELPCQWIQVTGNRGAS 478
Cdd:PLN02980 682 QEISFQIHAESSLTEPYVAHVISEALTSDSALFIGNSMAIRDADMYGCSSENySSRIVDMMLSAELPCQWIQVAGNRGAS 761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 479 GIDGLLSSATGFAVGCKKRVVCVVGDISFLHDTNGLAILKQRIARKPMTILVINNRGGGIFRLLPIAKKTEPSVLNQYFY 558
Cdd:PLN02980 762 GIDGLLSTAIGFAVGCNKRVLCVVGDISFLHDTNGLSILSQRIARKPMTILVINNHGGAIFSLLPIAKRTEPRVLNQYFY 841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 559 TAHDISIENLCLAHGVRYVHVGTKSELEDALFVPSVEEMDCIVEVESSINANAIVHSTLERFARQAAENSLGIVSASSFL 638
Cdd:PLN02980 842 TSHDISIENLCLAHGVRHLHVGTKSELEDALFTSQVEQMDCVVEVESSIDANAAFHSTLRKFACQAAEHALGILSESSCL 921
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 639 HPMIKNVLLCQVSGIQYSQYRVKLCDRPTICSDEFSQFHREGFILSLTLEDGSIGYGEVAPLNSNVENLMDVEGQLQLVL 718
Cdd:PLN02980 922 HSIIDGVFLCKISGMEYSLYRIQLCAPPTSASVDFSQFHREGFILSLSLEDGSVGFGEVAPLEIHEEDLLDVEEQLRFLL 1001
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 719 HLMNEAKFSYMLPLLNGSISSWIWSELGITASSIFPSVRCGLEMALLNAMAVRHDSSLLGILH-YQKEENGSAQPHSVQI 797
Cdd:PLN02980 1002 HVIKGAKISFMLPLLKGSFSSWIWSELGIPPSSIFPSVRCGLEMAILNAIAVRHGSSLLNILDpYQKDENGSEQSHSVQI 1081
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 798 CALLDSEGTPLEVAYVARKLVQEGFSAIKLKVGRRVSSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNS 877
Cdd:PLN02980 1082 CALLDSNGSPLEVAYVARKLVEEGFSAIKLKVGRRVSPIQDAAVIQEVRKAVGYQIELRADANRNWTYEEAIEFGSLVKS 1161
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 878 CNLKYIEEPVQNKDDLIRFHEETGLPVALDETLDDFEECPLRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGK 957
Cdd:PLN02980 1162 CNLKYIEEPVQDEDDLIKFCEETGLPVALDETIDKFEECPLRMLTKYTHPGIVAVVIKPSVVGGFENAALIARWAQQHGK 1241
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 958 MAVISAAYESGLGLSAYILFASYLEMENVKASTEQKQGTPPSVAHGLGTYRWLSEDVMMNTLGIFRSPYSGFVEGFIADA 1037
Cdd:PLN02980 1242 MAVISAAYESGLGLSAYIQFASYLEMQNAKASREMNKGTCPSVAHGLGTYRWLKEDVTMNPLGIFRSPYSGFIEASVADA 1321
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1038 SRNLKDVKINNDVIVRTSKGIPVRRYELRVDVDGFSHFIRVHDVGENAEGSVALFLHGFLGTGEEWIPIMTGISGSARCI 1117
Cdd:PLN02980 1322 SRNLQKFQINNDVIVRTFKEEQVRTYELRVDVDGFSCLIKVHEVGQNAEGSVVLFLHGFLGTGEDWIPIMKAISGSARCI 1401
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1118 SVDIPGHGRSRVQSHASETQTSPTFSMEMIAEALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSGSPG 1197
Cdd:PLN02980 1402 SIDLPGHGGSKIQNHAKETQTEPTLSVELVADLLYKLIEHITPGKVTLVGYSMGARIALYMALRFSDKIEGAVIISGSPG 1481
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1198 LKDPVARKIRSATDDSKARMMVDNGLYIFIENWYNGGLWKSLRNHPHFSKIAASRLLHGDVPSVAKLLSDLSSGRQPSLW 1277
Cdd:PLN02980 1482 LKDEVARKIRSAKDDSRARMLIDHGLEIFLENWYSGELWKSLRNHPHFNKIVASRLLHKDVPSLAKLLSDLSIGRQPSLW 1561
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1278 EELEDCDTNISLVFGEKDVKYKQIATRMYREMSKSKKSVNN----IIEIVEIPEAGHAVHLESPLRVILALRKFLTRVHN 1353
Cdd:PLN02980 1562 EDLKQCDTPLLLVVGEKDVKFKQIAQKMYREIGKSKESGNDkgkeIIEIVEIPNCGHAVHLENPLPVIRALRKFLTRLHN 1641
|
1370
....*....|....
gi 1063696695 1354 SSTETELSQKLLLA 1367
Cdd:PLN02980 1642 SSTPGELSQKLLLA 1655
|
|
| MenD |
COG1165 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport ... |
16-624 |
0e+00 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase [Coenzyme transport and metabolism]; 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440779 [Multi-domain] Cd Length: 567 Bit Score: 570.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 16 ANINAVWASAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAV 95
Cdd:COG1165 3 KNSNTLWARVLVEELVRLGVRHVVISPGSRSTPLTLAFARHPDLRLHSHVDERSAAFFALGLAKASGRPVALVCTSGTAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 96 SNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIP-VRMVLTTVDSALHWATGS 174
Cdd:COG1165 83 ANYYPAVIEAFYSGVPLIVLTADRPPELRDCGANQTIDQVGLFGNHVRWSADLPLPEADPDaLRYLRRTINRALAAALGP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 175 ACGPVHLNCPFRDPLDGSPTnwssnclngLDMWMSNAEPFTKYFQVQSHksdgVTTGQITEILQVIKEAKKGLLLIGAIH 254
Cdd:COG1165 163 PPGPVHINVPFREPLYPDPD---------EEDPLAAGGPWIRVTPPEPA----PSPEALAQLADELERAKRGLIVAGPLP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 255 TEDEIWASLL-LAKELMWPVVADVLSGVRlrklfkpfveklTHVFVDHLDHALFSDSVRNLIEFDVVIQVGSRITSKRVS 333
Cdd:COG1165 230 PPEELAEALAaLAEALGWPVLADPLSNLR------------HPNVISTYDLLLRNPEFAELLQPDLVIRFGGPPVSKRLK 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 334 QMLEKCFPFAYILVDKHPCRHDPSHLVTHRVQSNIVQF----ANCVLKSRFPWRRSklhghLQALDGAIAREMSfQISAE 409
Cdd:COG1165 298 QFLRRHPPAEHWVVDPSGEWRDPFHSLTRVIEADPEAFlealAERLPPADSAWLAR-----WLAAEQKARAAID-EYLAE 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 410 SSLTEPYVAHMLSKALTSKSALFIGNSMPIRDVDMYGCSSENSshvvdmmlsaelpcqwIQVTGNRGASGIDGLLSSATG 489
Cdd:COG1165 372 DPLSEGAVARRLLEALPEGSTLFVGNSMPVRDLDLFARPLPKG----------------VRVYANRGASGIDGTVSTALG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 490 FAVGCKKRVVCVVGDISFLHDTNGLAILKQriARKPMTILVINNRGGGIFRLLPIAKKTEPsvLNQYFYTAHDISIENLC 569
Cdd:COG1165 436 AALASGKPTVLLTGDLSFLHDLNGLLLLYE--LPPNLTIVVVNNDGGGIFSMLPGAKFEPE--FERFFGTPHGLDFEHLA 511
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1063696695 570 LAHGVRYVHVGTKSELEDAL--FVPSVEEMdcIVEVESSINANAIVHSTLERFARQA 624
Cdd:COG1165 512 AMYGLDYARVSSWEELREALaeFLPSDGPR--VLEVRTDREENAELLKALFAAVAAA 566
|
|
| menD |
TIGR00173 |
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought ... |
22-493 |
1.41e-144 |
|
2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylic-acid synthase; MenD was thought until recently to act as SHCHC synthase, but has recently been shown to act instead as SEPHCHC synthase. Conversion of SEPHCHC into SHCHC and pyruvate may occur spontaneously but is catalyzed efficiently, at least in some organisms, by MenH (see TIGR03695). 2-oxoglutarate decarboxylase/SHCHC synthase (menD) is a thiamine pyrophosphate enzyme involved in menaquinone biosynthesis. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 272941 [Multi-domain] Cd Length: 432 Bit Score: 446.66 E-value: 1.41e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 22 WASAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPA 101
Cdd:TIGR00173 1 WASVLVEELVRLGVRHVVISPGSRSTPLALALAEHPRLRVHVHIDERSAGFFALGLAKASGRPVAVVCTSGTAVANLLPA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 102 VVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIPVRMVLTTVDSALHWATGSACGPVHL 181
Cdd:TIGR00173 81 VIEAYYSGVPLIVLTADRPPELRGCGANQTIDQPGLFGSYVRWSVDLPLPEADEPLAYLRSTVDRALAQAQGAPPGPVHI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 182 NCPFRDPLDGSPtnwssnCLNGLDMWMsnAEPFTKYFQVQSHKSDGVTTGQITEILQvikeAKKGLLLIGAIHTEDEIWA 261
Cdd:TIGR00173 161 NVPFREPLYPDP------LLQPLQPWL--RSGVPTISTGPPVLDPESLQELWDRLRQ----AKRGLIIAGPLAGAEDAEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 262 SLLLAKELMWPVVADVLSGVRLrklfkpfvekLTHVFV-DHLDHALFSDSVRNLIEFDVVIQVGSRITSKRVSQMLEKcF 340
Cdd:TIGR00173 229 LAALAEALGWPLLADPLSGLRG----------GPHPLViDHYDLLLANAELREELQPDLVIRFGGPPVSKRLRQWLAR-A 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 341 PFAYILVDKHPCRHDPSHLVTHRVQSNIVQFANCVLKSRFPWRRSKLHGHLQAldGAIAREMSFQISAESSLTEPYVAHM 420
Cdd:TIGR00173 298 PAEYWVVDPRPGWLDPFHHATTRLEASPAAFAEALAGLLKNPAAAWLDRWLEA--EAKARAALREVLAEEPLSELSLARA 375
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063696695 421 LSKALTSKSALFIGNSMPIRDVDMYGcssensshvvdmmlsaELPCQWIQVTGNRGASGIDGLLSSATGFAVG 493
Cdd:TIGR00173 376 LSQLLPDGSALFVGNSMPIRDLDTFS----------------SPPDKPIRVFANRGASGIDGTLSTALGIAAA 432
|
|
| TPP_PYR_MenD |
cd07037 |
Pyrimidine (PYR) binding domain of ... |
24-185 |
1.53e-79 |
|
Pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate synthase (MenD) and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexadiene-1-carboxylate (SEPHCHC) synthase (MenD) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Escherichia coli MenD (EcMenD) is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. EcMenD catalyzes a Stetter-like conjugate addition of alpha-ketoglutarate to isochorismate, leading to the formation of SEPHCHC and carbon dioxide, this addition is the first committed step in the biosynthesis of vitamin K2 (menaquinone).
