|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02858 |
PLN02858 |
fructose-bisphosphate aldolase |
1-1373 |
0e+00 |
|
fructose-bisphosphate aldolase
Pssm-ID: 215463 [Multi-domain] Cd Length: 1378 Bit Score: 2544.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1 MSGVVGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAVVVVLSHPDQIQDVIFGDE 80
Cdd:PLN02858 3 SAGVVGFVGLDSLSFELASSLLRSGFKVQAFEISTPLMEKFCELGGHRCDSPAEAAKDAAALVVVLSHPDQVDDVFFGDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 81 GVMKGLQKDAVLLLSSTISTLQLQKLEKQLTEKREQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQN 160
Cdd:PLN02858 83 GAAKGLQKGAVILIRSTILPLQLQKLEKKLTERKEQIFLVDAYVSKGMSDLLNGKLMIIASGRSDAITRAQPFLSAMCQK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 161 LYTFEGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDD-IEGRFLDV 239
Cdd:PLN02858 163 LYTFEGEIGAGSKVKMVNELLEGIHLVASAEAMALGVRAGIHPWIIYDIISNAAGSSWIFKNHVPLLLKDDyIEGRFLNV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 240 LSQNLAIVEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAKISEKVLGVGILEAANRELYKPEDLAKEITTQAK 319
Cdd:PLN02858 243 LVQNLGIVLDMAKSLPFPLPLLAVAHQQLISGSSSMQGDDTATSLAKVWEKVFGVNILEAANRELYKPEDLAKQITMQAK 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 320 PVNRIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHL 399
Cdd:PLN02858 323 PVKRIGFIGLGAMGFGMASHLLKSNFSVCGYDVYKPTLVRFENAGGLAGNSPAEVAKDVDVLVIMVANEVQAENVLFGDL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 400 GAVEAIPSGATVVLASTVSPAFVSQLERRLENEGKDLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEK 479
Cdd:PLN02858 403 GAVSALPAGASIVLSSTVSPGFVIQLERRLENEGRDIKLVDAPVSGGVKRAAMGTLTIMASGTDEALKSAGSVLSALSEK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 480 LYVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDI 559
Cdd:PLN02858 483 LYVIKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFDIISNAGGTSWMFENRVPHMLDNDYTPYSALDI 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 560 FVKDLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIKVEGRLPVLKKQDLLKSLPAEWPSD 639
Cdd:PLN02858 563 FVKDLGIVSREGSSRKIPLHLSTVAHQLFLAGSASGWGRIDDAAVVKVYETLTGVKVEGRLPVLKKEDVLTSLPAEWPED 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 640 PTTDI-HRLNMGNSKTLVVLDDDPTGTQTVHDVEVLTEWSVESISEQFRKKPACFFILTNSRSLSPEKASELIKDICSNL 718
Cdd:PLN02858 643 PIDDIcHRLNMGNSKTLVVLDDDPTGTQTVHDVEVLTEWSVESISEQFRKKPACFFILTNSRSLSPEKASELIKDICRNL 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 719 CAASKEVGNADYTIVLRGDSTLRGHFPQEADAAVSILGEMDAWIICPFFLQGGRYTIDDVHYVADSDRLVPAGETEFAKD 798
Cdd:PLN02858 723 CAAAKSVGNVDYTIVLRGDSTLRGHFPEEADAAVSVLGEMDAWIICPFFLQGGRYTINDIHYVADSDRLVPAGETEFAKD 802
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 799 ASFGYKSSNLREWVEEKTAGVIPANSVQSISIQLLRKGGPDAVCEFLCSLKKGSTCIVNAASERDMAVFAAGMIQAELKG 878
Cdd:PLN02858 803 ASFGYKSSNLREWVEEKTKGRISANSVQSISIQLLRKGGPDAVCEHLCSLKKGSTCIVNAASERDMAVFAAGMIQAELKG 882
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 879 RSFLCRTAASFVSALIGIIPKDPVLPKDFESNKESSGALIVVGSYVPKTTKQVEELQSQHNQNLRSIEISVEKVALKSSE 958
Cdd:PLN02858 883 KRFLCRTAASFVSARIGIIPKPPVLPKDLESNKESSGGLIVVGSYVPKTTKQVEELKSQCGQSLRSIEVSVEKVAMKSSE 962
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 959 VRDEEIRRAVEMADAFLRAGRETLIMSSRELITGKTSSESLDINSKVSSALVEVVSQISTRPRYILAKGGITSSDTATKA 1038
Cdd:PLN02858 963 VRDEEISRAVEMADAFLRAGKDTLIMTSRELITGKTPSESLDINSKVSSALVEIVRRISTRPRYILAKGGITSSDLATKA 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1039 LKARRALVIGQALAGVPVWKLGPESRHPGVPYIVFPGNVGNSTALAEVVKSWSVVAGRSTKELLLNAEKGGYAVGAFNVY 1118
Cdd:PLN02858 1043 LEARRAKVVGQALAGVPLWKLGPESRHPGVPYIVFPGNVGDSTALAEVVKSWARPARSSTKELLLNAEKGGYAVGAFNVY 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1119 NLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQARVPISVHFDHGTTKHELLEALELGLDSVMVDGSH 1198
Cdd:PLN02858 1123 NLEGIEAVVAAAEAEKSPAILQVHPGALKQGGIPLVSCCIAAAEQASVPITVHFDHGTSKHELLEALELGFDSVMVDGSH 1202
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1199 LSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM-ETGIDALAVCIGNVHGKYPKSG 1277
Cdd:PLN02858 1203 LSFTENISYTKSISSLAHSKGLMVEAELGRLSGTEDGLTVEEYEAKLTDVDQAKEFIdETGIDALAVCIGNVHGKYPASG 1282
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1278 PNLKLDLLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYMEALSSGKKTDIVDVMSATKAAMK 1357
Cdd:PLN02858 1283 PNLRLDLLKELRALSSKKGVLLVLHGASGLPESLIKECIENGVRKFNVNTEVRTAYMEALSSPKKTDLIDVMSAAKEAMK 1362
|
1370
....*....|....*.
