|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
1-1374 |
0e+00 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 2539.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1 MSGVVGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAAVVVvLSHPDQIQDVIFGD 80
Cdd:PLN02858 3 SAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVV-LSHPDQVDDVFFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 81 EGVMKGLQKDAVLLLSSTISTLQLQKLEKQLTEKREQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQ 160
Cdd:PLN02858 82 EGAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 161 NLYTFEGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDD-IEGRFLD 239
Cdd:PLN02858 162 KLYTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDyIEGRFLN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 240 VLSQNLAIVEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAKISEKVLGVGILEAANRELYKPEDLAKEITTQA 319
Cdd:PLN02858 242 VLVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNILEAANRELYKPEDLAKQITMQA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 320 KPVNRIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGH 399
Cdd:PLN02858 322 KPVKRIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGD 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 400 LGAVEAIPSGATVVLASTVSPAFVSQLERRLENEGKDLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSE 479
Cdd:PLN02858 402 LGAVSALPAGASIVLSSTVSPGFVIQLERRLENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 480 KLYVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALD 559
Cdd:PLN02858 482 KLYVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALD 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 560 IFVKDLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIKVEGRLPVLKKQDLLKSLPAEWPS 639
Cdd:PLN02858 562 IFVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKVEGRLPVLKKEDVLTSLPAEWPE 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 640 DPTTDI-HRLNMGNSKTLVVLDDDPTGTQTVHDVEVLTEWSVESISEQFRKKPACFFILTNSRSLSPEKASELIKDICSN 718
Cdd:PLN02858 642 DPIDDIcHRLNMGNSKTLVVLDDDPTGTQTVHDVEVLTEWSVESISEQFRKKPACFFILTNSRSLSPEKASELIKDICRN 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 719 LCAASKEVGNADYTIVLRGDSTLRGHFPQEADAAVSILGEMDAWIICPFFLQGGRYTIDDVHYVADSDRLVPAGETEFAK 798
Cdd:PLN02858 722 LCAAAKSVGNVDYTIVLRGDSTLRGHFPEEADAAVSVLGEMDAWIICPFFLQGGRYTINDIHYVADSDRLVPAGETEFAK 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 799 DASFGYKSSNLREWVEEKTAGVIPANSVQSISIQLLRKGGPDAVCEFLCSLKKGSTCIVNAASERDMAVFAAGMIQAELK 878
Cdd:PLN02858 802 DASFGYKSSNLREWVEEKTKGRISANSVQSISIQLLRKGGPDAVCEHLCSLKKGSTCIVNAASERDMAVFAAGMIQAELK 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 879 GRSFLCRTAASFVSALIGIIPKDPVLPKDFESNKESSGALIVVGSYVPKTTKQVEELQSQHNQNLRSIEISVEKVALKSS 958
Cdd:PLN02858 882 GKRFLCRTAASFVSARIGIIPKPPVLPKDLESNKESSGGLIVVGSYVPKTTKQVEELKSQCGQSLRSIEVSVEKVAMKSS 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 959 EVRDEEIRRAVEMADAFLRAGRETLIMSSRELITGKTSSESLDINSKVSSALVEVVSQISTRPRYILAKGGITSSDTATK 1038
Cdd:PLN02858 962 EVRDEEISRAVEMADAFLRAGKDTLIMTSRELITGKTPSESLDINSKVSSALVEIVRRISTRPRYILAKGGITSSDLATK 1041
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1039 ALKARRALVIGQALAGVPVWKLGPESRHPGVPYIVFPGNVGNSTALAEVVKSWSVVAGRSTKELLLNAEKGGYAVGAFNV 1118
Cdd:PLN02858 1042 ALEARRAKVVGQALAGVPLWKLGPESRHPGVPYIVFPGNVGDSTALAEVVKSWARPARSSTKELLLNAEKGGYAVGAFNV 1121
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1119 YNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQARVPISVHFDHGTTKHELLEALELGLDSVMVDGS 1198
Cdd:PLN02858 1122 YNLEGIEAVVAAAEAEKSPAILQVHPGALKQGGIPLVSCCIAAAEQASVPITVHFDHGTSKHELLEALELGFDSVMVDGS 1201
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1199 HLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM-ETGIDALAVCIGNVHGKYPKS 1277
Cdd:PLN02858 1202 HLSFTENISYTKSISSLAHSKGLMVEAELGRLSGTEDGLTVEEYEAKLTDVDQAKEFIdETGIDALAVCIGNVHGKYPAS 1281
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1278 GPNLKLDLLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYMEALSSGKKTDIVDVMSATKAAM 1357
Cdd:PLN02858 1282 GPNLRLDLLKELRALSSKKGVLLVLHGASGLPESLIKECIENGVRKFNVNTEVRTAYMEALSSPKKTDLIDVMSAAKEAM 1361
|
1370
....*....|....*..
gi 186478598 1358 KAVIADKIRLFGSAGKA 1374
Cdd:PLN02858 1362 KAVVAEKLRLFGSAGKA 1378
|
|
| F_bP_aldolase |
pfam01116 |
Fructose-bisphosphate aldolase class-II; |
1098-1373 |
2.40e-96 |
|
Fructose-bisphosphate aldolase class-II;
Pssm-ID: 460071 Cd Length: 276 Bit Score: 310.50 E-value: 2.40e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQ---GGIPLVSCCISAAEQARVPISVHFD 1174
Cdd:pfam01116 2 NLKELLKKAKEGGYAVPAFNVNNLETVQAILEAAEEAKSPVILQVSPGAAAKyagGAEALAALVRAAAEAAGVPVALHLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1175 HGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQAQE 1254
Cdd:pfam01116 82 HGASFELIKEAIEAGFTSVMIDGSHLPFEENIAITKEVVEYAHARGVSVEAELGRIGGEEDGVVVD--EKLYTDPEEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1255 FME-TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTA 1333
Cdd:pfam01116 160 FVEaTGVDALAVAIGNVHGVY-KPGPKLDFDRLKEIQEAV---PVPLVLHGGSGVPDEDIRKAIKLGVCKINIDTDLQLA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 186478598 1334 YMEALSS-GKKTDIVDVMSATKAAMKAVIADKIRLFGSAGK 1373
Cdd:pfam01116 236 FTAAVREyPPNKDPRKYLRPAEEAMKEVVKEKIRLFGSAGK 276
|
|
| OtnK |
COG3395 |
D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family ... |
656-1089 |
1.37e-95 |
|
D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family [Carbohydrate transport and metabolism];
Pssm-ID: 442622 [Multi-domain] Cd Length: 415 Bit Score: 313.67 E-value: 1.37e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 656 LVVLDDDPTGTQTVHDVEVLTEWSVESI----SEQFRKKPACFFILTNSRSLSPEKASELIKDICSNLCAASKEVgnady 731
Cdd:COG3395 2 LGVIADDFTGATDVAVQLARAGLRTVLLlgvpTLALADDADAVVIATKSRSLPPEEAVARVREALAWLKAAGARL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 732 tIVLRGDSTLRGHFPQEADAAVSILGEmDAWIICPFFLQGGRYTIDDVHYVADsdrlVPAGETEFAKDASFGYKSSNLRE 811
Cdd:COG3395 77 -VYKKFDSTLRGNIGAETDALLDALGA-DAAVVVPAFPENGRTTVGGHLFVGG----VPLHETEMARDPVTPMTESDLPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 812 WVEEKTAGvipanSVQSISIQLLRKgGPDAVCEFLCSLKKGST--CIVNAASERDMAVFAAGMIQAElkgRSFLCRTAAS 889
Cdd:COG3395 151 LLAEQTKG-----PVGLVDLADVRA-GAEALRAALAALAAEGAriVVVDAVTDADLDAIAEALADLA---ERVLVVGSSG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 890 FVSALIGIIPKDPvlpkdfesnKESSGALIVVGSYVPKTTKQVEELQSQHnqNLRSIEISVEKVAlksSEVRDEEIRRAV 969
Cdd:COG3395 222 LAAALAAAPAALP---------PAGGPVLVVVGSCSPVTRRQLAALLAEP--GVPVVELDVERLL---DGEAEAEVERAL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 970 EMADAFLRAGRETLIMSSRELITGKTSSESLD---INSKVSSALVEVVSQI--STRPRYILAKGGITSSDtATKALKARR 1044
