|
Name |
Accession |
Description |
Interval |
E-value |
| FumC |
COG0114 |
Fumarate hydratase class II [Energy production and conversion]; Fumarate hydratase class II is ... |
45-491 |
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: 904.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:COG0114 16 VPADAYWGAQTQRSLENFPIGG--ERMPREFIRALALIKKAAARANAELGlLDAEKADAIVAAADEVIAGKLDDHFPLDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:COG0114 94 WQTGSGTQTNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALEERLLPALEHLRDTLEA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:COG0114 174 KAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPRLYELALGGTAVGTGLNAHPGFAERVAAELAEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:COG0114 254 TGLPFVSAPNKFEALAAHDALVELSGALKTLAVSLMKIANDIRWLASGPRCGLGEIRLPANEPGSSIMPGKVNPTQCEAL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:COG0114 334 TMVCAQVMGNDAAITFAGSSGNFELNVMKPVIAYNLLQSIRLLADACRSFADKCVAGIEANEERIEELLERSLMLVTALN 413
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 491
Cdd:COG0114 414 PHIGYDKAAKIAKKAHKEGRTLREAALELGLLSEEEFDRLVDPEKMTG 461
|
|
| fumC |
PRK00485 |
fumarate hydratase; Reviewed |
45-493 |
0e+00 |
|
fumarate hydratase; Reviewed
Pssm-ID: 234779 [Multi-domain] Cd Length: 464 Bit Score: 904.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:PRK00485 16 VPADALWGAQTQRSLENFPIGG--ERMPRELIRALALLKKAAARVNAELGlLDAEKADAIVAAADEVIAGKHDDHFPLDV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:PRK00485 94 WQTGSGTQSNMNVNEVIANRASELLGGELGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAVLAIVERLLPALEHLRDTLAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:PRK00485 174 KAEEFADIVKIGRTHLQDATPLTLGQEFSGYAAQLEHGIERIEAALPHLYELALGGTAVGTGLNAHPGFAERVAEELAEL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:PRK00485 254 TGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLASGPRCGLGEISLPENEPGSSIMPGKVNPTQCEAL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:PRK00485 334 TMVCAQVMGNDAAVTFAGSQGNFELNVFKPVIAYNFLQSIRLLADAMRSFADHCVVGIEPNRERIKELLERSLMLVTALN 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 493
Cdd:PRK00485 414 PHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRWVDPEKMTGPG 463
|
|
| Fumarase_classII |
cd01362 |
Class II fumarases; This subgroup contains Escherichia coli fumarase C, human mitochondrial ... |
45-489 |
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: 890.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:cd01362 12 VPADALWGAQTQRSLENFPIGG--ERMPRELIRALGLLKKAAAQANAELGlLDEEKADAIVQAADEVIAGKLDDHFPLVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:cd01362 90 WQTGSGTQTNMNVNEVIANRAIELLGGVLGSKKPVHPNDHVNMSQSSNDTFPTAMHIAAALALQERLLPALKHLIDALDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:cd01362 170 KADEFKDIVKIGRTHLQDATPLTLGQEFSGYAAQLEHAIARIEAALPRLYELALGGTAVGTGLNAHPGFAEKVAAELAEL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:cd01362 250 TGLPFVTAPNKFEALAAHDALVEASGALKTLAVSLMKIANDIRWLGSGPRCGLGELSLPENEPGSSIMPGKVNPTQCEAL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:cd01362 330 TMVAAQVMGNDAAITIAGSSGNFELNVFKPVIIYNLLQSIRLLADACRSFADKCVAGIEPNRERIAELLERSLMLVTALN 409
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 489
Cdd:cd01362 410 PHIGYDKAAKIAKKAHKEGLTLKEAALELGYLTEEEFDRLVDPEKM 455
|
|
| PLN00134 |
PLN00134 |
fumarate hydratase; Provisional |
45-492 |
0e+00 |
|
fumarate hydratase; Provisional
Pssm-ID: 215069 [Multi-domain] Cd Length: 458 Bit Score: 844.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:PLN00134 6 VPADKLWGAQTQRSLQNFEIGGERERMPEPIVRAFGIVKKAAAKVNMEYGlLDPDIGKAIMQAADEVAEGKLDDHFPLVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:PLN00134 86 WQTGSGTQTNMNANEVIANRAAEILGGPVGEKSPVHPNDHVNRSQSSNDTFPTAMHIAAATEIHSRLIPALKELHESLRA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:PLN00134 166 KSFEFKDIVKIGRTHLQDAVPLTLGQEFSGYATQVKYGLNRVQCTLPRLYELAQGGTAVGTGLNTKKGFDEKIAAAVAEE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:PLN00134 246 TGLPFVTAPNKFEALAAHDAFVELSGALNTVAVSLMKIANDIRLLGSGPRCGLGELNLPENEPGSSIMPGKVNPTQCEAL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:PLN00134 326 TMVCAQVMGNHVAITVGGSAGHFELNVFKPLIAYNLLHSIRLLGDASASFRKNCVRGIEANRERISKLLHESLMLVTALN 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 492
Cdd:PLN00134 406 PKIGYDKAAAVAKKAHKEGTTLKEAALKLGVLTAEEFDELVVPEKMTGP 454
|
|
| Aspartase_like |
cd01596 |
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ... |
45-485 |
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: 813.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:cd01596 12 VPADAYYGAQTQRALENFPISG--ERMPPELIRALALVKKAAALANAELGlLDEEKADAIVQACDEVIAGKLDDQFPLDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGsKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:cd01596 90 WQTGSGTSTNMNVNEVIANRALELLGGKKG-KYPVHPNDDVNNSQSSNDDFPPAAHIAAALALLERLLPALEQLQDALDA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:cd01596 169 KAEEFADIVKIGRTHLQDAVPLTLGQEFSGYAAQLARDIARIEAALERLRELNLGGTAVGTGLNAPPGYAEKVAAELAEL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:cd01596 249 TGLPFVTAPNLFEATAAHDALVEVSGALKTLAVSLSKIANDLRLLSSGPRAGLGEINLPANQPGSSIMPGKVNPVIPEAV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:cd01596 329 NMVAAQVIGNDTAITMAGSAGQLELNVFKPVIAYNLLQSIRLLANACRSFRDKCVEGIEANEERCKEYVENSLMLVTALN 408
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVK 485
Cdd:cd01596 409 PHIGYEKAAEIAKEALKEGRTLREAALELGLLTEEELDEILD 450
|
|
| fumC_II |
TIGR00979 |
