|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
42-501 |
0e+00 |
|
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is part of the Pathway/BioSystem: TCA cycle
Pssm-ID: 439884 [Multi-domain] Cd Length: 461 Bit Score: 912.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 42 FRTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVI 120
Cdd:COG0114 4 TRIEKDSMGEVEVPADAYWGAQTQRSLENFPIG--GERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 121 SGKLykQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNER 200
Cdd:COG0114 82 AGKL--DDHFPLDVWQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTR 280
Cdd:COG0114 160 LLPALEHLRDTLEAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSS 360
Cdd:COG0114 240 PGFAERVAAELAELTGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 361 IMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERID 440
Cdd:COG0114 320 IMPGKVNPTQCEALTMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIE 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78710009 441 KIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVNPKEMLG 501
Cdd:COG0114 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGRTLREAALELGlLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
42-503 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 908.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 42 FRTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVI 120
Cdd:PRK00485 4 TRIEKDSMGEVEVPADALWGAQTQRSLENFPIG--GERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 121 SGKLykQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNER 200
Cdd:PRK00485 82 AGKH--DDHFPLDVWQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVER 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTR 280
Cdd:PRK00485 160 LLPALEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSS 360
Cdd:PRK00485 240 PGFAERVAEELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 361 IMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERID 440
Cdd:PRK00485 320 IMPGKVNPTQCEALTMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIK 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78710009 441 KIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVNPKEMLGPK 503
Cdd:PRK00485 400 ELLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGyLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
43-499 |
0e+00 |
|
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial fumarase, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176465 [Multi-domain] Cd Length: 455 Bit Score: 892.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVIS 121
Cdd:cd01362 1 RIEKDSMGEVEVPADALWGAQTQRSLENFPIG--GERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 122 GKLykQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNERL 201
Cdd:cd01362 79 GKL--DDHFPLVVWQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 202 VPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRK 281
Cdd:cd01362 157 LPALKHLIDALDAKADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 282 GFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSSI 361
Cdd:cd01362 237 GFAEKVAAELAELTGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSI 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 362 MPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDK 441
Cdd:cd01362 317 MPGKVNPTQCEALTMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAE 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 78710009 442 IMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVNPKEM 499
Cdd:cd01362 397 LLERSLMLVTALNPHIGYDKAAKIAKKAHKEGLTLKEAALELGyLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
49-502 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 813.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 49 FGELKVPADKLYGAQTMRSKLNFPIGDIGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVISGKLYKq 127
Cdd:PLN00134 1 MGPIQVPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDD- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 128 gHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNERLVPAVTH 207
Cdd:PLN00134 80 -HFPLVVWQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 208 LRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRKGFAEKV 287
Cdd:PLN00134 159 LHESLRAKSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKI 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 288 AKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSSIMPGKVN 367
Cdd:PLN00134 239 AAAVAEETGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVN 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 368 PTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDKIMNESL 447
Cdd:PLN00134 319 PTQCEALTMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESL 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 78710009 448 MLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTGI-TEEQFKEWVNPKEMLGP 502
Cdd:PLN00134 399 MLVTALNPKIGYDKAAAVAKKAHKEGTTLKEAALKLGVlTAEEFDELVVPEKMTGP 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
43-495 |
0e+00 |
|
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.