gi 22329645 1358 AVIADKIRLFGSAGKA 1373
Cdd:PLN02858 1363 AVVAEKLRLFGSAGKA 1378
|
|
| F_bP_aldolase |
pfam01116 |
Fructose-bisphosphate aldolase class-II; |
1097-1372 |
2.39e-96 |
|
Fructose-bisphosphate aldolase class-II;
Pssm-ID: 460071 Cd Length: 276 Bit Score: 310.50 E-value: 2.39e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQ---GGIPLVSCCISAAEQARVPISVHFD 1173
Cdd:pfam01116 2 NLKELLKKAKEGGYAVPAFNVNNLETVQAILEAAEEAKSPVILQVSPGAAAKyagGAEALAALVRAAAEAAGVPVALHLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1174 HGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQAQE 1253
Cdd:pfam01116 82 HGASFELIKEAIEAGFTSVMIDGSHLPFEENIAITKEVVEYAHARGVSVEAELGRIGGEEDGVVVD--EKLYTDPEEAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1254 FME-TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTA 1332
Cdd:pfam01116 160 FVEaTGVDALAVAIGNVHGVY-KPGPKLDFDRLKEIQEAV---PVPLVLHGGSGVPDEDIRKAIKLGVCKINIDTDLQLA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 22329645 1333 YMEALSS-GKKTDIVDVMSATKAAMKAVIADKIRLFGSAGK 1372
Cdd:pfam01116 236 FTAAVREyPPNKDPRKYLRPAEEAMKEVVKEKIRLFGSAGK 276
|
|
| OtnK |
COG3395 |
D-threonate/D-erythronate kinase OtnK and related C4-acid sugar kinases, YgbK/DUF1537 family ... |
655-1088 |
1.36e-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: 1.36e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 655 LVVLDDDPTGTQTVHDVEVLTEWSVESI----SEQFRKKPACFFILTNSRSLSPEKASELIKDICSNLCAASKEVgnady 730
Cdd:COG3395 2 LGVIADDFTGATDVAVQLARAGLRTVLLlgvpTLALADDADAVVIATKSRSLPPEEAVARVREALAWLKAAGARL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 731 tIVLRGDSTLRGHFPQEADAAVSILGEmDAWIICPFFLQGGRYTIDDVHYVADsdrlVPAGETEFAKDASFGYKSSNLRE 810
Cdd:COG3395 77 -VYKKFDSTLRGNIGAETDALLDALGA-DAAVVVPAFPENGRTTVGGHLFVGG----VPLHETEMARDPVTPMTESDLPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 811 WVEEKTAGvipanSVQSISIQLLRKgGPDAVCEFLCSLKKGST--CIVNAASERDMAVFAAGMIQAElkgRSFLCRTAAS 888
Cdd:COG3395 151 LLAEQTKG-----PVGLVDLADVRA-GAEALRAALAALAAEGAriVVVDAVTDADLDAIAEALADLA---ERVLVVGSSG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 889 FVSALIGIIPKDPvlpkdfesnKESSGALIVVGSYVPKTTKQVEELQSQHnqNLRSIEISVEKVAlksSEVRDEEIRRAV 968
Cdd:COG3395 222 LAAALAAAPAALP---------PAGGPVLVVVGSCSPVTRRQLAALLAEP--GVPVVELDVERLL---DGEAEAEVERAL 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 969 EMADAFLRAGRETLIMSSRELITGKTSSESLD---INSKVSSALVEVVSQI--STRPRYILAKGGITSSDtATKALKARR 1043
Cdd:COG3395 288 AWALAALAAGRTVLIYTSRDPEDVADAQERLGrlaAGERIEAALAEIARRLleEAGVRRLIVAGGDTSGA-VLKALGIRG 366
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 22329645 1044 ALVIGQALAGVPVWKLgPESRHPGVPYIVFPGNVGNSTALAEVVK 1088
Cdd:COG3395 367 LRILGEIAPGVPLGRA-IGGDFDGLPVVLKGGNFGDEDFFARALE 410
|
|
| Fba |
COG0191 |
Fructose/tagatose bisphosphate aldolase [Carbohydrate transport and metabolism]; Fructose ... |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAAEQARVPISVHFDHG 1175
Cdd:COG0191 4 SLKELLDKAKEGGYAVPAFNVNNLETLQAILEAAEELNSPVILQVSEGAAKyAGLEYLAAMVRAAAEEASVPVALHLDHG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1176 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1255
Cdd:COG0191 84 ASFELIKRAIDAGFTSVMIDGSHLPFEENIAITKEVVEYAHAAGVSVEAELGVVGGEEDGVDVDDAEALYTDPEEAAEFV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1256 E-TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1334
Cdd:COG0191 164 EeTGVDALAVAIGTVHGVY-KGEPKLDFDRLKEIREAV---PVPLVLHGGSGVPDEEIREAIKLGVAKINIDTDLRLAFT 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22329645 1335 EAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:COG0191 240 AAVreylaENPDKYDPRKYLKPAREAMKEVVKEKIRLFGSAGKA 283
|
|
| TBP_aldolase_IIB |
cd00947 |
Tagatose-1,6-bisphosphate (TBP) aldolase and related Type B Class II aldolases. TBP aldolase ... |
1098-1371 |
2.33e-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: 2.33e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1098 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGI-PLVSCCISAAEQARVPISVHFDHGT 1176
Cdd:cd00947 1 TKELLKKAREGGYAVGAFNINNLETLKAILEAAEETRSPVILQISEGAIKYAGLeLLVAMVKAAAERASVPVALHLDHGS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1177 TKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQAQEFME 1256
Cdd:cd00947 81 SFELIKRAIRAGFSSVMIDGSHLPFEENVAKTKEVVELAHAYGVSVEAELGRIGGEEDGVVGD--EGLLTDPEEAEEFVE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1257 -TGIDALAVCIGNVHGKYPKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1335
Cdd:cd00947 159 eTGVDALAVAIGTSHGAYKGGEPKLDFDRLKEIAERV---NVPLVLHGGSGIPDEQIRKAIKLGVCKININTDLRLAFTA 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 22329645 1336 AL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAG 1371
Cdd:cd00947 236 ALreylaENPKEFDPRKYLAPAIEAVKEVVKHKMELFGSAG 276
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
323-608 |
2.84e-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: 2.84e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAV 402
Cdd:COG2084 3 KVGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 403 EAIPSGATVVLASTVSPAFVSQLERRLENEGkdLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLYV 482
Cdd:COG2084 83 AALRPGAVVVDMSTISPETARELAAAAAARG--VRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRIVH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 483 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDIFVK 562
Cdd:COG2084 161 V-GDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFALDLMLK 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22329645 563 DLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVY 608
Cdd:COG2084 240 DLGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIKLL 285
|
|
| gatY |
PRK09195 |
tagatose-bisphosphate aldolase; Reviewed |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1175
Cdd:PRK09195 5 STKQMLNNAQRGGYAVPAFNIHNLETMQVVVETAAELHSPVIIAGTPGTFSYAGTEyLLAIVSAAAKQYHHPLALHLDHH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1176 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1255
Cdd:PRK09195 85 EKFDDIAQKVRSGVRSVMIDGSHLPFAQNISLVKEVVDFCHRFDVSVEAELGRLGGQEDDLQVDEADALYTDPAQAREFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1256 E-TGIDALAVCIGNVHGKYpKSGPNLKLDllkELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1334