fumarate hydratase, class II; Putative fumarases from several species (Mycobacterium ... |
45-491 |
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: 803.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGgvTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:TIGR00979 13 VPADKYWGAQTQRSLENFKIG--TEKMPLELIHAFAILKKAAAIVNEDLGkLDAKKADAIVQAADEILAGKLDDHFPLVV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:TIGR00979 91 WQTGSGTQSNMNVNEVIANRAIELLGGKLGSKQPVHPNDHVNKSQSSNDTFPTAMHIAAVLAIKNQLIPALENLKKTLDA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:TIGR00979 171 KSKEFAHIVKIGRTHLQDATPLTLGQEFSGYVAQLEHGLERIAYSLPHLYELAIGGTAVGTGLNTHPGFDEKVAEEIAKE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:TIGR00979 251 TGLPFVTAPNKFEALAAHDAIVEAHGALKTLAASLMKIANDIRWLGSGPRCGLGELFIPENEPGSSIMPGKVNPTQCEAL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:TIGR00979 331 TMVCVQVMGNDATIGFAGSQGNFELNVFKPVIIYNFLQSVRLLSDAMESFRDHCVVGIEPNKERIQQLLNNSLMLVTALN 410
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLG 491
Cdd:TIGR00979 411 PHIGYDNAAKIAKKAHKEGITLKEAALELGLLSEEEFDEWVVPEQMVG 458
|
|
| PRK12425 |
PRK12425 |
class II fumarate hydratase; |
45-492 |
0e+00 |
|
class II fumarate hydratase;
Pssm-ID: 171490 [Multi-domain] Cd Length: 464 Bit Score: 602.30 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:PRK12425 14 VPEDAYWGAQTQRSLINFAIGK--ERMPLAVLHALALIKKAAARVNDRNGdLPADIARLIEQAADEVLDGQHDDQFPLVV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:PRK12425 92 WQTGSGTQSNMNVNEVIAGRANELAGNGRGGKSPVHPNDHVNRSQSSNDCFPTAMHIAAAQAVHEQLLPAIAELSGGLAE 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:PRK12425 172 QSARHAKLVKTGRTHMMDATPITFGQELSAFVAQLDYAERAIRAALPAVCELAQGGTAVGTGLNAPHGFAEAIAAELAAL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:PRK12425 252 SGLPFVTAPNKFAALAGHEPLVSLSGALKTLAVALMKIANDLRLLGSGPRAGLAEVRLPANEPGSSIMPGKVNPTQCEAL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:PRK12425 332 SMLACQVMGNDATIGFAASQGHLQLNVFKPVIIHNLLQSIRLLADGCRNFQQHCVAGLEPDAEQMAAHLERGLMLVTALN 411
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 492
Cdd:PRK12425 412 PHIGYDKAAEIAKKAYAEGTTLREAALALGYLTDEQFDAWVRPENMLEA 460
|
|
| AspA |
COG1027 |
Aspartate ammonia-lyase [Amino acid transport and metabolism]; |
43-493 |
0e+00 |
|
Aspartate ammonia-lyase [Amino acid transport and metabolism];
Pssm-ID: 440650 [Multi-domain] Cd Length: 460 Bit Score: 590.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 43 RMVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPL 121
Cdd:COG1027 10 REVPADAYYGIQTLRALENFPISGRPISDHPELIRALAMVKKAAALANRELGlLDKEKADAIVAACDEIIAGKLHDQFVV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 122 VVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDAL 201
Cdd:COG1027 90 DVIQGGAGTSTNMNANEVIANRALEILGGKKGDYDYVHPNDHVNMSQSTNDVYPTAIRLAL-LLLLRELLEALERLQEAF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 202 DAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVA 281
Cdd:COG1027 169 AAKAEEFADVLKMGRTQLQDAVPMTLGQEFGAYAVALARDRWRLYEAAELLREVNLGGTAIGTGLNAPPGYIELVVEHLA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 282 ALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCE 361
Cdd:COG1027 249 EITGLPLVRAENLIEATQDTDAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIPE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 362 AMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTA 441
Cdd:COG1027 329 VVNQVAFQVIGNDLTVTMAAEAGQLELNVFEPVIAYNLLESIELLTNACRTLREKCIDGITANEERCREYVENSIGLVTA 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 119590496 442 LNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 493
Cdd:COG1027 409 LNPYIGYEKAAEIAKEALATGKSVRELVLEKGLLTEEELDEILDPENMTGPG 460
|
|
| aspA |
PRK12273 |
aspartate ammonia-lyase; Provisional |
43-493 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237031 [Multi-domain] Cd Length: 472 Bit Score: 564.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 43 RMVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPL 121
Cdd:PRK12273 15 REVPADAYYGIHTLRAVENFPISGVKISDYPELIRALAMVKKAAALANKELGlLDEEKADAIVAACDEILAGKLHDQFVV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 122 VVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDAL 201
Cdd:PRK12273 95 DVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDAYPTAIRIAL-LLSLRKLLDALEQLQEAF 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 202 DAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVA 281
Cdd:PRK12273 174 EAKAKEFADILKMGRTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAIGTGLNAPPGYIELVVEKLA 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 282 ALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCE 361
Cdd:PRK12273 254 EITGLPLVPAEDLIEATQDTGAFVEVSGALKRLAVKLSKICNDLRLLSSGPRAGLNEINLPAVQAGSSIMPGKVNPVIPE 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 362 AMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTA 441
Cdd:PRK12273 334 VVNQVCFQVIGNDTTVTMAAEAGQLELNVMEPVIAYNLFESISILTNACRTLREKCIDGITANEERCREYVENSIGIVTA 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 119590496 442 LNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 493
Cdd:PRK12273 414 LNPYIGYENAAEIAKEALETGKSVRELVLERGLLTEEELDDILSPENMTHPG 465
|
|
| Aspartase |
cd01357 |
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ... |
43-482 |
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: 558.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 43 RMVPNDKYYGAQTVRSTMNFKIGGvtERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPL 121