Pssm-ID: 176468 [Multi-domain] Cd Length: 450 Bit Score: 813.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVIS 121
Cdd:cd01596 1 RIEKDSLGEVEVPADAYYGAQTQRALENFPIS--GERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 122 GKLykQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGsKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNERL 201
Cdd:cd01596 79 GKL--DDQFPLDVWQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 202 VPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRK 281
Cdd:cd01596 156 LPALEQLQDALDAKAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 282 GFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSSI 361
Cdd:cd01596 236 GYAEKVAAELAELTGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 362 MPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDK 441
Cdd:cd01596 316 MPGKVNPVIPEAVNMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 78710009 442 IMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVN 495
Cdd:cd01596 396 YVENSLMLVTALNPHIGYEKAAEIAKEALKEGRTLREAALELGlLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
42-501 |
0e+00 |
|
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium tuberculosis, Streptomyces coelicolor, Pseudomonas aeruginosa) branch deeply, although within the same branch of a phylogenetic tree rooted by aspartate ammonia-lyase sequences, and score between the trusted and noise cutoffs. [Energy metabolism, TCA cycle]
Pssm-ID: 130052 [Multi-domain] Cd Length: 458 Bit Score: 801.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 42 FRTEKDTFGELKVPADKLYGAQTMRSKLNFPIGDigERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVI 120
Cdd:TIGR00979 1 FRIEKDSMGEIQVPADKYWGAQTQRSLENFKIGT--EKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEIL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 121 SGKLykQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNER 200
Cdd:TIGR00979 79 AGKL--DDHFPLVVWQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTR 280
Cdd:TIGR00979 157 LIPALENLKKTLDAKSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSS 360
Cdd:TIGR00979 237 PGFDEKVAEEIAKETGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSS 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 361 IMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERID 440
Cdd:TIGR00979 317 IMPGKVNPTQCEALTMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQ 396
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78710009 441 KIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVNPKEMLG 501
Cdd:TIGR00979 397 QLLNNSLMLVTALNPHIGYDNAAKIAKKAHKEGITLKEAALELGlLSEEEFDEWVVPEQMVG 458
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
43-503 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 600.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMP--VIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDV 119
Cdd:COG1027 1 RIEKDLLGEREVPADAYYGIQTLRALENFPIS--GRPISDHpeLIRALAMVKKAAALANRELGlLDKEKADAIVAACDEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 120 ISGKLYKQghFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVgMELNE 199
Cdd:COG1027 79 IAGKLHDQ--FVVDVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 200 RLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNT 279
Cdd:COG1027 156 ELLEALERLQEAFAAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 280 RKGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGS 359
Cdd:COG1027 236 PPGYIELVVEHLAEITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 360 SIMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERI 439
Cdd:COG1027 316 SIMPGKVNPVIPEVVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERC 395
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 78710009 440 DKIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVNPKEMLGPK 503
Cdd:COG1027 396 REYVENSIGLVTALNPYIGYEKAAEIAKEALATGKSVRELVLEKGlLTEEELDEILDPENMTGPG 460
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
43-502 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 587.66 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIGDigERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVIS 121
Cdd:PRK12425 3 RTETDSLGPIEVPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 122 GKlyKQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNERL 201
Cdd:PRK12425 81 GQ--HDDQFPLVVWQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 202 VPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRK 281
Cdd:PRK12425 159 LPAIAELSGGLAEQSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 282 GFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSSI 361
Cdd:PRK12425 239 GFAEAIAAELAALSGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 362 MPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDK 441
Cdd:PRK12425 319 MPGKVNPTQCEALSMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAA 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78710009 442 IMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKEWVNPKEMLGP 502
Cdd:PRK12425 399 HLERGLMLVTALNPHIGYDKAAEIAKKAYAEGTTLREAALALGyLTDEQFDAWVRPENMLEA 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
42-503 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 575.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 42 FRTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERM-PMPV-IQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDD 118
Cdd:PRK12273 5 TRIEKDLLGEREVPADAYYGIHTLRAVENFPIS--GVKIsDYPElIRALAMVKKAAALANKELGlLDEEKADAIVAACDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 119 VISGKLYKQghFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVgMELN 198
Cdd:PRK12273 83 ILAGKLHDQ--FVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 199 ERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLN 278
Cdd:PRK12273 160 RKLLDALEQLQEAFEAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLN 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 279 TRKGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPG 358
Cdd:PRK12273 240 APPGYIELVVEKLAEITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 359 SSIMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKER 438
Cdd:PRK12273 320 SSIMPGKVNPVIPEVVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEER 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 78710009 439 IDKIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTGI-TEEQFKEWVNPKEMLGPK 503
Cdd:PRK12273 400 CREYVENSIGIVTALNPYIGYENAAEIAKEALETGKSVRELVLERGLlTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
43-492 |
0e+00 |
|
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.