Cdd:PRK09195 165 EaTGIDSLAVAIGTAHGMY-KGEPKLDFD---RLENIRQWVNIPLVLHGASGLPTKDIQQTIKLGICKVNVATELKIAFS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22329645 1335 EAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK09195 241 QALknyltEHPEANDPRHYLQPAKSAMKDVVSKVIADCGCEGKA 284
|
|
| gatY |
PRK12737 |
tagatose-bisphosphate aldolase subunit GatY; |
1097-1373 |
2.94e-74 |
|
tagatose-bisphosphate aldolase subunit GatY;
Pssm-ID: 183710 Cd Length: 284 Bit Score: 248.84 E-value: 2.94e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1175
Cdd:PRK12737 5 STKNMLKKAQAEGYAVPAFNIHNLETLQVVVETAAELRSPVILAGTPGTFSYAGTDyIVAIAEVAARKYNIPLALHLDHH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1176 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1255
Cdd:PRK12737 85 EDLDDIKKKVRAGIRSVMIDGSHLSFEENIAIVKEVVEFCHRYDASVEAELGRLGGQEDDLVVDEKDAMYTNPDAAAEFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1256 E-TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1334
Cdd:PRK12737 165 ErTGIDSLAVAIGTAHGLY-KGEPKLDFERLAEIREKVS---IPLVLHGASGVPDEDVKKAISLGICKVNVATELKIAFS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22329645 1335 EALSS-----GKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK12737 241 DAVKKyfyenPKANDPRKYMTPGKAAMKEVVREKIKVCGSEGKL 284
|
|
| PRK12857 |
PRK12857 |
class II fructose-1,6-bisphosphate aldolase; |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCI-SAAEQARVPISVHFDHG 1175
Cdd:PRK12857 5 TVAELLKKAEKGGYAVGAFNCNNMEIVQAIVAAAEAEKSPVIIQASQGAIKYAGIEYISAMVrTAAEKASVPVALHLDHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1176 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1255
Cdd:PRK12857 85 TDFEQVMKCIRNGFTSVMIDGSKLPLEENIALTKKVVEIAHAVGVSVEAELGKIGGTEDDITVDEREAAMTDPEEARRFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1256 -ETGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHALSskkGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1334
Cdd:PRK12857 165 eETGVDALAIAIGTAHGPY-KGEPKLDFDRLAKIKELV---NIPIVLHGSSGVPDEAIRKAISLGVRKVNIDTNIREAFV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 22329645 1335 EALSS--GKKTDIVD---VMSATKAAMKAVIADKIRLFGSAGKA 1373
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 ... |
655-893 |
1.11e-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: 1.11e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 655 LVVLDDDPTGTQTV------HDVEVLTewSVESISEQFRKKPACFFILTNSRSLSPEKASELIKDICSNLCAASKEVgna 728
Cdd:pfam07005 1 LGVIADDFTGAQDVgvqlakHGLRTLV--FLGVPDAARLPDADAVVIATNSRSLPPEEAVARVREALKWLAALGARL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 729 DYTIVLRGDSTLRGHFPQEADAAVSILGEMDAWIICPFFLQGGRYTIDDVHYVadsdRLVPAGETEFAKDASFGYKSSNL 808
Cdd:pfam07005 76 YYKVCSRFDSTLRGNIGAETDALLDALGAFDAAVVAPAFPEGGRTTIGGVLFV----NGVPLAETEFARDPVTPMTESDL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 809 REWVEEKTAGvipanSVQSISIQLLRKgGPDAVCEFLCSLKKGST--CIVNAASERDMAVFAAGMIQAelkGRSFLCRTA 886
Cdd:pfam07005 152 RRLLAEQTKL-----PVGLIDLDTLAD-GPEALREALAALLAQGVrvVVVDAVTDEDLAVIAEALLAL---GKRFLLVGS 222
|
....*..
gi 22329645 887 ASFVSAL 893
Cdd:pfam07005 223 AGLAAAL 229
|
|
| fruc_bis_ald_ |
TIGR01859 |
fructose-1,6-bisphosphate aldolase, class II, various bacterial and amitochondriate protist; ... |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGG-----IPLVsccISAAEQAR-VPISV 1170
Cdd:TIGR01859 3 NGKEILQKAKKEGYAVGAFNFNNLEWTQAILEAAEEENSPVIIQVSEGAIKYMGgykmaVAMV---KTLIERMSiVPVAL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1171 HFDHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQ 1250
Cdd:TIGR01859 80 HLDHGSSYESCIKAIKAGFSSVMIDGSHLPFEENLALTKKVVEIAHAKGVSVEAELGTLGGIEDGVDEK--EAELADPDE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1251 AQEFM-ETGIDALAVCIGNVHGKYPKSgPNLKLDLLKELHALSSKKgvfLVLHGASGLSENLIKECIENGVRKFNVNTEV 1329
Cdd:TIGR01859 158 AEQFVkETGVDYLAAAIGTSHGKYKGE-PGLDFERLKEIKELTNIP---LVLHGASGIPEEQIKKAIKLGIAKINIDTDC 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 22329645 1330 RTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:TIGR01859 234 RIAFTAAIrkvltEKKDEYDPRKILGPAREAIKETVKEKMRLFGSAGKA 282
|
|
| cbbA |
TIGR00167 |
ketose-bisphosphate aldolase; This model is under revision. Proteins found by this model ... |
1093-1373 |
2.33e-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: 2.33e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1093 VAGRSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISA---AEQARVPI 1168
Cdd:TIGR00167 1 MMLVDVKELLQDAKEEGYAIPAFNINNLETINAVLEAAAEEKSPVIIQFSNGAAKyIAGLGAISAMVKAmseAYPYGVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1169 SVHFDHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNV 1248
Cdd:TIGR00167 81 ALHLDHGASEEDCAQAVKAGFSSVMIDGSHEPFEENIELTKKVVERAHKMGVSVEAELGTLGGEEDGVSVADESALYTDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1249 NQAQEFME-TGIDALAVCIGNVHGKYpKSGPN-LKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVN 1326
Cdd:TIGR00167 161 EEAKEFVKlTGVDSLAAAIGNVHGVY-KGEPKgLDFERLEEIQKYVN---LPLVLHGGSGIPDEEIKKAISLGVVKVNID 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 22329645 1327 TEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:TIGR00167 237 TELQIAFAAAVrnyyaENKDYYDPRVWLRPGEKAMKEVVLEKIKLFGSANKA 288
|
|
| PRK06806 |
PRK06806 |
class II aldolase; |
1099-1373 |
7.83e-64 |
|
class II aldolase;
Pssm-ID: 180705 Cd Length: 281 Bit Score: 218.86 E-value: 7.83e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1099 KELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVS-CCISAAEQARVPISVHFDHGTT 1177
Cdd:PRK06806 7 KELLKKANQENYGVGAFSVANMEMVMGAIKAAEELNSPIILQIAEVRLNHSPLHLIGpLMVAAAKQAKVPVAVHFDHGMT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1178 KHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLtvEDYEAKLTNVNQAQEFM-E 1256
Cdd:PRK06806 87 FEKIKEALEIGFTSVMFDGSHLPLEENIQKTKEIVELAKQYGATVEAEIGRVGGSEDGS--EDIEMLLTSTTEAKRFAeE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1257 TGIDALAVCIGNVHGKYpKSGPNLKLDLLKELHalsSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNT----EVRTA 1332
Cdd:PRK06806 165 TDVDALAVAIGNAHGMY-NGDPNLRFDRLQEIN---DVVHIPLVLHGGSGISPEDFKKCIQHGIRKINVATatfnSVITA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 22329645 1333 YMEALSSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK06806 241 VNNLVLNTPYSDYFTYHQDVIKAAYENVKKHMQIFGSENKA 281
|
|
| PRK08185 |
PRK08185 |
hypothetical protein; Provisional |