Cdd:COG3395 288 AWALAALAAGRTVLIYTSRDPEDVADAQERLGrlaAGERIEAALAEIARRLleEAGVRRLIVAGGDTSGA-VLKALGIRG 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 186478598 1045 ALVIGQALAGVPVWKLgPESRHPGVPYIVFPGNVGNSTALAEVVK 1089
Cdd:COG3395 367 LRILGEIAPGVPLGRA-IGGDFDGLPVVLKGGNFGDEDFFARALE 410
|
|
| Fba |
COG0191 |
Fructose/tagatose bisphosphate aldolase [Carbohydrate transport and metabolism]; Fructose ... |
1098-1374 |
1.01e-92 |
|
Fructose/tagatose bisphosphate aldolase [Carbohydrate transport and metabolism]; Fructose/tagatose bisphosphate aldolase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 439961 Cd Length: 283 Bit Score: 300.47 E-value: 1.01e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAAEQARVPISVHFDHG 1176
Cdd:COG0191 4 SLKELLDKAKEGGYAVPAFNVNNLETLQAILEAAEELNSPVILQVSEGAAKyAGLEYLAAMVRAAAEEASVPVALHLDHG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1177 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1256
Cdd:COG0191 84 ASFELIKRAIDAGFTSVMIDGSHLPFEENIAITKEVVEYAHAAGVSVEAELGVVGGEEDGVDVDDAEALYTDPEEAAEFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1257 E-TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1335
Cdd:COG0191 164 EeTGVDALAVAIGTVHGVY-KGEPKLDFDRLKEIREAV---PVPLVLHGGSGVPDEEIREAIKLGVAKINIDTDLRLAFT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 186478598 1336 EAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:COG0191 240 AAVreylaENPDKYDPRKYLKPAREAMKEVVKEKIRLFGSAGKA 283
|
|
| TBP_aldolase_IIB |
cd00947 |
Tagatose-1,6-bisphosphate (TBP) aldolase and related Type B Class II aldolases. TBP aldolase ... |
1099-1372 |
2.35e-92 |
|
Tagatose-1,6-bisphosphate (TBP) aldolase and related Type B Class II aldolases. TBP aldolase is a tetrameric class II aldolase that catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phsophate to produce tagatose 1,6-bisphosphate. There is an absolute requirement for a divalent metal ion, usually zinc, and in addition the enzymes are activated by monovalent cations such as Na+. The type A and type B Class II FBPA's differ in the presence and absence of distinct indels in the sequence that result in differing loop lengths in the structures.
Pssm-ID: 238477 Cd Length: 276 Bit Score: 299.44 E-value: 2.35e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1099 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGI-PLVSCCISAAEQARVPISVHFDHGT 1177
Cdd:cd00947 1 TKELLKKAREGGYAVGAFNINNLETLKAILEAAEETRSPVILQISEGAIKYAGLeLLVAMVKAAAERASVPVALHLDHGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1178 TKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQAQEFME 1257
Cdd:cd00947 81 SFELIKRAIRAGFSSVMIDGSHLPFEENVAKTKEVVELAHAYGVSVEAELGRIGGEEDGVVGD--EGLLTDPEEAEEFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1258 -TGIDALAVCIGNVHGKYPKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1336
Cdd:cd00947 159 eTGVDALAVAIGTSHGAYKGGEPKLDFDRLKEIAERV---NVPLVLHGGSGIPDEQIRKAIKLGVCKININTDLRLAFTA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 186478598 1337 AL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAG 1372
Cdd:cd00947 236 ALreylaENPKEFDPRKYLAPAIEAVKEVVKHKMELFGSAG 276
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
324-609 |
2.86e-88 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 288.17 E-value: 2.86e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAV 403
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 404 EAIPSGATVVLASTVSPAFVSQLERRLENEGkdLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLYV 483
Cdd:COG2084 83 AALRPGAVVVDMSTISPETARELAAAAAARG--VRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 484 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDIFVK 563
Cdd:COG2084 161 V-GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 186478598 564 DLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVY 609
Cdd:COG2084 240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| gatY |
PRK09195 |
tagatose-bisphosphate aldolase; Reviewed |
1098-1374 |
2.48e-75 |
|
tagatose-bisphosphate aldolase; Reviewed
Pssm-ID: 181690 Cd Length: 284 Bit Score: 251.58 E-value: 2.48e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1176
Cdd:PRK09195 5 STKQMLNNAQRGGYAVPAFNIHNLETMQVVVETAAELHSPVIIAGTPGTFSYAGTEyLLAIVSAAAKQYHHPLALHLDHH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1177 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1256
Cdd:PRK09195 85 EKFDDIAQKVRSGVRSVMIDGSHLPFAQNISLVKEVVDFCHRFDVSVEAELGRLGGQEDDLQVDEADALYTDPAQAREFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1257 E-TGIDALAVCIGNVHGKYpKSGPNLKLDllkELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1335
Cdd:PRK09195 165 EaTGIDSLAVAIGTAHGMY-KGEPKLDFD---RLENIRQWVNIPLVLHGASGLPTKDIQQTIKLGICKVNVATELKIAFS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 186478598 1336 EAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK09195 241 QALknyltEHPEANDPRHYLQPAKSAMKDVVSKVIADCGCEGKA 284
|
|
| gatY |
PRK12737 |
tagatose-bisphosphate aldolase subunit GatY; |
1098-1374 |
2.95e-74 |
|
tagatose-bisphosphate aldolase subunit GatY;
Pssm-ID: 183710 Cd Length: 284 Bit Score: 248.84 E-value: 2.95e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1176
Cdd:PRK12737 5 STKNMLKKAQAEGYAVPAFNIHNLETLQVVVETAAELRSPVILAGTPGTFSYAGTDyIVAIAEVAARKYNIPLALHLDHH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1177 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1256
Cdd:PRK12737 85 EDLDDIKKKVRAGIRSVMIDGSHLSFEENIAIVKEVVEFCHRYDASVEAELGRLGGQEDDLVVDEKDAMYTNPDAAAEFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1257 E-TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1335
Cdd:PRK12737 165 ErTGIDSLAVAIGTAHGLY-KGEPKLDFERLAEIREKVS---IPLVLHGASGVPDEDVKKAISLGICKVNVATELKIAFS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 186478598 1336 EALSS-----GKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK12737 241 DAVKKyfyenPKANDPRKYMTPGKAAMKEVVREKIKVCGSEGKL 284
|
|
| PRK12857 |
PRK12857 |
class II fructose-1,6-bisphosphate aldolase; |
1098-1374 |
1.10e-71 |
|
class II fructose-1,6-bisphosphate aldolase;
Pssm-ID: 237235 Cd Length: 284 Bit Score: 241.17 E-value: 1.10e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCI-SAAEQARVPISVHFDHG 1176
Cdd:PRK12857 5 TVAELLKKAEKGGYAVGAFNCNNMEIVQAIVAAAEAEKSPVIIQASQGAIKYAGIEYISAMVrTAAEKASVPVALHLDHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1177 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1256
Cdd:PRK12857 85 TDFEQVMKCIRNGFTSVMIDGSKLPLEENIALTKKVVEIAHAVGVSVEAELGKIGGTEDDITVDEREAAMTDPEEARRFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1257 -ETGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1335
Cdd:PRK12857 165 eETGVDALAIAIGTAHGPY-KGEPKLDFDRLAKIKELV---NIPIVLHGSSGVPDEAIRKAISLGVRKVNIDTNIREAFV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 186478598 1336 EALSS--GKKTDIVD---VMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK12857 241 ARLREvlEKNPDEIDprkILGPAREAAKEVIREKIRLFGSAGKA 284
