|
Name |
Accession |
Description |
Interval |
E-value |
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
5-422 |
0e+00 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 768.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 5 LKENTLIQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCAS 84
Cdd:PRK08639 1 MTVKMTVSAKDIDKAAKRLKDVVPETPLQRNDYLSEKYGANVYLKREDLQPVRSYKLRGAYNAISQLSDEELAAGVVCAS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 85 AGNHAQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEYVDIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVM 164
Cdd:PRK08639 81 AGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVRFFGGEFVEIVLVGDTFDDSAAAAQEYAEETGATFIPPFDDPDVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 165 AGQGTTAVEILNDIEVE--PHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVD 242
Cdd:PRK08639 161 AGQGTVAVEILEQLEKEgsPDYVFVPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAASMKAALEAGKPVTLEKIDKFVD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 243 GAAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNNDIG 322
Cdd:PRK08639 241 GAAVARVGDLTFEILKDVVDDVVLVPEGAVCTTILELYNKEGIVAEPAGALSIAALELYKDEIKGKTVVCVISGGNNDIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 323 RMQEIKERSMIYEGLQHYFIVNFPQRAGALREFLDEVLGPNDDISRFEYTKKNNRSKGPALVGIELKERDDYAALIDRMN 402
Cdd:PRK08639 321 RMPEIKERSLIYEGLKHYFIVNFPQRPGALREFLDDVLGPNDDITRFEYLKKNNRETGPVLVGIELKDAEDYDGLIERME 400
|
410 420
....*....|....*....|
gi 495621819 403 KKGFHYVEVNKDQDLFHLFI 422
Cdd:PRK08639 401 AFGPSYIDINPNEPLYNLLI 420
|
|
| THD1 |
TIGR02079 |
threonine dehydratase; This model represents threonine dehydratase, the first step in the ... |
14-422 |
0e+00 |
|
threonine dehydratase; This model represents threonine dehydratase, the first step in the pathway converting threonine into isoleucine. At least two other clades of biosynthetic threonine dehydratases have been characterized by models (TIGR01124 and TIGR01127). Those sequences described by this model are exclusively found in species containg the rest of the isoleucine pathway and which are generally lacking in members of the those other two clades of threonine dehydratases. Members of this clade are also often gene clustered with other elements of the isoleucine pathway. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 273957 [Multi-domain] Cd Length: 409 Bit Score: 610.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 14 KDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGVA 93
Cdd:TIGR02079 1 QDIEAARKRLKEVVPHTPLQLNERLSEKYGANIYLKREDLQPVRSYKIRGAYNFLKQLSDAQLAKGVVCASAGNHAQGFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 94 YSCKYLGIHGKIFMPATTPRQKVSQVELFGKEYVDIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVE 173
Cdd:TIGR02079 81 YACRHLGVHGTVFMPATTPKQKIDRVKIFGGEFIEIILVGDTFDQCAAAAREHVEDHGGTFIPPFDDPRIIEGQGTVAAE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 174 ILNDIEVEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGEKT 253
Cdd:TIGR02079 161 ILDQLPEKPDYVVVPVGGGGLISGLTTYLAGTSPKTKIIGVEPEGAPSMKASLEAGEVVTLDKIDNFVDGAAVKRVGDLN 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 254 FTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNNDIGRMQEIKERSMI 333
Cdd:TIGR02079 241 FKALKDVPDEVTLVPEGAVCTTILDLYNLEGIVAEPAGALSIAALERLGEEIKGKTVVCVVSGGNNDIERTEEIRERSLL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 334 YEGLQHYFIVNFPQRAGALREFLDEVLGPNDDISRFEYTKKNNRSKGPALVGIELKERDDYAALIDRMNKKGFHYVEVNK 413
Cdd:TIGR02079 321 YEGLKHYFIVRFPQRPGALREFLNDVLGPNDDITRFEYTKKSNRETGPALIGIELNDKEDFAGLLERMAAADIHYEDINE 400
|
....*....
gi 495621819 414 DQDLFHLFI 422
Cdd:TIGR02079 401 NDILYNLLI 409
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
9-336 |
3.60e-144 |
|
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the Pathway/BioSystem: Isoleucine, leucine, valine biosynthesis
Pssm-ID: 440784 [Multi-domain] Cd Length: 327 Bit Score: 413.28 E-value: 3.60e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 9 TLIQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNH 88
Cdd:COG1171 4 LMPTLADIEAAAARIAGVVRRTPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNALASLSEEERARGVVAASAGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 89 AQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQG 168
Cdd:COG1171 84 AQGVAYAARLLGIPATIVMPETAPAVKVAATRAYGAE---VVLHGDTYDDAEAAAAELAEEEGATFVHPFDDPDVIAGQG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 169 TTAVEILNDIEvEPHFLF------------AsvggggllsgvgTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDS 236
Cdd:COG1171 161 TIALEILEQLP-DLDAVFvpvggggliagvA------------AALKALSPDIRVIGVEPEGAAAMYRSLAAGEPVTLPG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 237 IDKFVDGAAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSG 316
Cdd:COG1171 228 VDTIADGLAVGRPGELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAALAALLAGKERLKGKRVVVVLSG 307
|
330 340
....*....|....*....|
gi 495621819 317 GNNDIGRMQEIKERSMIYEG 336
Cdd:COG1171 308 GNIDPDRLAEILERGLVGEG 327
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
13-320 |
1.35e-135 |
|
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. Although the nitrogen atoms of most amino acids are transferred to alpha-ketoglutarate before removal, the alpha-amino group of threonine can be directly converted into NH4+. The direct deamination is catalyzed by threonine dehydratase, in which pyridoxal phosphate (PLP) is the prosthetic group. Threonine dehydratase is widely distributed in all three major phylogenetic divisions.
Pssm-ID: 107205 [Multi-domain] Cd Length: 304 Bit Score: 390.69 E-value: 1.35e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 13 VKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGV 92
Cdd:cd01562 1 LEDILAAAARIKPVVRRTPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKGVVAASAGNHAQGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 93 AYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAV 172
Cdd:cd01562 81 AYAAKLLGIPATIVMPETAPAAKVDATRAYGAE---VVLYGEDFDEAEAKARELAEEEGLTFIHPFDDPDVIAGQGTIGL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 173 EILNDIEvEPHFLF------------AsvggggllsgvgTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKF 240
Cdd:cd01562 158 EILEQVP-DLDAVFvpvggggliagiA------------TAVKALSPNTKVIGVEPEGAPAMAQSLAAGKPVTLPEVDTI 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 241 VDGAAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNND 320
Cdd:cd01562 225 ADGLAVKRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALALAALLSGKLDLKGKKVVVVLSGGNID 304
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
13-414 |
4.43e-115 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 345.59 E-value: 4.43e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 13 VKDILKAHqnLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGV 92
Cdd:PRK09224 6 LRKILTAR--VYDVAQETPLEKAPKLSARLGNQVLLKREDLQPVFSFKLRGAYNKMAQLTEEQLARGVITASAGNHAQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 93 AYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAV 172
Cdd:PRK09224 84 ALSAARLGIKAVIVMPVTTPDIKVDAVRAFGGE---VVLHGDSFDEAYAHAIELAEEEGLTFIHPFDDPDVIAGQGTIAM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 173 EILNDIEVEPHFLF------------AsvggggllsgvgTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKF 240
Cdd:PRK09224 161 EILQQHPHPLDAVFvpvggggliagvA------------AYIKQLRPEIKVIGVEPEDSACLKAALEAGERVDLPQVGLF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 241 VDGAAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAAL--DAHREEIKGKNVVCIVSGGN 318
Cdd:PRK09224 229 ADGVAVKRIGEETFRLCQEYVDDVITVDTDEICAAIKDVFEDTRSIAEPAGALALAGLkkYVAQHGIEGETLVAILSGAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 319 NDIGRMQEIKERSMIYEGLQHYFIVNFPQRAGALREFLdEVLGpNDDISRFEYtKKNNRSKGPALVGIELKERDDY-AAL 397
Cdd:PRK09224 309 MNFDRLRYVAERAELGEQREALLAVTIPEEPGSFLKFC-ELLG-GRNVTEFNY-RYADAKEAHIFVGVQLSRGQEErAEI 385
|
410
....*....|....*..