Pssm-ID: 132920 [Multi-domain] Cd Length: 162 Bit Score: 258.58 E-value: 1.53e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 24 SAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVV 103
Cdd:cd07037 1 QALVEELKRLGVRDVVISPGSRSAPLALAAAEHPEFRLHVRVDERSAAFFALGLAKASGRPVAVVCTSGTAVANLLPAVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 104 EASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIPVRMVLTTVDSALHWATGSACGPVHLNC 183
Cdd:cd07037 81 EAYYSGVPLLVLTADRPPELRGTGANQTIDQVGLFGDYVRWSVDLPPPEDDDDLWYLLRLANRAVLEALSAPPGPVHLNL 160
|
..
gi 1063696695 184 PF 185
Cdd:cd07037 161 PF 162
|
|
| menH_SHCHC |
TIGR03695 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the ... |
1086-1349 |
8.06e-63 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; This protein catalyzes the formation of SHCHC, or (1 R,6 R)-2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate, by elmination of pyruvate from 2-succinyl-5-enolpyruvyl-6-hydroxy-3-cyclohexene-1-carboxylate (SEPHCHC). Note that SHCHC synthase activity previously was attributed to MenD, which in fact is SEPHCHC synthase. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 274729 [Multi-domain] Cd Length: 252 Bit Score: 214.77 E-value: 8.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1086 EGSVALFLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGRSrvQSHASETqtspTFSMEMIAEALYK-LIEQITPGKVT 1164
Cdd:TIGR03695 1 AKPVLVFLHGFLGSGADWQALIEALGPHFRCLAIDLPGHGSS--QSPSDIE----RYDFEEAAQLLLAtLLDQLGIEPFF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1165 IVGYSMGARIALYMALRFSNKIEGAVVVSGSPGLKDPVARKIRSATDDSKARMMVDNGLYIFIENWYNGGLWKSLRNHPH 1244
Cdd:TIGR03695 75 LVGYSMGGRIALYYALQYPERVQGLILESGSPGLQTEEERAARRQNDEQLAQRFEQEGLEAFLDDWYQQPLFASQKNLPP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1245 F--SKIAASRlLHGDVPSVAKLLSDLSSGRQPSLWEELEDCDTNISLVFGEKDVKYKQIATRMYREMSKSKKSVnniiei 1322
Cdd:TIGR03695 155 EqrQALRAER-LANNPEGLAKMLRATGLGKQPSLWPKLQALKIPVLYLCGERDEKFVQIAKEMQKLIPNLTLHI------ 227
|
250 260
....*....|....*....|....*..
gi 1063696695 1323 veIPEAGHAVHLESPLRVILALRKFLT 1349
Cdd:TIGR03695 228 --IPNAGHNIHLENPEAFAKILLAFLE 252
|
|
| TPP_SHCHC_synthase |
cd02009 |
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of ... |
412-589 |
1.27e-56 |
|
Thiamine pyrophosphate (TPP) family, SHCHC synthase subfamily, TPP-binding module; composed of proteins similar to Escherichia coli 2-succinyl-6-hydroxyl-2,4-cyclohexadiene-1-carboxylic acid (SHCHC) synthase (also called MenD). SHCHC synthase plays a key role in the menaquinone biosynthetic pathway, converting isochorismate and 2-oxoglutarate to SHCHC, pyruvate and carbon dioxide. The enzyme requires TPP and a divalent metal cation for activity.
Pssm-ID: 238967 [Multi-domain] Cd Length: 175 Bit Score: 193.97 E-value: 1.27e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 412 LTEPYVAHMLSKALTSKSALFIGNSMPIRDVDMYGCSSENSshvvdmmlsaelpcqwIQVTGNRGASGIDGLLSSATGFA 491
Cdd:cd02009 1 LTEPALARALPDHLPEGSQLFVGNSMPIRDLDLFALPSDKT----------------VRVFANRGASGIDGTLSTALGIA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 492 VGCKKRVVCVVGDISFLHDTNGLAILKQriARKPMTILVINNRGGGIFRLLPIAKKTEpsVLNQYFYTAHDISIENLCLA 571
Cdd:cd02009 65 LATDKPTVLLTGDLSFLHDLNGLLLGKQ--EPLNLTIVVINNNGGGIFSLLPQASFED--EFERLFGTPQGLDFEHLAKA 140
|
170
....*....|....*...
gi 1063696695 572 HGVRYVHVGTKSELEDAL 589
Cdd:cd02009 141 YGLEYRRVSSLDELEQAL 158
|
|
| MenC |
COG1441 |
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase ... |
678-1016 |
7.47e-49 |
|
O-succinylbenzoate synthase [Coenzyme transport and metabolism]; O-succinylbenzoate synthase is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 441050 [Multi-domain] Cd Length: 325 Bit Score: 176.99 E-value: 7.47e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 678 REGFILSLTlEDGSIGYGEVAPLNS-NVENLMDVEGQLQLVLHlmneakfsymlpllngsisSWIWSELgITASSIFPSV 756
Cdd:COG1441 27 RDGLLVRLQ-EGGREGWGEIAPLPGfSQETLEQAEQQALAWLQ-------------------RWLAGDL-LDEKSLLPSV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 757 RCGLEMALLNamavrhdssLLGILHyqkeengsaQPHSVQICALLdsEGTPLEVayVARKLVQEGFSAIKLKVGRRvSSV 836
Cdd:COG1441 86 AFGLSCALAE---------LEGELP---------EAANYRAAPLC--SGDPDEL--IARLNQMPGEKVAKVKVGLY-EAV 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 837 QDALVMQEVRRAVGvQIELRADANCRWTFEEAREFGLLVNSCNLK---YIEEPVQNKDDLIRFHEETGLPVALDETLDDf 913
Cdd:COG1441 143 RDGMVVNLLLEAIP-DLRLRLDANRSWTLDKAVQFAKYVNPEHRSriaFLEEPCKTPEESREFARETGIAIAWDESVRE- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 914 EECPLRMLtkythPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYILFASYLemenvkasteqk 993
Cdd:COG1441 221 PDFRVEAE-----PGVAAIVIKPTLVGSLQRCRQLIEQAHQLGLQAVISSSIESSLGLTQLARLAAWL------------ 283
|
330 340
....*....|....*....|...
gi 1063696695 994 qgTPPSVAhGLGTYRWLSEDVMM 1016
Cdd:COG1441 284 --TPDTAP-GLDTLDLMQAQLLR 303
|
|
| OSBS |
cd03320 |
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2, ... |
657-1006 |
1.03e-42 |
|
o-Succinylbenzoate synthase (OSBS) catalyzes the conversion of 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate (SHCHC) to 4-(2'-carboxyphenyl)-4-oxobutyrate (o-succinylbenzoate or OSB), a reaction in the menaquinone biosynthetic pathway. Menaquinone is an essential cofactor for anaerobic growth in eubacteria and some archaea. OSBS belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239436 [Multi-domain] Cd Length: 263 Bit Score: 157.04 E-value: 1.03e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 657 QYRVKLcDRPTICSDEfSQFHREGFILSLTLEDGSIGYGEVAPLnsnvenlmdvegqlqlvlhlmneakfsymlpllngs 736
Cdd:cd03320 5 PYSLPL-SRPLGTSRG-RLTRRRGLLLRLEDLTGPVGWGEIAPL------------------------------------ 46
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 737 isswiwselgitassifpSVRCGLEMALLNAMAvrhdssllgilhyqkEENGSAQPH-SVQICALLdsEGTPLEVAYVAR 815
Cdd:cd03320 47 ------------------PLAFGIESALANLEA---------------LLVGFTRPRnRIPVNALL--PAGDAAALGEAK 91
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 816 KLVQEGFSAIKLKVGRRvSSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPVQNkDDLIR 895
Cdd:cd03320 92 AAYGGGYRTVKLKVGAT-SFEEDLARLRALREALPADAKLRLDANGGWSLEEALAFLEALAAGRIEYIEQPLPP-DDLAE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 896 FHE-ETGLPVALDETLDDFEEcpLRMLTKYTHPGivAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAY 974
Cdd:cd03320 170 LRRlAAGVPIALDESLRRLDD--PLALAAAGALG--ALVLKPALLGGPRALLELAEEARARGIPAVVSSALESSIGLGAL 245
|
330 340 350
....*....|....*....|....*....|..
gi 1063696695 975 ILFASYLemenvkasteqkqgTPPSVAHGLGT 1006
Cdd:cd03320 246 AHLAAAL--------------PPLPAACGLGT 263
|
|
| RspA |
COG4948 |
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane ... |
674-979 |
8.01e-39 |
|
L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily [Cell wall/membrane/envelope biogenesis, General function prediction only]; L-alanine-DL-glutamate epimerase or related enzyme of enolase superfamily is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 443975 [Multi-domain] Cd Length: 359 Bit Score: 149.20 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 674 SQFHREGFILSLTLEDGSIGYGEVAPLNSNVEnlmdvegqlqLVLHLMNEakfsYMLPLLNG-SISSW--IWSELGiTAS 750
Cdd:COG4948 25 TRTERDVVLVRVETDDGITGWGEAVPGGTGAE----------AVAAALEE----ALAPLLIGrDPLDIeaLWQRLY-RAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 751 SIFPSVRCGLEMALLNAMAVRHD---SSLLGilhyqkeenGsAQPHSVQICALLdSEGTPLEVAYVARKLVQEGFSAIKL 827
Cdd:COG4948 90 PGNPAAKAAVDMALWDLLGKALGvpvYQLLG---------G-KVRDRVPVYATL-GIDTPEEMAEEAREAVARGFRALKL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 828 KVGRRvsSVQDAL-VMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPV--QNKDDLIRFHEETGLPV 904
Cdd:COG4948 159 KVGGP--DPEEDVeRVRAVREAVGPDARLRVDANGAWTLEEAIRLLRALEDLGLEWIEQPLpaEDLEGLAELRRATPVPI 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063696695 905 ALDETLDDFEECPlRMLTKythpGIVAVV-IKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYILFAS 979
Cdd:COG4948 237 AADESLTSRADFR-RLIEA----GAVDIVnIKLSKVGGLTEALRIAALAEAHGVPVMPHCMLESGIGLAAALHLAA 307
|
|
| menC_gamma/gm+ |
TIGR01927 |
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase ... |
664-1014 |
3.62e-34 |
|
o-succinylbenzoate synthase; This model describes the enzyme o-succinylbenzoic acid synthetase (menC) that is involved in one of the steps of the menaquinone biosynthesis pathway. It takes SHCHC and makes it into 2-succinylbenzoate. Included in this model are gamma proteobacteria and archaea. Many of the com-names of the proteins identified by the model are identified as O-succinylbenzoyl-CoA synthase in error. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 273880 [Multi-domain] Cd Length: 307 Bit Score: 133.78 E-value: 3.62e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 664 DRPTICSDEFSQfHREGFILSLTlEDGSIGYGEVAPLNS-NVENLmdvEGQLQLVLHLMNEakfsymlpLLNGSISSWiw 742
Cdd:TIGR01927 8 DAPVVTRHGLLA-RREGLIVRLT-DEGRTGWGEIAPLPGfGTETL---AEALDFCRALIEE--------ITRGDIEAI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 743 selgitaSSIFPSVRCGLEMAllnamavrhdssllgilHYQKEENGSAQPHSVQICALLDSeGTPLEVAYVARKlvQEGF 822
Cdd:TIGR01927 73 -------DDQLPSVAFGFESA-----------------LIELESGDELPPASNYYVALLPA-GDPALLLLRSAK--AEGF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 823 SAIKLKVGRRvSSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSC---NLKYIEEPVQNKDDLIRFHEE 899
Cdd:TIGR01927 126 RTFKWKVGVG-ELAREGMLVNLLLEALPDKAELRLDANGGLSPDEAQQFLKALDPNlrgRIAFLEEPLPDADEMSAFSEA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 900 TGLPVALDETLddfeeCPLRMLTKYTHPGI-VAVVIKPSVVGGFENaalIARWAQQHGKM---AVISAAYESGLGLSAYI 975
Cdd:TIGR01927 205 TGTAIALDESL-----WELPQLADEYGPGWrGALVIKPAIIGSPAK---LRDLAQKAHRLglqAVFSSVFESSIALGQLA 276
|
330 340 350
....*....|....*....|....*....|....*....