Cdd:cd01357 10 REVPADAYYGIQTLRALENFPISG--LKIHPELIRALAMVKKAAALANAELGlLDEEKAEAIVKACDEIIAGKLHDQFVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 122 VVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDAL 201
Cdd:cd01357 88 DVIQGGAGTSTNMNANEVIANRALELLGHEKGEYQYVHPNDHVNMSQSTNDVYPTALRLAL-ILLLRKLLDALAALQEAF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 202 DAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVA 281
Cdd:cd01357 167 QAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYKARERLREVNLGGTAIGTGINAPPGYIELVVEKLS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 282 ALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCE 361
Cdd:cd01357 247 EITGLPLKRAENLIDATQNTDAFVEVSGALKRLAVKLSKIANDLRLLSSGPRAGLGEINLPAVQPGSSIMPGKVNPVIPE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 362 AMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTA 441
Cdd:cd01357 327 VVNQVAFQVIGNDLTITMAAEAGQLELNVFEPVIAYNLLESIDILTNAVRTLRERCIDGITANEERCREYVENSIGIVTA 406
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 119590496 442 LNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDE 482
Cdd:cd01357 407 LNPYIGYEAAAEIAKEALETGRSVRELVLEEGLLTEEELDE 447
|
|
| PRK13353 |
PRK13353 |
aspartate ammonia-lyase; Provisional |
43-493 |
0e+00 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 183992 [Multi-domain] Cd Length: 473 Bit Score: 544.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 43 RMVPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPL 121
Cdd:PRK13353 15 KEVPAEAYYGIQTLRAVENFPITGY--KIHPELIRAFAQVKKAAALANADLGlLPRRIAEAIVQACDEILAGKLHDQFIV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 122 VVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEvLLPGLQKLHDAL 201
Cdd:PRK13353 93 DPIQGGAGTSTNMNANEVIANRALELLGGEKGDYHYVSPNDHVNMAQSTNDVFPTAIRIAALNLLEG-LLAAMGALQDVF 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 202 DAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVA 281
Cdd:PRK13353 172 EEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQAREHLYEVNLGGTAVGTGLNADPEYIERVVKHLA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 282 ALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCE 361
Cdd:PRK13353 252 AITGLPLVGAEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLRLLSSGPRTGLGEINLPAVQPGSSIMPGKVNPVMPE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 362 AMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTA 441
Cdd:PRK13353 332 VVNQIAFQVIGNDVTITLAAEAGQLELNVMEPVIAFNLLESISILTNACRAFTDNCVKGIEANEERCKEYVEKSVGIATA 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 119590496 442 LNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGPK 493
Cdd:PRK13353 412 LNPHIGYEAAARIAKEAIATGRSVRELALENGLLSEEELDLILDPFRMTHPG 463
|
|
| aspA |
TIGR00839 |
aspartate ammonia-lyase; This enzyme, aspartate ammonia-lyase, shows local homology to a ... |
43-492 |
3.95e-147 |
|
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: 429.25 E-value: 3.95e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 43 RMVPNDKYYGAQTVRSTMNFKIGGVTERMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAE-GKLNDHFP 120
Cdd:TIGR00839 10 REVPADAYYGIHTLRASENFYISNNKISDIPEFVRGMVMVKKAAALANKELGtIPESIANAIVAACDEILNnGKCHDQFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 121 LVVWQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDA 200
Cdd:TIGR00839 90 VDVYQGGAGTSVNMNTNEVIANLALELMGHQKGEYQYLNPNDHVNKSQSTNDAYPTGFRIAV-YSSLIKLVDAINQLRDG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 201 LDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKV 280
Cdd:TIGR00839 169 FEQKAKEFADILKMGRTQLQDAVPMTLGQEFEAFSILLEEEVKNIKRTAELLLEVNLGATAIGTGLNTPPEYSPLVVKKL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 281 AALTGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQC 360
Cdd:TIGR00839 249 AEVTGLPCVPAENLIEATSDCGAYVMVHGALKRLAVKMSKICNDLRLLSSGPRAGLNEINLPELQAGSSIMPAKVNPVVP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 361 EAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVT 440
Cdd:TIGR00839 329 EVVNQVCFKVIGNDTTVTLAAEAGQLQLNVMEPVIGQAMFESIHILTNACYNLTDKCVNGITANKEICEGYVFNSIGIVT 408
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 119590496 441 ALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 492
Cdd:TIGR00839 409 YLNPFIGHHNGDIVGKICAETGKSVREVVLEKGLLTEEELDDIFSVENLMHP 460
|
|
| Lyase_1 |
pfam00206 |
Lyase; |
45-372 |
5.07e-145 |
|
Lyase;
Pssm-ID: 425524 [Multi-domain] Cd Length: 312 Bit Score: 417.93 E-value: 5.07e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGVTermptpvIKAFGILKRAAAEVNQDYgldPKIANAIMKAADEVAE-GKLNDHFPLVV 123
Cdd:pfam00206 5 VPADALMGIFTDRSRFNFRLGEED-------IKGLAALKKAAAKANVIL---KEEAAAIIKALDEVAEeGKLDDQFPLKV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISnraiEMLGgelgskIPVHPNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDA 203
Cdd:pfam00206 75 WQEGSGTAVNMNLNEVIG----ELLG------QLVHPNDHVHTGQSSNDQVPTALRLALKDALSEVLLPALRQLIDALKE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPR-IYELAAGGTAVGTGLNTRIGFAEKVAAKVAA 282
Cdd:pfam00206 145 KAKEFADIVKPGRTHLQDATPVTLGQELSGYAVALTRDRERLQQLLPRlLVLPLGGGTAVGTGLNADPEFAELVAKELGF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 283 LTGLPfVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrSGLGELILPENEPGSSIMPGKVNPTQCEA 362
Cdd:pfam00206 225 FTGLP-VKAPNSFEATSDRDAVVELSGALALLATSLSKFAEDLRLLSSGP-AGLVELSLAEGEPGSSIMPGKVNPDQLEL 302
|
330
....*....|
gi 119590496 363 MTMVAAQVMG 372
Cdd:pfam00206 303 LTGKAGRVMG 312
|
|
| PRK14515 |
PRK14515 |
aspartate ammonia-lyase; Provisional |
45-492 |
5.79e-141 |
|
aspartate ammonia-lyase; Provisional