Pssm-ID: 176462 [Multi-domain] Cd Length: 450 Bit Score: 562.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVIS 121
Cdd:cd01357 1 RIEHDLLGEREVPADAYYGIQTLRALENFPIS--GLKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 122 GKLYKQghFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVgMELNERL 201
Cdd:cd01357 79 GKLHDQ--FVVDVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLAL-ILLLRKL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 202 VPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRK 281
Cdd:cd01357 156 LDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 282 GFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSSI 361
Cdd:cd01357 236 GYIELVVEKLSEITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 362 MPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDK 441
Cdd:cd01357 316 MPGKVNPVIPEVVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCRE 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 78710009 442 IMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTG-ITEEQFKE 492
Cdd:cd01357 396 YVENSIGIVTALNPYIGYEAAAEIAKEALETGRSVRELVLEEGlLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
42-503 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 543.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 42 FRTEKDTFGELKVPADKLYGAQTMRSKLNFPIGdiGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVI 120
Cdd:PRK13353 5 MRIEHDLLGEKEVPAEAYYGIQTLRAVENFPIT--GYKIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACDEIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 121 SGKLykQGHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELnER 200
Cdd:PRK13353 83 AGKL--HDQFIVDPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLL-EG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTR 280
Cdd:PRK13353 160 LLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNAD 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSS 360
Cdd:PRK13353 240 PEYIERVVKHLAAITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 361 IMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERID 440
Cdd:PRK13353 320 IMPGKVNPVMPEVVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCK 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78710009 441 KIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTGI-TEEQFKEWVNPKEMLGPK 503
Cdd:PRK13353 400 EYVEKSVGIATALNPHIGYEAAARIAKEAIATGRSVRELALENGLlSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
43-502 |
8.09e-152 |
|
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a number of other lyases, as modeled by pfam00206. Fumarate hydratase scores as high as 570 bits against this model. [Energy metabolism, Amino acids and amines]
Pssm-ID: 213564 [Multi-domain] Cd Length: 468 Bit Score: 441.58 E-value: 8.09e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIGDIGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVI- 120
Cdd:TIGR00839 1 RIEEDLLGEREVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILn 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 121 SGKLYKQghFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVgMELNER 200
Cdd:TIGR00839 81 NGKCHDQ--FPVDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAV-YSSLIK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTR 280
Cdd:TIGR00839 158 LVDAINQLRDGFEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTP 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSS 360
Cdd:TIGR00839 238 PEYSPLVVKKLAEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 361 IMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERID 440
Cdd:TIGR00839 318 IMPAKVNPVVPEVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICE 397
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 78710009 441 KIMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTGI-TEEQFKEWVNPKEMLGP 502
Cdd:TIGR00839 398 GYVFNSIGIVTYLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLlTEEELDDIFSVENLMHP 460
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
43-502 |
3.98e-139 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 409.77 E-value: 3.98e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 43 RTEKDTFGELKVPADKLYGAQTMRSKLNFPIgdIGERMPMPVIQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVIS 121
Cdd:PRK14515 12 RIEKDFLGEKEVPNYAYYGVQTMRAVENFPI--TGYKIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQEILD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 122 GKLYKqgHFPLVIWQTGSGTQTNMNTNEVISNAAIKMMGGELGSKKPVHPNDHVNKSQSSNDTFPTAIHISVgMELNERL 201
Cdd:PRK14515 90 GKWHD--HFIVDPIQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALEGL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 202 VPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRK 281
Cdd:PRK14515 167 LQTMGYMHDVFELKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADP 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 282 GFAEKVAKRISELTCLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPENEPGSSI 361
Cdd:PRK14515 247 EYIEAVVKHLAAISELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 362 MPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDK 441
Cdd:PRK14515 327 MPGKVNPVMPEVINQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKE 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 78710009 442 IMNESLMLVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTGI-TEEQFKEWVNPKEMLGP 502
Cdd:PRK14515 407 YVEKSVGIITAVNPHIGYEAAARVAKEAIATGQSVRELCVKNGVlSQEDLELILDPFEMTHP 468
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
50-383 |
1.85e-137 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 399.05 E-value: 1.85e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 50 GELKVPADKLYGAQTMRSKLNFPIGDigermpmPVIQAMGILKKACAEVNKDYGldgKVSDAVSCACDDVI-SGKLykQG 128
Cdd:pfam00206 1 GRFTVPADALMGIFTDRSRFNFRLGE-------EDIKGLAALKKAAAKANVILK---EEAAAIIKALDEVAeEGKL--DD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 129 HFPLVIWQTGSGTQTNMNTNEVIsnaaikmmgGELgSKKPVHPNDHVNKSQSSNDTFPTAIHISVGMELNERLVPAVTHL 208
Cdd:pfam00206 69 QFPLKVWQEGSGTAVNMNLNEVI---------GEL-LGQLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 209 RDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRV-YELALGGTAVGTGLNTRKGFAEKV 287
Cdd:pfam00206 139 IDALKEKAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRLlVLPLGGGTAVGTGLNADPEFAELV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 288 AKRISELTCLPfVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPrCGLGELMLPENEPGSSIMPGKVN 367
Cdd:pfam00206 219 AKELGFFTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVN 296
|
330
....*....|....*.
gi 78710009 368 PTQCESMTMLCAQVMG 383
Cdd:pfam00206 297 PDQLELLTGKAGRVMG 312
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
85-435 |
1.57e-122 |
|
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.