|
|
| SBD_N |
pfam07005 |
Sugar-binding N-terminal domain; This is the N-terminal domain found in proteins in a range of ... |
656-894 |
1.12e-68 |
|
Sugar-binding N-terminal domain; This is the N-terminal domain found in proteins in a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. Structural analysis of the whole protein indicates the N- and C-termini act together to produce a surface into which a threonate-ADP complex is bound, demonstrating that a sugar binding site is on the N-terminal domain, and a nucleotide binding site is in the C-terminal domain. There is a critical motif, DDXTG, at approximately residues 22-25. Proteins containing this domain have been predicted as kinases. Some members are associated with PdxA2 by physical clustering and gene fusion with PdxA2. Some members that are fused with PdxA2 have been shown to be involved in L-4-hydroxythreonine (4HT) phosphorylation, part of the alternative pathway to make PLP (pyridoxal 5'-phosphate) out of a toxic metabolite, 4HT. However, 4HT phosphorylation might not be the main function of this group of proteins. Moreover, some members that are not associated with pdxA2, and even one that is associated with pdxA2, have lost 4HT kinase activity. Functional analysis demonstrate that family members include D-Threonate kinases (DtnK), D-Erythronate kinases (DenK) and 3-Oxo-tetronate kinases (OtnK).
Pssm-ID: 462065 Cd Length: 229 Bit Score: 230.50 E-value: 1.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 656 LVVLDDDPTGTQTV------HDVEVLTewSVESISEQFRKKPACFFILTNSRSLSPEKASELIKDICSNLCAASKEVgna 729
Cdd:pfam07005 1 LGVIADDFTGAQDVgvqlakHGLRTLV--FLGVPDAARLPDADAVVIATNSRSLPPEEAVARVREALKWLAALGARL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 730 DYTIVLRGDSTLRGHFPQEADAAVSILGEMDAWIICPFFLQGGRYTIDDVHYVadsdRLVPAGETEFAKDASFGYKSSNL 809
Cdd:pfam07005 76 YYKVCSRFDSTLRGNIGAETDALLDALGAFDAAVVAPAFPEGGRTTIGGVLFV----NGVPLAETEFARDPVTPMTESDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 810 REWVEEKTAGvipanSVQSISIQLLRKgGPDAVCEFLCSLKKGST--CIVNAASERDMAVFAAGMIQAelkGRSFLCRTA 887
Cdd:pfam07005 152 RRLLAEQTKL-----PVGLIDLDTLAD-GPEALREALAALLAQGVrvVVVDAVTDEDLAVIAEALLAL---GKRFLLVGS 222
|
....*..
gi 186478598 888 ASFVSAL 894
Cdd:pfam07005 223 AGLAAAL 229
|
|
| fruc_bis_ald_ |
TIGR01859 |
fructose-1,6-bisphosphate aldolase, class II, various bacterial and amitochondriate protist; ... |
1098-1374 |
2.32e-68 |
|
fructose-1,6-bisphosphate aldolase, class II, various bacterial and amitochondriate protist; This model represents of one of several subtypes of the class II fructose-1,6-bisphosphate aldolase, an enzyme of glycolysis. The subtypes are split into several models to allow separation of a family of tagatose bisphosphate aldolases. This form is found in Gram-positive bacteria, a variety of Gram-negative, and in amitochondriate protists. The class II enzymes share homology with tagatose bisphosphate aldolase but not with class I aldolase. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 130918 Cd Length: 282 Bit Score: 231.87 E-value: 2.32e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGG-----IPLVsccISAAEQAR-VPISV 1171
Cdd:TIGR01859 3 NGKEILQKAKKEGYAVGAFNFNNLEWTQAILEAAEEENSPVIIQVSEGAIKYMGgykmaVAMV---KTLIERMSiVPVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1172 HFDHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQ 1251
Cdd:TIGR01859 80 HLDHGSSYESCIKAIKAGFSSVMIDGSHLPFEENLALTKKVVEIAHAKGVSVEAELGTLGGIEDGVDEK--EAELADPDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1252 AQEFM-ETGIDALAVCIGNVHGKYPKSgPNLKLDLLKELHALSSKKgvfLVLHGASGLSENLIKECIENGVRKFNVNTEV 1330
Cdd:TIGR01859 158 AEQFVkETGVDYLAAAIGTSHGKYKGE-PGLDFERLKEIKELTNIP---LVLHGASGIPEEQIKKAIKLGIAKINIDTDC 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 186478598 1331 RTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:TIGR01859 234 RIAFTAAIrkvltEKKDEYDPRKILGPAREAIKETVKEKMRLFGSAGKA 282
|
|
| cbbA |
TIGR00167 |
ketose-bisphosphate aldolase; This model is under revision. Proteins found by this model ... |
1094-1374 |
2.34e-68 |
|
ketose-bisphosphate aldolase; This model is under revision. Proteins found by this model include fructose-bisphosphate and tagatose-bisphosphate aldolase. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 272938 Cd Length: 288 Bit Score: 231.82 E-value: 2.34e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1094 VAGRSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISA---AEQARVPI 1169
Cdd:TIGR00167 1 MMLVDVKELLQDAKEEGYAIPAFNINNLETINAVLEAAAEEKSPVIIQFSNGAAKyIAGLGAISAMVKAmseAYPYGVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1170 SVHFDHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNV 1249
Cdd:TIGR00167 81 ALHLDHGASEEDCAQAVKAGFSSVMIDGSHEPFEENIELTKKVVERAHKMGVSVEAELGTLGGEEDGVSVADESALYTDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1250 NQAQEFME-TGIDALAVCIGNVHGKYpKSGPN-LKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVN 1327
Cdd:TIGR00167 161 EEAKEFVKlTGVDSLAAAIGNVHGVY-KGEPKgLDFERLEEIQKYVN---LPLVLHGGSGIPDEEIKKAISLGVVKVNID 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 186478598 1328 TEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:TIGR00167 237 TELQIAFAAAVrnyyaENKDYYDPRVWLRPGEKAMKEVVLEKIKLFGSANKA 288
|
|
| PRK06806 |
PRK06806 |
class II aldolase; |
1100-1374 |
7.84e-64 |
|
class II aldolase;
Pssm-ID: 180705 Cd Length: 281 Bit Score: 218.86 E-value: 7.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1100 KELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVS-CCISAAEQARVPISVHFDHGTT 1178
Cdd:PRK06806 7 KELLKKANQENYGVGAFSVANMEMVMGAIKAAEELNSPIILQIAEVRLNHSPLHLIGpLMVAAAKQAKVPVAVHFDHGMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1179 KHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLtvEDYEAKLTNVNQAQEFM-E 1257
Cdd:PRK06806 87 FEKIKEALEIGFTSVMFDGSHLPLEENIQKTKEIVELAKQYGATVEAEIGRVGGSEDGS--EDIEMLLTSTTEAKRFAeE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1258 TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHalsSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNT----EVRTA 1333
Cdd:PRK06806 165 TDVDALAVAIGNAHGMY-NGDPNLRFDRLQEIN---DVVHIPLVLHGGSGISPEDFKKCIQHGIRKINVATatfnSVITA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 186478598 1334 YMEALSSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK06806 241 VNNLVLNTPYSDYFTYHQDVIKAAYENVKKHMQIFGSENKA 281
|
|
| PRK08185 |
PRK08185 |
hypothetical protein; Provisional |
1100-1374 |
2.42e-57 |
|
hypothetical protein; Provisional
Pssm-ID: 181275 Cd Length: 283 Bit Score: 199.95 E-value: 2.42e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1100 KELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQARVPISVHFDHGTTK 1179
Cdd:PRK08185 2 KELLKVAKEHQFAVGAFNVADSCFLRAVVEEAEANNAPAIIAIHPNELDFLGDNFFAYVRERAKRSPVPFVIHLDHGATI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1180 HELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTedGLTVEDYEAKL--TNVNQAQEFME 1257
Cdd:PRK08185 82 EDVMRAIRCGFTSVMIDGSLLPYEENVALTKEVVELAHKVGVSVEGELGTIGNT--GTSIEGGVSEIiyTDPEQAEDFVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1258 -TGIDALAVCIGNVHGKYPKSG-PNLKLDLLKELHAlssKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1335
Cdd:PRK08185 160 rTGVDTLAVAIGTAHGIYPKDKkPELQMDLLKEINE---RVDIPLVLHGGSANPDAEIAESVQLGVGKINISSDMKYAFF 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 186478598 1336 EALSS--GKKTDIVD---VM-SATKAAmKAVIADKIRLFGSAGKA 1374
Cdd:PRK08185 237 KKVREilSDNPSLYEpnqIYpSAIEAA-KEVVRHKMDLFNSTGKA 280
|
|
| PRK05835 |
PRK05835 |
class II fructose-1,6-bisphosphate aldolase; |
1097-1373 |
8.98e-52 |
|
class II fructose-1,6-bisphosphate aldolase;
Pssm-ID: 180280 [Multi-domain] Cd Length: 307 Bit Score: 184.79 E-value: 8.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1097 RSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCIS--AAEQARVPISVHFD 1174
Cdd:PRK05835 3 VKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASEGAIKYMGIDMAVGMVKimCERYPHIPVALHLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1175 HGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQE 1254
Cdd:PRK05835 83 HGTTFESCEKAVKAGFTSVMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGIEDNISVDEKDAVLVNPKEAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1255 FM-ETGIDALAVCIGNVHGKYP-KSGPNLKLDLLKELHALSSkkgVFLVLHGASGLSENL-------------------- 1312
Cdd:PRK05835 163 FVkESQVDYLAPAIGTSHGAFKfKGEPKLDFERLQEVKRLTN---IPLVLHGASAIPDDVrksyldaggdlkgskgvpfe 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186478598 1313 -IKECIENGVRKFNVNTEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGK 1373
Cdd:PRK05835 240 fLQESVKGGINKVNTDTDLRIAFIAEVrkvanEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANK 306
|
|
| kbaY |
PRK12738 |
tagatose-bisphosphate aldolase subunit KbaY; |
1098-1373 |
6.08e-51 |
|
tagatose-bisphosphate aldolase subunit KbaY;
Pssm-ID: 183711 Cd Length: 286 Bit Score: 181.77 E-value: 6.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1176
Cdd:PRK12738 5 STKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTPGTFKHIALEeIYALCSAYSTTYNMPLALHLDHH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1177 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1256
Cdd:PRK12738 85 ESLDDIRRKVHAGVRSAMIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELGRLGGVEDDMSVDAESAFLTDPQEAKRFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1257 E-TGIDALAVCIGNVHGKYPKSgPNLKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1335
Cdd:PRK12738 165 ElTGVDSLAVAIGTAHGLYSKT-PKIDFQRLAEIREVVD---VPLVLHGASDVPDEFVRRTIELGVTKVNVATELKIAFA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 186478598 1336 EAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGK 1373
Cdd:PRK12738 241 GAVkawfaENPQGNDPRYYMRVGMDAMKEVVRNKINVCGSANR 283
|
|
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
327-609 |
5.66e-50 |
|
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that catalyzes the NAD+-dependent oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde of the valine catabolism pathway. In Pseudomonas aeruginosa, 3-hydroxyisobutyrate dehydrogenase (mmsB) is co-induced with methylmalonate-semialdehyde dehydrogenase (mmsA) when grown on medium containing valine as the sole carbon source. The positive transcriptional regulator of this operon (mmsR) is located upstream of these genes and has been identified as a member of the XylS/AraC family of transcriptional regulators. 3-hydroxyisobutyrate dehydrogenase shares high sequence homology to the characterized 3-hydroxyisobutyrate dehydrogenase from rat liver with conservation of proposed NAD+ binding residues at the N-terminus (G-8,10,13,24 and D-31). This enzyme belongs to the 3-hydroxyacid dehydrogenase family, sharing a common evolutionary origin and enzymatic mechanism with 6-phosphogluconate. HIBADH exhibits sequence similarity to the NAD binding domain of 6-phosphogluconate dehydrogenase above trusted (pfam03446). [Energy metabolism, Amino acids and amines]
Pssm-ID: 130753 [Multi-domain] Cd Length: 288 Bit Score: 179.22 E-value: 5.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 327 FIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAVEAI 406
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 407 PSGATVVLASTVSPAFVSQLERRLENEGkdLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLyVIKG 486
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHG--AVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNI-VHCG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 487 GCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFE--NRVPHMLD-----NDYTPYSALD 559
Cdd:TIGR01692 158 DHGAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPqapasNGYQGGFGTA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 186478598 560 IFVKDLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVY 609
Cdd:TIGR01692 238 LMLKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
|
|
| PRK08610 |
PRK08610 |
fructose-bisphosphate aldolase; Reviewed |
1098-1374 |
4.89e-49 |
|
fructose-bisphosphate aldolase; Reviewed
Pssm-ID: 181501 Cd Length: 286 Bit Score: 176.33 E-value: 4.89e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAA---EQARVPISVHF 1173
Cdd:PRK08610 5 SMKEMLIDAKENGYAVGQYNLNNLEFTQAILEASQEENAPVILGVSEGAARyMSGFYTVVKMVEGLmhdLNITIPVAIHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1174 DHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDyeAKLTNVNQAQ 1253
Cdd:PRK08610 85 DHGSSFEKCKEAIDAGFTSVMIDASHSPFEENVATTKKVVEYAHEKGVSVEAELGTVGGQEDDVVADG--IIYADPKECQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1254 EFME-TGIDALAVCIGNVHGKYpKSGPNLKldlLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRT 1332
Cdd:PRK08610 163 ELVEkTGIDALAPALGSVHGPY-KGEPKLG---FKEMEEIGLSTGLPLVLHGGTGIPTKDIQKAIPFGTAKINVNTENQI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 186478598 1333 AYMEALSS--GKKTDIVD---VMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK08610 239 ASAKAVRDvlNNDKEVYDprkYLGPAREAIKETVKGKIKEFGTSNRA 285
|
|
| PRK06801 |
PRK06801 |
ketose 1,6-bisphosphate aldolase; |
1098-1374 |
3.32e-46 |
|
ketose 1,6-bisphosphate aldolase;
Pssm-ID: 180701 Cd Length: 286 Bit Score: 168.01 E-value: 3.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1176
Cdd:PRK06801 5 SLANGLAHARKHGYALGAFNVLDSHFLRALFAAAKQERSPFIINIAEVHFKYISLEsLVEAVKFEAARHDIPVVLNLDHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1177 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDG-LTVEDYEAKLTNVNQAQEF 1255