1099-1373 |
2.41e-57 |
|
hypothetical protein; Provisional
Pssm-ID: 181275 Cd Length: 283 Bit Score: 199.95 E-value: 2.41e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1099 KELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQARVPISVHFDHGTTK 1178
Cdd:PRK08185 2 KELLKVAKEHQFAVGAFNVADSCFLRAVVEEAEANNAPAIIAIHPNELDFLGDNFFAYVRERAKRSPVPFVIHLDHGATI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1179 HELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTedGLTVEDYEAKL--TNVNQAQEFME 1256
Cdd:PRK08185 82 EDVMRAIRCGFTSVMIDGSLLPYEENVALTKEVVELAHKVGVSVEGELGTIGNT--GTSIEGGVSEIiyTDPEQAEDFVS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1257 -TGIDALAVCIGNVHGKYPKSG-PNLKLDLLKELHAlssKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1334
Cdd:PRK08185 160 rTGVDTLAVAIGTAHGIYPKDKkPELQMDLLKEINE---RVDIPLVLHGGSANPDAEIAESVQLGVGKINISSDMKYAFF 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 22329645 1335 EALSS--GKKTDIVD---VM-SATKAAmKAVIADKIRLFGSAGKA 1373
Cdd:PRK08185 237 KKVREilSDNPSLYEpnqIYpSAIEAA-KEVVRHKMDLFNSTGKA 280
|
|
| PRK05835 |
PRK05835 |
class II fructose-1,6-bisphosphate aldolase; |
1096-1372 |
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 22329645 1096 RSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCIS--AAEQARVPISVHFD 1173
Cdd:PRK05835 3 VKGNEILLKAHKEGYGVGAFNFVNFEMLNAIFEAGNEENSPLFIQASEGAIKYMGIDMAVGMVKimCERYPHIPVALHLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1174 HGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQE 1253
Cdd:PRK05835 83 HGTTFESCEKAVKAGFTSVMIDASHHAFEENLELTSKVVKMAHNAGVSVEAELGRLMGIEDNISVDEKDAVLVNPKEAEQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1254 FM-ETGIDALAVCIGNVHGKYP-KSGPNLKLDLLKELHALSSkkgVFLVLHGASGLSENL-------------------- 1311
Cdd:PRK05835 163 FVkESQVDYLAPAIGTSHGAFKfKGEPKLDFERLQEVKRLTN---IPLVLHGASAIPDDVrksyldaggdlkgskgvpfe 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22329645 1312 -IKECIENGVRKFNVNTEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGK 1372
Cdd:PRK05835 240 fLQESVKGGINKVNTDTDLRIAFIAEVrkvanEDKSQFDLRKFFSPAQLALKNVVKERMKLLGSANK 306
|
|
| kbaY |
PRK12738 |
tagatose-bisphosphate aldolase subunit KbaY; |
1097-1372 |
6.07e-51 |
|
tagatose-bisphosphate aldolase subunit KbaY;
Pssm-ID: 183711 Cd Length: 286 Bit Score: 181.77 E-value: 6.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1175
Cdd:PRK12738 5 STKYLLQDAQANGYAVPAFNIHNAETIQAILEVCSEMRSPVILAGTPGTFKHIALEeIYALCSAYSTTYNMPLALHLDHH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1176 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDYEAKLTNVNQAQEFM 1255
Cdd:PRK12738 85 ESLDDIRRKVHAGVRSAMIDGSHFPFAENVKLVKSVVDFCHSQDCSVEAELGRLGGVEDDMSVDAESAFLTDPQEAKRFV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1256 E-TGIDALAVCIGNVHGKYPKSgPNLKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYM 1334
Cdd:PRK12738 165 ElTGVDSLAVAIGTAHGLYSKT-PKIDFQRLAEIREVVD---VPLVLHGASDVPDEFVRRTIELGVTKVNVATELKIAFA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 22329645 1335 EAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGK 1372
Cdd:PRK12738 241 GAVkawfaENPQGNDPRYYMRVGMDAMKEVVRNKINVCGSANR 283
|
|
| HIBADH |
TIGR01692 |
3-hydroxyisobutyrate dehydrogenase; 3-hydroxyisobutyrate dehydrogenase is an enzyme that ... |
326-608 |
5.65e-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: 5.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 326 FIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAVEAI 405
Cdd:TIGR01692 1 FIGLGNMGGPMAANLLKAGHPVRVFDLFPDAVEEAVAAGAQAAASPAEAAEGADRVITMLPAGQHVISVYSGDEGILPKV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 406 PSGATVVLASTVSPAFVSQLERRLENEGkdLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLyVIKG 485
Cdd:TIGR01692 81 AKGSLLIDCSTIDPDSARKLAELAAAHG--AVFMDAPVSGGVGGARAGTLTFMVGGVAEEFAAAEPVLGPMGRNI-VHCG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 486 GCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFE--NRVPHMLD-----NDYTPYSALD 558
Cdd:TIGR01692 158 DHGAGQAAKICNNMLLGISMIGTAEAMALGEKLGLDPKVLFEIANTSSGRCWSSDtyNPVPGVMPqapasNGYQGGFGTA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 22329645 559 IFVKDLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVY 608
Cdd:TIGR01692 238 LMLKDLGLAQDAAKSAGAPTPLGALARQLYSLFDDKGHGGKDFSSVIQLL 287
|
|
| PRK08610 |
PRK08610 |
fructose-bisphosphate aldolase; Reviewed |
1097-1373 |
4.88e-49 |
|
fructose-bisphosphate aldolase; Reviewed
Pssm-ID: 181501 Cd Length: 286 Bit Score: 176.33 E-value: 4.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAA---EQARVPISVHF 1172
Cdd:PRK08610 5 SMKEMLIDAKENGYAVGQYNLNNLEFTQAILEASQEENAPVILGVSEGAARyMSGFYTVVKMVEGLmhdLNITIPVAIHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1173 DHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDyeAKLTNVNQAQ 1252
Cdd:PRK08610 85 DHGSSFEKCKEAIDAGFTSVMIDASHSPFEENVATTKKVVEYAHEKGVSVEAELGTVGGQEDDVVADG--IIYADPKECQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1253 EFME-TGIDALAVCIGNVHGKYpKSGPNLKldlLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRT 1331
Cdd:PRK08610 163 ELVEkTGIDALAPALGSVHGPY-KGEPKLG---FKEMEEIGLSTGLPLVLHGGTGIPTKDIQKAIPFGTAKINVNTENQI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 22329645 1332 AYMEALSS--GKKTDIVD---VMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK08610 239 ASAKAVRDvlNNDKEVYDprkYLGPAREAIKETVKGKIKEFGTSNRA 285
|
|
| PRK06801 |
PRK06801 |
ketose 1,6-bisphosphate aldolase; |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIP-LVSCCISAAEQARVPISVHFDHG 1175
Cdd:PRK06801 5 SLANGLAHARKHGYALGAFNVLDSHFLRALFAAAKQERSPFIINIAEVHFKYISLEsLVEAVKFEAARHDIPVVLNLDHG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1176 TTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDG-LTVEDYEAKLTNVNQAQEF 1254
Cdd:PRK06801 85 LHFEAVVRALRLGFSSVMFDGSTLEYEENVRQTREVVKMCHAVGVSVEAELGAVGGDEGGaLYGEADSAKFTDPQLARDF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1255 ME-TGIDALAVCIGNVHGKYpKSGPnlKLDlLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAY 1333
Cdd:PRK06801 165 VDrTGIDALAVAIGNAHGKY-KGEP--KLD-FARLAAIHQQTGLPLVLHGGSGISDADFRRAIELGIHKINFYTGMSQAA 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 22329645 1334 MEALS------SGKKTDIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK06801 241 LAAVEqrmthrHAIYDEFAELLLGIEEAISDTVAQQMRIFGSAGQA 286