Pssm-ID: 176461 [Multi-domain] Cd Length: 325 Bit Score: 361.43 E-value: 1.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 85 IQAMGILKKACAEVNKDYG-LDGKVSDAVSCACDDVISGKlykqghFPLVIWQTGSGTQTNMNTNEVISNAAikmmgGEL 163
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGI------AADQVEQEGSGTHDVMAVEEVLAERA-----GEL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 164 gskkpvhPNDHVNKSQSSNDTFPTAIHISVgMELNERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFS 243
Cdd:cd01334 70 -------NGGYVHTGRSSNDIVDTALRLAL-RDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELA 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 244 GYTQQLTNGLERIKGCLPRVYELALGGTAVGTGLNTRKGFAEKVAKRISEltclpFVSAPNKFEALAARDAMVEVHGVLN 323
Cdd:cd01334 142 AWAAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAELLGF-----FGPAPNSTQAVSDRDFLVELLSALA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 324 TIAVSLMKIANDIRLLGSGprcGLGELMLPEN-EPGSSIMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVF 402
Cdd:cd01334 217 LLAVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVD 293
|
330 340 350
....*....|....*....|....*....|...
gi 78710009 403 KPLVVSNVLRSIRLLADGSMTFSKNCvEGLQAN 435
Cdd:cd01334 294 SPVEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
145-419 |
6.70e-63 |
|
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.
Pssm-ID: 176466 [Multi-domain] Cd Length: 231 Bit Score: 204.76 E-value: 6.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 145 MNTNEVISNAAIKMMGGELGSKkpvhpndHVNKSQSSNDtFPTAIHISVGMELNERLVPAVTHLRDALKSKSDEFKDIIK 224
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 225 IGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGClprvyelalggtavgtglntrkgfaekvakriseltclpfvsapn 304
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 305 kfealaardAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRCGLGELMLPeNEPGSSIMPGKVNPTQCESMTMLCAQVMGN 384
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270
....*....|....*....|....*....|....*
gi 78710009 385 QVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLAD 419
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLID 225
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
199-501 |
2.63e-33 |
|
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis
Pssm-ID: 439786 [Multi-domain] Cd Length: 436 Bit Score: 130.97 E-value: 2.63e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 199 ERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGtAVGTgLN 278
Cdd:COG0015 116 ELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT-YA 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 279 TRKGFAEKVAKRISE---LTCLPFVS--APnkfealaaRDAMVEVHGVLNTIAVSLMKIANDIRLLGsgpRCGLGELMLP 353
Cdd:COG0015 194 AHGEAWPEVEERVAEklgLKPNPVTTqiEP--------RDRHAELFSALALIAGSLEKIARDIRLLQ---RTEVGEVEEP 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 354 --ENEPGSSIMPGKVNPTQCESMTMLCAQVMGNQVAV----------TIGGSngHFELnvfkplvvsNVLRSIRLLADGS 421
Cdd:COG0015 263 faKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALlealaswherDLSDS--SVER---------NILPDAFLLLDGA 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 422 MTFSKNCVEGLQANKERIDKIMNESLMLV------TALNPH-IGYDKA-ALI---AKTAHKNKTTLKE-----EALKTGI 485
Cdd:COG0015 332 LERLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGREEAyELVkelARGAWEEGNDLREllaadPEIPAEL 411
|
330
....*....|....*.
gi 78710009 486 TEEQFKEWVNPKEMLG 501
Cdd:COG0015 412 SKEELEALFDPANYLG 427
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
208-501 |
6.41e-31 |
|
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.
Pssm-ID: 176469 [Multi-domain] Cd Length: 437 Bit Score: 124.28 E-value: 6.41e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 208 LRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGtAVGT-------GLNTR 280
Cdd:cd01597 125 LLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGTlaslgdqGLAVQ 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVakrisELTClPFVSapnkfeALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGsgpRCGLGELMLP--ENEPG 358
Cdd:cd01597 204 EALAAEL-----GLGV-PAIP------WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIGEVAEPfaKGRGG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 359 SSIMPGKVNPTQCESMTMLCAQVMGnQVAVTI---------GGSNGHFELnvfkplvvsNVLRSIRLLADGSMTFSKNCV 429
Cdd:cd01597 269 SSTMPHKRNPVGCELIVALARRVPG-LAALLLdamvqeherDAGAWHAEW---------IALPEIFLLASGALEQAEFLL 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 430 EGLQANKERIDK--------IMNESLMLvtALNPHIGYDKA----ALIAKTAHKNKTTLKEE-----ALKTGITEEQFKE 492
Cdd:cd01597 339 SGLEVNEDRMRAnldltgglILSEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVlledpEVAAYLSDEELDA 416
|
....*....