gi 1063696695 976 LFASYLemenvkasteqkqgTPPSVAHGLGTYRWLSEDV 1014
Cdd:TIGR01927 277 RLAAKL--------------SPDPAAVGFTTALLRAQDL 301
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1062-1351 |
1.56e-29 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 117.79 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1062 RYELRVDVDGFShfIRVHDVGEnaEGSVALFLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGRSrvqshaseTQTSPT 1141
Cdd:COG0596 2 STPRFVTVDGVR--LHYREAGP--DGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRS--------DKPAGG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1142 FSMEMIAEALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVsgspglkDPVARKIRsatddskarmmvdn 1221
Cdd:COG0596 70 YTLDDLADDLAALLDALGLERVVLVGHSMGGMVALELAARHPERVAGLVLV-------DEVLAALA-------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1222 glyifienwyngglwkslrnhphfskiaasRLLHGDVPSVAKLLSDLSSGRQPSLWEELEDCDTNISLVFGEKDVKYK-Q 1300
Cdd:COG0596 129 ------------------------------EPLRRPGLAPEALAALLRALARTDLRERLARITVPTLVIWGEKDPIVPpA 178
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1063696695 1301 IATRMYREMSKSkksvnniiEIVEIPEAGHAVHLESPLRVILALRKFLTRV 1351
Cdd:COG0596 179 LARRLAELLPNA--------ELVVLPGAGHFPPLEQPEAFAAALRDFLARL 221
|
|
| PRK05105 |
PRK05105 |
O-succinylbenzoate synthase; Provisional |
657-973 |
2.93e-29 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235345 [Multi-domain] Cd Length: 322 Bit Score: 119.94 E-value: 2.93e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 657 QYRVKLcDRPTICSDEFSQfHREGFILSLTlEDGSIGYGEVAPLNS-NVENLMDVEGQLQLVLhlmneakfsymlpllng 735
Cdd:PRK05105 8 RYQIPM-DAGVPLRKQRLK-TRDGLVVQLR-EGEREGWGEIAPLPGfSQETLEEAQEALLAWL----------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 736 siSSWIWSELGITASSiFPSVRCGLEMALLnamavrhdsSLLGILhyqkeeNGSAQPHSVQICAlldseGTPLEVAYVAR 815
Cdd:PRK05105 68 --NNWLAGDCDDELSQ-YPSVAFGLSCALA---------ELAGTL------PQAANYRTAPLCY-----GDPDELILKLA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 816 KLvqEGFSAIKLKVGRrVSSVQDALVMQEVRRAVGvQIELRADANCRWTFEEAREFGLLVNSCNLK---YIEEPVQNKDD 892
Cdd:PRK05105 125 DM--PGEKVAKVKVGL-YEAVRDGMLVNLLLEAIP-DLKLRLDANRGWTLEKAQQFAKYVPPDYRHriaFLEEPCKTPDD 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 893 LIRFHEETGLPVALDETL--DDFEecpLRMltkytHPGIVAVVIKPSVVGGFEN-AALIARwAQQHGKMAVISAAYESGL 969
Cdd:PRK05105 201 SRAFARATGIAIAWDESLrePDFQ---FEA-----EPGVRAIVIKPTLTGSLEKcQELIEQ-AHALGLRAVISSSIESSL 271
|
....
gi 1063696695 970 GLSA 973
Cdd:PRK05105 272 GLTQ 275
|
|
| MLE_like |
cd03315 |
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this ... |
757-982 |
9.36e-29 |
|
Muconate lactonizing enzyme (MLE) like subgroup of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and residues that can function as general acid/base catalysts, a Lys-X-Lys motif and another conserved lysine. Despite these conserved residues, the members of the MLE subgroup, like muconate lactonizing enzyme, o-succinylbenzoate synthase (OSBS) and N-acylamino acid racemase (NAAAR), catalyze different reactions.
Pssm-ID: 239431 [Multi-domain] Cd Length: 265 Bit Score: 117.06 E-value: 9.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 757 RCGLEMALLNAMAVRHDSSLlgilhyqkEENGSAQPHSVQICALLDSeGTPLEVAYVARKLVQEGFSAIKLKVGRRvsSV 836
Cdd:cd03315 45 KAAVDMALWDLWGKRLGVPV--------YLLLGGYRDRVRVAHMLGL-GEPAEVAEEARRALEAGFRTFKLKVGRD--PA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 837 QDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPVQNKD--DLIRFHEETGLPVALDE---TLD 911
Cdd:cd03315 114 RDVAVVAALREAVGDDAELRVDANRGWTPKQAIRALRALEDLGLDYVEQPLPADDleGRAALARATDTPIMADEsafTPH 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063696695 912 D-FEECPLRmltkythpGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYILFASYLE 982
Cdd:cd03315 194 DaFRELALG--------AADAVNIKTAKTGGLTKAQRVLAVAEALGLPVMVGSMIESGLGTLANAHLAAALR 257
|
|
| PRK11126 |
PRK11126 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional |
1092-1348 |
8.95e-28 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase; Provisional
Pssm-ID: 236855 [Multi-domain] Cd Length: 242 Bit Score: 113.40 E-value: 8.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1092 FLHGFLGTGEEWIPIMTgISGSARCISVDIPGHGRSRVQSHASETQTSptfsmEMIAEALYKLIEQitpgKVTIVGYSMG 1171
Cdd:PRK11126 7 FLHGLLGSGQDWQPVGE-ALPDYPRLYIDLPGHGGSAAISVDGFADVS-----RLLSQTLQSYNIL----PYWLVGYSLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1172 ARIALYMAL--RFSnKIEGAVVVSGSPGLKDPVARKIRSATDDSKARMMVDNGLYIFIENWYNGGLWKSLrNHPHFSKIA 1249
Cdd:PRK11126 77 GRIAMYYACqgLAG-GLCGLIVEGGNPGLQNAEERQARWQNDRQWAQRFRQEPLEQVLADWYQQPVFASL-NAEQRQQLV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1250 ASRLL-HGdvPSVAKLLSDLSSGRQPSLWEELEDCDTNISLVFGEKDVKYKQIATRmyremskskksvnNIIEIVEIPEA 1328
Cdd:PRK11126 155 AKRSNnNG--AAVAAMLEATSLAKQPDLRPALQALTFPFYYLCGERDSKFQALAQQ-------------LALPLHVIPNA 219
|
250 260
....*....|....*....|
gi 1063696695 1329 GHAVHLESPLRVILALRKFL 1348
Cdd:PRK11126 220 GHNAHRENPAAFAASLAQIL 239
|
|
| L-Ala-DL-Glu_epimerase |
cd03319 |
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The ... |
688-978 |
5.85e-24 |
|
L-Ala-D/L-Glu epimerase catalyzes the epimerization of L-Ala-D/L-Glu and other dipeptides. The genomic context and the substrate specificity of characterized members of this family from E.coli and B.subtilis indicates a possible role in the metabolism of the murein peptide of peptidoglycan, of which L-Ala-D-Glu is a component. L-Ala-D/L-Glu epimerase is a member of the enolase-superfamily, which is characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239435 [Multi-domain] Cd Length: 316 Bit Score: 104.19 E-value: 5.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 688 EDGSIGYGEVAPLnsnvenlMDVEGQ-LQLVLhlmneAKFSYMLPLLNGSISSW--IWSELGiTASSIFPSVRCGLEMAL 764
Cdd:cd03319 34 LDGITGYGEAAPT-------PRVTGEtVESVL-----AALKSVRPALIGGDPRLekLLEALQ-ELLPGNGAARAAVDIAL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 765 LNAMAVRHDSSLlgilhyqKEENGSAQPHSVqICALLDSEGTPLEVAYVARKLVQEGFSAIKLKVGRrvSSVQDALVMQE 844
Cdd:cd03319 101 WDLEAKLLGLPL-------YQLWGGGAPRPL-ETDYTISIDTPEAMAAAAKKAAKRGFPLLKIKLGG--DLEDDIERIRA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 845 VRRAVGvQIELRADANCRWTFEEAREF-GLLVNScNLKYIEEPV--QNKDDLIRFHEETGLPVALDETLDDFEECP-LRM 920
Cdd:cd03319 171 IREAAP-DARLRVDANQGWTPEEAVELlRELAEL-GVELIEQPVpaGDDDGLAYLRDKSPLPIMADESCFSAADAArLAG 248
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1063696695 921 LTKYTHpgivaVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYILFA 978
Cdd:cd03319 249 GGAYDG-----INIKLMKTGGLTEALRIADLARAAGLKVMVGCMVESSLSIAAAAHLA 301
|
|
| MR_MLE_C |
pfam13378 |
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins ... |
810-973 |
6.11e-24 |
|
Enolase C-terminal domain-like; This domain appears at the C-terminus of many of the proteins that carry the MR_MLE_N pfam02746 domain. EC:4.2.1.40.
Pssm-ID: 463862 [Multi-domain] Cd Length: 217 Bit Score: 101.49 E-value: 6.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 810 VAYVARKLVQEGFSAIKLKVGRRvsSVQDAL-VMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPV- 887
Cdd:pfam13378 3 AAEARRAVEARGFRAFKLKVGGP--DPEEDVeRVRAVREAVGPGVDLMVDANGAWSVAEAIRLARALEELGLLWIEEPVp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 888 -QNKDDLIRFHEETGLPVALDETLDDFEECpLRMLTKythpGIVAVV-IKPSVVGGFENAALIARWAQQHGkMAVISAAY 965
Cdd:pfam13378 81 pDDLEGLARLRRATPVPIATGESLYSREDF-RRLLEA----GAVDIVqPDVTRVGGITEALKIAALAEAFG-VPVAPHSG 154
|
....*...
gi 1063696695 966 ESGLGLSA 973
Cdd:pfam13378 155 GGPIGLAA 162
|
|
| TPP_PYR_POX_like |
cd07035 |
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP ... |
25-184 |
1.55e-22 |
|
Pyrimidine (PYR) binding domain of POX and related proteins; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) and related protiens subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. For glyoxylate carboligase, which belongs to this subfamily, but lacks this conserved glutamate, the rate of the initial TPP activation step is reduced but the ensuing steps of the enzymic reaction proceed efficiently. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites, for many the active sites lie between PP and PYR domains on different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate. This subfamily includes pyruvate decarboxylase (PDC) and indolepyruvate decarboxylase (IPDC). PDC catalyzes the conversion of pyruvate to acetaldehyde and CO2 in alcoholic fermentation. IPDC plays a role in the indole-3-pyruvic acid (IPA) pathway in plants and various plant-associated bacteria, it catalyzes the decarboxylation of IPA to IAA. This subfamily also includes the large catalytic subunit of acetohydroxyacid synthase (AHAS). AHAS catalyzes the condensation of two molecules of pyruvate to give the acetohydroxyacid, 2-acetolactate, a precursor of the branched chain amino acids, valine and leucine. AHAS also catalyzes the condensation of pyruvate and 2-ketobutyrate to form 2-aceto-2-hydroxybutyrate in isoleucine biosynthesis. Methanococcus jannaschii sulfopyruvate decarboxylase (MjComDE) and phosphonopyruvate decarboxylase (PpyrDc) also belong to this subfamily. PpyrDc is a homotrimeric enzyme having the PP and PYR domains tandemly arranged on the same subunit. It functions in the biosynthesis of C-P compounds such as bialaphos tripeptide in Streptomyces hygroscopicus. MjComDE is a dodecamer having the PYR and PP domains on different subunits, it has six alpha (PYR/ComD) subunits and six beta (PP/ComE) subunits. MjComDE catalyzes the decarboxylation of sulfopyruvic acid to sulfoacetaldehyde in the coenzyme M pathway.