gi 495621819 398 IDRMNKKGFHYVEVNKD 414
Cdd:PRK09224 386 IAQLRAHGYPVVDLSDD 402
|
|
| ilvA_2Cterm |
TIGR01124 |
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ... |
16-415 |
1.06e-108 |
|
threonine ammonia-lyase, biosynthetic, long form; This model describes a form of threonine ammonia-lyase, a pyridoxal-phosphate dependent enzyme, with two copies of the threonine dehydratase C-terminal domain (pfam00585). Members with known function participate in isoleucine biosynthesis and are inhibited by isoleucine. Alternate name: threonine deaminase, threonine dehydratase. Forms scoring between the trusted and noise cutoff tend to branch with this subgroup of threonine ammonia-lyase phylogenetically but have only a single copy of the C-terminal domain. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130194 [Multi-domain] Cd Length: 499 Bit Score: 329.39 E-value: 1.06e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 16 ILKAhqNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGVAYS 95
Cdd:TIGR01124 6 ILTA--RVYEAAQETPLQKAAKLSERLGNRILIKREDLQPVFSFKLRGAYNKMAQLSPEQKARGVIAASAGNHAQGVAFS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 96 CKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVEIL 175
Cdd:TIGR01124 84 AARLGLKALIVMPETTPDIKVDAVRGFGGE---VVLHGANFDDAKAKAIELSQEKGLTFIHPFDDPLVIAGQGTLALEIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 176 NDIEVEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGEKTFT 255
Cdd:TIGR01124 161 RQVANPLDAVFVPVGGGGLAAGVAALIKQLMPEIKVIGVEPTDSDCMKQALDAGEPVDLDQVGLFADGVAVKRVGDETFR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 256 SLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAH--REEIKGKNVVCIVSGGNNDIGRMQEIKERSMI 333
Cdd:TIGR01124 241 LCQQYLDDIVTVDTDEVCAAIKDLFEDTRAVAEPAGALALAGLKKYvaLHGIRGQTLVAILSGANMNFHRLRYVSERCEL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 334 YEGLQHYFIVNFPQRAGALREFLdEVLGpNDDISRFEYtKKNNRSKGPALVGIELKERDDYAALIDRMNKKGFHYVEVNK 413
Cdd:TIGR01124 321 GEQREALLAVTIPEQPGSFLKFC-ELLG-NRNITEFNY-RYADRKDAHIFVGVQLSNPQERQEILARLNDGGYSVVDLTD 397
|
..
gi 495621819 414 DQ 415
Cdd:TIGR01124 398 DE 399
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
12-415 |
5.21e-94 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 292.09 E-value: 5.21e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 12 QVKDILKAHqnLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQG 91
Cdd:PRK12483 22 YLRKILAAR--VYDVARETPLQRAPNLSARLGNQVLLKREDLQPVFSFKIRGAYNKMARLPAEQLARGVITASAGNHAQG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 92 VAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTA 171
Cdd:PRK12483 100 VALAAARLGVKAVIVMPRTTPQLKVDGVRAHGGE---VVLHGESFPDALAHALKLAEEEGLTFVPPFDDPDVIAGQGTVA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 172 VEILNDIEVEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGE 251
Cdd:PRK12483 177 MEILRQHPGPLDAIFVPVGGGGLIAGIAAYVKYVRPEIKVIGVEPDDSNCLQAALAAGERVVLGQVGLFADGVAVAQIGE 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 252 KTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALD--AHREEIKGKNVVCIVSGGNNDIGRMQEIKE 329
Cdd:PRK12483 257 HTFELCRHYVDEVVTVSTDELCAAIKDIYDDTRSITEPAGALAVAGIKkyAEREGIEGQTLVAIDSGANVNFDRLRHVAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 330 RSMIYEGLQHYFIVNFPQRAGALREFLdEVLGPNdDISRFEYTKKNNRSkGPALVGIELKERDD-YAALIDRMNKKGFHY 408
Cdd:PRK12483 337 RAELGEQREAIIAVTIPEQPGSFKAFC-AALGKR-QITEFNYRYADARE-AHLFVGVQTHPRHDpRAQLLASLRAQGFPV 413
|
....*..
gi 495621819 409 VEVNKDQ 415
Cdd:PRK12483 414 LDLTDDE 420
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
22-417 |
1.91e-86 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 274.88 E-value: 1.91e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 22 NLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGVAYSCKYLGI 101
Cdd:PLN02550 102 KVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDKGVICSSAGNHAQGVALSAQRLGC 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 102 HGKIFMPATTPRQKVSQVELFGkeyVDIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVEILNDIEVE 181
Cdd:PLN02550 182 DAVIAMPVTTPEIKWQSVERLG---ATVVLVGDSYDEAQAYAKQRALEEGRTFIPPFDHPDVIAGQGTVGMEIVRQHQGP 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 182 PHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGEKTFTSLQSVV 261
Cdd:PLN02550 259 LHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEPSDANAMALSLHHGERVMLDQVGGFADGVAVKEVGEETFRLCRELV 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 262 DKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHRE--EIKGKNVVCIVSGGNNDIGRMQEIKERSMIYEGLQH 339
Cdd:PLN02550 339 DGVVLVSRDAICASIKDMFEEKRSILEPAGALALAGAEAYCKyyGLKDENVVAITSGANMNFDRLRIVTELADVGRQQEA 418
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495621819 340 YFIVNFPQRAGALREFLDEVlGPNdDISRFEYtKKNNRSKGPALVGIELKERDDYAALIDRMNKKGFHYVEVNkDQDL 417
Cdd:PLN02550 419 VLATFMPEEPGSFKRFCELV-GPM-NITEFKY-RYSSEKEALVLYSVGVHTEQELQALKKRMESAQLRTVNLT-SNDL 492
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
5-329 |
9.59e-79 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 246.96 E-value: 9.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 5 LKENTLIQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCAS 84
Cdd:PRK08638 3 ITYDLPVAIDDIIEAKQRLAGRIRKTPLPRSNYLSERCKGEIFLKLENMQRTGSFKIRGAFNKLSSLTDAEKRKGVVACS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 85 AGNHAQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVM 164
Cdd:PRK08638 83 AGNHAQGVALSCALLGIDGKVVMPKGAPKSKVAATCGYGAE---VVLHGDNFNDTIAKVEEIVEEEGRTFIPPYDDPKVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 165 AGQGTTAVEILNDI-EVEPhfLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDG 243
Cdd:PRK08638 160 AGQGTIGLEILEDLwDVDT--VIVPIGGGGLIAGIAVALKSINPTIHIIGVQSENVHGMAASFYAGEITTHRTTGTLADG 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 244 AAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHR--EEIKGKNVVCIVSGGNNDI 321
Cdd:PRK08638 238 CDVSRPGNLTYEIVRELVDDIVLVSEDEIRNAMKDLIQRNKVVTEGAGALATAALLSGKldQYIQNKKVVAIISGGNVDL 317
|
....*...