|
|
| MmsB |
COG2084 |
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
5-286 |
1.38e-45 |
|
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism];
Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 166.44 E-value: 1.38e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 5 VGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAVVVVLSHPDQIQDVIFGDEGVMK 84
Cdd:COG2084 4 VGFIGLGAMGAPMARNLLKAGHEVTVWNRTPAKAEALVAAGARVAASPAEAAAAADVVITMLPDDAAVEEVLLGEDGLLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 85 GLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLyTF 164
Cdd:COG2084 84 ALRPGAVVVDMSTISPETARELAAAAAAR--GVRYLDAPVSGGPAGAEAGTLTIMVGGDEAAFERARPVLEAMGKRI-VH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 165 EGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDDIEGRF-LDVLSQN 243
Cdd:COG2084 161 VGDAGAGQAAKLANNLLLAGTMAALAEALALAEKAGLDPETLLEVLSGGAAGSWVLENRGPRMLAGDFDPGFaLDLMLKD 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 22329645 244 LAIVEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAK 286
Cdd:COG2084 241 LGLALEAARAAGVPLPLAAAARQLYARAVAAGHGDEDFSALIK 283
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
323-616 |
2.61e-45 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 165.99 E-value: 2.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAV 402
Cdd:PRK11559 4 KVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGENGII 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 403 EAIPSGATVVLASTVSPaFVSQlERRLENEGKDLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLyV 482
Cdd:PRK11559 84 EGAKPGTVVIDMSSIAP-LASR-EIAAALKAKGIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGSV-V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 483 IKGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDIFVK 562
Cdd:PRK11559 161 HTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFRIDLHIK 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 22329645 563 DLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIKV 616
Cdd:PRK11559 241 DLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEV 294
|
|
| PRK07709 |
PRK07709 |
fructose-bisphosphate aldolase; Provisional |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAAEQ---ARVPISVHF 1172
Cdd:PRK07709 5 SMKEMLNKALEGKYAVGQFNMNNLEWTQAILAAAEEEKSPVILGVSEGAARhMTGFKTVVAMVKALIEemnITVPVAIHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1173 DHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEDyeAKLTNVNQAQ 1252
Cdd:PRK07709 85 DHGSSFEKCKEAIDAGFTSVMIDASHHPFEENVETTKKVVEYAHARNVSVEAELGTVGGQEDDVIAEG--VIYADPAECK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1253 EFME-TGIDALAVCIGNVHGKYpKSGPNLKldlLKELHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRT 1331
Cdd:PRK07709 163 HLVEaTGIDCLAPALGSVHGPY-KGEPNLG---FAEMEQVRDFTGVPLVLHGGTGIPTADIEKAISLGTSKINVNTENQI 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 22329645 1332 AYMEALSS--GKKTDIVD---VMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK07709 239 EFTKAVREvlNKDQEVYDprkFIGPGRDAIKATVIGKIREFGSNGKA 285
|
|
| gatY |
PRK07998 |
class II aldolase; |
1098-1369 |
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 22329645 1098 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCIS-AAEQARVPISVHFDHGT 1176
Cdd:PRK07998 6 GRILLDRIQEKHVLAGAFNTTNLETTISILNAIERSGLPNFIQIAPTNAQLSGYDYIYEIVKrHADKMDVPVSLHLDHGK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1177 TKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGlTVEDYEAKlTNVNQAQEFME 1256
Cdd:PRK07998 86 TFEDVKQAVRAGFTSVMIDGAALPFEENIAFTKEAVDFAKSYGVPVEAELGAILGKEDD-HVSEADCK-TEPEKVKDFVE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1257 -TGIDALAVCIGNVHGKypKSGPNLKLDLLKELHALSSkkgVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1335
Cdd:PRK07998 164 rTGCDMLAVSIGNVHGL--EDIPRIDIPLLKRIAEVSP---VPLVIHGGSGIPPEILRSFVNYKVAKVNIASDLRKAFIT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 22329645 1336 ALssGK-------KTDIVDVMSATKAAMKAVIADKIRLFGS 1369
Cdd:PRK07998 239 TV--GKayvnnhnEANLARVMAKAKQAVEEDVYSKIKMMNS 277
|
|
| PRK07315 |
PRK07315 |
fructose-bisphosphate aldolase; Provisional |
1097-1373 |
4.99e-44 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 180926 Cd Length: 293 Bit Score: 161.98 E-value: 4.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFK-QGGIPLVSCCISAAEQA---RVPISVHF 1172
Cdd:PRK07315 5 SAEKFVQAARDNGYAVGGFNTNNLEWTQAILRAAEAKKAPVLIQTSMGAAKyMGGYKVCKNLIENLVESmgiTVPVAIHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1173 DHGTTKHELLEALELGLdSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTvedYEAKLTNVNQAQ 1252
Cdd:PRK07315 85 DHGHYEDALECIEVGYT-SIMFDGSHLPVEENLKLAKEVVEKAHAKGISVEAEVGTIGGEEDGII---GKGELAPIEDAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1253 EFMETGIDALAVCIGNVHGKYPKSGPNLKLDLLKELHAlsSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTA 1332
Cdd:PRK07315 161 AMVETGIDFLAAGIGNIHGPYPENWEGLDLDHLEKLTE--AVPGFPIVLHGGSGIPDDQIQEAIKLGVAKVNVNTECQIA 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 22329645 1333 Y-------------MEALSSGKKT-DIVDVMSATKAAMKAVIADKIRLFGSAGKA 1373
Cdd:PRK07315 239 FanatrkfardyeaNEAEYDKKKLfDPRKFLAPGVKAIQASVEERIDVFGSANKA 293
|
|
| PRK09196 |
PRK09196 |
fructose-bisphosphate aldolase class II; |
1097-1373 |
3.89e-42 |
|
fructose-bisphosphate aldolase class II;
Pssm-ID: 181691 Cd Length: 347 Bit Score: 158.20 E-value: 3.89e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQA--RVPISVHFDH 1174
Cdd:PRK09196 5 SLRQLLDHAAEHGYGVPAFNVNNLEQVQAIMEAADETDSPVILQASAGARKYAGEPFLRHLILAAVEEypHIPVVMHQDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1175 GTTKHELLEALELGLDSVMVDGSHL-------SFTENLSYTKSITELARSKNIMVEAELGRL-------SGTEDGLTVE- 1239
Cdd:PRK09196 85 GNSPATCQRAIQLGFTSVMMDGSLKadgktpaSYEYNVDVTRKVVEMAHACGVSVEGELGCLgsletgmGGEEDGHGAEg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1240 --DYEAKLTNVNQAQEFME-TGIDALAVCIGNVHGKY----PKSGPNLKLDLLKELHAlsSKKGVFLVLHGASGLSENL- 1311
Cdd:PRK09196 165 klSHDQLLTDPEEAADFVKkTQVDALAIAIGTSHGAYkftrKPTGDVLAIDRIKEIHA--RLPNTHLVMHGSSSVPQELl 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1312 --------------------IKECIENGVRKFNVNTEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRL 1366
Cdd:PRK09196 243 diineyggdmpetygvpveeIQEGIKHGVRKVNIDTDLRLAMTGAIrrflaENPSEFDPRKYLKPAMEAMKKICKARYEA 322
|
....*..