Pssm-ID: 132918 [Multi-domain] Cd Length: 155 Bit Score: 95.29 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 25 AIIEECTRLGLTYFCVAPGSRSSHLaIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVVE 104
Cdd:cd07035 2 ALVEALKAEGVDHVFGVPGGAILPL-LDALARSGIRYILVRHEQGAVGMADGYARATGKPGVVLVTSGPGLTNAVTGLAN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 105 ASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIPVrmvlttVDSALHWATGSACGPVHLNCP 184
Cdd:cd07035 81 AYLDSIPLLVITGQRPTAGEGRGAFQEIDQVALFRPITKWAYRVTSPEEIPEA------LRRAFRIALSGRPGPVALDLP 154
|
|
| TPP_enzyme_N |
pfam02776 |
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain; |
23-184 |
1.01e-21 |
|
Thiamine pyrophosphate enzyme, N-terminal TPP binding domain;
Pssm-ID: 460690 [Multi-domain] Cd Length: 169 Bit Score: 93.45 E-value: 1.01e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 23 ASAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAV 102
Cdd:pfam02776 2 AEALADVLKALGVDTVFGVPGGHILPLLDALAKSPGIRYVLTRHEQGAAFAADGYARATGKPGVVLVTSGPGATNALTGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 103 VEASEDFLPLLLLTADRPPELQGVGANQA-INQINHFGSFVRFFFNLPPPTDLIPVrmvlttVDSALHWATGSACGPVHL 181
Cdd:pfam02776 82 ANAYVDSVPLLVISGQRPRSLVGRGALQQeLDQLALFRPVTKWAVRVTSADEIPEV------LRRAFRAALSGRPGPVYL 155
|
...
gi 1063696695 182 NCP 184
Cdd:pfam02776 156 EIP 158
|
|
| TPP_enzyme_M_2 |
pfam16582 |
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine ... |
201-433 |
2.95e-20 |
|
Middle domain of thiamine pyrophosphate; TPP_enzyme_M_2 is the middle domain of thiamine pyrophosphate in sequences not captured by pfam00205. This enzyme is necessary for the first step of the biosynthesis of menaquinone, or vitamin K2, an important cofactor in electron transport in bacteria.
Pssm-ID: 435442 Cd Length: 207 Bit Score: 90.45 E-value: 2.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 201 LNGLDMWMSNAEPFTKYFQVQShksDGVTTGQITEILQvikeaKKGLLLIGAIhTEDEIWASLLLAKELMWPVVADVLSG 280
Cdd:pfam16582 3 LAPLGDWLQQNKPWLRYQAQQL---EVPTHDDWDFWRQ-----KKGVIVAGRL-SAEEGMQLAAWAQKLGWPLLTDVQSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 281 VrlrklfkpfVEKLTHVfvdhlDHALFSDSVRN-LIEFDVVIQVGSRITSKRVSQMLEKCFPFAYILVDKHPCRHDPSHL 359
Cdd:pfam16582 74 T---------GQPLPYA-----DLWLANPTAREeLAQADIVIQFGGRLTSKRLLQFLAACKPHEYWLVDPLPGRLDPAHH 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1063696695 360 VTHRVQSNIVQFANCVL-KSRFPWRRSklhghLQALDGAIAREMSFQIsaESSLTEPYVAHMLSKALTSKSALFI 433
Cdd:pfam16582 140 RGRRFVASVGEWLRAHPpLRQAPWALE-----LLALSEFLASFIEQQV--GGEFGEAQLAHRIAALLPDQGQLFI 207
|
|
| PRK02714 |
PRK02714 |
o-succinylbenzoate synthase; |
678-1013 |
3.02e-20 |
|
o-succinylbenzoate synthase;
Pssm-ID: 235061 [Multi-domain] Cd Length: 320 Bit Score: 93.54 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 678 REGFILSLTLEDGSIGYGEVAPLNS-NVENLmdvegqlqlvlhlmNEA-KFSYMLPllnGSISSwiwsELGITASSIFPS 755
Cdd:PRK02714 28 REGIILRLTDETGKIGWGEIAPLPWfGSETL--------------EEAlAFCQQLP---GEITP----EQIFSIPDALPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 756 VRCGLEMALLNAMAVRHDSSLlgilhyqkeengsaqpHSVQICALLDSEGTPLEVAyvaRKLVQEGFSAIKLKVGRRVSS 835
Cdd:PRK02714 87 CQFGFESALENESGSRSNVTL----------------NPLSYSALLPAGEAALQQW---QTLWQQGYRTFKWKIGVDPLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 836 VQDALVMQEVRRaVGVQIELRADANCRWTFEEA-REFGLLVNSCNLK--YIEEP--VQNKDDLIRFHEETGLPVALDETL 910
Cdd:PRK02714 148 QELKIFEQLLER-LPAGAKLRLDANGGLSLEEAkRWLQLCDRRLSGKieFIEQPlpPDQFDEMLQLSQDYQTPIALDESV 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 911 ddfeeCPLRMLTKYTH---PGIvaVVIKPSVVGgfeNAALIARWAQQHGKMAVISAAYESGLGLSAYILFAsylemenvk 987
Cdd:PRK02714 227 -----ANLAQLQQCYQqgwRGI--FVIKPAIAG---SPSRLRQFCQQHPLDAVFSSVFETAIGRKAALALA--------- 287
|
330 340
....*....|....*....|....*.
gi 1063696695 988 asteQKQGTPPSvAHGLGTYRWLSED 1013
Cdd:PRK02714 288 ----AELSRPDR-ALGFGVTHWFSDE 308
|
|
| IlvB |
COG0028 |
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino ... |
23-589 |
3.21e-20 |
|
Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme [Amino acid transport and metabolism, Coenzyme transport and metabolism]; Acetolactate synthase large subunit or other thiamine pyrophosphate-requiring enzyme is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 439799 [Multi-domain] Cd Length: 548 Bit Score: 96.38 E-value: 3.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 23 ASAIIEECTRLGLTY-FCVaPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPA 101
Cdd:COG0028 6 ADALVEALEAEGVETvFGV-PGGAILPLYDALRRQSGIRHILVRHEQGAAFMADGYARATGKPGVCLVTSGPGATNLVTG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 102 VVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLPPPTDLIPVrmvlttVDSALHWATGSACGPVHL 181
Cdd:COG0028 85 LADAYMDSVPVLAITGQVPTSLIGRGAFQEVDQVGLFRPITKWSYLVTDPEDLPEV------LRRAFRIATSGRPGPVVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 182 NCPfrdpldgsptnwssnclngLDMWMSNAEPFTKYFQVQSHKSDGV-TTGQITEILQVIKEAKKGLLLIG--AIHteDE 258
Cdd:COG0028 159 DIP-------------------KDVQAAEAEEEPAPPELRGYRPRPApDPEAIEEAAELLAAAKRPVILAGggARR--AG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 259 IWASLL-LAKELMWPVVADVLS-GVrlrklfkpfveklthvfVDHlDHALF--------SDSVRNLI-EFDVVIQVGSRI 327
Cdd:COG0028 218 AAEELRaLAERLGAPVVTTLMGkGA-----------------FPE-DHPLYlgmlgmhgTPAANEALaEADLVLAVGARF 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 328 tSKRVSQMLEKCFPFAYIL-VDkhpcrHDPSHL-----VTHRVQSNIVQFANCVLKsRFPWRRSKLHGHLQALDGAIARE 401
Cdd:COG0028 280 -DDRVTGNWDEFAPDAKIIhID-----IDPAEIgknypVDLPIVGDAKAVLAALLE-ALEPRADDRAAWLARIAAWRAEY 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 402 MSFQISAESSLTEPYVAHMLSKALTSKSALFignsmpirdvdmygcsSENSSHvvdMMLSAelpcQWIQVTGNRG--ASG 479
Cdd:COG0028 353 LAAYAADDGPIKPQRVIAALREALPDDAIVV----------------TDVGQH---QMWAA----RYLRFRRPRRflTSG 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 480 IDGLLSSATGFAVGCK-----KRVVCVVGDISFLHDTNGLAILKQ-RIarkPMTILVINNRGGGIfrllpIAKKTEPSVL 553
Cdd:COG0028 410 GLGTMGYGLPAAIGAKlarpdRPVVAITGDGGFQMNLQELATAVRyGL---PVKVVVLNNGGLGM-----VRQWQELFYG 481
|
570 580 590
....*....|....*....|....*....|....*..
gi 1063696695 554 NQYFYTA-HDISIENLCLAHGVRYVHVGTKSELEDAL 589
Cdd:COG0028 482 GRYSGTDlPNPDFAKLAEAFGAKGERVETPEELEAAL 518
|
|
| MR_like |
cd03316 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup ... |
685-973 |
2.37e-19 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. Members of the MR subgroup are mandelate racemase, D-glucarate/L-idarate dehydratase (GlucD), D-altronate/D-mannonate dehydratase , D-galactonate dehydratase (GalD) , D-gluconate dehydratase (GlcD), and L-rhamnonate dehydratase (RhamD).
Pssm-ID: 239432 [Multi-domain] Cd Length: 357 Bit Score: 91.52 E-value: 2.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 685 LTLEDGSIGYGEVAPLNSNvenlmdvegqlQLVLHLMNEakfsYMLPLLNG----SISSwIWSEL----------GITAS 750
Cdd:cd03316 31 VTTDDGITGWGEAYPGGRP-----------SAVAAAIED----LLAPLLIGrdplDIER-LWEKLyrrlfwrgrgGVAMA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 751 SIfpsvrCGLEMALLNAMAVRHDSSLLGILhyqkeenGSAQPHSVQI-CALLDSEGTPLEVAYVARKLVQEGFSAIKLKV 829
Cdd:cd03316 95 AI-----SAVDIALWDIKGKAAGVPVYKLL-------GGKVRDRVRVyASGGGYDDSPEELAEEAKRAVAEGFTAVKLKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 830 GRRVSSVQ----DALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPV--QNKDDLIRFHEETGLP 903
Cdd:cd03316 163 GGPDSGGEdlreDLARVRAVREAVGPDVDLMVDANGRWDLAEAIRLARALEEYDLFWFEEPVppDDLEGLARLRQATSVP 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063696695 904 VALDETLDDFEECpLRMLTKythpGIVAVVIkPSV--VGGFENAALIARWAQQHGkMAVISAAYESGLGLSA 973
Cdd:cd03316 243 IAAGENLYTRWEF-RDLLEA----GAVDIIQ-PDVtkVGGITEAKKIAALAEAHG-VRVAPHGAGGPIGLAA 307
|
|
| TPP_enzyme_PYR |
cd06586 |
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine ... |
25-185 |
5.31e-18 |
|
Pyrimidine (PYR) binding domain of thiamine pyrophosphate (TPP)-dependent enzymes; Thiamine pyrophosphate (TPP) family, pyrimidine (PYR) binding domain; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. A polar interaction between the conserved glutamate of the PYR domain and the N1' of the TPP aminopyrimidine ring is shared by most TPP-dependent enzymes, and participates in the activation of TPP. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this group. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. In the case of 2-oxoisovalerate dehydrogenase (2OXO), sulfopyruvate decarboxylase (ComDE), and the E1 component of human pyruvate dehydrogenase complex (E1- PDHc) the PYR and PP domains appear on different subunits. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. For many of these enzymes the active sites lie between PP and PYR domains on different subunits. However, for the homodimeric enzymes 1-deoxy-D-xylulose 5-phosphate synthase (DXS) and Desulfovibrio africanus pyruvate:ferredoxin oxidoreductase (PFOR), each active site lies at the interface of the PYR and PP domains from the same subunit.