gi 495621819 322 GRMQEIKE 329
Cdd:PRK08638 318 SRVSQITG 325
|
|
| ilvA_1Cterm |
TIGR01127 |
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the ... |
30-410 |
6.19e-76 |
|
threonine ammonia-lyase, medium form; A form of threonine dehydratase with two copies of the C-terminal domain pfam00585 is described by TIGR01124. This model describes a phylogenetically distinct form with a single copy of pfam00585. This form branches with the catabolic threonine dehydratase of E. coli; many members are designated as catabolic for this reason. However, the catabolic form lacks any pfam00585 domain. Many members of this model are found in species with other Ile biosynthetic enzymes. [Amino acid biosynthesis, Pyruvate family]
Pssm-ID: 130197 [Multi-domain] Cd Length: 380 Bit Score: 241.19 E-value: 6.19e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGVAYSCKYLGIHGKIFMPA 109
Cdd:TIGR01127 1 TPLIYSTTLSDITGSEVYLKLENLQKTGSFKIRGALNKIANLSEDQRQRGVVAASAGNHAQGVAYAAKKFGIKAVIVMPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 110 TTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVEILNDIevePHF--LFA 187
Cdd:TIGR01127 81 SAPPSKVKATKSYGAE---VILHGDDYDEAYAFATSLAEEEGRVFVHPFDDEFVMAGQGTIGLEIMEDI---PDVdtVIV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 188 SVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGEKTFTSLQSVVDKISLV 267
Cdd:TIGR01127 155 PVGGGGLISGVASAAKQINPNVKVIGVEAEGAPSMYESLREGKIKAVESVRTIADGIAVKKPGDLTFNIIKEYVDDVVTV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 268 PEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNNDIGRMQEIKERSMIYEGLQHYFIVNFPQ 347
Cdd:TIGR01127 235 DEEEIANAIYLLLERHKILAEGAGAAGVAALLEQKVDVKGKKIAVVLSGGNIDLNLLNKIIEKGLVKSGRKVRIETVLPD 314
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495621819 348 RAGALREFLDEVLGPNDDISRFEYTKKNNR-SKGPALVGIEL--KERDDYAALIDRMNKKGFHYVE 410
Cdd:TIGR01127 315 RPGALYHLLESIAEARANIVKIDHDRLSKEiPPGFAMVEITLetRGKEHLDEILKILRDMGYNFYV 380
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
11-352 |
2.81e-73 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 234.79 E-value: 2.81e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 11 IQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQ 90
Cdd:PRK07334 5 VTLADIRAAAARLAGQVLRTPCVHSRTLSQITGAEVWLKFENLQFTASFKERGALNKLLLLTEEERARGVIAMSAGNHAQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 91 GVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTT 170
Cdd:PRK07334 85 GVAYHAQRLGIPATIVMPRFTPTVKVERTRGFGAE---VVLHGETLDEARAHARELAEEEGLTFVHPYDDPAVIAGQGTV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 171 AVEILND--------IEVEPHFLFAsvggggllsGVGTYMKNIAPETEIIAVEPLGAASLHAsHEKGEVVTLDSiDKFVD 242
Cdd:PRK07334 162 ALEMLEDapdldtlvVPIGGGGLIS---------GMATAAKALKPDIEIIGVQTELYPSMYA-AIKGVALPCGG-STIAE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 243 GAAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNNDIG 322
Cdd:PRK07334 231 GIAVKQPGQLTLEIVRRLVDDILLVSEADIEQAVSLLLEIEKTVVEGAGAAGLAALLAYPERFRGRKVGLVLSGGNIDTR 310
|
330 340 350
....*....|....*....|....*....|
gi 495621819 323 RMQEIKERSMIYEGLQHYFIVNFPQRAGAL 352
Cdd:PRK07334 311 LLANVLLRGLVRAGRLARLRVDIRDRPGAL 340
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
30-316 |
9.21e-65 |
|
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate dependent enzymes. This family includes: serine dehydratase EC:4.2.1.13 P20132, threonine dehydratase EC:4.2.1.16, tryptophan synthase beta chain EC:4.2.1.20, threonine synthase EC:4.2.99.2, cysteine synthase EC:4.2.99.8 P11096, cystathionine beta-synthase EC:4.2.1.22, 1-aminocyclopropane-1-carboxylate deaminase EC:4.1.99.4.
Pssm-ID: 459749 [Multi-domain] Cd Length: 295 Bit Score: 209.47 E-value: 9.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGVAYSCKYLGIHGKIFMPA 109
Cdd:pfam00291 8 TPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEGEGGKTVVEASSGNHGRALAAAAARLGLKVTIVVPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 110 TTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVK-CGDKEKREFIHPFDDLDVMAGQGTTAVEILNDIEVEPHFLFAS 188
Cdd:pfam00291 88 DAPPGKLLLMRALGAE---VVLVGGDYDEAVAAARElAAEGPGAYYINQYDNPLNIEGYGTIGLEILEQLGGDPDAVVVP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 189 VGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRI-GEKTFTSLQSVVDKISLV 267
Cdd:pfam00291 165 VGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSLAAGRPVPVPVADTIADGLGVGDEpGALALDLLDEYVGEVVTV 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 495621819 268 PEGKVCTTILELYNQCAIVAEPAGALPIAALDAH-REEIKGK-NVVCIVSG 316
Cdd:pfam00291 245 SDEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGELKGGdRVVVVLTG 295
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
13-327 |
1.51e-59 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 196.45 E-value: 1.51e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 13 VKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGV 92
Cdd:PRK06815 4 FDAILEAHQRLRPQVRVTPLEHSPLLSQHTGCEVYLKCEHLQHTGSFKFRGASNKLRLLNEAQRQQGVITASSGNHGQGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 93 AYSCKYLGIHGKIFMPATTPRQKVSQVELFGkeyVDIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAV 172
Cdd:PRK06815 84 ALAAKLAGIPVTVYAPEQASAIKLDAIRALG---AEVRLYGGDALNAELAARRAAEQQGKVYISPYNDPQVIAGQGTIGM 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 173 EILNDIEvEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAA--VQRiG 250
Cdd:PRK06815 161 ELVEQQP-DLDAVFVAVGGGGLISGIATYLKTLSPKTEIIGCWPANSPSLYTSLEAGEIVEVAEQPTLSDGTAggVEP-G 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495621819 251 EKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNNDIGRMQEI 327
Cdd:PRK06815 239 AITFPLCQQLIDQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRYQGKKVAVVLCGKNIVLEKYLEA 315
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
30-317 |
3.70e-59 |
|
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP)-dependent enzymes catalyzes beta-replacement and beta-elimination reactions. This CD corresponds to aminocyclopropane-1-carboxylate deaminase (ACCD), tryptophan synthase beta chain (Trp-synth_B), cystathionine beta-synthase (CBS), O-acetylserine sulfhydrylase (CS), serine dehydratase (Ser-dehyd), threonine dehydratase (Thr-dehyd), diaminopropionate ammonia lyase (DAL), and threonine synthase (Thr-synth). ACCD catalyzes the conversion of 1-aminocyclopropane-1-carboxylate to alpha-ketobutyrate and ammonia. Tryptophan synthase folds into a tetramer, where the beta chain is the catalytic PLP-binding subunit and catalyzes the formation of L-tryptophan from indole and L-serine. CBS is a tetrameric hemeprotein that catalyzes condensation of serine and homocysteine to cystathionine. CS is a homodimer that catalyzes the formation of L-cysteine from O-acetyl-L-serine. Ser-dehyd catalyzes the conversion of L- or D-serine to pyruvate and ammonia. Thr-dehyd is active as a homodimer and catalyzes the conversion of L-threonine to 2-oxobutanoate and ammonia. DAL is also a homodimer and catalyzes the alpha, beta-elimination reaction of both L- and D-alpha, beta-diaminopropionate to form pyruvate and ammonia. Thr-synth catalyzes the formation of threonine and inorganic phosphate from O-phosphohomoserine.