Pssm-ID: 237743 [Multi-domain] Cd Length: 479 Bit Score: 414.01 E-value: 5.79e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 45 VPNDKYYGAQTVRSTMNFKIGGVteRMPTPVIKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFPLVV 123
Cdd:PRK14515 23 VPNYAYYGVQTMRAVENFPITGY--KIHEGLIKAFAIVKKAAALANTDVGrLELNKGGAIAEAAQEILDGKWHDHFIVDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 124 WQTGSGTQTNMNVNEVISNRAIEMLGGELGSKIPVHPNDHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDA 203
Cdd:PRK14515 101 IQGGAGTSMNMNANEVIANRALELLGMEKGDYHYISPNSHVNMAQSTNDAFPTAIHIAT-LNALEGLLQTMGYMHDVFEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 204 KSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAKVAAL 283
Cdd:PRK14515 180 KAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRVLERDMKRIQQSRQHLYEVNMGATAVGTGLNADPEYIEAVVKHLAAI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 284 TGLPFVTAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAM 363
Cdd:PRK14515 260 SELPLVGAEDLVDATQNTDAYTEVSAALKVCMMNMSKIANDLRLMASGPRVGLAEIMLPARQPGSSIMPGKVNPVMPEVI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 364 TMVAAQVMGNHVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALN 443
Cdd:PRK14515 340 NQIAFQVIGNDHTICLASEAGQLELNVMEPVLVFNLLQSISIMNNGFRAFTDNCLKGIEANEDRLKEYVEKSVGIITAVN 419
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 119590496 444 PHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDMLGP 492
Cdd:PRK14515 420 PHIGYEAAARVAKEAIATGQSVRELCVKNGVLSQEDLELILDPFEMTHP 468
|
|
| Lyase_I |
cd01334 |
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ... |
76-424 |
1.23e-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: 1.23e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 76 IKAFGILKRAAAEVNQDYG-LDPKIANAIMKAADEVAEGKLNDHFplvvWQTGSGTQTNMNVNEVISNRAIEMlggelgs 154
Cdd:cd01334 1 IRADLQVEKAHAKALAELGlLPKEAAEAILAALDEILEGIAADQV----EQEGSGTHDVMAVEEVLAERAGEL------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 155 kipvhpNDHVNKSQSSNDTFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGY 234
Cdd:cd01334 70 ------NGGYVHTGRSSNDIVDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAW 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 235 VQQVKYAMTRIKAAMPRIYELAAGGTAVGTGLNTRIGFAEKVAAkvaaLTGLpFVTAPNKFEALAAHDALVELSGAMNTT 314
Cdd:cd01334 144 AAELERDLERLEEALKRLNVLPLGGGAVGTGANAPPIDRERVAE----LLGF-FGPAPNSTQAVSDRDFLVELLSALALL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 315 ACSLMKIANDIRFLGSGprsGLGELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTVGGSNGHFELNVFKP 393
Cdd:cd01334 219 AVSLSKIANDLRLLSSG---EFGEVELPDAkQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSP 295
|
330 340 350
....*....|....*....|....*....|.
gi 119590496 394 MMIKNVLHSARLLGDASVSFTENCvVGIQAN 424
Cdd:cd01334 296 VEREALPDSFDLLDAALRLLTGVL-EGLEVN 325
|
|
| Lyase_I_like |
cd01594 |
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ... |
134-414 |
5.51e-64 |
|
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: 207.08 E-value: 5.51e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 134 MNVNEVISNRAIEMLGGELGSKipvhpndHVNKSQSSNDtFPTAMHIAAAIEVHEVLLPGLQKLHDALDAKSKEFAQIIK 213
Cdd:cd01594 14 ALVEEVLAGRAGELAGGLHGSA-------LVHKGRSSND-IGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 214 IGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyelaaggtavgtglntrigfaekvaakvaaltglpfvtapn 293
Cdd:cd01594 86 PGRTHLQDAQPVTLGYELRAWAQVLGRDLERLEEA--------------------------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 294 kfealaahdALVELSGAMNTTACSLMKIANDIRFLGSGPRSGLGELILPeNEPGSSIMPGKVNPTQCEAMTMVAAQVMGN 373
Cdd:cd01594 121 ---------AVAEALDALALAAAHLSKIAEDLRLLLSGEFGELGEPFLP-GQPGSSIMPQKVNPVAAELVRGLAGLVIGN 190
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 119590496 374 HVAVTVGGSNGHFELNVFKPMMIKNVLHSARLLGDASVSFT 414
Cdd:cd01594 191 LVAVLTALKGGPERDNEDSPSMREILADSLLLLIDALRLLL 231
|
|
| FumaraseC_C |
pfam10415 |
Fumarase C C-terminus; Fumarase C catalyzes the stereo-specific interconversion of fumarate to ... |
438-489 |
7.09e-28 |
|
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: 105.09 E-value: 7.09e-28
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 119590496 438 LVTALNPHIGYDKAAKIAKTAHKNGSTLKETAIELGYLTAEQFDEWVKPKDM 489
Cdd:pfam10415 1 LVTALNPHIGYDKAAEIAKEALKTGRTLREAALELGLLTEEELDEILDPENM 52
|
|
| PurB |
COG0015 |
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ... |
185-491 |
9.90e-26 |
|
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: 109.40 E-value: 9.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 185 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 264
Cdd:COG0015 113 EALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARERVLVGKIGG-AVGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 265 GLNtrigfaekvaakvaaltglpFVTAPNKFEALAA----------------HDALVELSGAMNTTACSLMKIANDIRFL 328
Cdd:COG0015 192 YAA--------------------HGEAWPEVEERVAeklglkpnpvttqiepRDRHAELFSALALIAGSLEKIARDIRLL 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 329 GsgpRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGN--HVAVTV------GGSNGHFELNVFkPMMIkn 398
Cdd:COG0015 252 Q---RTEVGEVeePFAKGQVGSSAMPHKRNPIDSENIEGLARLARALaaALLEALaswherDLSDSSVERNIL-PDAF-- 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 399 vlhsarLLGDASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IG----YDKAAKIAKTAHKNGSTLKE 467
Cdd:COG0015 326 ------LLLDGALERLLKLLEGLVVNPERMRANLDLTGGLVlseavlMALVRRgLGreeaYELVKELARGAWEEGNDLRE 399
|
330 340
....*....|....*....|....*....