gi 78710009 493 WVNPKEMLG 501
Cdd:cd01597 417 LLDPANYLG 425
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
178-462 |
1.22e-30 |
|
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176467 [Multi-domain] Cd Length: 381 Bit Score: 122.61 E-value: 1.22e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 178 SQSSNDTfPTAIHISVGMELnerLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIK 257
Cdd:cd01595 89 SQDINDT-ALALQLRDALDI---ILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLE 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 258 GCLPRVYELALGGtAVGTGLNtrkgFAEKVAKrISELTC----LPFVSAPNKFEAlaaRDAMVEVHGVLNTIAVSLMKIA 333
Cdd:cd01595 165 EARERVLVGGISG-AVGTHAS----LGPKGPE-VEERVAeklgLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIA 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 334 NDIRLLGsgpRCGLGELMLP--ENEPGSSIMPGKVNPTQCESMTMLCAQVMGNQVAV----------TIGGSngHFElnv 401
Cdd:cd01595 236 TDIRLLQ---RTEIGEVEEPfeKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPAlenlvqwherDLSDS--SVE--- 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 402 fkplvvSNVLRSIRLLADGSMTFSKNCVEGLQANKERIDK--------IMNESLMlvTALNPH-IGYDKA 462
Cdd:cd01595 308 ------RNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRnldltwglILSEAVM--MALAKKgLGRQEA 369
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
174-501 |
2.69e-27 |
|
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that catalyzes step 8 in the purine biosynthesis pathway for de novo synthesis of IMP and also the final reaction in the two-step sequence from IMP to AMP. [Purines, pyrimidines, nucleosides, and nucleotides, Purine ribonucleotide biosynthesis]
Pssm-ID: 273345 [Multi-domain] Cd Length: 435 Bit Score: 113.98 E-value: 2.69e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 174 HVNKSQSSNDTFPTAIHISVgMELNERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGL 253
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLL-RDALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 254 ERIKGCLPRVyelALGGT--AVGTGLNTRKGFAEkVAKRISELTCLPFVSAPNKFEAlaaRDAMVEVHGVLNTIAVSLMK 331
Cdd:TIGR00928 169 ERLLQAKERI---KVGGIsgAVGTHAAAYPLVEE-VEERVTEFLGLKPVPISTQIEP---RDRHAELLDALALLATTLEK 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 332 IANDIRLLgsgPRCGLGELMLP--ENEPGSSIMPGKVNPTQCESMTMLCaqVMGNQVAVTIGGSNGH-FELNVFKPLVVS 408
Cdd:TIGR00928 242 FAVDIRLL---QRTEHFEVEEPfgKGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLwHERDLTDSSVER 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 409 NVLRSIRLLADGSMTFSKNCVEGLQANKERIDKIMNESLMLVTALNPHI-------GYDKA-----ALIAKTAHKNKTTL 476
Cdd:TIGR00928 317 VILPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAyeivrELAMGAAEVDEPDL 396
|
330 340 350
....*....|....*....|....*....|
gi 78710009 477 KE-----EALKTGITEEQFKEWVNPKEMLG 501
Cdd:TIGR00928 397 LEflledERITKYLKEEELAELLDPETYIG 426
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
449-499 |
3.03e-23 |
|
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to L-malate as part of the Kreb's cycle. The full-length protein forms a tetramer with visible globular shape. FumaraseC_C is the C-terminal 65 residues referred to as domain 3. The core of the molecule consists of a bundle of 20 alpha-helices from the five-helix bundle of domain 2. The projections from the core of the tetramer are generated from domains 1 and 3 of each subunit. FumaraseC_C does not appear to be part of either the active site or the activation site but is helical in structure forming a little bundle.