Pssm-ID: 107202 [Multi-domain] Cd Length: 244 Bit Score: 193.12 E-value: 3.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENG--IVCASAGNHAQGVAYSCKYLGIHGKIFM 107
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKLPKgvIIESTGGNTGIALAAAAARLGLKCTIVM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 108 PATTPRQKVSQVELFGkeyVDIILTGDTFDDSYHEAVK-CGDKEKREFIHPFDDLDVMAGQGTTAVEILNDI-EVEPHFL 185
Cdd:cd00640 81 PEGASPEKVAQMRALG---AEVVLVPGDFDDAIALAKElAEEDPGAYYVNQFDNPANIAGQGTIGLEILEQLgGQKPDAV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 186 F------------AsvggggllsgvgTYMKNIAPETEIIAVEPlgaaslhashekgEVVTldsidkfvdgaavqrigekt 253
Cdd:cd00640 158 VvpvggggniagiA------------RALKELLPNVKVIGVEP-------------EVVT-------------------- 192
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495621819 254 ftslqsvvdkislVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEI-KGKNVVCIVSGG 317
Cdd:cd00640 193 -------------VSDEEALEAIRLLAREEGILVEPSSAAALAAALKLAKKLgKGKTVVVILTGG 244
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
9-323 |
7.66e-55 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 184.45 E-value: 7.66e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 9 TLIQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNH 88
Cdd:PRK07048 4 LLPTYDDVAAAAARLAGVAHRTPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNALSQFSPEQRRAGVVTFSSGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 89 AQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEYVdiiltgdTFDDSYHEAVKCGDK--EKREF--IHPFDDLDVM 164
Cdd:PRK07048 84 AQAIALSARLLGIPATIVMPQDAPAAKVAATRGYGGEVV-------TYDRYTEDREEIGRRlaEERGLtlIPPYDHPHVI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 165 AGQGTTAVEILNdiEVEP-HFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDG 243
Cdd:PRK07048 157 AGQGTAAKELFE--EVGPlDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEAGNDGQQSFRSGEIVHIDTPRTIADG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 244 AAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNNDIGR 323
Cdd:PRK07048 235 AQTQHLGNYTFPIIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEPTGCLGAAAALRGKVPLKGKRVGVIISGGNVDLAR 314
|
|
| eutB |
PRK07476 |
threonine dehydratase; Provisional |
11-327 |
2.82e-54 |
|
threonine dehydratase; Provisional
Pssm-ID: 236025 [Multi-domain] Cd Length: 322 Bit Score: 182.86 E-value: 2.82e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 11 IQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQ 90
Cdd:PRK07476 1 VSLADIYRARRRIAGRVRRTPLVASASLSARAGVPVWLKLETLQPTGSFKLRGATNALLSLSAQERARGVVTASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 91 GVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTT 170
Cdd:PRK07476 81 ALAYAARALGIRATICMSRLVPANKVDAIRALGAE---VRIVGRSQDDAQAEVERLVREEGLTMVPPFDDPRIIAGQGTI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 171 AVEILNDI-EVEPHF-------LFASVGGGgllsgvgtyMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVD 242
Cdd:PRK07476 158 GLEILEALpDVATVLvplsgggLASGVAAA---------VKAIRPAIRVIGVSMERGAAMHASLAAGRPVQVEEVPTLAD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 243 --GAAVQRIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNND 320
Cdd:PRK07476 229 slGGGIGLDNRYTFAMCRALLDDVVLLDEAEIAAGIRHAYREERLVVEGAGAVGIAALLAGKIAARDGPIVVVVSGANID 308
|
....*..
gi 495621819 321 IGRMQEI 327
Cdd:PRK07476 309 MELHRRI 315
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
10-333 |
5.62e-50 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 172.26 E-value: 5.62e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 10 LIQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQL-PKEKLENGIVCASAGNH 88
Cdd:PRK06608 4 LQNPQNIAAAHNRIKQYLHLTPIVHSESLNEMLGHEIFFKVESLQKTGAFKVRGVLNHLLELkEQGKLPDKIVAYSTGNH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 89 AQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTgDTFDDSyHEAVKCGDKEKREFIHPFDDLDVMAGQG 168
Cdd:PRK06608 84 GQAVAYASKLFGIKTRIYLPLNTSKVKQQAALYYGGE---VILT-NTRQEA-EEKAKEDEEQGFYYIHPSDSDSTIAGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 169 TTAVEILNDIEVEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTL-DSIDKFVDGAAVQ 247
Cdd:PRK06608 159 TLCYEALQQLGFSPDAIFASCGGGGLISGTYLAKELISPTSLLIGSEPLNANDAYLSLKNNKIYRLnYSPNTIADGLKTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 248 RIGEKTFTSLQSvVDKISLVPEGKV------CTTILELYnqcaivAEPAGALPIAALDAH-REEIKGKNVVCIVSGGNND 320
Cdd:PRK06608 239 SVSARTFEYLKK-LDDFYLVEEYEIyywtawLTHLLKVI------CEPSSAINMVAVVNWlKTQSKPQKLLVILSGGNID 311
|
330
....*....|...
gi 495621819 321 IGRMQEIKERSMI 333
Cdd:PRK06608 312 PILYNELWKEDYL 324
|
|
| PLN02970 |
PLN02970 |
serine racemase |
11-326 |
4.09e-42 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 150.98 E-value: 4.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 11 IQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQ 90
Cdd:PLN02970 9 ADLSSIREARKRIAPFIHRTPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEKGVVTHSSGNHAA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 91 GVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTT 170
Cdd:PLN02970 89 ALALAAKLRGIPAYIVVPKNAPACKVDAVIRYGGI---ITWCEPTVESREAVAARVQQETGAVLIHPYNDGRVISGQGTI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 171 AVEILNDIEvEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQrIG 250
Cdd:PLN02970 166 ALEFLEQVP-ELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGADDAAQSKAAGEIITLPVTNTIADGLRAS-LG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 251 EKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAAldAHREEIK-------GKNVVCIVSGGNNDIGR 323
Cdd:PLN02970 244 DLTWPVVRDLVDDVITVDDKEIIEAMKLCYERLKVVVEPSGAIGLAA--ALSDSFRsnpawkgCKNVGIVLSGGNVDLGV 321
|
...