gi 22329645 1367 FGSAGKA 1373
Cdd:PRK09196 323 FGTAGQA 329
|
|
| PRK13399 |
PRK13399 |
fructose-bisphosphate aldolase class II; |
1097-1373 |
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 22329645 1097 STKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVSCCISAAEQA--RVPISVHFDH 1174
Cdd:PRK13399 5 TLRQLLDHAAENGYGVPAFNVNNMEQILAIMEAAEATDSPVILQASRGARKYAGDAMLRHMVLAAAEMypDIPICLHQDH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1175 GTTKHELLEALELGLDSVMVDGSHL-------SFTENLSYTKSITELARSKNIMVEAELGRL-------SGTEDGLTVE- 1239
Cdd:PRK13399 85 GNSPATCQSAIRSGFTSVMMDGSLLadgktpaSYDYNVDVTRRVTEMAHAVGVSVEGELGCLgsletgeAGEEDGVGAEg 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1240 --DYEAKLTNVNQAQEFM-ETGIDALAVCIGNVHGKY----PKSGPNLKLDLLKELHAlsSKKGVFLVLHGASGLSENL- 1311
Cdd:PRK13399 165 klSHDQMLTDPDQAVDFVqRTGVDALAIAIGTSHGAYkftrKPDGDILAIDRIEEIHA--RLPNTHLVMHGSSSVPQELq 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1312 --------------------IKECIENGVRKFNVNTEVRTAYMEAL-----SSGKKTDIVDVMSATKAAMKAVIADKIRL 1366
Cdd:PRK13399 243 eiinayggkmketygvpveeIQRGIKHGVRKVNIDTDIRLAMTGAIrkvlaEHPSEFDPRKALKPAMKAMTALCKQRFEA 322
|
....*..
gi 22329645 1367 FGSAGKA 1373
Cdd:PRK13399 323 FGTAGQA 329
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
323-483 |
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 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGhLGAV 402
Cdd:pfam03446 1 KIGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 403 EAIPSGATVVLASTVSPAFVSQLERRLENegKDLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLYV 482
Cdd:pfam03446 80 PGLKPGDIIIDGSTSSPEDARRRAKELKE--KGLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVTY 157
|
.
gi 22329645 483 I 483
Cdd:pfam03446 158 I 158
|
|
| PRK07084 |
PRK07084 |
class II fructose-1,6-bisphosphate aldolase; |
1098-1373 |
4.31e-37 |
|
class II fructose-1,6-bisphosphate aldolase;
Pssm-ID: 180829 Cd Length: 321 Bit Score: 142.94 E-value: 4.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1098 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPGAFKQGGIPLVS-CCISAAEQAR-----VPISVH 1171
Cdd:PRK07084 12 TREMFAKAVKGGYAIPAYNFNNMEQLQAIIQACVETKSPVILQVSKGARKYANATLLRyMAQGAVEYAKelgcpIPIVLH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1172 FDHGTTKHELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELGRLSGTEDGLTVEdyEAKLTNVNQA 1251
Cdd:PRK07084 92 LDHGDSFELCKDCIDSGFSSVMIDGSHLPYEENVALTKKVVEYAHQFDVTVEGELGVLAGVEDEVSAE--HHTYTQPEEV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1252 QEFME-TGIDALAVCIGNVHGKYP-KSG---PNLKLDLLKELhalsSKK--GVFLVLHGASGLSENLIKECIENG----- 1319
Cdd:PRK07084 170 EDFVKkTGVDSLAISIGTSHGAYKfKPGqcpPPLRFDILEEI----EKRipGFPIVLHGSSSVPQEYVKTINEYGgklkd 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22329645 1320 ----------------VRKFNVNTEVRTAYMEALSS--GKKTDIVD---VMSATKAAMKAVIADKIR-LFGSAGKA 1373
Cdd:PRK07084 246 aigipeeqlrkaaksaVCKINIDSDGRLAMTAAIRKvfDEKPEEFDprkYLGPARDELKKLYKHKIInVLGSNGKA 321
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
324-615 |
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 22329645 324 IGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAVE 403
Cdd:PRK15461 4 IAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVCE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 404 AIPSGATVVLASTVSPAFVSQLERRLENEGkdLKLVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLyVI 483
Cdd:PRK15461 84 GLSRDALVIDMSTIHPLQTDKLIADMQAKG--FSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNEL-IN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 484 KGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGG------TSWmfENRVphmLDNDYTPYSAL 557
Cdd:PRK15461 161 AGGPGMGIRVKLINNYMSIALNALSAEAAVLCEALGLSFDVALKVMSGTAAgkghftTTW--PNKV---LKGDLSPAFMI 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 22329645 558 DIFVKDLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIK 615
Cdd:PRK15461 236 DLAHKDLGIALDVANQLHVPMPLGAASREVYSQARAAGRGRQDWSAILEQVRVSAGLT 293
|
|
| FTBP_aldolase_II |
cd00453 |
Fructose/tagarose-bisphosphate aldolase class II. This family includes fructose-1, ... |
1098-1370 |
7.49e-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: 7.49e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1098 TKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHP-GAFKQGGIPLVSC----------------CISA 1160
Cdd:cd00453 1 VQKVFQVAKENNFALPAVNCVGTDSINAVLETAAKVKAPVIVQFSNgGASFIAGKGVKSDvpqgaailgaisgahhVHQM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1161 AEQARVPISVHFDHGTTK-------------HELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMVEAELG 1227
Cdd:cd00453 81 AEHYGVPVILHTDHCAKKllpwidglldageKHFAATGKPLFSSHMIDLSEESLQENIEICSKYLERMSKIGMTLEIELG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1228 RLSGTEDGLTVE--DYEAKLTNVNQAQEFME-----TGIDALAVCIGNVHGKYPKSGPNLKLDLLKELHALSSKKG---- 1296
Cdd:cd00453 161 CTGGEEDGVDNShmDASALYTQPEDVDYAYTelskiSPRFTIAASFGNVHGVYKKGNVVLTPTILRDSQEYVSKKHnlph 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1297 --VFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYMEA---------------LSSGKKTDIVDV--------MSA 1351
Cdd:cd00453 241 nsLNFVFHGGSGSTAQEIKDSVSYGVVKMNIDTDTQWATWEGvlnyykaneaylqgqLGNPKGEDQPNKkyydprvwLRA 320
|
330
....*....|....*....
gi 22329645 1352 TKAAMKAVIADKIRLFGSA 1370
Cdd:cd00453 321 GQTSMIARLEKAFQELNAI 339
|
|
| NBD_C |
pfam17042 |
Nucleotide-binding C-terminal domain; This is the C-terminal domain found in proteins in a ... |
917-1083 |
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 22329645 917 LIVVGSYVPKTTKQVEELQSQHnqNLRSIEISVEKVAlkSSEVRDEEIRRAVEMADAFLRAGRETLIMSSRELITGKTsS 996
Cdd:pfam17042 1 LVVVGSCSPKTTAQLAALLAER--GVVVVELDVEALL--DEEAREEEIERALAEALAALASGKDVVVYTSRGPEDVAA-L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 997 ESLDIN-------SKVSSALVEVVSQISTRP--RYILAkGGITSSDTAtKALKARRALVIGQALAGVPVWKLgpeSRHPG 1067
Cdd:pfam17042 76 DSLQAAlglsragARISAALAEIARGLLARGvrGLVVA-GGDTSGAVL-KALGIRGLRVLGEIAPGVPLGRL---IGAPG 150
|
170
....*....|....*.