Pssm-ID: 463083 [Multi-domain] Cd Length: 52 Bit Score: 92.38 E-value: 3.03e-23
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 78710009 449 LVTALNPHIGYDKAALIAKTAHKNKTTLKEEALKTGI-TEEQFKEWVNPKEM 499
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLlTEEELDEILDPENM 52
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
181-449 |
5.71e-21 |
|
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176464 [Multi-domain] Cd Length: 387 Bit Score: 94.54 E-value: 5.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 181 SNDTFPTAIhiSVGM-ELNERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGC 259
Cdd:cd01360 91 SSDVVDTAL--ALQLrEALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKEA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 260 LPRVYELALGGtAVGTGLNtrkgFAEKVAKRISELTCLPFVSAPNKfeaLAARDAMVEVHGVLNTIAVSLMKIANDIRLL 339
Cdd:cd01360 169 RERILVGKISG-AVGTYAN----LGPEVEERVAEKLGLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRHL 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 340 gsgPRCGLGELMLP--ENEPGSSIMPGKVNPTQCESMTMLCAQVMGNQVAVtiggsnghFELNVF---KPLVVSNVLRSI 414
Cdd:cd01360 241 ---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLARVIRSNVIPA--------LENVALwheRDISHSSVERVI 309
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 78710009 415 ----RLLADGSMTFSKNCVEGLQANKERIDK--------IMNESLML 449
Cdd:cd01360 310 lpdaTILLDYILRRMTRVLENLVVYPENMRRnlnltkglIFSQRVLL 356
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
201-478 |
3.70e-18 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 86.99 E-value: 3.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGtAVGTgLNTR 280
Cdd:PRK09053 127 LEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGT-LASL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 281 KGFAEKVAKRISELTCLPFVSAPNKfealAARDAMVEVHGVLNTIAVSLMKIANDIRLLgsgPRCGLGELMLP--ENEPG 358
Cdd:PRK09053 205 GEQALPVAQALAAELQLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDVSLL---MQTEVGEVFEPaaAGKGG 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 359 SSIMPGKVNPTQCESM------------TMLCAQVMGNQVAVtiGGSNGHFElnvfkplvvsnVLRSIRLLADGSMTFSK 426
Cdd:PRK09053 278 SSTMPHKRNPVGCAAVltaatrapglvaTLFAAMPQEHERAL--GGWHAEWD-----------TLPELACLAAGALAQMA 344
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 78710009 427 NCVEGLQANKERIDK--------IMNESLMLvtALNPHIGYDKA-ALI---AKTAHKNKTTLKE 478
Cdd:PRK09053 345 QIVEGLEVDAARMRAnldlthglILAEAVML--ALADRIGRLDAhHLVeqaSKRAVAEGRHLRD 406
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
180-500 |
2.20e-16 |
|
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.
Pssm-ID: 176463 [Multi-domain] Cd Length: 435 Bit Score: 81.05 E-value: 2.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 180 SSNDTFPTAIHISVGMELnERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGC 259
Cdd:cd01359 86 SRNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLERLADA 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 260 LPRVYELALGGTA-VGTGLNTRKgfaEKVAKRiseltcLPFVS-APNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIR 337
Cdd:cd01359 165 YKRVNVSPLGAGAlAGTTFPIDR---ERTAEL------LGFDGpTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLI 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 338 LLGSGPRcGLGELmlpeneP-----GSSIMPGKVNPTQCESMTMLCAQVMGNQVAV--TIGG--SNGHFELNVFKPLV-- 406
Cdd:cd01359 236 LWSTQEF-GFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLltTLKGlpLAYNKDLQEDKEPLfd 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 407 -VSNVLRSIRLLADgsmtfsknCVEGLQANKERIDKIMNESLMLVTALN---------P-HIGYDKAALIAKTAHKNKTT 475
Cdd:cd01359 309 aVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDLAdylvrekgvPfREAHHIVGRAVRLAEEKGKD 380
|
330 340 350
....*....|....*....|....*....|
gi 78710009 476 LKEEALKT-----GITEEQFKEWVNPKEML 500
Cdd:cd01359 381 LSDLTLAElqaisPLFEEDVREALDPENSV 410
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
189-447 |
1.46e-15 |
|
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.
Pssm-ID: 176471 [Multi-domain] Cd Length: 436 Bit Score: 78.90 E-value: 1.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 189 IHISVGMELnerLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELAL 268
Cdd:cd03302 106 IQIRDALDL---ILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGV 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 269 GGTaVGTG---LNTRKGFAEKVA---KRISELtcLPFVSAPNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGsg 342
Cdd:cd03302 183 KGT-TGTQasfLDLFEGDHDKVEaldELVTKK--AGFKKVYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIRLLA-- 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 343 prcGLGELMLP--ENEPGSSIMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHFELNVFKPLVVSNVLRSIRLLADG 420
Cdd:cd03302 258 ---NLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMNLASNAAQTASTQWFERTLDDSANRRIAIPEAFLAADA 334
|
250 260
....*....|....*....|....*..