gi 495621819 324 MQE 326
Cdd:PLN02970 322 LWE 324
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
46-320 |
1.06e-41 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 149.33 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 46 VYLKREDLQVVRSFKLRGAFNKMsqLPKEKLENGIVCASAGNHAQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKE 125
Cdd:PRK08246 39 VWLKLEHLQHTGSFKARGAFNRL--LAAPVPAAGVVAASGGNAGLAVAYAAAALGVPATVFVPETAPPAKVARLRALGAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 126 YVdiiLTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVEILNDIevePHF-----------LFASVGGGgl 194
Cdd:PRK08246 117 VV---VVGAEYADALEAAQAFAAETGALLCHAYDQPEVLAGAGTLGLEIEEQA---PGVdtvlvavggggLIAGIAAW-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 195 lsgvgtymknIAPETEIIAVEPLGAASLHASHEKGEVVtldsiDKFVDGAAV-----QRIGEKTFTSLQSVVDKISLVPE 269
Cdd:PRK08246 189 ----------FEGRARVVAVEPEGAPTLHAALAAGEPV-----DVPVSGIAAdslgaRRVGEIAFALARAHVVTSVLVSD 253
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 495621819 270 GKVCTTILELYNQCAIVAEPAGALPIAALDAHR-EEIKGKNVVCIVSGGNND 320
Cdd:PRK08246 254 EAIIAARRALWEELRLAVEPGAATALAALLSGAyVPAPGERVAVVLCGANTD 305
|
|
| ectoine_eutB |
TIGR02991 |
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted ... |
11-321 |
3.63e-40 |
|
ectoine utilization protein EutB; Members of this protein family are EutB, a predicted arylmalonate decarboxylase found in a conserved ectoine utilization operon of species that include Sinorhizobium meliloti 1021 (where it is known to be induced by ectoine), Mesorhizobium loti, Silicibacter pomeroyi, Agrobacterium tumefaciens, and Pseudomonas putida. Members of this family resemble threonine dehydratases.
Pssm-ID: 132036 [Multi-domain] Cd Length: 317 Bit Score: 145.77 E-value: 3.63e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 11 IQVKDILKAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQ 90
Cdd:TIGR02991 1 VTLQDIERAAARISGRVEETPLVESPSLSELCGVPVHLKLEHRQTTGSFKLRGATNAVLSLSDTQRAAGVVAASTGNHGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 91 GVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTT 170
Cdd:TIGR02991 81 ALAYAAAEEGVRATICMSELVPQNKVDEIRRLGAE---VRIVGRSQDDAQEEVERLVADRGLTMLPPFDHPDIVAGQGTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 171 AVEILNDIEvEPHFLFASVGGGGLLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVD--GAAVQR 248
Cdd:TIGR02991 158 GLEVVEQMP-DLATVLVPLSGGGLASGVAMAVKAARPDTRVIGVSMERGAAMKASLQAGRPVLVAELPTLADslGGGIGL 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495621819 249 IGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVcIVSGGNNDI 321
Cdd:TIGR02991 237 DNRVTFAMCKALLDEIVLVSEAEIAAGIRHAYAEEREIVEGAGAVGIAALLAGKIKNPGPCAV-IVSGRNIDM 308
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
8-322 |
6.44e-38 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 140.53 E-value: 6.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 8 NTLIQVKDILKAHQNLKDVVIHTPLQKNERLSeryecnVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGN 87
Cdd:PRK08813 18 DVAVSVADVLAAQARLRRYLSPTPLHYAERFG------VWLKLENLQRTGSYKVRGALNALLAGLERGDERPVICASAGN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 88 HAQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGkeyVDIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQ 167
Cdd:PRK08813 92 HAQGVAWSAYRLGVQAITVMPHGAPQTKIAGVAHWG---ATVRQHGNSYDEAYAFARELADQNGYRFLSAFDDPDVIAGQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 168 GTTAVEILNDievEPHFLFASVGGGGLLSGVGTYMKNIApeTEIIAVEPLGAASLhASHEKGEVVTLDSIDKFVDGAAVQ 247
Cdd:PRK08813 169 GTVGIELAAH---APDVVIVPIGGGGLASGVALALKSQG--VRVVGAQVEGVDSM-ARAIRGDLREIAPVATLADGVKVK 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495621819 248 RIGEKTFTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAAldahREEIKGKNVVCIVSGGNNDIG 322
Cdd:PRK08813 243 IPGFLTRRLCSSLLDDVVIVREAELRETLVRLALEEHVIAEGAGALALAA----GRRVSGKRKCAVVSGGNIDAT 313
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
29-330 |
3.41e-30 |
|
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the conversion of L- , D-serine, or L-threonine to pyruvate/ketobutyrate and ammonia.
Pssm-ID: 107209 Cd Length: 316 Bit Score: 118.56 E-value: 3.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 29 HTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKE--KLENGIVCASAGNHAQGVAYSCKYLGIHGKIF 106
Cdd:cd06448 1 KTPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQglNECVHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 107 MPATTPRQKVSQVELFGkeyVDIILTGDT-FDDSYHEAVKCGDKEKR-EFIHPFDDLDVMAGQGTTAVEILNDIEVEPHF 184
Cdd:cd06448 81 VPESTKPRVVEKLRDEG---ATVVVHGKVwWEADNYLREELAENDPGpVYVHPFDDPLIWEGHSSMVDEIAQQLQSQEKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 185 -----------LFASVGGGGLlsgvgtymKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGEKT 253
Cdd:cd06448 158 daivcsvggggLLNGIVQGLE--------RNGWGDIPVVAVETEGAHSLNASLKAGKLVTLPKITSVATSLGAKTVSSQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 254 FTSLQSVVDKISLVPEGKVCTTILELYNQCAIVAEPAGALPIAA--------LDAHREEIKGKNVVCIVSGGNN-DIGRM 324
Cdd:cd06448 230 LEYAQEHNIKSEVVSDRDAVQACLRFADDERILVEPACGAALAVvysgkildLQLEVLLTPLDNVVVVVCGGSNiTLEQL 309
|
....*.
gi 495621819 325 QEIKER 330
Cdd:cd06448 310 KEYKKQ 315
|
|
| ACT_ThrD-I_2 |
cd04907 |
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine ... |
338-421 |
1.49e-29 |
|
Second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes the second of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153179 [Multi-domain] Cd Length: 81 Bit Score: 109.95 E-value: 1.49e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 338 QHYFIVNFPQRAGALREFLDEvLGPNDDISRFEYTKKNNrSKGPALVGIELKERdDYAALIDRMNKKGFHYVEVNKDQDL 417
Cdd:cd04907 1 ERLFRFEFPERPGALKKFLNE-LLPKWNITLFHYRNQGS-DYGRVLVGIQVPDA-DLDELKERLDALGYPYQEETDNPAY 77
|
....
gi 495621819 418 FHLF 421
Cdd:cd04907 78 KLFL 81
|
|
| Thr_dehydrat_C |
pfam00585 |
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all ... |
329-420 |
2.52e-29 |
|
C-terminal regulatory domain of Threonine dehydratase; Threonine dehydratases pfam00291 all contain a carboxy terminal region. This region may have a regulatory role. Some members contain two copies of this region. This family is homologous to the pfam01842 domain.