gi 22329645 1068 VPYIVFPGNVGNSTAL 1083
Cdd:pfam17042 151 LPVVLKGGNFGDEDAL 166
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
488-608 |
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 22329645 488 GAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPH-MLDNDYTPYSALDIFVKDLGI 566
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPQrVLSRDFDPGFALDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 22329645 567 VTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVY 608
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIRLL 122
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
323-616 |
2.02e-29 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 119.74 E-value: 2.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFSVcGYDVYKPTLVRFENAGGLAANSPAEVTKDVDVLVIMVTNEVQAEDVLYGHLGAV 402
Cdd:PRK15059 2 KLGFIGLGIMGTPMAINLARAGHQL-HVTTIGPVADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 403 EAIPSGATVVLASTVSPAFVSQLERRLENEGKDLklVDAPVSGGVKRAAMGELTIMASGTDEALKSAGLVLSALSEKLYV 482
Cdd:PRK15059 81 KASLKGKTIVDMSSISPIETKRFARQVNELGGDY--LDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNITL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 483 IkGGCGAGSGVKMVNQLLAGVHIASAAEAMAFGARLGLNTRKLFNVISNSGGTSWMFENRVPHMLDNDYTPYSALDIFVK 562
Cdd:PRK15059 159 V-GGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 22329645 563 DLGIVTREGSSRKVPLHISTVAHQLFLAGSAAGWGRIDDAGVVKVYETLAGIKV 616
Cdd:PRK15059 238 DLNLALQSAKALALNLPNTATCQELFNTCAANGGSQLDHSALVQALELMANHKL 291
|
|
| PRK15461 |
PRK15461 |
sulfolactaldehyde 3-reductase; |
4-266 |
1.03e-28 |
|
sulfolactaldehyde 3-reductase;
Pssm-ID: 185358 [Multi-domain] Cd Length: 296 Bit Score: 117.65 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 4 VVGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAVVVVLSHPDQIQDVIFGDEGVM 83
Cdd:PRK15461 3 AIAFIGLGQMGSPMASNLLKQGHQLQVFDVNPQAVDALVDKGATPAASPAQAAAGAEFVITMLPNGDLVRSVLFGENGVC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 84 KGLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLYT 163
Cdd:PRK15461 83 EGLSRDALVIDMSTIHPLQTDKLIADMQAK--GFSMMDVPVGRTSDNAITGTLLLLAGGTAEQVERATPILMAMGNELIN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 164 fEGEIGAGSKVKMVNELLeGIHLVA-AVEAISLGSQAGVHPWILYDIIS-NAAG-----NSWIYKnhiplLLKDDIEGRF 236
Cdd:PRK15461 161 -AGGPGMGIRVKLINNYM-SIALNAlSAEAAVLCEALGLSFDVALKVMSgTAAGkghftTTWPNK-----VLKGDLSPAF 233
|
250 260 270
....*....|....*....|....*....|.
gi 22329645 237 L-DVLSQNLAIVEDKAKSLPFPVPLLAVARQ 266
Cdd:PRK15461 234 MiDLAHKDLGIALDVANQLHVPMPLGAASRE 264
|
|
| garR |
PRK11559 |
tartronate semialdehyde reductase; Provisional |
1-296 |
5.98e-28 |
|
tartronate semialdehyde reductase; Provisional
Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 115.53 E-value: 5.98e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1 MSGVVGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAVVVVLSHPDQIQDVIFGDE 80
Cdd:PRK11559 1 MTMKVGFIGLGIMGKPMSKNLLKAGYSLVVYDRNPEAVAEVIAAGAETASTAKAVAEQCDVIITMLPNSPHVKEVALGEN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 81 GVMKGLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQN 160
Cdd:PRK11559 81 GIIEGAKPGTVVIDMSSIAPLASREIAAALKAK--GIEMLDAPVSGGEPKAIDGTLSVMVGGDKAIFDKYYDLMKAMAGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 161 LyTFEGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDDIEGRF-LDV 239
Cdd:PRK11559 159 V-VHTGDIGAGNVTKLANQVIVALNIAAMSEALVLATKAGVNPDLVYQAIRGGLAGSTVLDAKAPMVMDRNFKPGFrIDL 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 22329645 240 LSQNLAIVEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAKISEKVLGVGI 296
Cdd:PRK11559 238 HIKDLANALDTSHGVGAPLPLTAAVMEMMQALKADGLGTADHSALACYYEKLAKVEV 294
|
|
| FBP_aldolase_IIA |
cd00946 |
Class II Type A, Fructose-1,6-bisphosphate (FBP) aldolases. The enzyme catalyses the ... |
1095-1335 |
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 22329645 1095 GRSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPG--AFKQG-GIP------LVSCCISAAEQAR 1165
Cdd:cd00946 1 GDDVLKLFDYAKENGFAIPAVNCTSSSTINAVLEAARDAKSPIIIQFSNGgaAFYAGkGLKnekqkaSIAGAIAAAHHVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1166 -------VPISVHFDHGTTKHELLEALELGLD-------------SVMVDGSHLSFTENLSYTKSITELARSKNIMVEAE 1225
Cdd:cd00946 81 smaehygVPVVLHTDHCAKKLLPWFDGLLEADeeyfkqhgeplfsSHMLDLSEEPLEENIEICKKYLERMAKINMWLEME 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1226 LGRLSGTEDGltVEDYEAKLTNVNQAQEFMETGIDAL---------AVCIGNVHGKYpKSGpNLKL---------DLLKE 1287
Cdd:cd00946 161 IGITGGEEDG--VDNSGVDNAELYTQPEDVWYVYEALskispnfsiAAAFGNVHGVY-KPG-NVKLqpeilgehqDYVRE 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 22329645 1288 LHALSSKKGVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1335
Cdd:cd00946 237 KLGLADDKPLYFVFHGGSGSTKEEIREAISYGVVKMNIDTDTQWAYWE 284
|
|
| NAD_binding_11 |
pfam14833 |
NAD-binding of NADP-dependent 3-hydroxyisobutyrate dehydrogenase; 3-Hydroxyisobutyrate is a ... |
169-286 |
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 22329645 169 GAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIP-LLLKDDIEGRF-LDVLSQNLAI 246
Cdd:pfam14833 1 GAGQAVKAANNLLVAINLAATSEALALAVKAGLDPEVVLEVLNGGSGRSNALENKFPqRVLSRDFDPGFaLDLMLKDLGL 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 22329645 247 VEDKAKSLPFPVPLLAVARQQLISGISQMQGDDTATSLAK 286
Cdd:pfam14833 81 ALDLARALGVPLPLTALAAQLYQAAAAQGGGDADHSAIIR 120
|
|
| PRK09197 |
PRK09197 |
fructose-bisphosphate aldolase; Provisional |
1092-1335 |
6.10e-17 |
|
fructose-bisphosphate aldolase; Provisional