gi 78710009 421 SMTFSKNCVEGLQANKERIDKIMNESL 447
Cdd:cd03302 335 ILITLQNISEGLVVYPKVIERHIRQEL 361
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
149-384 |
2.16e-15 |
|
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]
Pssm-ID: 129918 [Multi-domain] Cd Length: 455 Bit Score: 78.16 E-value: 2.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 149 EVISNAAIKMMGGELGSKkpvhpndhVNKSQSSNDTFPTAIHISVGMELNErLVPAVTHLRDALKSKSDEFKDIIKIGRT 228
Cdd:TIGR00838 83 MAIERELIDRVGEDLGGK--------LHTGRSRNDQVATDLRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYT 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 229 HLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAV-GTGLNTRKgfaekvaKRISELtcLPFVSA-PNKF 306
Cdd:TIGR00838 154 HLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALaGTGFPIDR-------EYLAEL--LGFDAVtENSL 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 78710009 307 EALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPrcgLGELMLP-ENEPGSSIMPGKVNPTQCESMTMLCAQVMGN 384
Cdd:TIGR00838 225 DAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---FGFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGN 300
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
321-501 |
3.02e-14 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 71.60 E-value: 3.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 321 VLNTIAVSLMKIANDIRLLgSGPRCGLGELMLPENEPGSSIMPGKVNPTQCESMTMLCAQVMGNQVAVTIGGSNGHfELN 400
Cdd:PRK08937 22 VLALIATSLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSYLVTALENVPLWH-ERD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 401 VFkplvVSNVLR----SIRLLADGSMTFSKNCVEGLQANKERIDKIMNESLMLVTALNPHIGYDKAALIAKTAH------ 470
Cdd:PRK08937 100 LS----HSSAERialpDAFLALDYILNRFVNILENLVVFPENIERNLDKTLGFIATERVLLELVEKGMGREEAHelirek 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 78710009 471 -----KNKTTLKE-----EALKTGITEEQFKEWVNPKEMLG 501
Cdd:PRK08937 176 ameawKNQKDLRElleadERFTKQLTKEELDELFDPEAFVG 216
|
|
| ArgH |
COG0165 |
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ... |
199-453 |
2.44e-13 |
|
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 439935 [Multi-domain] Cd Length: 462 Bit Score: 72.06 E-value: 2.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 199 ERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAV-GTGL 277
Cdd:COG0165 127 LELIEALLALQEALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALaGTTF 206
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 278 NT-RkgfaEKVAKRiseltcLPFVS-APNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRcGLGELmlpen 355
Cdd:COG0165 207 PIdR----ERTAEL------LGFDGpTENSLDAVSDRDFALEFLSAASLIMVHLSRLAEELILWSSSEF-GFVEL----- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 356 eP-----GSSIMPGKVNPTQCESMTMLCAQVMGNQVAVtiggsnghfeLNVFK--PL---------------VVSNVLRS 413
Cdd:COG0165 271 -PdafstGSSIMPQKKNPDVAELIRGKTGRVIGNLTGL----------LTTMKglPLaynkdlqedkeplfdAVDTLKLC 339
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 78710009 414 IRLLADgsmtfsknCVEGLQANKERIDKIMNESLMLVTAL 453
Cdd:COG0165 340 LRLFAG--------MIATLKVNRERMREAAGAGFSTATDL 371
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
180-368 |
1.78e-12 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 69.41 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 180 SSNDTFPTAIHISVGMELNErLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGC 259
Cdd:PRK00855 110 SRNDQVATDLRLYLRDEIDE-IAELLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYAEMLARDLERLRDA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 260 LPRVYELALGGTA-VGTGLNTRKgfaEKVAK-----RISEltclpfvsapNKFEALAARDAMVEVHGVLNTIAVSLMKIA 333
Cdd:PRK00855 189 RKRVNRSPLGSAAlAGTTFPIDR---ERTAEllgfdGVTE----------NSLDAVSDRDFALEFLSAASLLMVHLSRLA 255
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 78710009 334 NDIRLLGSgPRCGLGELmlpeneP-----GSSIMPGKVNP 368
Cdd:PRK00855 256 EELILWSS-QEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
200-389 |
4.13e-10 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 62.05 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 200 RLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALGGTAV-GTGLN 278
Cdd:PLN02646 141 VIRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALaGTGLP 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 279 TRKGFAEKVakriseltcLPFVSA-PNKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPrcgLGELMLPEN-E 356
Cdd:PLN02646 221 IDRFMTAKD---------LGFTAPmRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---FGFVTPSDAvS 288
|
170 180 190
....*....|....*....|....*....|...