gi 119590496 468 tAIE-----LGYLTAEQFDEWVKPKDMLG 491
Cdd:COG0015 400 -LLAadpeiPAELSKEELEALFDPANYLG 427
|
|
| Adenylsuccinate_lyase_like |
cd01595 |
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ... |
185-459 |
1.12e-24 |
|
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: 105.28 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 185 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 264
Cdd:cd01595 103 DALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGKKFAVWAAELLRHLERLEEARERVLVGGISG-AVGT 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 265 GLNtrigFAEKVAAKVAALT---GLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLGELIL 341
Cdd:cd01595 182 HAS----LGPKGPEVEERVAeklGLKVPPITTQIEP---RDRIAELLSALALIAGTLEKIATDIRLLQ---RTEIGEVEE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 342 P--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvavtvggsnghfelnvFKPMMIKNVL-------HSA--RLLG--- 407
Cdd:cd01595 252 PfeKGQVGSSTMPHKRNPIDSENIEGLARLVRAL-----------------AAPALENLVQwherdlsDSSveRNILpda 314
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119590496 408 ----DASVSFTENCVVGIQANTERINKLMNESLMLV------TALNPH-IGYDKAAKIAKTAH 459
Cdd:cd01595 315 flllDAALSRLQGLLEGLVVNPERMRRNLDLTWGLIlseavmMALAKKgLGRQEAYELVKEEN 377
|
|
| pCLME |
cd01597 |
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ... |
185-491 |
8.47e-22 |
|
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: 97.70 E-value: 8.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 185 EVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGT 264
Cdd:cd01597 113 DALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLKVAVWLSELLRHRERLDELRPRVLVVQFGG-AAGT 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 265 -------GLNTRIGFaekvaakvAALTGLPFVTAPnkfeALAAHDALVELSGAMNTTACSLMKIANDIRFLGsgpRSGLG 337
Cdd:cd01597 192 laslgdqGLAVQEAL--------AAELGLGVPAIP----WHTARDRIAELASFLALLTGTLGKIARDVYLLM---QTEIG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 338 ELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGnHVAVTV---------GGSNGHFELNVFKPMMIknvlhsarlL 406
Cdd:cd01597 257 EVAEPfaKGRGGSSTMPHKRNPVGCELIVALARRVPG-LAALLLdamvqeherDAGAWHAEWIALPEIFL---------L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 407 GDASVSFTENCVVGIQANTERINK--------LMNESLMLvtALNPHIGYDKA----AKIAKTAHKNGSTLKETAIE--- 471
Cdd:cd01597 327 ASGALEQAEFLLSGLEVNEDRMRAnldltgglILSEAVMM--ALAPKLGRQEAhdlvYEACMRAVEEGRPLREVLLEdpe 404
|
330 340
....*....|....*....|.
gi 119590496 472 -LGYLTAEQFDEWVKPKDMLG 491
Cdd:cd01597 405 vAAYLSDEELDALLDPANYLG 425
|
|
| purB |
TIGR00928 |
adenylosuccinate lyase; This family consists of adenylosuccinate lyase, the enzyme that ... |
163-491 |
9.08e-22 |
|
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: 97.42 E-value: 9.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 163 HVNKSQSSNDTFPTAMHIAAAiEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAM 242
Cdd:TIGR00928 90 FIHFGATSNDIVDTALALLLR-DALEIILPKLKQLIDRLKELAVEYKDTVMLGRTHGQHAEPTTLGKRFALWAEEMLRQL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 243 TRIKAAMPRIYELAAGGtAVGTGLNTRIGFAEKVAAKVAALtGLPFVTAPNKFEAlaaHDALVELSGAMNTTACSLMKIA 322
Cdd:TIGR00928 169 ERLLQAKERIKVGGISG-AVGTHAAAYPLVEEVEERVTEFL-GLKPVPISTQIEP---RDRHAELLDALALLATTLEKFA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 323 NDIRFLgsgPRSGLGEL--ILPENEPGSSIMPGKVNPTQCEAMTMVAaqVMGNHVAVTVGGSNGH-FELNVFKPMMIKNV 399
Cdd:TIGR00928 244 VDIRLL---QRTEHFEVeePFGKGQVGSSAMPHKRNPIDFENVCGLA--RVIRGYASPALENAPLwHERDLTDSSVERVI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 400 LHSARLLGDASVSFTENCVVGIQANTERINKLMNESLMLVTALNPHI-------GYDKAAKIAK-----TAHKNGSTLKE 467
Cdd:TIGR00928 319 LPDAFILADIMLKTTLKVVKKLVVNPENILRNLDLTLGLIASERVLIalvergmGREEAYEIVRelamgAAEVDEPDLLE 398
|
330 340
....*....|....*....|....*...