Pssm-ID: 236406 Cd Length: 350 Bit Score: 84.08 E-value: 6.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1092 VVAGRSTKELLLNAEKGGYAVGAFNVYNLEGIEAVVAAAEEENSPAILQVHPG--AFKQG-GIPLVSC------CISAAE 1162
Cdd:PRK09197 3 VATGEDYQEMFDRAKENGFALPAVNVVGTDSINAVLEGAAEAKSPVIIQFSNGgaAFIAGkGVKDDGQgaavlgAIAGAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1163 QAR-------VPISVHFDHGTTKH-------------ELLEALELGLDSVMVDGSHLSFTENLSYTKSITELARSKNIMV 1222
Cdd:PRK09197 83 HVHevaehygVPVILHTDHCAKKLlpwidglldagekHFAAGGKPLFSSHMIDLSEEPLEENIEICSKYLERMAKAGMTL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 1223 EAELGRLSGTEDGLTVEDYE-AKL-TnvnQAQEFMETgIDAL---------AVCIGNVHGKYpKSGpNLKL--DLLKELH 1289
Cdd:PRK09197 163 EIELGVTGGEEDGVDNSHEDnSKLyT---QPEDVLYA-YEALgkisgrftiAASFGNVHGVY-KPG-NVKLrpEILKDSQ 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 22329645 1290 ALSSKK------GVFLVLHGASGLSENLIKECIENGVRKFNVNTEVRTAYME 1335
Cdd:PRK09197 237 EYVSKKfglpakPFDFVFHGGSGSTLEEIREAVSYGVVKMNIDTDTQWAFWR 288
|
|
| NAD_binding_2 |
pfam03446 |
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
5-162 |
8.10e-17 |
|
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: 79.05 E-value: 8.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 5 VGFVGLDSFSFELASSLLRSGFKVQAFEISTELVEKFIELGGHKCDSPADVGKAAAAVVVVLSHPDQIQDVIFGdEGVMK 84
Cdd:pfam03446 2 IGFIGLGVMGSPMALNLLKAGYTVTVYNRTPEKVEELVAAGAIAAASPAEFVAGLDVVITMVPAGAAVDAVIFG-EGLLP 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22329645 85 GLQKDAVLLLSSTISTLQLQKLEKQLTEKreQIFVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLY 162
Cdd:pfam03446 81 GLKPGDIIIDGSTSSPEDARRRAKELKEK--GLHFLDAPVSGGEAGAENGTLSIMVGGDEEAFERVKPILEAMGACVT 156
|
|
| PRK15059 |
PRK15059 |
2-hydroxy-3-oxopropionate reductase; |
5-257 |
2.15e-13 |
|
2-hydroxy-3-oxopropionate reductase;
Pssm-ID: 185019 [Multi-domain] Cd Length: 292 Bit Score: 72.36 E-value: 2.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 5 VGFVGLDSFSFELASSLLRSGFKVQAFEISTeLVEKFIELGGHKCDSPADVGKAAAAVVVVLSHPDQIQDVIFGDEGVMK 84
Cdd:PRK15059 3 LGFIGLGIMGTPMAINLARAGHQLHVTTIGP-VADELLSLGAVSVETARQVTEASDIIFIMVPDTPQVEEVLFGENGCTK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 85 GLQKDAVLLLSSTISTLQLQKLEKQLTEKREQifVVDAYVLKGMSELLDGKLMIIASGRSDSITRAQPYLTAMCQNLyTF 164
Cdd:PRK15059 82 ASLKGKTIVDMSSISPIETKRFARQVNELGGD--YLDAPVSGGEIGAREGTLSIMVGGDEAVFERVKPLFELLGKNI-TL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 165 EGEIGAGSKVKMVNELLEGIHLVAAVEAISLGSQAGVHPWILYDIISNAAGNSWIYKNHIPLLLKDDIEGRFLDVLSQ-- 242
Cdd:PRK15059 159 VGGNGDGQTCKVANQIIVALNIEAVSEALLFASKAGADPVRVRQALMGGFASSRILEVHGERMIKRTFNPGFKIALHQkd 238
|
250
....*....|....*.
gi 22329645 243 -NLAIVEDKAKSLPFP 257
Cdd:PRK15059 239 lNLALQSAKALALNLP 254
|
|
| PRK09599 |
PRK09599 |
NADP-dependent phosphogluconate dehydrogenase; |
323-496 |
8.06e-11 |
|
NADP-dependent phosphogluconate dehydrogenase;
Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 64.77 E-value: 8.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVD---VLVIMV-----TNEVQAEdv 394
Cdd:PRK09599 2 QLGMIGLGRMGGNMARRLLRGGHEVVGYDRNPEAVEALAEEGATGADSLEELVAKLPaprVVWLMVpageiTDATIDE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 395 LYGHLGAVEAIPSGATvvlastvspAFVSQLERRLEN-EGKDLKLVDAPVSGGVKRAAMGeLTIMASGTDEALKSAGLVL 473
Cdd:PRK09599 80 LAPLLSPGDIVIDGGN---------SYYKDDIRRAELlAEKGIHFVDVGTSGGVWGLERG-YCLMIGGDKEAVERLEPIF 149
|
170 180
....*....|....*....|....*.
gi 22329645 474 SALS---EKLYVIKGGCGAGSGVKMV 496
Cdd:PRK09599 150 KALApraEDGYLHAGPVGAGHFVKMV 175
|
|
| YqeC |
COG1023 |
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism]; |
323-496 |
1.61e-10 |
|
6-phosphogluconate dehydrogenase (decarboxylating) [Carbohydrate transport and metabolism];
Pssm-ID: 440646 [Multi-domain] Cd Length: 300 Bit Score: 63.96 E-value: 1.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVRFENAGGLAANSPAEVTKDVD---VLVIMV-----TNEVQAEdv 394
Cdd:COG1023 2 QIGMIGLGKMGGNMARRLLRHGHEVVGYDRNPEAVAALAAEGATGADSLEELVAKLPaprVVWLMVpageiTDQVIEE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 395 LYGHLGAVEAIPSGA------TVVLASTVSPafvsqlerrlenegKDLKLVDAPVSGGVKRAAMGeLTIMASGTDEALKS 468
Cdd:COG1023 80 LAPLLEPGDIVIDGGnsnykdDIRRAEELAE--------------KGIHFVDVGTSGGVWGLENG-YCLMIGGDKEAVER 144
|
170 180 190
....*....|....*....|....*....|.
gi 22329645 469 AGLVLSALS---EKLYVIKGGCGAGSGVKMV 496
Cdd:COG1023 145 LEPIFKALApgaENGYLHCGPVGAGHFVKMV 175
|
|
| ProC |
COG0345 |
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
323-439 |
2.67e-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: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22329645 323 RIGFIGLGAMGFGMAAHLLKSNFS---VCGYDVYKPTLVRFENAGGL-AANSPAEVTKDVDVLVIMVTNEvQAEDVLygh 398
Cdd:COG0345 4 KIGFIGAGNMGSAIIKGLLKSGVPpedIIVSDRSPERLEALAERYGVrVTTDNAEAAAQADVVVLAVKPQ-DLAEVL--- 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 22329645 399 LGAVEAIPSGATVV-LASTVSpafVSQLERRLeneGKDLKLV 439
Cdd:COG0345 80 EELAPLLDPDKLVIsIAAGVT---LATLEEAL---GGGAPVV 115
|
|
| PRK06130 |
PRK06130 |
3-hydroxybutyryl-CoA dehydrogenase; Validated |
320-359 |
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 22329645 320 PVNRIGFIGLGAMGFGMAAHLLKSNFSVCGYDVYKPTLVR 359
Cdd:PRK06130 3 PIQNLAIIGAGTMGSGIAALFARKGLQVVLIDVMEGALER 42
|
|
| PLN02688 |
PLN02688 |
pyrroline-5-carboxylate reductase |
322-385 |
7.57e-03 |
|
pyrroline-5-carboxylate reductase
Pssm-ID: 178291 [Multi-domain] Cd Length: 266 Bit Score: 39.94 E-value: 7.57e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 22329645 322 NRIGFIGLGAMGFGMAAHLLKSNF----SVCGYDVYKPTLVR-FENAGGLAANSPAEVTKDVDVLVIMV 385
Cdd:PLN02688 1 FRVGFIGAGKMAEAIARGLVASGVvppsRISTADDSNPARRDvFQSLGVKTAASNTEVVKSSDVIILAV 69
|
|
| |