Pssm-ID: 395467 [Multi-domain] Cd Length: 91 Bit Score: 109.68 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 329 ERSMIYEGLQHYFIVNFPQRAGALREFLDEVLGPNdDISRFEYTKKNNrSKGPALVGIELKERDDYAALIDRMNKKGFHY 408
Cdd:pfam00585 1 ERALLGEGLEALLAVEFPEQPGALLTFLDLLGGRN-NITLFEYRKHGD-KNGCVLVGIELSQAEDLDEFIERLNKLGYDY 78
|
90
....*....|..
gi 495621819 409 VEVNKDQDLFHL 420
Cdd:pfam00585 79 EDLSDNEAAYEH 90
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
38-320 |
1.01e-23 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 100.84 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 38 LSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEK-LENGIVCASAGNHAQGVAYSCKYLGIHGKIFMPATTPRQKV 116
Cdd:PRK06110 30 LAERLGCEVWVKHENHTPTGAFKVRGGLVYFDRLARRGpRVRGVISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 117 SQVELFGKEYVDiilTGDTFDDSYHEAVKCGDKEKREFIHPFDDlDVMAGQGTTAVEILN---DIEVephfLFASVGGGG 193
Cdd:PRK06110 110 AAMRALGAELIE---HGEDFQAAREEAARLAAERGLHMVPSFHP-DLVRGVATYALELFRavpDLDV----VYVPIGMGS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 194 LLSGVGTYMKNIAPETEIIAVEPLGAASLHASHEKGEVVTLDSIDKFVDGAAVQRIGEKTFTSLQSVVDKISLVPEGKVC 273
Cdd:PRK06110 182 GICGAIAARDALGLKTRIVGVVSAHAPAYALSFEAGRVVTTPVATTLADGMACRTPDPEALEVIRAGADRIVRVTDDEVA 261
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 495621819 274 TTILELYNQCAIVAEPAGALPIAALDAHREEIKGKNVVCIVSGGNND 320
Cdd:PRK06110 262 AAMRAYFTDTHNVAEGAGAAALAAALQERERLAGKRVGLVLSGGNID 308
|
|
| ACT_ThrD-I |
cd04885 |
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); ... |
341-410 |
5.74e-23 |
|
Tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase); This CD includes each of two tandem C-terminal ACT domains of threonine dehydratase I (ThrD-I; L-threonine hydrolyase) which catalyzes the committed step in branched chain amino acid biosynthesis in plants and microorganisms, the pyridoxal 5'-phosphate (PLP)-dependent dehydration/deamination of L-threonine (or L-serine) to 2-ketobutyrate (or pyruvate). ThrD-I is a cooperative, feedback-regulated (isoleucine and valine) allosteric enzyme that forms a tetramer and contains four pyridoxal phosphate moieties. Members of this CD belong to the superfamily of ACT regulatory domains.
Pssm-ID: 153157 [Multi-domain] Cd Length: 68 Bit Score: 91.41 E-value: 5.74e-23
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 341 FIVNFPQRAGALREFLdEVLGPNDDISRFEYTKKnNRSKGPALVGIELKERDDYAALIDRMNKKGFHYVE 410
Cdd:cd04885 1 FAVTFPERPGALKKFL-ELLGPPRNITEFHYRNQ-GGDEARVLVGIQVPDREDLAELKERLEALGYPYVD 68
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
29-314 |
5.75e-15 |
|
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS is a unique heme-containing enzyme that catalyzes a pyridoxal 5'-phosphate (PLP)-dependent condensation of serine and homocysteine to give cystathionine. Deficiency of CBS leads to homocystinuria, an inherited disease of sulfur metabolism characterized by increased levels of the toxic metabolite homocysteine. Cysteine synthase on the other hand catalyzes the last step of cysteine biosynthesis. This subgroup also includes an O-Phosphoserine sulfhydrylase found in hyperthermophilic archaea which produces L-cysteine from sulfide and the more thermostable O-phospho-L-serine.
Pssm-ID: 107204 [Multi-domain] Cd Length: 291 Bit Score: 74.86 E-value: 5.75e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 29 HTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLPKE-KLENG--IVCASAGNHAQGVAYSCKYLGIHGKI 105
Cdd:cd01561 2 NTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRgLLKPGttIIEPTSGNTGIGLAMVAAAKGYRFII 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 106 FMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGD---KEKREFIHP--FDDLD-VMAGQGTTAVEILNDIE 179
Cdd:cd01561 82 VMPETMSEEKRKLLRALGAE---VILTPEAEADGMKGAIAKARelaAETPNAFWLnqFENPAnPEAHYETTAPEIWEQLD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 180 VEPHFLFASVGgggllsgvgT---------YMKNIAPETEIIAVEPLGAASLHASHEKgevvtldsidkfvdGAAVQRIG 250
Cdd:cd01561 159 GKVDAFVAGVG---------TggtitgvarYLKEKNPNVRIVGVDPVGSVLFSGGPPG--------------PHKIEGIG 215
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495621819 251 EKTFTSL--QSVVDKISLVPEGKVCTTILELYNQCAIVAEP-AGALPIAALDAHREEIKGKNVVCIV 314
Cdd:cd01561 216 AGFIPENldRSLIDEVVRVSDEEAFAMARRLAREEGLLVGGsSGAAVAAALKLAKRLGPGKTIVTIL 282
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
30-316 |
8.23e-15 |
|
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last reaction in the synthesis of threonine from aspartate. It proceeds by converting O-phospho-L-homoserine (OPH) into threonine and inorganic phosphate. In plants, OPH is an intermediate between the methionine and threonine/isoleucine pathways. Thus threonine synthase competes for OPH with cystathionine-gamma-synthase, the first enzyme in the methionine pathway. These enzymes are in general dimers. Members of this CD, Thr-synth_1, are widely distributed in bacteria, archaea and higher plants.
Pssm-ID: 107206 [Multi-domain] Cd Length: 324 Bit Score: 74.94 E-value: 8.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYE-CNVYLKREDLQVVRSFKLRGAFNKMSQLpKEKLENGIVCASAGNHAQGVAYSCKYLGIHGKIFMP 108
Cdd:cd01563 23 TPLVRAPRLGERLGgKNLYVKDEGLNPTGSFKDRGMTVAVSKA-KELGVKAVACASTGNTSASLAAYAARAGIKCVVFLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 109 ATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKekrefiHPFDDLDVM-----AGQGTTAVEILNDIEVE-P 182
Cdd:cd01563 102 AGKALGKLAQALAYGAT---VLAVEGNFDDALRLVRELAEE------NWIYLSNSLnpyrlEGQKTIAFEIAEQLGWEvP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 183 HFLF----------AsvggggllsgvgtYMK---------NIAPETEIIAVEPLGAASLHASHEKG--EVVTLDSIDKFV 241
Cdd:cd01563 173 DYVVvpvgnggnitA-------------IWKgfkelkelgLIDRLPRMVGVQAEGAAPIVRAFKEGkdDIEPVENPETIA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 242 DGAavqRIGEKtfTSLQSVVDKIS-------LVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREE---IKGKNVV 311
Cdd:cd01563 240 TAI---RIGNP--ASGPKALRAVResggtavAVSDEEILEAQKLLARTEGIFVEPASAASLAGLKKLREEgiiDKGERVV 314
|
....*
gi 495621819 312 CIVSG 316
Cdd:cd01563 315 VVLTG 319
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
30-316 |
2.74e-12 |
|
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the Pathway/BioSystem: Threonine biosynthesis
Pssm-ID: 440264 [Multi-domain] Cd Length: 394 Bit Score: 67.92 E-value: 2.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQLpKEKLENGIVCASAGNHAQGVAYSCKYLGIHGKIFMPA 109
Cdd:COG0498 67 TPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLA-LERGAKTIVCASSGNGSAALAAYAARAGIEVFVFVPE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 110 T-TPRQKVSQVELFGkeyVDIILTGDTFDDSYHEAVKCGDKEkrEF-----IHPFddldVMAGQGTTAVEILNDIEVEPH 183
Cdd:COG0498 146 GkVSPGQLAQMLTYG---AHVIAVDGNFDDAQRLVKELAADE--GLyavnsINPA----RLEGQKTYAFEIAEQLGRVPD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 184 FLF--------------ASVGGGGLLSGVGTymkniaPetEIIAVEPLGAASLHASHEKGEVV-------TL-DSID--- 238
Cdd:COG0498 217 WVVvptgnggnilagykAFKELKELGLIDRL------P--RLIAVQATGCNPILTAFETGRDEyeperpeTIaPSMDign 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 239 -----KFVD------GAAVQrigektftslqsvvdkislVPEGKVCTTILELYNQCAIVAEPAGALPIAALDAHREEI-- 305
Cdd:COG0498 289 psngeRALFalresgGTAVA-------------------VSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEGei 349
|
330
....*....|..