Pssm-ID: 132915 [Multi-domain] Cd Length: 154 Bit Score: 82.39 E-value: 5.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 25 AIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKPAVIITSsGTAVSNLLPAVVE 104
Cdd:cd06586 2 AFAEVLTAWGVRHVFGYPGDEISSLLDALREGDKRIIDTVIHELGAAGAAAGYARAGGPPVVIVTS-GTGLLNAINGLAD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 105 ASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSfvrfffnlppptdlIPVRMVLTTVDSAL-------HWATGSACG 177
Cdd:cd06586 81 AAAEHLPVVFLIGARGISAQAKQTFQSMFDLGMYRS--------------IPEANISSPSPAELpagidhaIRTAYASQG 146
|
....*...
gi 1063696695 178 PVHLNCPF 185
Cdd:cd06586 147 PVVVRLPR 154
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
1091-1337 |
6.99e-18 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 84.86 E-value: 6.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1091 LFLHGFLGTGEEWIPIMTGISGS-ARCISVDIPGHGRSRVQSHASEtqtsptFSMEMIAEALYKLIEQITPGKVTIVGYS 1169
Cdd:pfam00561 4 LLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDD------YRTDDLAEDLEYILEALGLEKVNLVGHS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1170 MGARIALYMALRFSNKIEGAVVVSGspglkdpvarkIRSATDDSKARMMVDNGLYIFIENWYNGGLWKSLRNHPHFSKiA 1249
Cdd:pfam00561 78 MGGLIALAYAAKYPDRVKALVLLGA-----------LDPPHELDEADRFILALFPGFFDGFVADFAPNPLGRLVAKLL-A 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1250 ASRLLHGDVPSVAKLLSDLSSGRQP----------SLWEELEDCDTNISLVFGEKDVKYkqIATRM-----YREMSKSKK 1314
Cdd:pfam00561 146 LLLLRLRLLKALPLLNKRFPSGDYAlakslvtgalLFIETWSTELRAKFLGRLDEPTLI--IWGDQdplvpPQALEKLAQ 223
|
250 260
....*....|....*....|...
gi 1063696695 1315 SVNNIIEIVeIPEAGHAVHLESP 1337
Cdd:pfam00561 224 LFPNARLVV-IPDAGHFAFLEGP 245
|
|
| MLE |
cd03318 |
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis, ... |
682-979 |
3.07e-17 |
|
Muconate Lactonizing Enzyme (MLE), an homooctameric enzyme, catalyses the conversion of cis,cis-muconate (CCM) to muconolactone (ML) in the catechol branch of the beta-ketoadipate pathway. This pathway is used in soil microbes to breakdown lignin-derived aromatics, catechol and protocatechuate, to citric acid cycle intermediates. Some bacterial species are also capable of dehalogenating chloroaromatic compounds by the action of chloromuconate lactonizing enzymes (Cl-MLEs). MLEs are members of the enolase superfamily characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239434 [Multi-domain] Cd Length: 365 Bit Score: 85.06 E-value: 3.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 682 ILSLTLEDGSIGYGEVAPLNSNVENLMDVEGQLQLVLHlmneakfsYMLPLLNGSISSWIwSELGITASSIFP---SVRC 758
Cdd:cd03318 32 LVRLTTSDGVVGIGEATTPGGPAWGGESPETIKAIIDR--------YLAPLLIGRDATNI-GAAMALLDRAVAgnlFAKA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 759 GLEMALLNAMAVRHD---SSLLGilhyqkeenGSAQpHSVQICALLDSEGTPLEVAYVARKLVQEGFSAIKLKVGRRvsS 835
Cdd:cd03318 103 AIEMALLDAQGRRLGlpvSELLG---------GRVR-DSLPVAWTLASGDTERDIAEAEEMLEAGRHRRFKLKMGAR--P 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 836 VQDALV-MQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPV--QNKDDLIRFHEETGLPVALDETLDD 912
Cdd:cd03318 171 PADDLAhVEAIAKALGDRASVRVDVNQAWDESTAIRALPRLEAAGVELIEQPVprENLDGLARLRSRNRVPIMADESVSG 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063696695 913 FEEcplrMLtKYTHPGIVAVV-IKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYI-LFAS 979
Cdd:cd03318 251 PAD----AF-ELARRGAADVFsLKIAKSGGLRRAQKVAAIAEAAGIALYGGTMLESSIGTAASAhLFAT 314
|
|
| MR_MLE |
smart00922 |
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) ... |
810-902 |
9.24e-17 |
|
Mandelate racemase / muconate lactonizing enzyme, C-terminal domain; Mandelate racemase (MR) and muconate lactonizing enzyme (MLE) are two bacterial enzymes involved in aromatic acid catabolism. They catalyze mechanistically distinct reactions yet they are related at the level of their primary, quaternary (homooctamer) and tertiary structures.. This entry represents the C-terminal region of these proteins.
Pssm-ID: 214914 [Multi-domain] Cd Length: 97 Bit Score: 76.94 E-value: 9.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 810 VAYVARKLVQEGFSAIKLKVGRRvsSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPV-- 887
Cdd:smart00922 5 AEAARRAVAEAGFRAVKVKVGGG--PLEDLARVAAVREAVGPDADLMVDANGAWTAEEAIRALEALDELGLEWIEEPVpp 82
|
90
....*....|....*
gi 1063696695 888 QNKDDLIRFHEETGL 902
Cdd:smart00922 83 DDLEGLAELRRATPI 97
|
|
| NAAAR |
cd03317 |
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of ... |
674-979 |
2.34e-16 |
|
N-acylamino acid racemase (NAAAR), an octameric enzyme that catalyzes the racemization of N-acylamino acids. NAAARs act on a broad range of N-acylamino acids rather than amino acids. Enantiopure amino acids are of industrial interest as chiral building blocks for antibiotics, herbicides, and drugs. NAAAR is a member of the enolase superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239433 [Multi-domain] Cd Length: 354 Bit Score: 82.28 E-value: 2.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 674 SQFHREGFILSLTLEDGSIGYGEVaplnSNVENLMDVEGQLQLVLHLMNEakfsYMLPLLNGSISSwIWSELGITASSI- 752
Cdd:cd03317 20 TLNEREFLIVELTDEEGITGYGEV----VAFEGPFYTEETNATAWHILKD----YLLPLLLGREFS-HPEEVSERLAPIk 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 753 -FPSVRCGLEMALLNAMAVRHDSSLLGILHYQKEEngsaQPHSVQIcALLDSEGTPLEVAyvaRKLVQEGFSAIKLKVGR 831
Cdd:cd03317 91 gNNMAKAGLEMAVWDLYAKAQGQSLAQYLGGTRDS----IPVGVSI-GIQDDVEQLLKQI---ERYLEEGYKRIKLKIKP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 832 RVssvqDALVMQEVRRAVGvQIELRADANCRWTFEEAR------EFGLLvnscnlkYIEEPVQNkDDLI---RFHEETGL 902
Cdd:cd03317 163 GW----DVEPLKAVRERFP-DIPLMADANSAYTLADIPllkrldEYGLL-------MIEQPLAA-DDLIdhaELQKLLKT 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1063696695 903 PVALDETLDDFEECplRMLTKYthpGIVAVV-IKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSAYILFAS 979
Cdd:cd03317 230 PICLDESIQSAEDA--RKAIEL---GACKIInIKPGRVGGLTEALKIHDLCQEHGIPVWCGGMLESGIGRAHNVALAS 302
|
|
| enolase_like |
cd00308 |
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is ... |
826-973 |
6.32e-16 |
|
Enolase-superfamily, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion. Enolase superfamily contains different enzymes, like enolases, glutarate-, fucanate- and galactonate dehydratases, o-succinylbenzoate synthase, N-acylamino acid racemase, L-alanine-DL-glutamate epimerase, mandelate racemase, muconate lactonizing enzyme and 3-methylaspartase.
Pssm-ID: 238188 [Multi-domain] Cd Length: 229 Bit Score: 78.52 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 826 KLKVGRRVSSVQDALVM--QEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPV--QNKDDLIRFHEETG 901
Cdd:cd00308 66 LLGGGSRDRVPAYGSIErvRAVREAFGPDARLAVDANGAWTPKEAIRLIRALEKYGLAWIEEPCapDDLEGYAALRRRTG 145
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063696695 902 LPVALDETLDDFeECPLRMLtkyTHPGIVAVVIKPSVVGGFENAALIARWAQQHGKMAVISAAYESGLGLSA 973
Cdd:cd00308 146 IPIAADESVTTV-DDALEAL---ELGAVDILQIKPTRVGGLTESRRAADLAEAFGIRVMVHGTLESSIGTAA 213
|
|
| PRK02901 |
PRK02901 |
O-succinylbenzoate synthase; Provisional |
826-1014 |
1.17e-12 |
|
O-succinylbenzoate synthase; Provisional
Pssm-ID: 235084 [Multi-domain] Cd Length: 327 Bit Score: 70.77 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 826 KLKVGRRVSSV-QDALVMQEVRRAVGVQIELRADANCRWTFEEA-REFGLLVNSCNLKYIEEPVQNKDDLIRFHEETGLP 903
Cdd:PRK02901 107 KVKVAEPGQTLaDDVARVNAVRDALGPDGRVRVDANGGWSVDEAvAAARALDADGPLEYVEQPCATVEELAELRRRVGVP 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 904 VALDETL---DDfeecPLRMLTkyTHPGIVAVViKPSVVGGFENAALIARwaqQHGKMAVISAAYESGLGLSAYILFASY 980
Cdd:PRK02901 187 IAADESIrraED----PLRVAR--AGAADVAVL-KVAPLGGVRAALDIAE---QIGLPVVVSSALDTSVGIAAGLALAAA 256
|
170 180 190
....*....|....*....|....*....|....*.
gi 1063696695 981 LemenvkasteqkqgtpPSVAH--GLGTYRWLSEDV 1014
Cdd:PRK02901 257 L----------------PELDHacGLATGGLFEEDV 276
|
|
| bioH |
TIGR01738 |
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for ... |
1086-1196 |
5.98e-12 |
|
pimelyl-[acyl-carrier protein] methyl ester esterase; This CoA-binding enzyme is required for the production of pimeloyl-coenzyme A, the substrate of the BioF protein early in the biosynthesis of biotin. Its exact function is unknown, but is proposed in ref 2. This enzyme belongs to the alpha/beta hydrolase fold family (pfam00561). Members of this family are restricted to the Proteobacteria. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273783 [Multi-domain] Cd Length: 245 Bit Score: 67.15 E-value: 5.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1086 EGSVALFL-HGFLGTGEEWIPIMTGISGSARCISVDIPGHGRSRVQShasetqtspTFSMEMIAEAlyklIEQITPGKVT 1164
Cdd:TIGR01738 2 QGNVHLVLiHGWGMNAEVFRCLDEELSAHFTLHLVDLPGHGRSRGFG---------PLSLADMAEA----IAAQAPDPAI 68
|
90 100 110
....*....|....*....|....*....|..
gi 1063696695 1165 IVGYSMGARIALYMALRFSNKIEGAVVVSGSP 1196
Cdd:TIGR01738 69 WLGWSLGGLVALHIAATHPDRVRALVTVASSP 100
|
|
| mandelate_racemase |
cd03321 |
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that ... |
759-891 |
8.95e-11 |
|
Mandelate racemase (MR) catalyzes the Mg2+-dependent 1,1-proton transfer reaction that interconverts the enantiomers of mandelic acid. MR is the first enzyme in the bacterial pathway that converts mandelic acid to benzoic acid and allows this pathway to utilize either enantiomer of mandelate. MR belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239437 [Multi-domain] Cd Length: 355 Bit Score: 65.20 E-value: 8.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 759 GLEMALLNAMAVRHDSSLLGILhyqkeengSAQPHSVQIcalLDSEGTPLEVAYVAR--KLVQEGFSAIKLKVGRRVSSv 836
Cdd:cd03321 103 GIDMAAWDALAKVHGLPLAKLL--------GGNPRPVQA---YDSHGLDGAKLATERavTAAEEGFHAVKTKIGYPTAD- 170
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063696695 837 QDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPVQNKD 891
Cdd:cd03321 171 EDLAVVRSIRQAVGDGVGLMVDYNQSLTVPEAIERGQALDQEGLTWIEEPTLQHD 225
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
1066-1181 |
2.02e-10 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 64.19 E-value: 2.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1066 RVDVDGfsHFIRVHDVGENAEGSVaLFLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGRSrvqshaseTQTSPTFSME 1145
Cdd:PRK14875 113 KARIGG--RTVRYLRLGEGDGTPV-VLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGAS--------SKAVGAGSLD 181
|
90 100 110
....*....|....*....|....*....|....*.