gi 119590496 468 TAIELG----YLTAEQFDEWVKPKDMLG 491
Cdd:TIGR00928 399 FLLEDEritkYLKEEELAELLDPETYIG 426
|
|
| Adenylsuccinate_lyase_1 |
cd01360 |
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ... |
170-367 |
4.52e-15 |
|
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: 76.82 E-value: 4.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 170 SNDTFPTA--MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKA 247
Cdd:cd01360 91 SSDVVDTAlaLQLREALDI---ILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFALWYAEFKRHLERLKE 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 248 AMPRIYELAAGGtAVGTGLNtrIGFAEKVAAKVAAltGLPFVTAPNKfeaLAAHDALVELSGAMNTTACSLMKIANDIRF 327
Cdd:cd01360 168 ARERILVGKISG-AVGTYAN--LGPEVEERVAEKL--GLKPEPISTQ---VIQRDRHAEYLSTLALIASTLEKIATEIRH 239
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 119590496 328 LgsgPRSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVA 367
Cdd:cd01360 240 L---QRTEVLEVEEPfsKGQKGSSAMPHKRNPILSENICGLA 278
|
|
| argH |
TIGR00838 |
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ... |
98-486 |
2.77e-14 |
|
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: 74.70 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 98 KIANAIMKAADEVAEGKLNDHFPLvvwqtgsgtqtnMNVNEVISNRAIEMLGGELGSKIpvhpndHVNKSQssNDTFPTA 177
Cdd:TIGR00838 55 KIIEGLNELKEEGREGPFILDPDD------------EDIHMAIERELIDRVGEDLGGKL------HTGRSR--NDQVATD 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 178 MHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 257
Cdd:TIGR00838 115 LRLYLRDHVLE-LAEALLDLQDALIELAEKHVETLMPGYTHLQRAQPITLAHHLLAYAEMLLRDYERLQDALKRVNVSPL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 258 GGTAV-GTGLntrigfaEKVAAKVAALTGLPFVTApNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 336
Cdd:TIGR00838 194 GSGALaGTGF-------PIDREYLAELLGFDAVTE-NSLDAVSDRDFILELLFVAALIMVHLSRFAEDLILWSTGE---F 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 337 GELILP-ENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVtvggsnghfelnvfkpMMIKNVLHSA---------RLL 406
Cdd:TIGR00838 263 GFVELPdEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGM----------------LMTLKALPLAynrdlqedkEPL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 407 GDaSVSFTENCV-------VGIQANTERINKLMNESLMLVTALNPHI---------GYDKAAKIAKTAHKNGSTLKETAI 470
Cdd:TIGR00838 327 FD-ALKTVELSLematgmlDTITVNKERMEEAASAGFSNATELADYLvrkgvpfreAHHIVGELVATAIERGKGLEELTL 405
|
410
....*....|....*.
gi 119590496 471 ELGYLTAEQFDEWVKP 486
Cdd:TIGR00838 406 EELQKFSPEFDEDVYE 421
|
|
| PurB |
cd01598 |
PurB_like adenylosuccinases (adenylosuccinate lyase, ASL); This subgroup contains EcASL, the ... |
177-357 |
1.50e-10 |
|
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: 63.02 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 177 AMHIAAAIevHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKaampRIYELA 256
Cdd:cd01598 110 ALMIKEAR--NEVILPLLKEIIDSLKKLAKEYADVPMLSRTHGQPATPTTLGKELAVFVYRLERQYKQLK----QIEILG 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 257 AGGTAVGT------------------GLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAM---NTTa 315
Cdd:cd01598 184 KFNGAVGNfnahlvaypdvdwrkfseFFVTSLG-----------LTWNPYTT------QIEPHDYIAELFDALariNTI- 245
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 119590496 316 csLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 357
Cdd:cd01598 246 --LIDLCRDIwgyislGYFKQKVKKG---------EVGSSTMPHKVNP 282
|
|
| PRK09053 |
PRK09053 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
188-372 |
1.67e-10 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 181627 [Multi-domain] Cd Length: 452 Bit Score: 63.11 E-value: 1.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 188 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGtAVGTGLN 267
Cdd:PRK09053 125 DLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALLRHRQRLAALRPRALVLQFGG-AAGTLAS 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 268 TRIGFAEKVAAKVAALtGLPFVTAPNKfealAAHDALVELSGAMNTTACSLMKIANDIRFLgsgPRSGLGELILP--ENE 345
Cdd:PRK09053 204 LGEQALPVAQALAAEL-QLALPALPWH----TQRDRIAEFASALGLLAGTLGKIARDVSLL---MQTEVGEVFEPaaAGK 275
|
170 180
....*....|....*....|....*..