Cdd:PRK06801 85 LHFEAVVRALRLGFSSVMFDGSTLEYEENVRQTREVVKMCHAVGVSVEAELGAVGGDEGGaLYGEADSAKFTDPQLARDF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1256 ME-TGIDALAVCIGNVHGKYpKSGPnlKLDlLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAY 1334
Cdd:PRK06801 165 VDrTGIDALAVAIGNAHGKY-KGEP--KLD-FARLAAIHQQTGLPLVLHGGSGISDADFRRAIELGIHKINFYTGMSQAA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 186478598 1335 MEALS------SGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK06801 241 LAAVEqrmthrHAIYDEFAELLLGIEEAISDTVAQQMRIFGSAGQA 286
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
324-617 |
2.62e-45 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 165.99 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAV 403
Cdd:PRK11559 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 404 EAIPSGATVVLASTVSPaFVSQlERRLENEGKDLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLyV 483
Cdd:PRK11559 84 EGAKPGTVVIDMSSIAP-LASR-EIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSV-V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 484 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDIFVK 563
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 186478598 564 DLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIKV 617
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEV 294
|
|
| PRK07709 |
PRK07709 |
fructose-bisphosphate aldolase; Provisional |
1098-1374 |
2.03e-44 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 169068 Cd Length: 285 Bit Score: 162.92 E-value: 2.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAAEQ---ARVPISVHF 1173
Cdd:PRK07709 5 SMKEMLNKALEGKYAVGQFNMNNLEWTQAILAAAEEEKSPVILGVSEGAARhMTGFKTVVAMVKALIEemnITVPVAIHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1174 DHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDyeAKLTNVNQAQ 1253
Cdd:PRK07709 85 DHGSSFEKCKEAIDAGFTSVMIDASHHPFEENVETTKKVVEYAHARNVSVEAELGTVGGQEDDVIAEG--VIYADPAECK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1254 EFME-TGIDALAVCIGNVHGKYpKSGPNLKldlLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRT 1332
Cdd:PRK07709 163 HLVEaTGIDCLAPALGSVHGPY-KGEPNLG---FAEMEQVRDFTGVPLVLHGGTGIPTADIEKAISLGTSKINVNTENQI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 186478598 1333 AYMEALSS--GKKTDIVD---VMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK07709 239 EFTKAVREvlNKDQEVYDprkFIGPGRDAIKATVIGKIREFGSNGKA 285
|
|
| gatY |
PRK07998 |
class II aldolase; |
1099-1370 |
3.95e-44 |
|
class II aldolase;
Pssm-ID: 181192 Cd Length: 283 Bit Score: 161.85 E-value: 3.95e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1099 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCIS-AAEQARVPISVHFDHGT 1177
Cdd:PRK07998 6 GRILLDRIQEKHVLAGAFNTTNLETTISILNAIERSGLPNFIQIAPTNAQLSGYDYIYEIVKrHADKMDVPVSLHLDHGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1178 TKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGlTVEDYEAKlTNVNQAQEFME 1257
Cdd:PRK07998 86 TFEDVKQAVRAGFTSVMIDGAALPFEENIAFTKEAVDFAKSYGVPVEAELGAILGKEDD-HVSEADCK-TEPEKVKDFVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1258 -TGIDALAVCIGNVHGKypKSGPNLKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1336
Cdd:PRK07998 164 rTGCDMLAVSIGNVHGL--EDIPRIDIPLLKRIAEVSP---VPLVIHGGSGIPPEILRSFVNYKVAKVNIASDLRKAFIT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 186478598 1337 ALssGK-------KTDIVDVMSATKAAMKAVIADKIRLFGS 1370
Cdd:PRK07998 239 TV--GKayvnnhnEANLARVMAKAKQAVEEDVYSKIKMMNS 277
|
|
| PRK07315 |
PRK07315 |
fructose-bisphosphate aldolase; Provisional |
1098-1374 |
5.00e-44 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 180926 Cd Length: 293 Bit Score: 161.98 E-value: 5.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAAEQA---RVPISVHF 1173
Cdd:PRK07315 5 SAEKFVQAARDNGYAVGGFNTNNLEWTQAILRAAEAKKAPVLIQTSMGAAKyMGGYKVCKNLIENLVESmgiTVPVAIHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1174 DHGTTKHELLEALELGLdSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTvedYEAKLTNVNQAQ 1253
Cdd:PRK07315 85 DHGHYEDALECIEVGYT-SIMFDGSHLPVEENLKLAKEVVEKAHAKGISVEAEVGTIGGEEDGII---GKGELAPIEDAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1254 EFMETGIDALAVCIGNVHGKYPKSGPNLKLDLLKELHAlsSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTA 1333
Cdd:PRK07315 161 AMVETGIDFLAAGIGNIHGPYPENWEGLDLDHLEKLTE--AVPGFPIVLHGGSGIPDDQIQEAIKLGVAKVNVNTECQIA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 186478598 1334 Y-------------MEALSSGKKT-DIVDVMSATKAAMKAVIADKIRLFGSAGKA 1374
Cdd:PRK07315 239 FanatrkfardyeaNEAEYDKKKLfDPRKFLAPGVKAIQASVEERIDVFGSANKA 293
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
5-287 |
5.51e-44 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 161.82 E-value: 5.51e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 5 VGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAAVVVvLSHPDQIQDVIFGDEGVM 84
Cdd:COG2084 4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITM-LPDDAAVEEVLLGEDGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 85 KGLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLyT 164
Cdd:COG2084 83 AALRPGAVVVDMSTISPETARELAAAAAAR--GVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRI-V 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 165 FEGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDDIEGRF-LDVLSQ 243
Cdd:COG2084 160 HVGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFaLDLMLK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 186478598 244 NLAIVEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAK 287
Cdd:COG2084 240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIK 283
|
|
| PRK09196 |
PRK09196 |
fructose-bisphosphate aldolase class II; |
1098-1374 |
3.90e-42 |
|
fructose-bisphosphate aldolase class II;
Pssm-ID: 181691 Cd Length: 347 Bit Score: 158.20 E-value: 3.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQA--RVPISVHFDH 1175
Cdd:PRK09196 5 SLRQLLDHAAEHGYGVPAFNVNNLEQVQAIMEAADETDSPVILQASAGARKYAGEPFLRHLILAAVEEypHIPVVMHQDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1176 GTTKHELLEALELGLDSVMVDGSHL-------SFTENLSYTKSITELARSKNIMVEAELGRL-------SGTEDGLTVE- 1240
Cdd:PRK09196 85 GNSPATCQRAIQLGFTSVMMDGSLKadgktpaSYEYNVDVTRKVVEMAHACGVSVEGELGCLgsletgmGGEEDGHGAEg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1241 --DYEAKLTNVNQAQEFME-TGIDALAVCIGNVHGKY----PKSGPNLKLDLLKELHAlsSKKGVFLVLHGASGLSENL- 1312
Cdd:PRK09196 165 klSHDQLLTDPEEAADFVKkTQVDALAIAIGTSHGAYkftrKPTGDVLAIDRIKEIHA--RLPNTHLVMHGSSSVPQELl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1313 --------------------IKECIENGVRKFNVNTEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRL 1367
Cdd:PRK09196 243 diineyggdmpetygvpveeIQEGIKHGVRKVNIDTDLRLAMTGAIrrflaENPSEFDPRKYLKPAMEAMKKICKARYEA 322
|
....*..