gi 495621819 306 -KGKNVVCIVSG 316
Cdd:COG0498 350 dPDEPVVVLSTG 361
|
|
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
18-314 |
2.55e-09 |
|
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the Pathway/BioSystem: Cysteine biosynthesis
Pssm-ID: 439802 [Multi-domain] Cd Length: 301 Bit Score: 58.14 E-value: 2.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 18 KAHQNLKDVVIHTPLQKNERLSERYECNVYLKREDLQVVRSFKLRGAFNkmsqLPKEKLENG-------IVCASAGNHAQ 90
Cdd:COG0031 2 RIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALS----MIEDAEKRGllkpggtIVEATSGNTGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 91 GVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILT-GDTFDDSYHEAVK--CgdKEKREFIHP--FDDLD-VM 164
Cdd:COG0031 78 GLAMVAAAKGYRLILVMPETMSKERRALLRAYGAE---VVLTpGAEGMKGAIDKAEelA--AETPGAFWPnqFENPAnPE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 165 AGQGTTAVEILNDIEVEPHFLFASVGgggllsgvgT---------YMKNIAPETEIIAVEPLGAASL----HASHEkgev 231
Cdd:COG0031 153 AHYETTGPEIWEQTDGKVDAFVAGVG---------TggtitgvgrYLKERNPDIKIVAVEPEGSPLLsggePGPHK---- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 232 vtldsidkfvdgaaVQRIGEKTFTSL--QSVVDKISLVPEGKVCTTILELYNQCAIVAEP-AGALPIAALDAHREEIKGK 308
Cdd:COG0031 220 --------------IEGIGAGFVPKIldPSLIDEVITVSDEEAFAMARRLAREEGILVGIsSGAAVAAALRLAKRLGPGK 285
|
....*.
gi 495621819 309 NVVCIV 314
Cdd:COG0031 286 TIVTIL 291
|
|
| PRK13803 |
PRK13803 |
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional |
30-145 |
1.04e-08 |
|
bifunctional phosphoribosylanthranilate isomerase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 237513 [Multi-domain] Cd Length: 610 Bit Score: 57.13 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYECNVYLKREDLQVVRSFKLRgafNKMSQ--LPKE-KLENGIVCASAGNHAQGVAYSCKYLGIHGKIF 106
Cdd:PRK13803 272 TPLTEAKRLSDIYGARIYLKREDLNHTGSHKIN---NALGQalLAKRmGKTRIIAETGAGQHGVATATACALFGLKCTIF 348
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 495621819 107 MPAT-TPRQ--KVSQVELFGKEYVDIILTGDTFDDSYHEAVK 145
Cdd:PRK13803 349 MGEEdIKRQalNVERMKLLGANVIPVLSGSKTLKDAVNEAIR 390
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
30-178 |
1.58e-08 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 56.36 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKnERLSERYECNVYLKREDLQVVRSFKLRGAFNKMSQ-LPKEklENGIVCASAGNHAQGV-AYSCKyLGIHGKIFM 107
Cdd:PRK05638 67 TPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLATVAVSYgLPYA--ANGFIVASDGNAAASVaAYSAR-AGKEAFVVV 142
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495621819 108 PATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVEILNDI 178
Cdd:PRK05638 143 PRKVDKGKLIQMIAFGAK---IIRYGESVDEAIEYAEELARLNGLYNVTPEYNIIGLEGQKTIAFELWEEI 210
|
|
| PRK13802 |
PRK13802 |
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional |
30-145 |
3.43e-07 |
|
bifunctional indole-3-glycerol phosphate synthase/tryptophan synthase subunit beta; Provisional
Pssm-ID: 184335 [Multi-domain] Cd Length: 695 Bit Score: 52.34 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSER------YECNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLENGIVCASAGNHAQGVAYSCKYLGIHG 103
Cdd:PRK13802 327 SPLTEAPRFAERvkektgLDARVFLKREDLNHTGAHKINNALGQALLVKRMGKTRVIAETGAGQHGVATATVCAMLGLKC 406
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 495621819 104 KIFMPATTPRQK---VSQVELFGKEYVDIILTGDTFDDSYHEAVK 145
Cdd:PRK13802 407 RIYMGQIDARRQalnVARMRMLGAEVVEVTLGDRILKDAINEALR 451
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
30-175 |
3.98e-07 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 51.80 E-value: 3.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYEC-NVYLKREDlqvVR----SFK-LRGAF-----------NKMSQLPKEKLENG----------IVC 82
Cdd:PRK08206 45 TPLVALPDLAAELGVgSILVKDES---YRfglnAFKaLGGAYavarllaeklgLDISELSFEELTSGevreklgditFAT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 83 ASAGNHAQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGKEyvdIILTGDTFDDSYHEAVKCGDKEKREFIH------ 156
Cdd:PRK08206 122 ATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAE---CIITDGNYDDSVRLAAQEAQENGWVVVQdtaweg 198
|
170 180
....*....|....*....|...
gi 495621819 157 ----PfddLDVMAGQGTTAVEIL 175
Cdd:PRK08206 199 yeeiP---TWIMQGYGTMADEAV 218
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
45-319 |
2.05e-06 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 49.44 E-value: 2.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 45 NVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLeNGIVCASAGNHAQGVAYSCKYLGIHGKIFMPATTPRQKVSQVELFGK 124
Cdd:PRK08329 73 KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI-NEVVIDSSGNAALSLALYSLSEGIKVHVFVSYNASKEKISLLSRLGA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 125 E--YVDiiltGDTFdDSYHEAVKCGDKEKREFIHPFDDLDVMAGQGTTAVEILNDIEVePHFLFASVGGGGLLS------ 196
Cdd:PRK08329 152 ElhFVE----GDRM-EVHEEAVKFSKRNNIPYVSHWLNPYFLEGTKTIAYEIYEQIGV-PDYAFVPVGSGTLFLgiwkgf 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 197 GVGTYMKNIAPETEIIAVEPLGAASL-HASHEKgevvtldsiDKFVDGAAV---QRIgEKTFTSLQSVVDKISLVPEGKV 272
Cdd:PRK08329 226 KELHEMGEISKMPKLVAVQAEGYESLcKRSKSE---------NKLADGIAIpepPRK-EEMLRALEESNGFCISVGEEET 295
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 495621819 273 CTTILELYNQCAIVaEPAGALPIAALDAHREE--IKGKNVVCIVSGGNN 319
Cdd:PRK08329 296 RAALHWLRRMGFLV-EPTSAVALAAYWKLLEEglIEGGSKVLLPLSGSG 343
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
30-125 |
3.41e-06 |
|
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the last two steps in the biosynthesis of L-tryptophan via its alpha and beta reactions. In the alpha reaction, indole 3-glycerol phosphate is cleaved reversibly to glyceraldehyde 3-phosphate and indole at the active site of the alpha subunit. In the beta reaction, indole undergoes a PLP-dependent reaction with L-serine to form L-tryptophan at the active site of the beta subunit. Members of this CD, Trp-synth_B, are found in all three major phylogenetic divisions.