gi 78710009 357 PGSSIMPGKVNPTQCESMTMLCAQVMGNQVAVT 389
Cdd:PLN02646 289 TGSSIMPQKKNPDPMELVRGKSARVIGDLVTVL 321
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
173-377 |
8.54e-08 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 54.29 E-value: 8.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 173 DHVNKSQSSNDTFPTAIHISVGMeLNERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNG 252
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRLKA-ASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 253 LERIKGCLPRVYELALGGtAVGTgLNTRKGFAEKVAKRISELtcLPFVSAPnkfEALAARDAMVEVHGVLNTIAVSLMKI 332
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKR--LGLEDAP---QWHSQRDFIADFAHLLSLVTGSLGKF 251
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 78710009 333 ANDIRLLGSGPrcglGELMLPENEpGSSIMPGKVNPTQCESMTML 377
Cdd:PRK05975 252 GQDIALMAQAG----DEISLSGGG-GSSAMPHKQNPVAAETLVTL 291
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
199-383 |
5.95e-07 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 52.09 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 199 ERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALG-GTAVGTGL 277
Cdd:PRK12308 126 QQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTAY 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 278 NTRKgfaEKVAKRiseltcLPFVSAP-NKFEALAARDAMVEVHGVLNTIAVSLMKIANDIRLLGSGPRcglGELMLPEN- 355
Cdd:PRK12308 206 PIDR---EALAHN------LGFRRATrNSLDSVSDRDHVMELMSVASISMLHLSRLAEDLIFYNSGES---GFIELADTv 273
|
170 180
....*....|....*....|....*...
gi 78710009 356 EPGSSIMPGKVNPTQCESMTMLCAQVMG 383
Cdd:PRK12308 274 TSGSSLMPQKKNPDALELIRGKTGRVYG 301
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
201-383 |
1.43e-06 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 50.75 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 201 LVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGCLPRVYELALG-GTAVGTGLNT 279
Cdd:PRK04833 128 LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGsGALAGTAYEI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 280 RKgfaEKVAKRiseltcLPFVSAP-NKFEALAARDAMVEVhgvLNTIAVSLM---KIANDIRLLGSGpRCGLGELMlPEN 355
Cdd:PRK04833 208 DR---EQLAGW------LGFASATrNSLDSVSDRDHVLEL---LSDASISMVhlsRFAEDLIFFNSG-EAGFVELS-DRV 273
|
170 180
....*....|....*....|....*...
gi 78710009 356 EPGSSIMPGKVNPTQCESMTMLCAQVMG 383
Cdd:PRK04833 274 TSGSSLMPQKKNPDALELIRGKCGRVQG 301
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
197-368 |
5.71e-05 |
|
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the product of the purB gene in Escherichia coli, and related proteins. It is a member of the Lyase class I family of the Lyase_I superfamily. Members of the Lyase class I family function as homotetramers to catalyze similar beta-elimination reactions in which a Calpha-N or Calpha-O bond is cleaved with the subsequent release of fumarate as one of the products. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two non-sequential steps in the de novo purine biosynthesis pathway: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylosuccinate (SAMP) into adenosine monophosphate (AMP).
Pssm-ID: 176470 [Multi-domain] Cd Length: 425 Bit Score: 45.30 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 197 LNERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLT---NGLERIKgclprvYELALGGtAV 273
Cdd:cd01598 117 RNEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLErqyKQLKQIE------ILGKFNG-AV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 274 GT---------GLNTRKgFAEKVAKRISeLTCLPFVSAPNKFEALAA-RDAMVEvhgvLNTIavsLMKIANDIRLLGSgp 343
Cdd:cd01598 190 GNfnahlvaypDVDWRK-FSEFFVTSLG-LTWNPYTTQIEPHDYIAElFDALAR----INTI---LIDLCRDIWGYIS-- 258
|
170 180
....*....|....*....|....*
gi 78710009 344 rCGLGELMLPENEPGSSIMPGKVNP 368
Cdd:cd01598 259 -LGYFKQKVKKGEVGSSTMPHKVNP 282
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
197-275 |
2.42e-04 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 43.59 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 78710009 197 LNERLVPAVTHLRDALKSKSDEFKDIIKIGRTHLMDAVPLTLGQEFSGYTQQLTNGLERIKGClprvyELA--LGGtAVG 274
Cdd:PRK09285 139 REEVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EILgkING-AVG 212
|
.
gi 78710009 275 T 275
Cdd:PRK09285 213 N 213
|
|
| |