gi 1063696695 1146 MIAEALYKLIEQITPGKVTIVGYSMGARIALYMALR 1181
Cdd:PRK14875 182 ELAAAVLAFLDALGIERAHLVGHSMGGAVALRLAAR 217
|
|
| YvaK |
COG1647 |
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism]; |
1091-1353 |
8.64e-10 |
|
Esterase/lipase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 441253 [Multi-domain] Cd Length: 246 Bit Score: 60.73 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1091 LFLHGFLGTGEEWIPImtgisgsAR--------CISVDIPGHGRSRvqshASETQTSPTFSMEMIAEALYKLIEQitPGK 1162
Cdd:COG1647 19 LLLHGFTGSPAEMRPL-------AEalakagytVYAPRLPGHGTSP----EDLLKTTWEDWLEDVEEAYEILKAG--YDK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1163 VTIVGYSMGARIALYMALRFSNkIEGAVVVSGSPGLKD------PVARKIRsatdDSKARMMVDNGLYIFIENWYNGGLW 1236
Cdd:COG1647 86 VIVIGLSMGGLLALLLAARYPD-VAGLVLLSPALKIDDpsapllPLLKYLA----RSLRGIGSDIEDPEVAEYAYDRTPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1237 KSLRNHPHFSKIAASRLLHGDVPsvakllsdlssgrqpslweeledcdtnISLVFGEKD--VKYKQiATRMYREMSKSKK 1314
Cdd:COG1647 161 RALAELQRLIREVRRDLPKITAP---------------------------TLIIQSRKDevVPPES-ARYIYERLGSPDK 212
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1063696695 1315 svnniiEIVEIPEAGHAVHLESPL-RVILALRKFLTRVHN 1353
Cdd:COG1647 213 ------ELVWLEDSGHVITLDKDReEVAEEILDFLERLAA 246
|
|
| TPP_enzyme_C |
pfam02775 |
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain; |
484-589 |
9.32e-10 |
|
Thiamine pyrophosphate enzyme, C-terminal TPP binding domain;
Pssm-ID: 460689 [Multi-domain] Cd Length: 151 Bit Score: 58.75 E-value: 9.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 484 LSSATGFAVGC-KKRVVCVVGDISFLHDTNGLAILKQRiaRKPMTILVINNRGGGIFRLLPIAKKTEPSVlNQYFYTAHD 562
Cdd:pfam02775 34 LPAAIGAKLARpDRPVVAIAGDGGFQMNLQELATAVRY--NLPITVVVLNNGGYGMTRGQQTPFGGGRYS-GPSGKILPP 110
|
90 100
....*....|....*....|....*..
gi 1063696695 563 ISIENLCLAHGVRYVHVGTKSELEDAL 589
Cdd:pfam02775 111 VDFAKLAEAYGAKGARVESPEELEEAL 137
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1070-1193 |
1.16e-09 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 60.02 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1070 DGFSHFIRVHDVGENAEGSVaLFLHGFLGTGEEWIPIMT-----GIsgsaRCISVDIPGHGRSrvqshASETQTSPTFSm 1144
Cdd:COG2267 12 DGLRLRGRRWRPAGSPRGTV-VLVHGLGEHSGRYAELAEalaaaGY----AVLAFDLRGHGRS-----DGPRGHVDSFD- 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1063696695 1145 EMIA--EALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVS 1193
Cdd:COG2267 81 DYVDdlRAALDALRARPGLPVVLLGHSMGGLIALLYAARYPDRVAGLVLLA 131
|
|
| TPP_enzymes |
cd00568 |
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic ... |
473-603 |
7.28e-09 |
|
Thiamine pyrophosphate (TPP) enzyme family, TPP-binding module; found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. These enzymes include, among others, the E1 components of the pyruvate, the acetoin and the branched chain alpha-keto acid dehydrogenase complexes.
Pssm-ID: 238318 [Multi-domain] Cd Length: 168 Bit Score: 56.49 E-value: 7.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 473 GNRGASGIDGLLSSATGFAVGCK-----KRVVCVVGDISFLHDTNGLAILKQriARKPMTILVINNRGGGIFRLLPIAKK 547
Cdd:cd00568 37 RRFLTSTGFGAMGYGLPAAIGAAlaapdRPVVCIAGDGGFMMTGQELATAVR--YGLPVIVVVFNNGGYGTIRMHQEAFY 114
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1063696695 548 TEPSVLNQYfytaHDISIENLCLAHGVRYVHVGTKSELEDALFVPSVEEMDCIVEV 603
Cdd:cd00568 115 GGRVSGTDL----SNPDFAALAEAYGAKGVRVEDPEDLEAALAEALAAGGPALIEV 166
|
|
| D-glucarate_dehydratase |
cd03323 |
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to ... |
676-915 |
1.63e-08 |
|
D-Glucarate dehydratase (GlucD) catalyzes the dehydration of both D-glucarate and L-idarate to form 5-keto-4-deoxy-D-glucarate (5-KDG) , the initial reaction of the catabolic pathway for (D)-glucarate. GlucD belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and that is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239439 [Multi-domain] Cd Length: 395 Bit Score: 58.49 E-value: 1.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 676 FHREgfILSLTLEDGSIGYGEVAPLNSNVENLMD-----VEGQLQLV-LHLMNEAKFSYMLPLLNGSisswiwsELGITA 749
Cdd:cd03323 28 FTRN--IVELTDDNGNTGVGESPGGAEALEALLEaarslVGGDVFGAyLAVLESVRVAFADRDAGGR-------GLQTFD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 750 SSIFPSVRCGLEMALLNAM--------------AVRHDSSLLGILHYQKEENGSAQPHSvqicALLDSEG---TPLEVAY 812
Cdd:cd03323 99 LRTTVHVVTAFEVALLDLLgqalgvpvadllggGQRDSVPFLAYLFYKGDRHKTDLPYP----WFRDRWGealTPEGVVR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 813 VARKLVQE-GFSAIKLKVGRRVSSvQDALVMQEVRRAVGvQIELRADANCRWTFEEAREFGLLVNScNLKYIEEPVQNKD 891
Cdd:cd03323 175 LARAAIDRyGFKSFKLKGGVLPGE-EEIEAVKALAEAFP-GARLRLDPNGAWSLETAIRLAKELEG-VLAYLEDPCGGRE 251
|
250 260
....*....|....*....|....
gi 1063696695 892 DLIRFHEETGLPVALDETLDDFEE 915
Cdd:cd03323 252 GMAEFRRATGLPLATNMIVTDFRQ 275
|
|
| PRK08979 |
PRK08979 |
acetolactate synthase 3 large subunit; |
71-278 |
6.78e-08 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181602 [Multi-domain] Cd Length: 572 Bit Score: 57.14 E-value: 6.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 71 AFH-AIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLP 149
Cdd:PRK08979 54 AVHmADGYARATGKVGVVLVTSGPGATNTITGIATAYMDSIPMVVLSGQVPSNLIGNDAFQECDMIGISRPVVKHSFLVK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 150 PPTDlIPvrmvlTTVDSALHWATGSACGPVHLNCPfrdpldgsptnwsSNCLNGL---------DMWMSNAEPFTkyfqv 220
Cdd:PRK08979 134 DAED-IP-----EIIKKAFYIASTGRPGPVVIDLP-------------KDCLNPAilhpyeypeSIKMRSYNPTT----- 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063696695 221 QSHKsdgvttGQITEILQVIKEAKKGLLLIGA---IHTEDEiwASLLLAKELMWPVVADVL 278
Cdd:PRK08979 190 SGHK------GQIKRGLQALLAAKKPVLYVGGgaiISGADK--QILQLAEKLNLPVVSTLM 242
|
|
| MR_like_3 |
cd03328 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this ... |
818-921 |
1.45e-07 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 3. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239444 [Multi-domain] Cd Length: 352 Bit Score: 55.11 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 818 VQEGFSAIKLKVGRrvSSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPVQNKD----DL 893
Cdd:cd03328 150 VAQGIPRVKMKIGR--DPRRDPDRVAAARRAIGPDAELFVDANGAYSRKQALALARAFADEGVTWFEEPVSSDDlaglRL 227
|
90 100 110
....*....|....*....|....*....|.
gi 1063696695 894 IRFHEETGLPVALDE---TLDDFEecplRML 921
Cdd:cd03328 228 VRERGPAGMDIAAGEyayTLAYFR----RLL 254
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
1082-1194 |
7.40e-07 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 51.45 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1082 GENAEGSVaLFLHGFLGTGEEWIPIMTGISG-SARCISVD---IPGHGRSR----VQSHASETQTSPTFSMEMIAEALYK 1153
Cdd:COG0400 1 GGPAAPLV-VLLHGYGGDEEDLLPLAPELALpGAAVLAPRapvPEGPGGRAwfdlSFLEGREDEEGLAAAAEALAAFIDE 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1063696695 1154 LIEQ--ITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSG 1194
Cdd:COG0400 80 LEARygIDPERIVLAGFSQGAAMALSLALRRPELLAGVVALSG 122
|
|
| PLN02470 |
PLN02470 |
acetolactate synthase |
5-259 |
1.00e-06 |
|
acetolactate synthase
Pssm-ID: 215261 [Multi-domain] Cd Length: 585 Bit Score: 53.20 E-value: 1.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 5 ETEVSNFLRDEANINAvwaSAIIEECTRLGLTYFCVAPGSRSSHLAIAAANHPLTTCLACFDERSLAFHAIGYAKGSLKP 84
Cdd:PLN02470 1 ETFQSRFAPDEPRKGA---DILVEALEREGVDTVFAYPGGASMEIHQALTRSNCIRNVLCRHEQGEVFAAEGYAKASGKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 85 AVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFnLPPPTDLIPvrmvlTTV 164
Cdd:PLN02470 78 GVCIATSGPGATNLVTGLADALLDSVPLVAITGQVPRRMIGTDAFQETPIVEVTRSITKHNY-LVMDVEDIP-----RVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 165 DSALHWATGSACGPVHLNCPFRDPLDGSPTNWSSNC-LNGldmWMSNAEPFtkyfqvqshksdgVTTGQITEILQVIKEA 243
Cdd:PLN02470 152 REAFFLASSGRPGPVLVDIPKDIQQQLAVPNWNQPMkLPG---YLSRLPKP-------------PEKSQLEQIVRLISES 215
|
250
....*....|....*...
gi 1063696695 244 KKGLLLIGA--IHTEDEI 259
Cdd:PLN02470 216 KRPVVYVGGgcLNSSEEL 233
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
1091-1335 |
1.12e-06 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 50.94 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1091 LFLHGFlgtGEEWIPIMTGISGSARCISVDIPGHGRSRvqshasetqtSPTFSMEMIAEALYKLIEQITPGKVTIVGYSM 1170
Cdd:pfam12697 2 VLVHGA---GLSAAPLAALLAAGVAVLAPDLPGHGSSS----------PPPLDLADLADLAALLDELGAARPVVLVGHSL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1171 GARIALYMALRFSNKiegAVVVSGSPGLKDPVARKIRSAtddskarmmvdnglyifienwynGGLWKSLRNHPHFSKIAA 1250
Cdd:pfam12697 69 GGAVALAAAAAALVV---GVLVAPLAAPPGLLAALLALL-----------------------ARLGAALAAPAWLAAESL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1251 SRLLHGDVPSVAKL------LSDLSSGRQPSLWEELEDCDTNIsLVFGEKDVKYKQIATRMYREMSKSKksvnniieIVE 1324
Cdd:pfam12697 123 ARGFLDDLPADAEWaaalarLAALLAALALLPLAAWRDLPVPV-LVLAEEDRLVPELAQRLLAALAGAR--------LVV 193
|
250
....*....|.