gi 186478598 1368 FGSAGKA 1374
Cdd:PRK09196 323 FGTAGQA 329
|
|
| PRK13399 |
PRK13399 |
fructose-bisphosphate aldolase class II; |
1098-1374 |
1.72e-37 |
|
fructose-bisphosphate aldolase class II;
Pssm-ID: 184029 Cd Length: 347 Bit Score: 144.92 E-value: 1.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1098 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQA--RVPISVHFDH 1175
Cdd:PRK13399 5 TLRQLLDHAAENGYGVPAFNVNNMEQILAIMEAAEATDSPVILQASRGARKYAGDAMLRHMVLAAAEMypDIPICLHQDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1176 GTTKHELLEALELGLDSVMVDGSHL-------SFTENLSYTKSITELARSKNIMVEAELGRL-------SGTEDGLTVE- 1240
Cdd:PRK13399 85 GNSPATCQSAIRSGFTSVMMDGSLLadgktpaSYDYNVDVTRRVTEMAHAVGVSVEGELGCLgsletgeAGEEDGVGAEg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1241 --DYEAKLTNVNQAQEFM-ETGIDALAVCIGNVHGKY----PKSGPNLKLDLLKELHAlsSKKGVFLVLHGASGLSENL- 1312
Cdd:PRK13399 165 klSHDQMLTDPDQAVDFVqRTGVDALAIAIGTSHGAYkftrKPDGDILAIDRIEEIHA--RLPNTHLVMHGSSSVPQELq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1313 --------------------IKECIENGVRKFNVNTEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRL 1367
Cdd:PRK13399 243 eiinayggkmketygvpveeIQRGIKHGVRKVNIDTDIRLAMTGAIrkvlaEHPSEFDPRKALKPAMKAMTALCKQRFEA 322
|
....*..
gi 186478598 1368 FGSAGKA 1374
Cdd:PRK13399 323 FGTAGQA 329
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
324-484 |
1.82e-37 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 138.37 E-value: 1.82e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGhLGAV 403
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 404 EAIPSGATVVLASTVSPAFVSQLERRLENegKDLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLYV 483
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKE--KGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTY 157
|
.
gi 186478598 484 I 484
Cdd:pfam03446 158 I 158
|
|
| PRK07084 |
PRK07084 |
class II fructose-1,6-bisphosphate aldolase; |
1099-1374 |
4.32e-37 |
|
class II fructose-1,6-bisphosphate aldolase;
Pssm-ID: 180829 Cd Length: 321 Bit Score: 142.94 E-value: 4.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1099 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVS-CCISAAEQAR-----VPISVH 1172
Cdd:PRK07084 12 TREMFAKAVKGGYAIPAYNFNNMEQLQAIIQACVETKSPVILQVSKGARKYANATLLRyMAQGAVEYAKelgcpIPIVLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1173 FDHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQA 1252
Cdd:PRK07084 92 LDHGDSFELCKDCIDSGFSSVMIDGSHLPYEENVALTKKVVEYAHQFDVTVEGELGVLAGVEDEVSAE--HHTYTQPEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1253 QEFME-TGIDALAVCIGNVHGKYP-KSG---PNLKLDLLKELhalsSKK--GVFLVLHGASGLSENLIKECIENG----- 1320
Cdd:PRK07084 170 EDFVKkTGVDSLAISIGTSHGAYKfKPGqcpPPLRFDILEEI----EKRipGFPIVLHGSSSVPQEYVKTINEYGgklkd 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 186478598 1321 ----------------VRKFNVNTEVRTAYMEALSS--GKKTDIVD---VMSATKAAMKAVIADKIR-LFGSAGKA 1374
Cdd:PRK07084 246 aigipeeqlrkaaksaVCKINIDSDGRLAMTAAIRKvfDEKPEEFDprkYLGPARDELKKLYKHKIInVLGSNGKA 321
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
325-616 |
5.12e-37 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 141.92 E-value: 5.12e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 325 IGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAVE 404
Cdd:PRK15461 4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 405 AIPSGATVVLASTVSPAFVSQLERRLENEGkdLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLyVI 484
Cdd:PRK15461 84 GLSRDALVIDMSTIHPLQTDKLIADMQAKG--FSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNEL-IN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 485 KGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGG------TSWmfENRVphmLDNDYTPYSAL 558
Cdd:PRK15461 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAgkghftTTW--PNKV---LKGDLSPAFMI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 186478598 559 DIFVKDLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIK 616
Cdd:PRK15461 236 DLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGLT 293
|
|
| FTBP_aldolase_II |
cd00453 |
Fructose/tagarose-bisphosphate aldolase class II. This family includes fructose-1, ... |
1099-1371 |
7.50e-37 |
|
Fructose/tagarose-bisphosphate aldolase class II. This family includes fructose-1,6-bisphosphate (FBP) and tagarose 1,6-bisphosphate (TBP) aldolases. FBP-aldolase is homodimeric and used in gluconeogenesis and glycolysis; the enzyme controls the condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to yield fructose-1,6-bisphosphate. TBP-aldolase is tetrameric and produces tagarose-1,6-bisphosphate. There is an absolute requirement for a divalent metal ion, usually zinc, and in addition the enzymes are activated by monovalent cations such as Na+. Although structurally similar, the class I aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 238255 Cd Length: 340 Bit Score: 142.64 E-value: 7.50e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1099 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHP-GAFKQGGIPLVSC----------------CISA 1161
Cdd:cd00453 1 VQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNgGASFIAGKGVKSDvpqgaailgaisgahhVHQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1162 AEQARVPISVHFDHGTTK-------------HELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELG 1228
Cdd:cd00453 81 AEHYGVPVILHTDHCAKKllpwidglldageKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1229 RLSGTEDGLTVE--DYEAKLTNVNQAQEFME-----TGIDALAVCIGNVHGKYPKSGPNLKLDLLKELHALSSKKG---- 1297
Cdd:cd00453 161 CTGGEEDGVDNShmDASALYTQPEDVDYAYTelskiSPRFTIAASFGNVHGVYKKGNVVLTPTILRDSQEYVSKKHnlph 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1298 --VFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYMEA---------------LSSGKKTDIVDV--------MSA 1352
Cdd:cd00453 241 nsLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGvlnyykaneaylqgqLGNPKGEDQPNKkyydprvwLRA 320
|
330
....*....|....*....