gi 119590496 346 PGSSIMPGKVNPTQCEAMTMVAAQVMG 372
Cdd:PRK09053 276 GGSSTMPHKRNPVGCAAVLTAATRAPG 302
|
|
| Adenylsuccinate_lyase_2 |
cd03302 |
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ... |
188-372 |
3.47e-09 |
|
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: 58.87 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 188 EVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAAGGTaVGTG-- 265
Cdd:cd03302 113 DLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTTVGKRACLWIQDLLMDLRNLERLRDDLRFRGVKGT-TGTQas 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 266 --------------LNTRI----GFaekvaAKVAALTGLpfvTAPNKFEALAAhDALVELsGAmnttacSLMKIANDIRF 327
Cdd:cd03302 192 fldlfegdhdkveaLDELVtkkaGF-----KKVYPVTGQ---TYSRKVDIDVL-NALSSL-GA------TAHKIATDIRL 255
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 119590496 328 LgsgprSGLGELILP--ENEPGSSIMPGKVNPTQCEAMTMVAAQVMG 372
Cdd:cd03302 256 L-----ANLKEVEEPfeKGQIGSSAMPYKRNPMRSERCCSLARHLMN 297
|
|
| PRK09285 |
PRK09285 |
adenylosuccinate lyase; Provisional |
177-357 |
3.58e-09 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236452 [Multi-domain] Cd Length: 456 Bit Score: 58.61 E-value: 3.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 177 AMHIAAAIEvhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAmpriyELA 256
Cdd:PRK09285 132 ALMLKEARE--EVLLPALRELIDALKELAHEYADVPMLSRTHGQPATPTTLGKEMANVAYRLERQLKQLEAV-----EIL 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 257 A--GGtAVGTgLN-------------------TRIGfaekvaakvaaLTGLPFVTA--PnkfealaaHDALVELSGAM-- 311
Cdd:PRK09285 205 GkiNG-AVGN-YNahlaaypevdwhafsrefvESLG-----------LTWNPYTTQieP--------HDYIAELFDAVar 263
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 119590496 312 -NTtacSLMKIANDI------RFLGSGPRSGlgelilpenEPGSSIMPGKVNP 357
Cdd:PRK09285 264 fNT---ILIDLDRDVwgyislGYFKQKTKAG---------EIGSSTMPHKVNP 304
|
|
| PLN02646 |
PLN02646 |
argininosuccinate lyase |
100-379 |
6.21e-09 |
|
argininosuccinate lyase
Pssm-ID: 215348 [Multi-domain] Cd Length: 474 Bit Score: 58.20 E-value: 6.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 100 ANAIMKAADEVAEGKLNDHFplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvhpndHVNKSQssNDTFPT--A 177
Cdd:PLN02646 70 RDSILDGLDEIEKEIEAGKF---EWRPD-----REDVHMNNEARLTELIG-EPAKKL------HTARSR--NDQVATdtR 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 178 MHIAAAIEVhevLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYAMTRIKAAMPRIYELAA 257
Cdd:PLN02646 133 LWCRDAIDV---IRKRIKTLQVALVELAEKNVDLVVPGYTHLQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPL 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 258 GGTAV-GTGLntriGFAEKVAAKVAALTGLpfvtAPNKFEALAAHDALVELSGAMNTTACSLMKIANDIRFLGSGPrsgL 336
Cdd:PLN02646 210 GSCALaGTGL----PIDRFMTAKDLGFTAP----MRNSIDAVSDRDFVLEFLFANSITAIHLSRLGEEWVLWASEE---F 278
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 119590496 337 GELILPEN-EPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 379
Cdd:PLN02646 279 GFVTPSDAvSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLA 322
|
|
| Argininosuccinate_lyase |
cd01359 |
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ... |
80-442 |
6.92e-08 |
|
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: 54.86 E-value: 6.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 80 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGSGtqtnmNVNEVISNRAIEMLGgELGSKIpvh 159
Cdd:cd01359 27 GILTEEEAA---------KILAGLAKIRAEIEAGAF-------ELDPEDE-----DIHMAIERRLIERIG-DVGGKL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 160 pndHVNKSqsSNDTFPTAMHIAAAIEVhEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVK 239
Cdd:cd01359 82 ---HTGRS--RNDQVATDLRLYLRDAL-LELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 240 YAMTRIKAAMPRIYELAAGGTA-VGTGLN-------TRIGFAEKvaakvaaltglpfvtAPNKFEALAAHDALVELSGAM 311
Cdd:cd01359 156 RDLERLADAYKRVNVSPLGAGAlAGTTFPidrertaELLGFDGP---------------TENSLDAVSDRDFVLEFLSAA 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 312 NTTACSLMKIANDIRFLGSGPRsGLGELilpeneP-----GSSIMPGKVNPTQCEAMTMVAAQVMGNHVAV--TVGG--S 382
Cdd:cd01359 221 ALLMVHLSRLAEDLILWSTQEF-GFVEL------PdaystGSSIMPQKKNPDVLELIRGKAGRVIGALAGLltTLKGlpL 293
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119590496 383 NGHFELNVFKPMM---IKNVLHSARLLGDasvsftenCVVGIQANTERINKLMNESLMLVTAL 442
Cdd:cd01359 294 AYNKDLQEDKEPLfdaVDTLIASLRLLTG--------VISTLTVNPERMREAAEAGFSTATDL 348
|
|
| PRK12308 |
PRK12308 |
argininosuccinate lyase; |
150-361 |
1.41e-06 |
|
argininosuccinate lyase;
Pssm-ID: 183425 [Multi-domain] Cd Length: 614 Bit Score: 50.94 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 150 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 229
Cdd:PRK12308 97 GDLGKKL------HTGRSR--NDQVATDLKLWCRQQGQQLLL-ALDQLQQQMVNVAERHQGTVLPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 230 EFSGYVQQVKYAMTRIKAAMPRIYELAAG-GTAVGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAAH 301
Cdd:PRK12308 168 WCLAYVEMFERDYSRLEDALTRLDTCPLGsGALAGTAypidreaLAHNLGFRRATR---------------NSLDSVSDR 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119590496 302 DALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGEliLPEN-EPGSSIMPGKVNPTQCE 361
Cdd:PRK12308 233 DHVMELMSVASISMLHLSRLAEDLIFYNSG-ESGFIE--LADTvTSGSSLMPQKKNPDALE 290
|
|
| PRK08937 |
PRK08937 |
adenylosuccinate lyase; Provisional |
317-491 |
3.79e-06 |
|
adenylosuccinate lyase; Provisional
Pssm-ID: 236352 [Multi-domain] Cd Length: 216 Bit Score: 47.72 E-value: 3.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 317 SLMKIANDIRFLgSGPRSGLGELILPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNhvAVTVGGSNGH-FELNVFKPMM 395
Cdd:PRK08937 29 SLEKFANEIRLL-QRSEIREVEEPFAKGQKGSSAMPHKRNPIGSERITGLARVLRSY--LVTALENVPLwHERDLSHSSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 396 IKNVLHSARLLGDASVSFTENCVVGIQANTERINK--------LMNESLMLvTALNPHIG----YDKAAKIAKTAHKNGS 463
Cdd:PRK08937 106 ERIALPDAFLALDYILNRFVNILENLVVFPENIERnldktlgfIATERVLL-ELVEKGMGreeaHELIREKAMEAWKNQK 184
|
170 180 190
....*....|....*....|....*....|..