gi 1063696695 1325 IPEAGHAVHLE 1335
Cdd:pfam12697 194 LPGAGHLPLDD 204
|
|
| PRK03592 |
PRK03592 |
haloalkane dehalogenase; Provisional |
1066-1228 |
6.41e-06 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 235135 Cd Length: 295 Bit Score: 49.61 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1066 RVDVDGfsHFIRVHDVGEnaeGSVALFLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGRS-------RVQSHASetqt 1138
Cdd:PRK03592 11 RVEVLG--SRMAYIETGE---GDPIVFLHGNPTSSYLWRNIIPHLAGLGRCLAPDLIGMGASdkpdidyTFADHAR---- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1139 sptfsmemiaeALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKIEGAVV---VSGSPGLKD------PVARKIRsa 1209
Cdd:PRK03592 82 -----------YLDAWFDALGLDDVVLVGHDWGSALGFDWAARHPDRVRGIAFmeaIVRPMTWDDfppavrELFQALR-- 148
|
170
....*....|....*....
gi 1063696695 1210 TDDSKARMMVDNGLyiFIE 1228
Cdd:PRK03592 149 SPGEGEEMVLEENV--FIE 165
|
|
| DAP2 |
COG1506 |
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism]; |
1089-1350 |
8.68e-06 |
|
Dipeptidyl aminopeptidase/acylaminoacyl peptidase [Amino acid transport and metabolism];
Pssm-ID: 441115 [Multi-domain] Cd Length: 234 Bit Score: 48.47 E-value: 8.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1089 VALFLHGFLGTGEE----WIPIMT--GISgsarCISVDIPGHGRSRVQshasetqtsptFSMEMIAEALY---KLIEQ-- 1157
Cdd:COG1506 25 VVVYVHGGPGSRDDsflpLAQALAsrGYA----VLAPDYRGYGESAGD-----------WGGDEVDDVLAaidYLAARpy 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1158 ITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSGSPGLKdpvarkirsatddskarmMVDNGLYIFIEnWYNGGLWK 1237
Cdd:COG1506 90 VDPDRIGIYGHSYGGYMALLAAARHPDRFKAAVALAGVSDLR------------------SYYGTTREYTE-RLMGGPWE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1238 SLRNHPHFSKIAAsrllhgdvpsVAKLlsdlssgRQPSLweeledcdtnisLVFGEKD--VKYKQiATRMYREMSKSKKS 1315
Cdd:COG1506 151 DPEAYAARSPLAY----------ADKL-------KTPLL------------LIHGEADdrVPPEQ-AERLYEALKKAGKP 200
|
250 260 270
....*....|....*....|....*....|....*
gi 1063696695 1316 VnniiEIVEIPEAGHAVHLESPLRVILALRKFLTR 1350
Cdd:COG1506 201 V----ELLVYPGEGHGFSGAGAPDYLERILDFLDR 231
|
|
| TPP_IOR_alpha |
cd02008 |
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of ... |
460-594 |
9.91e-06 |
|
Thiamine pyrophosphate (TPP) family, IOR-alpha subfamily, TPP-binding module; composed of proteins similar to indolepyruvate ferredoxin oxidoreductase (IOR) alpha subunit. IOR catalyzes the oxidative decarboxylation of arylpyruvates, such as indolepyruvate or phenylpyruvate, which are generated by the transamination of aromatic amino acids, to the corresponding aryl acetyl-CoA.
Pssm-ID: 238966 [Multi-domain] Cd Length: 178 Bit Score: 47.66 E-value: 9.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 460 LSAELPCQWIQVTGNRGASGidgllSSATGFA-VGCKKRVVCVVGDISFLHdtNGLAILKQRIARK-PMTILVINNR--- 534
Cdd:cd02008 38 LGALPPLNAIDTCTCMGASI-----GVAIGMAkASEDKKVVAVIGDSTFFH--SGILGLINAVYNKaNITVVILDNRtta 110
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063696695 535 --GGGifrllPIakktePSVLNQYFYTAHDISIENLCLAHGVRYVHV-------GTKSELEDALFVPSV 594
Cdd:cd02008 111 mtGGQ-----PH-----PGTGKTLTEPTTVIDIEALVRAIGVKRVVVvdpydlkAIREELKEALAVPGV 169
|
|
| Fes |
COG2382 |
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism]; |
1089-1231 |
7.00e-05 |
|
Enterochelin esterase or related enzyme [Inorganic ion transport and metabolism];
Pssm-ID: 441948 [Multi-domain] Cd Length: 314 Bit Score: 46.38 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1089 VALFLHGFLGTGEEWIPIMtGI---------SGSAR-CISVDIPGHGRSRVqshASETQTSPTFsMEMIAEALYKLIEQI 1158
Cdd:COG2382 114 VLYLLDGGGGDEQDWFDQG-RLptildnliaAGKIPpMIVVMPDGGDGGDR---GTEGPGNDAF-ERFLAEELIPFVEKN 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1159 -----TPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSGS------PGLKDPVARKIRSATDDSKARMMVDNGLYifi 1227
Cdd:COG2382 189 yrvsaDPEHRAIAGLSMGGLAALYAALRHPDLFGYVGSFSGSfwwppgDADRGGWAELLAAGAPKKPLRFYLDVGTE--- 265
|
....
gi 1063696695 1228 ENWY 1231
Cdd:COG2382 266 DDLL 269
|
|
| rTSbeta_L-fuconate_dehydratase |
cd03324 |
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also ... |
814-892 |
7.17e-05 |
|
Human rTS beta is encoded by the rTS gene which, through alternative RNA splicing, also encodes rTS alpha whose mRNA is complementary to thymidylate synthase mRNA. rTS beta expression is associated with the production of small molecules that appear to mediate the down-regulation of thymidylate synthase protein by a novel intercellular signaling mechanism. A member of this family, from Xanthomonas, has been characterized to be a L-fuconate dehydratase. rTS beta belongs to the enolase superfamily of enzymes, characterized by the presence of an enolate anion intermediate which is generated by abstraction of the alpha-proton of the carboxylate substrate by an active site residue and is stabilized by coordination to the essential Mg2+ ion.
Pssm-ID: 239440 [Multi-domain] Cd Length: 415 Bit Score: 46.95 E-value: 7.17e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1063696695 814 ARKLVQEGFSAIKLKVGRRVSsvQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEEPVqNKDD 892
Cdd:cd03324 204 CKEALAQGFTHFKLKVGADLE--DDIRRCRLAREVIGPDNKLMIDANQRWDVPEAIEWVKQLAEFKPWWIEEPT-SPDD 279
|
|
| PRK07979 |
PRK07979 |
acetolactate synthase 3 large subunit; |
71-278 |
9.98e-05 |
|
acetolactate synthase 3 large subunit;
Pssm-ID: 181185 [Multi-domain] Cd Length: 574 Bit Score: 46.77 E-value: 9.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 71 AFH-AIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFnLP 149
Cdd:PRK07979 54 AVHmADGLARATGEVGVVLVTSGPGATNAITGIATAYMDSIPLVVLSGQVATSLIGYDAFQECDMVGISRPVVKHSF-LV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 150 PPTDLIPvrmvlTTVDSALHWATGSACGPVHLNCP--FRDPLDGSPTNWSSnclnglDMWMSNAEPftkyfQVQSHKsdg 227
Cdd:PRK07979 133 KQTEDIP-----QVLKKAFWLAASGRPGPVVVDLPkdILNPANKLPYVWPE------SVSMRSYNP-----TTQGHK--- 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1063696695 228 vttGQITEILQVIKEAKKGLLLIGAIHTEDEIWASLL-LAKELMWPVVADVL 278
Cdd:PRK07979 194 ---GQIKRALQTLVAAKKPVVYVGGGAINAACHQQLKeLVEKLNLPVVSSLM 242
|
|
| PRK10349 |
PRK10349 |
pimeloyl-ACP methyl ester esterase BioH; |
1085-1196 |
1.06e-04 |
|
pimeloyl-ACP methyl ester esterase BioH;
Pssm-ID: 137836 [Multi-domain] Cd Length: 256 Bit Score: 45.39 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1085 AEGSVAL-FLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGRSRvqshasetqTSPTFSMEMIAEAlyklIEQITPGKV 1163
Cdd:PRK10349 10 GQGNVHLvLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSR---------GFGALSLADMAEA----VLQQAPDKA 76
|
90 100 110
....*....|....*....|....*....|...
gi 1063696695 1164 TIVGYSMGARIALYMALRFSNKIEGAVVVSGSP 1196
Cdd:PRK10349 77 IWLGWSLGGLVASQIALTHPERVQALVTVASSP 109
|
|
| PRK07525 |
PRK07525 |
sulfoacetaldehyde acetyltransferase; Validated |
64-187 |
1.45e-04 |
|
sulfoacetaldehyde acetyltransferase; Validated
Pssm-ID: 236042 [Multi-domain] Cd Length: 588 Bit Score: 46.14 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 64 CFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVR 143
Cdd:PRK07525 49 VAHEQNAGHMADGYTRVTGRMGMVIGQNGPGITNFVTAVATAYWAHTPVVLVTPQAGTKTIGQGGFQEAEQMPMFEDMTK 128
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1063696695 144 FFFNLPPPTdlipvRM--VLTTV-DSALhwatgSACGPVHLNCPfRD 187
Cdd:PRK07525 129 YQEEVRDPS-----RMaeVLNRVfDKAK-----RESGPAQINIP-RD 164
|
|
| EstA |
COG1075 |
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and ... |
1091-1179 |
2.32e-04 |
|
Triacylglycerol esterase/lipase EstA, alpha/beta hydrolase fold [Lipid transport and metabolism];
Pssm-ID: 440693 [Multi-domain] Cd Length: 106 Bit Score: 41.74 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1091 LFLHGFLGTGEEWIPIMTGISGS-ARCISVDIPGHGRSrvqshasetqtsptfsMEMIAEALYKLIEQI---TP-GKVTI 1165
Cdd:COG1075 9 VLVHGLGGSAASWAPLAPRLRAAgYPVYALNYPSTNGS----------------IEDSAEQLAAFVDAVlaaTGaEKVDL 72
|
90
....*....|....
gi 1063696695 1166 VGYSMGARIALYMA 1179
Cdd:COG1075 73 VGHSMGGLVARYYL 86
|
|
| TPP_BFDC |
cd02002 |
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins ... |
487-589 |
3.49e-04 |
|
Thiamine pyrophosphate (TPP) family, BFDC subfamily, TPP-binding module; composed of proteins similar to Pseudomonas putida benzoylformate decarboxylase (BFDC). P. putida BFDC plays a role in the mandelate pathway, catalyzing the conversion of benzoylformate to benzaldehyde and carbon dioxide. This enzyme is dependent on TPP and a divalent metal cation as cofactors.