gi 186478598 1353 TKAAMKAVIADKIRLFGSA 1371
Cdd:cd00453 321 GQTSMIARLEKAFQELNAI 339
|
|
| NBD_C |
pfam17042 |
Nucleotide-binding C-terminal domain; This is the C-terminal domain found in proteins in a ... |
918-1084 |
1.63e-35 |
|
Nucleotide-binding C-terminal domain; This is the C-terminal domain found in proteins in a range of Proteobacteria as well as the Gram-positive Oceanobacillus iheyensis. Structural analysis of the whole protein indicates the N- and C-termini act together to produce a surface into which a threonate-ADP complex is bound, demonstrating that a sugar binding site is on the N-terminal domain, and a nucleotide binding site is in the C-terminal domain. There is a critical motif, DDXTG, at approximately residues 22-25. Proteins containing this domain have been predicted as kinases. Some members are associated with PdxA2 by physical clustering and gene fusion with PdxA2. Some members that are fused with PdxA2 have been shown to be involved in L-4-hydroxythreonine (4HT) phosphorylation, part of the alternative pathway to make PLP (pyridoxal 5'-phosphate) out of a toxic metabolite, 4HT. However, 4HT phosphorylation might not be the main function of this group of proteins. Moreover, some members that are not associated with pdxA2, and even one that is associated with pdxA2, have lost 4HT kinase activity. Functional analysis demonstrate that family members include D-Threonate kinases (DtnK), D-Erythronate kinases (DenK) and 3-Oxo-tetronate kinases (OtnK).
Pssm-ID: 465337 Cd Length: 166 Bit Score: 133.08 E-value: 1.63e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 918 LIVVGSYVPKTTKQVEELQSQHnqNLRSIEISVEKVAlkSSEVRDEEIRRAVEMADAFLRAGRETLIMSSRELITGKTsS 997
Cdd:pfam17042 1 LVVVGSCSPKTTAQLAALLAER--GVVVVELDVEALL--DEEAREEEIERALAEALAALASGKDVVVYTSRGPEDVAA-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 998 ESLDIN-------SKVSSALVEVVSQISTRP--RYILAkGGITSSDTAtKALKARRALVIGQALAGVPVWKLgpeSRHPG 1068
Cdd:pfam17042 76 DSLQAAlglsragARISAALAEIARGLLARGvrGLVVA-GGDTSGAVL-KALGIRGLRVLGEIAPGVPLGRL---IGAPG 150
|
170
....*....|....*.
gi 186478598 1069 VPYIVFPGNVGNSTAL 1084
Cdd:pfam17042 151 LPVVLKGGNFGDEDAL 166
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
489-609 |
6.10e-34 |
|
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.
Pssm-ID: 434252 [Multi-domain] Cd Length: 122 Bit Score: 126.87 E-value: 6.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 489 GAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPH-MLDNDYTPYSALDIFVKDLGI 567
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPQrVLSRDFDPGFALDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 186478598 568 VTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVY 609
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
324-617 |
2.03e-29 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 119.74 E-value: 2.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFSVcGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAV 403
Cdd:PRK15059 2 KLGFIGLGIMGTPMAINLARAGHQL-HVTTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 404 EAIPSGATVVLASTVSPAFVSQLERRLENEGKDLklVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLYV 483
Cdd:PRK15059 81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDY--LDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 484 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDIFVK 563
Cdd:PRK15059 159 V-GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 186478598 564 DLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIKV 617
Cdd:PRK15059 238 DLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKL 291
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
4-267 |
3.95e-27 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 113.03 E-value: 3.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 4 VVGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAAVVVvLSHPDQIQDVIFGDEGV 83
Cdd:PRK15461 3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITM-LPNGDLVRSVLFGENGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 84 MKGLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLY 163
Cdd:PRK15461 82 CEGLSRDALVIDMSTIHPLQTDKLIADMQAK--GFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 164 TfEGEIGAGSKVKMVNELLeGIHLVA-AVEAISLGSQAGVHPWILYDIIS-NAAG-----NSWIYKnhiplLLKDDIEGR 236
Cdd:PRK15461 160 N-AGGPGMGIRVKLINNYM-SIALNAlSAEAAVLCEALGLSFDVALKVMSgTAAGkghftTTWPNK-----VLKGDLSPA 232
|
250 260 270
....*....|....*....|....*....|..
gi 186478598 237 FL-DVLSQNLAIVEDKAKSLPFPVPLLAVARQ 267
Cdd:PRK15461 233 FMiDLAHKDLGIALDVANQLHVPMPLGAASRE 264
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-297 |
1.98e-26 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 110.91 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1 MSGVVGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAAVVVVLSHPdQIQDVIFGD 80
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSP-HVKEVALGE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 81 EGVMKGLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQ 160
Cdd:PRK11559 80 NGIIEGAKPGTVVIDMSSIAPLASREIAAALKAK--GIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 161 NLyTFEGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDDIEGRF-LD 239
Cdd:PRK11559 158 SV-VHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFrID 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 186478598 240 VLSQNLAIVEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAKISEKVLGVGI 297
Cdd:PRK11559 237 LHIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEV 294
|
|
| FBP_aldolase_IIA |
cd00946 |
Class II Type A, Fructose-1,6-bisphosphate (FBP) aldolases. The enzyme catalyses the ... |
1096-1336 |
2.21e-23 |
|
Class II Type A, Fructose-1,6-bisphosphate (FBP) aldolases. The enzyme catalyses the zinc-dependent, reversible aldol condensation of dihydroxyacetone phosphate with glyceraldehyde-3-phosphate to form fructose-1,6-bisphosphate. FBP aldolase is homodimeric and used in gluconeogenesis and glycolysis. The type A and type B Class II FBPA's differ in the presence and absence of distinct indels in the sequence that result in differing loop lengths in the structures.