gi 119590496 464 TLKETAIE----LGYLTAEQFDEWVKPKDMLG 491
Cdd:PRK08937 185 DLRELLEAderfTKQLTKEELDELFDPEAFVG 216
|
|
| PLN02848 |
PLN02848 |
adenylosuccinate lyase |
186-361 |
1.02e-05 |
|
adenylosuccinate lyase
Pssm-ID: 178440 [Multi-domain] Cd Length: 458 Bit Score: 47.81 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 186 VHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSgyvqQVKYAMTRIKAAMP--RIYELAAGGT--- 260
Cdd:PLN02848 142 VNSVVLPTMDEIIKAISSLAHEFAYVPMLSRTHGQPASPTTLGKEMA----NFAYRLSRQRKQLSevKIKGKFAGAVgny 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 261 -------------AVGTGLNTRIGfaekvaakvaaLTGLPFVTapnkfeALAAHDALVELSGAMNTTACSLMKIANDIRF 327
Cdd:PLN02848 218 nahmsaypevdwpAVAEEFVTSLG-----------LTFNPYVT------QIEPHDYMAELFNAVSRFNNILIDFDRDIWS 280
|
170 180 190
....*....|....*....|....*....|....
gi 119590496 328 LGSgprSGLGELILPENEPGSSIMPGKVNPTQCE 361
Cdd:PLN02848 281 YIS---LGYFKQITKAGEVGSSTMPHKVNPIDFE 311
|
|
| PRK00855 |
PRK00855 |
argininosuccinate lyase; Provisional |
80-357 |
4.46e-05 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179143 [Multi-domain] Cd Length: 459 Bit Score: 45.91 E-value: 4.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 80 GILKRAAAEvnqdygldpKIANAIMKAADEVAEGKLndhfplvVWQTGsgtqtNMNVNEVISNRAIEMLGgELGSKIpvH 159
Cdd:PRK00855 51 GILSEEEAE---------KILAGLDEILEEIEAGKF-------EFSPE-----LEDIHMAIEARLTERIG-DVGGKL--H 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 160 P----NDHVnksqssndtfPTAMHIAAAIEVHEVLLpGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYV 235
Cdd:PRK00855 107 TgrsrNDQV----------ATDLRLYLRDEIDEIAE-LLLELQKALLDLAEEHADTIMPGYTHLQRAQPVTFGHHLLAYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 236 QQVKYAMTRIKAAMPRIYELAAGGTA-VGTGLNT-------RIGFAEkvaakvaaltglpfVTApNKFEALAAHDALVEL 307
Cdd:PRK00855 176 EMLARDLERLRDARKRVNRSPLGSAAlAGTTFPIdrertaeLLGFDG--------------VTE-NSLDAVSDRDFALEF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 119590496 308 SGAMNTTACSLMKIANDIrFLGSGPRSGLGELilpeneP-----GSSIMPGKVNP 357
Cdd:PRK00855 241 LSAASLLMVHLSRLAEEL-ILWSSQEFGFVEL------PdafstGSSIMPQKKNP 288
|
|
| PRK04833 |
PRK04833 |
argininosuccinate lyase; Provisional |
150-379 |
1.80e-04 |
|
argininosuccinate lyase; Provisional
Pssm-ID: 179883 [Multi-domain] Cd Length: 455 Bit Score: 43.82 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 150 GELGSKIpvhpndHVNKSQssNDTFPTAMHIAAAIEVHEvLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQ 229
Cdd:PRK04833 97 GDLGKKL------HTGRSR--NDQVATDLKLWCKDQVAE-LLTALRQLQSALVETAENNQDAVMPGYTHLQRAQPVTFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 230 EFSGYVQQVKYAMTRIKAAMPR--IYELAAGGTAvGTG-------LNTRIGFAEKVAakvaaltglpfvtapNKFEALAA 300
Cdd:PRK04833 168 WCLAYVEMLARDESRLQDALKRldVSPLGSGALA-GTAyeidreqLAGWLGFASATR---------------NSLDSVSD 231
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119590496 301 HDALVELSGAMNTTACSLMKIANDIRFLGSGpRSGLGELIlPENEPGSSIMPGKVNPTQCEAMTMVAAQVMGNHVAVTV 379
Cdd:PRK04833 232 RDHVLELLSDASISMVHLSRFAEDLIFFNSG-EAGFVELS-DRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLM 308
|
|
| PRK05975 |
PRK05975 |
3-carboxy-cis,cis-muconate cycloisomerase; Provisional |
162-376 |
6.59e-04 |
|
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
Pssm-ID: 168324 [Multi-domain] Cd Length: 351 Bit Score: 41.96 E-value: 6.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 162 DHVNKSQSSNDTFPTAMHIAAaIEVHEVLLPGLQKLHDALDAKSKEFAQIIKIGRTHTQDAVPLTLGQEFSGYVQQVKYA 241
Cdd:PRK05975 100 AHVHFGATSQDVIDTSLMLRL-KAASEILAARLGALIARLDALEATFGQNALMGHTRMQAAIPITVADRLASWRAPLLRH 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119590496 242 MTRIKAAMPRIYELAAGGtAVGTgLNTRIGFAEKVAAKVAALTGLPfvTAPnkfEALAAHDALVELSGAMNTTACSLMKI 321
Cdd:PRK05975 179 RDRLEALRADVFPLQFGG-AAGT-LEKLGGKAAAVRARLAKRLGLE--DAP---QWHSQRDFIADFAHLLSLVTGSLGKF 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 119590496 322 ANDIRFLgsgprSGLGELILPENEPGSSIMPGKVNPTQCEAMTMV----AAQVMGNHVA 376
Cdd:PRK05975 252 GQDIALM-----AQAGDEISLSGGGGSSAMPHKQNPVAAETLVTLarfnATQVSGLHQA 305
|
|
| |