Pssm-ID: 238960 [Multi-domain] Cd Length: 178 Bit Score: 42.97 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 487 ATGFAVGCKKR-VVCVVGDISFLHDTNGLAIlkqrIARK--PMTILVINNRGGGIFRLlpiakktepSVLNQYFYTAH-- 561
Cdd:cd02002 58 AVGAALANPDRkVVAIIGDGSFMYTIQALWT----AARYglPVTVVILNNRGYGALRS---------FLKRVGPEGPGen 124
|
90 100 110
....*....|....*....|....*....|....*...
gi 1063696695 562 ----------DISIENLCLAHGVRYVHVGTKSELEDAL 589
Cdd:cd02002 125 apdgldlldpGIDFAAIAKAFGVEAERVETPEELDEAL 162
|
|
| PRK08155 |
PRK08155 |
acetolactate synthase large subunit; |
67-130 |
6.09e-04 |
|
acetolactate synthase large subunit;
Pssm-ID: 181257 [Multi-domain] Cd Length: 564 Bit Score: 44.31 E-value: 6.09e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063696695 67 ERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQ 130
Cdd:PRK08155 60 EQGAGFIAQGMARTTGKPAVCMACSGPGATNLVTAIADARLDSIPLVCITGQVPASMIGTDAFQ 123
|
|
| TPP_PYR_POX |
cd07039 |
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) ... |
67-138 |
7.27e-04 |
|
Pyrimidine (PYR) binding domain of POX; Thiamine pyrophosphate (TPP family), pyrimidine (PYR) binding domain of pyruvate oxidase (POX) subfamily. The PYR domain is found in many key metabolic enzymes which use TPP (also known as thiamine diphosphate) as a cofactor. TPP binds in the cleft formed by a PYR domain and a PP domain. The PYR domain, binds the aminopyrimidine ring of TPP, the PP domain binds the diphosphate residue. The PYR and PP domains have a common fold, but do not share strong sequence conservation. The PP domain is not included in this sub-family. Most TPP-dependent enzymes have the PYR and PP domains on the same subunit although these domains can be alternatively arranged in the primary structure. TPP-dependent enzymes are multisubunit proteins, the smallest catalytic unit being a dimer-of-active sites. Lactobacillus plantarum POX is a homotetramer (dimer-of-homodimers), having two active sites per homodimer lying between PYR and PP domains of different subunits. POX decarboxylates pyruvate, producing hydrogen peroxide and the energy-storage metabolite acetylphosphate.
Pssm-ID: 132922 [Multi-domain] Cd Length: 164 Bit Score: 41.77 E-value: 7.27e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063696695 67 ERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHF 138
Cdd:cd07039 47 EEAAAFAASAEAKLTGKLGVCLGSSGPGAIHLLNGLYDAKRDRAPVLAIAGQVPTDELGTDYFQEVDLLALF 118
|
|
| PRK03204 |
PRK03204 |
haloalkane dehalogenase; Provisional |
1077-1347 |
1.15e-03 |
|
haloalkane dehalogenase; Provisional
Pssm-ID: 179554 [Multi-domain] Cd Length: 286 Bit Score: 42.54 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1077 RVHDVGENAeGSVALFLHGFLGTGEEWIPIMTGISGSARCISVDIPGHGrsrvqshASETQTSPTFSMEMIAEALYKLIE 1156
Cdd:PRK03204 25 RIHYIDEGT-GPPILLCHGNPTWSFLYRDIIVALRDRFRCVAPDYLGFG-------LSERPSGFGYQIDEHARVIGEFVD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1157 QITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSGSPGLKDPVARKIRSATDDSKA--RMMVDNGLYI--FIENWYN 1232
Cdd:PRK03204 97 HLGLDRYLSMGQDWGGPISMAVAVERADRVRGVVLGNTWFWPADTLAMKAFSRVMSSPPvqYAILRRNFFVerLIPAGTE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1233 GGLWKSLRNH-----PHFSKIAASRLLHGDVPSVAKLLSDLSS------GRQPSLweeledcdtnisLVFGEKDVKY--K 1299
Cdd:PRK03204 177 HRPSSAVMAHyravqPNAAARRGVAEMPKQILAARPLLARLARevpatlGTKPTL------------LVWGMKDVAFrpK 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1063696695 1300 QIATRMYREMSKskksvnniIEIVEIPEAGHAVHLESPLRVILAL-RKF 1347
Cdd:PRK03204 245 TILPRLRATFPD--------HVLVELPNAKHFIQEDAPDRIAAAIiERF 285
|
|
| PRK07710 |
PRK07710 |
acetolactate synthase large subunit; |
71-252 |
1.93e-03 |
|
acetolactate synthase large subunit;
Pssm-ID: 236076 [Multi-domain] Cd Length: 571 Bit Score: 42.44 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 71 AFHAI-GYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAINQINHFGSFVRFFFNLP 149
Cdd:PRK07710 65 AIHAAeGYARISGKPGVVIATSGPGATNVVTGLADAMIDSLPLVVFTGQVATSVIGSDAFQEADIMGITMPVTKHNYQVR 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 150 PPTDLIPVrmvlttVDSALHWATGSACGPVHLNCPfRDpLDGSPTNWSSNCLNGLDMWMSNAEPftKYFqvqshksdgvt 229
Cdd:PRK07710 145 KASDLPRI------IKEAFHIATTGRPGPVLIDIP-KD-MVVEEGEFCYDVQMDLPGYQPNYEP--NLL----------- 203
|
170 180
....*....|....*....|...
gi 1063696695 230 tgQITEILQVIKEAKKGLLLIGA 252
Cdd:PRK07710 204 --QIRKLVQAVSVAKKPVILAGA 224
|
|
| MR_like_4 |
cd03329 |
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this ... |
806-911 |
2.01e-03 |
|
Mandelate racemase (MR)-like subfamily of the enolase superfamily, subgroup 4. Enzymes of this subgroup share three conserved carboxylate ligands for the essential divalent metal ion (usually Mg2+), two aspartates and a glutamate, and conserved catalytic residues, a Lys-X-Lys motif and a conserved histidine-aspartate dyad. This subgroup's function is unknown.
Pssm-ID: 239445 [Multi-domain] Cd Length: 368 Bit Score: 42.00 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 806 TPLEVAYVARKLVQEGFSAIKLKVGRRVSSVQDALVMQEVRRAVGVQIELRADANCRWTFEEAREFGLLVNSCNLKYIEE 885
Cdd:cd03329 143 SPEAYADFAEECKALGYRAIKLHPWGPGVVRRDLKACLAVREAVGPDMRLMHDGAHWYSRADALRLGRALEELGFFWYED 222
|
90 100
....*....|....*....|....*...
gi 1063696695 886 PVQNKD--DLIRFHEETGLPVALDETLD 911
Cdd:cd03329 223 PLREASisSYRWLAEKLDIPILGTEHSR 250
|
|
| TPP_BZL_OCoD_HPCL |
cd02004 |
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of ... |
478-589 |
2.03e-03 |
|
Thiamine pyrophosphate (TPP) family, BZL_OCoD_HPCL subfamily, TPP-binding module; composed of proteins similar to benzaldehyde lyase (BZL), oxalyl-CoA decarboxylase (OCoD) and 2-hydroxyphytanoyl-CoA lyase (2-HPCL). Pseudomonas fluorescens biovar I BZL cleaves the acyloin linkage of benzoin producing 2 molecules of benzaldehyde and enabling the Pseudomonas to grow on benzoin as the sole carbon and energy source. OCoD has a role in the detoxification of oxalate, catalyzing the decarboxylation of oxalyl-CoA to formate. 2-HPCL is a peroxisomal enzyme which plays a role in the alpha-oxidation of 3-methyl-branched fatty acids, catalyzing the cleavage of 2-hydroxy-3-methylacyl-CoA into formyl-CoA and a 2-methyl-branched fatty aldehyde. All these enzymes depend on Mg2+ and TPP for activity.
Pssm-ID: 238962 [Multi-domain] Cd Length: 172 Bit Score: 40.59 E-value: 2.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 478 SGIDGLLSSATGFAVGCK-----KRVVCVVGDISFLH-----DTnglailkqrIARK--PMTILVINNRG-GGIFRLLPI 544
Cdd:cd02004 44 AGTFGTLGVGLGYAIAAAlarpdKRVVLVEGDGAFGFsgmelET---------AVRYnlPIVVVVGNNGGwYQGLDGQQL 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1063696695 545 AKKTEPSVLNQYFYTAHDisieNLCLAHGVRYVHVGTKSELEDAL 589
Cdd:cd02004 115 SYGLGLPVTTLLPDTRYD----LVAEAFGGKGELVTTPEELKPAL 155
|
|
| DLH |
COG0412 |
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism]; |
1156-1219 |
2.10e-03 |
|
Dienelactone hydrolase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440181 [Multi-domain] Cd Length: 226 Bit Score: 41.11 E-value: 2.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063696695 1156 EQITPGKVTIVGYSMGARIALYMALRFSnKIEGAVVVSGSPGLKDPVARkirsaTDDSKARMMV 1219
Cdd:COG0412 104 PEVDAGRVGVVGFCFGGGLALLAAARGP-DLAAAVSFYGGLPADDLLDL-----AARIKAPVLL 161
|
|
| PRK08978 |
PRK08978 |
acetolactate synthase 2 catalytic subunit; Reviewed |
62-132 |
2.15e-03 |
|
acetolactate synthase 2 catalytic subunit; Reviewed
Pssm-ID: 181601 [Multi-domain] Cd Length: 548 Bit Score: 42.17 E-value: 2.15e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063696695 62 LACFDERSLAFHAIGYAKGSLKPAVIITSSGTAVSNLLPAVVEASEDFLPLLLLTADRPPELQGVGANQAI 132
Cdd:PRK08978 42 LLCRHEQGAAMAAIGYARATGKVGVCIATSGPGATNLITGLADALLDSVPVVAITGQVSSPLIGTDAFQEI 112
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1117-1212 |
2.15e-03 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 41.38 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1117 ISVDIPGHGRSRVQSHASetqtsptfSMEMIAEALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKieG-----AVV 1191
Cdd:COG3208 36 LAVQLPGRGDRLGEPPLT--------SLEELADDLAEELAPLLDRPFALFGHSMGALLAFELARRLERR--GrplpaHLF 105
|
90 100
....*....|....*....|...
gi 1063696695 1192 VSGS--PGLKDPvARKIRSATDD 1212
Cdd:COG3208 106 VSGRraPHLPRR-RRPLHDLSDA 127
|
|
| COG4099 |
COG4099 |
Predicted peptidase [General function prediction only]; |
1141-1194 |
4.37e-03 |
|
Predicted peptidase [General function prediction only];
Pssm-ID: 443275 [Multi-domain] Cd Length: 235 Bit Score: 40.34 E-value: 4.37e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1141 TFSMEMIAEALYKLIEQIT------PGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSG 1194
Cdd:COG4099 99 YWSDTKALDAVLALLDDLIaeyridPDRIYLTGLSMGGYGTWDLAARYPDLFAAAVPICG 158
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1129-1196 |
5.73e-03 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 40.06 E-value: 5.73e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1063696695 1129 VQSHASETQTSPTFSMEMIAEALYKLIEQITP-GKVTIVGYSMGARIALYMALRFSNKIEG--AVVVSGSP 1196
Cdd:pfam00975 32 VQYPGRGRGEPPLNSIEALADEYAEALRQIQPeGPYALFGHSMGGMLAFEVARRLERQGEAvrSLFLSDAS 102
|
|
| PRK10673 |
PRK10673 |
esterase; |
1117-1196 |
8.84e-03 |
|
esterase;
Pssm-ID: 182637 [Multi-domain] Cd Length: 255 Bit Score: 39.71 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063696695 1117 ISVDIPGHGRSrvqshasetQTSPTFSMEMIAEALYKLIEQITPGKVTIVGYSMGARIALYMALRFSNKIEGAVVVSGSP 1196
Cdd:PRK10673 46 IQVDMRNHGLS---------PRDPVMNYPAMAQDLLDTLDALQIEKATFIGHSMGGKAVMALTALAPDRIDKLVAIDIAP 116
|
|
| |