Pssm-ID: 107207 Cd Length: 365 Bit Score: 48.69 E-value: 3.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYE-CNVYLKREDLQVVRSFKLRGA-----FNKmsQLPKEKL--ENGivcasAGNHAQGVAYSCKYLGI 101
Cdd:cd06446 35 TPLYRAKRLSEYLGgAKIYLKREDLNHTGAHKINNAlgqalLAK--RMGKKRViaETG-----AGQHGVATATACALFGL 107
|
90 100
....*....|....*....|....*..
gi 495621819 102 HGKIFMPATTPRQK---VSQVELFGKE 125
Cdd:cd06446 108 ECEIYMGAVDVERQplnVFRMELLGAE 134
|
|
| PLN02618 |
PLN02618 |
tryptophan synthase, beta chain |
23-145 |
5.53e-06 |
|
tryptophan synthase, beta chain
Pssm-ID: 215333 Cd Length: 410 Bit Score: 48.21 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 23 LKDVV-IHTPLQKNERLSERYE------CNVYLKREDLQVVRSFKLRGAFNKmSQLPKEKLENGIVCAS-AGNHAQGVAY 94
Cdd:PLN02618 59 LKDYVgRETPLYFAERLTEHYKradgegPEIYLKREDLNHTGAHKINNAVAQ-ALLAKRLGKKRIIAETgAGQHGVATAT 137
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 495621819 95 SCKYLGIHGKIFMPAT-TPRQK--VSQVELFGKEYVDIILTGDTFDDSYHEAVK 145
Cdd:PLN02618 138 VCARFGLECIVYMGAQdMERQAlnVFRMRLLGAEVRPVHSGTATLKDATSEAIR 191
|
|
| trpB |
TIGR00263 |
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the ... |
30-145 |
9.82e-06 |
|
tryptophan synthase, beta subunit; Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan. the beta chain contains the functional domain for or the synthesis of tryptophan from indole and serine. The enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-P attachment site is contained within the conserved region [LIVM]-x-H-x-G-[STA]-H-K-x-N] [K is the pyridoxal-P attachment site] which is present between residues 90-100 of the model. [Amino acid biosynthesis, Aromatic amino acid family]
Pssm-ID: 272987 Cd Length: 385 Bit Score: 47.36 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERY-ECNVYLKREDLQVVRSFKLRgafNKMSQ------LPKEKL--ENGivcasAGNHAQGVAYSCKYLG 100
Cdd:TIGR00263 51 TPLTFAPNLTEALgGAKIYLKREDLNHTGAHKIN---NALGQallakrMGKKRIiaETG-----AGQHGVATATAAALLG 122
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 495621819 101 IHGKIFMPAT-TPRQK--VSQVELFGKEYVDIILTGDTFDDSYHEAVK 145
Cdd:TIGR00263 123 LDCEVYMGAEdVERQKpnVFRMELLGAKVIPVTSGSGTLKDAVNEALR 170
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
30-128 |
2.99e-05 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 45.76 E-value: 2.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYEC-NVYLKREDLQVVRSFKLRGAFNKMSQlPKEKLENGIVCASAGNHAQGVAYSCKYLGIHGKIFMP 108
Cdd:PRK08197 80 TPLLPLPRLGKALGIgRLWVKDEGLNPTGSFKARGLAVGVSR-AKELGVKHLAMPTNGNAGAAWAAYAARAGIRATIFMP 158
|
90 100
....*....|....*....|..
gi 495621819 109 ATTPRQKVSQVELFGKE--YVD 128
Cdd:PRK08197 159 ADAPEITRLECALAGAElyLVD 180
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
29-182 |
5.01e-05 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 45.11 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 29 HTPLQKNErlseryecNVYLKREDLQVVRSFKLRGAFNKMSQLPKEKLeNGIVCASAGNHAQGVAYSCKYLGIHGKIFMP 108
Cdd:PRK06450 58 RTPLIKKG--------NIWFKLDFLNPTGSYKDRGSVTLISYLAEKGI-KQISEDSSGNAGASIAAYGAAAGIEVKIFVP 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495621819 109 ATTPRQKVSQVELFGKEYVDIiltGDTFDDSYHEAVKCGDKEKREFIHP-FDDldvmaGQGTTAVEILNDIEVEP 182
Cdd:PRK06450 129 ETASGGKLKQIESYGAEVVRV---RGSREDVAKAAENSGYYYASHVLQPqFRD-----GIRTLAYEIAKDLDWKI 195
|
|
| TrpB |
COG0133 |
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta ... |
30-125 |
6.63e-04 |
|
Tryptophan synthase beta chain [Amino acid transport and metabolism]; Tryptophan synthase beta chain is part of the Pathway/BioSystem: Aromatic amino acid biosynthesis
Pssm-ID: 439903 Cd Length: 400 Bit Score: 41.56 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYE-CNVYLKREDLQVVRSFKLRgafNKMSQ------LPKEKL--ENGivcasAGNHaqGVAYS--CKY 98
Cdd:COG0133 62 TPLYFAERLSEKLGgAKIYLKREDLNHTGAHKIN---NALGQallakrMGKKRIiaETG-----AGQH--GVATAtaAAL 131
|
90 100 110
....*....|....*....|....*....|
gi 495621819 99 LGIHGKIFMPAT-TPRQK--VSQVELFGKE 125
Cdd:COG0133 132 LGLECVVYMGEEdIERQAlnVFRMKLLGAE 161
|
|
| PRK13028 |
PRK13028 |
tryptophan synthase subunit beta; Provisional |
30-127 |
9.71e-04 |
|
tryptophan synthase subunit beta; Provisional
Pssm-ID: 183851 Cd Length: 402 Bit Score: 41.00 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYE-CNVYLKREDLQVVRSFKLRgafNKMSQ------LPKEKL--ENGivcasAGNHAQGVAYSCKYLG 100
Cdd:PRK13028 63 TPLYHAKRLSEELGgAQIYLKREDLNHTGAHKIN---NCLGQallakrMGKKRLiaETG-----AGQHGVATATAAALFG 134
|
90 100 110
....*....|....*....|....*....|
gi 495621819 101 IHGKIFMPAT-TPRQK--VSQVELFGKEYV 127
Cdd:PRK13028 135 LECEIYMGEVdIERQHpnVFRMKLLGAEVV 164
|
|
| PRK04346 |
PRK04346 |
tryptophan synthase subunit beta; Validated |
30-127 |
6.33e-03 |
|
tryptophan synthase subunit beta; Validated
Pssm-ID: 235288 Cd Length: 397 Bit Score: 38.51 E-value: 6.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495621819 30 TPLQKNERLSERYE-CNVYLKREDLQVVRSFKLRgafNKMSQ------LPKEKL--ENGivcasAGNHaqGVAYS--CKY 98
Cdd:PRK04346 59 TPLYFAERLSEHLGgAKIYLKREDLNHTGAHKIN---NVLGQallakrMGKKRIiaETG-----AGQH--GVATAtaAAL 128
|
90 100 110
....*....|....*....|....*....|..
gi 495621819 99 LGIHGKIFMPAT-TPRQK--VSQVELFGKEYV 127
Cdd:PRK04346 129 LGLECVIYMGAEdVERQAlnVFRMKLLGAEVV 160
|
|
| |