Pssm-ID: 238476 Cd Length: 345 Bit Score: 103.22 E-value: 2.21e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1096 GRSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPG--AFKQG-GIP------LVSCCISAAEQAR 1166
Cdd:cd00946 1 GDDVLKLFDYAKENGFAIPAVNCTSSSTINAVLEAARDAKSPIIIQFSNGgaAFYAGkGLKnekqkaSIAGAIAAAHHVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1167 -------VPISVHFDHGTTKHELLEALELGLD-------------SVMVDGSHLSFTENLSYTKSITELARSKNIMVEAE 1226
Cdd:cd00946 81 smaehygVPVVLHTDHCAKKLLPWFDGLLEADeeyfkqhgeplfsSHMLDLSEEPLEENIEICKKYLERMAKINMWLEME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1227 LGRLSGTEDGltVEDYEAKLTNVNQAQEFMETGIDAL---------AVCIGNVHGKYpKSGpNLKL---------DLLKE 1288
Cdd:cd00946 161 IGITGGEEDG--VDNSGVDNAELYTQPEDVWYVYEALskispnfsiAAAFGNVHGVY-KPG-NVKLqpeilgehqDYVRE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 186478598 1289 LHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1336
Cdd:cd00946 237 KLGLADDKPLYFVFHGGSGSTKEEIREAISYGVVKMNIDTDTQWAYWE 284
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
170-287 |
2.20e-21 |
|
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a central metabolite in the valine catabolic pathway, and is reversibly oxidized to methylmalonate semi-aldehyde by a specific dehydrogenase belonging to the 3-hydroxyacid dehydrogenase family. The reaction is NADP-dependent and this region of the enzyme binds NAD. The NAD-binding domain of 6-phosphogluconate dehydrogenase adopts an alpha helical structure.
Pssm-ID: 434252 [Multi-domain] Cd Length: 122 Bit Score: 91.05 E-value: 2.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 170 GAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIP-LLLKDDIEGRF-LDVLSQNLAI 247
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFaLDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186478598 248 VEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAK 287
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIR 120
|
|
| PRK09197 |
PRK09197 |
fructose-bisphosphate aldolase; Provisional |
1093-1336 |
6.11e-17 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 236406 Cd Length: 350 Bit Score: 84.08 E-value: 6.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1093 VVAGRSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPG--AFKQG-GIPLVSC------CISAAE 1163
Cdd:PRK09197 3 VATGEDYQEMFDRAKENGFALPAVNVVGTDSINAVLEGAAEAKSPVIIQFSNGgaAFIAGkGVKDDGQgaavlgAIAGAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1164 QAR-------VPISVHFDHGTTKH-------------ELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMV 1223
Cdd:PRK09197 83 HVHevaehygVPVILHTDHCAKKLlpwidglldagekHFAAGGKPLFSSHMIDLSEEPLEENIEICSKYLERMAKAGMTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 1224 EAELGRLSGTEDGLTVEDYE-AKL-TnvnQAQEFMETgIDAL---------AVCIGNVHGKYpKSGpNLKL--DLLKELH 1290
Cdd:PRK09197 163 EIELGVTGGEEDGVDNSHEDnSKLyT---QPEDVLYA-YEALgkisgrftiAASFGNVHGVY-KPG-NVKLrpEILKDSQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 186478598 1291 ALSSKK------GVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1336
Cdd:PRK09197 237 EYVSKKfglpakPFDFVFHGGSGSTLEEIREAVSYGVVKMNIDTDTQWAFWR 288
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
5-163 |
3.29e-15 |
|
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold.
Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 74.43 E-value: 3.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 5 VGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKaAAAAVVVVLSHPDQIQDVIFGdEGVM 84
Cdd:pfam03446 2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVA-GLDVVITMVPAGAAVDAVIFG-EGLL 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478598 85 KGLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLY 163
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKEK--GLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVT 156
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
5-258 |
1.22e-12 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 70.05 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 5 VGFVGLDSFSFELASSLLRSGFKVQAFEISTeLVEKFIELGGHKCDSPADVGKAAAAAVVVVLSHPdQIQDVIFGDEGVM 84
Cdd:PRK15059 3 LGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVSVETARQVTEASDIIFIMVPDTP-QVEEVLFGENGCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 85 KGLQKDAVLLLSSTISTLQLQKLEKQLTEKREQifVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLyT 164
Cdd:PRK15059 81 KASLKGKTIVDMSSISPIETKRFARQVNELGGD--YLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNI-T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 165 FEGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDDIEGRFLDVLSQ- 243
Cdd:PRK15059 158 LVGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQk 237
|
250
....*....|....*..
gi 186478598 244 --NLAIVEDKAKSLPFP 258
Cdd:PRK15059 238 dlNLALQSAKALALNLP 254
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
324-497 |
8.07e-11 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 64.77 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVD---VLVIMV-----TNEVQAEdv 395
Cdd:PRK09599 2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVpageiTDATIDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 396 LYGHLGAVEAIPSGATvvlastvspAFVSQLERRLEN-EGKDLKLVDAPVSGGVKRAAMGeLTIMASGTDEALKSAGLVL 474
Cdd:PRK09599 80 LAPLLSPGDIVIDGGN---------SYYKDDIRRAELlAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIF 149
|
170 180
....*....|....*....|....*.
gi 186478598 475 SALS---EKLYVIKGGCGAGSGVKMV 497
Cdd:PRK09599 150 KALApraEDGYLHAGPVGAGHFVKMV 175
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
324-497 |
1.62e-10 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 63.96 E-value: 1.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVD---VLVIMV-----TNEVQAEdv 395
Cdd:COG1023 2 QIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVpageiTDQVIEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 396 LYGHLGAVEAIPSGA------TVVLASTVSPafvsqlerrlenegKDLKLVDAPVSGGVKRAAMGeLTIMASGTDEALKS 469
Cdd:COG1023 80 LAPLLEPGDIVIDGGnsnykdDIRRAEELAE--------------KGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVER 144
|
170 180 190
....*....|....*....|....*....|.
gi 186478598 470 AGLVLSALS---EKLYVIKGGCGAGSGVKMV 497
Cdd:COG1023 145 LEPIFKALApgaENGYLHCGPVGAGHFVKMV 175
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
324-440 |
2.68e-05 |
|
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis
Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 47.37 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186478598 324 RIGFIGLGAMGFGMAAHLLKSNFS---VCGYDVYKPTLVRFENAGGL-AANSPAEVTKDVDVLVIMVTNEvQAEDVLygh 399
Cdd:COG0345 4 KIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERYGVrVTTDNAEAAAQADVVVLAVKPQ-DLAEVL--- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 186478598 400 LGAVEAIPSGATVV-LASTVSpafVSQLERRLeneGKDLKLV 440
Cdd:COG0345 80 EELAPLLDPDKLVIsIAAGVT---LATLEEAL---GGGAPVV 115
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
321-360 |
2.94e-03 |
|
3-hydroxybutyryl-CoA dehydrogenase; Validated
Pssm-ID: 235707 [Multi-domain] Cd Length: 311 Bit Score: 41.30 E-value: 2.94e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 186478598 321 PVNRIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVR 360
Cdd:PRK06130 3 PIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALER 42
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
323-386 |
7.58e-03 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 39.94 E-value: 7.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 186478598 323 NRIGFIGLGAMGFGMAAHLLKSNF----SVCGYDVYKPTLVR-FENAGGLAANSPAEVTKDVDVLVIMV 386
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVvppsRISTADDSNPARRDvFQSLGVKTAASNTEVVKSSDVIILAV 69
|
|
| |
