|
Name |
Accession |
Description |
Interval |
E-value |
| CysK |
COG0031 |
Cysteine synthase [Amino acid transport and metabolism]; Cysteine synthase is part of the ... |
1-300 |
3.23e-167 |
|
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: 466.06 E-value: 3.23e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 1 MKLCENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLA 80
Cdd:COG0031 1 MRIYDSILELIGNTPLVRLNRLSPGPGAEIYAKLESFNPGGSVKDRIALSMIEDAEKRGLLKPGGTIVEATSGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 81 MNAAAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTAL 160
Cdd:COG0031 81 MVAAAKGYRLILVMPETMSKERRALLRAYGAEVVLTPGAEGMKGAIDKAEELAAETPGAFWPNQFENPANPEAHYETTGP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 161 EIYEQMDGELDAFVatagtggtitgtgETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEI 240
Cdd:COG0031 161 EIWEQTDGKVDAFVagvgtggtitgvgRYLKERNPDIKIVAVEPEGSPLLSGGEPGPHKIEGIGAGFVPKILDPSLIDEV 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 241 IQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVLCIAPDTGERYLS 300
Cdd:COG0031 241 ITVSDEEAFAMARRLAREEGILVGISSGAAVAAALRLAKRLGPGKTIVTILPDSGERYLS 300
|
|
| cysK |
TIGR01139 |
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine ... |
7-304 |
2.87e-163 |
|
cysteine synthase A; This model distinguishes cysteine synthase A (CysK) from cysteine synthase B (CysM). CysM differs in having a broader specificity that also allows the use of thiosulfate to produce cysteine thiosulfonate. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273465 Cd Length: 298 Bit Score: 456.06 E-value: 2.87e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 7 VTELIGDTPVVRLsKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAK 86
Cdd:TIGR01139 1 ISELIGNTPLVRL-NRIEGCNANVFVKLEGRNPSGSVKDRIALNMIWDAEKRGLLKPGKTIVEPTSGNTGIALAMVAAAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 87 GYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNS-FIPQQFENPANPNIHRYTTALEIYEQ 165
Cdd:TIGR01139 80 GYKLILTMPETMSIERRKLLKAYGAELVLTPGAEGMKGAIAKAEEIAASTPNSyFMLQQFENPANPEIHRKTTGPEIWRD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 166 MDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEIIQIAD 245
Cdd:TIGR01139 160 TDGKLDAFVAGVGTGGTITGVGEVLKEQKPNIKIVAVEPAESPVLSGGKPGPHKIQGIGAGFIPKNLNRSVIDEVITVSD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446684939 246 EEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVLCIAPDTGERYLSMGLF 304
Cdd:TIGR01139 240 EEAIETARRLAAEEGILVGISSGAAVAAALKLAKRPEPDKLIVVILPSTGERYLSTPLF 298
|
|
| cysKM |
TIGR01136 |
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and ... |
7-304 |
4.00e-153 |
|
cysteine synthase; This model discriminates cysteine synthases (EC 2.5.1.47) (both CysK and CysM) from cystathionine beta-synthase, a protein found primarily in eukaryotes and carrying a C-terminal CBS domain lacking from this protein. Bacterial proteins lacking the CBS domain but otherwise showing resemblamnce to cystathionine beta-synthases and considerable phylogenetic distance from known cysteine synthases were excluded from the seed and score below the trusted cutoff. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273463 Cd Length: 299 Bit Score: 430.16 E-value: 4.00e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 7 VTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAK 86
Cdd:TIGR01136 1 IEELIGNTPLVRLNRLAPGCDARVLAKLEGFNPSGSVKDRIALSMILDAEKRGLLKPGDTIIEATSGNTGIALAMVAAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 87 GYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTALEIYEQM 166
Cdd:TIGR01136 81 GYKLILTMPETMSLERRKLLRAYGAELILTPGEEGMKGAIDKAEELAAETNKYVMLDQFENPANPEAHYKTTGPEIWRDT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 167 DGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEIIQIADE 246
Cdd:TIGR01136 161 DGRIDHFVAGVGTGGTITGVGRYLKEQNPNIQIVAVEPAESPVLSGGEPGPHKIQGIGAGFIPKILDLSLIDEVITVSDE 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446684939 247 EALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLG-AGKKVLCIAPDTGERYLSMGLF 304
Cdd:TIGR01136 241 DAIETARRLAREEGILVGISSGAAVAAALKLAKRLEnADKVIVAILPDTGERYLSTGLF 299
|
|
| CBS_like |
cd01561 |
CBS_like: This subgroup includes Cystathionine beta-synthase (CBS) and Cysteine synthase. CBS ... |
12-300 |
3.77e-147 |
|
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: 414.99 E-value: 3.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAKGYKAI 91
Cdd:cd01561 1 GNTPLVRLNRLSPGTGAEIYAKLEFFNPGGSVKDRIALYMIEDAEKRGLLKPGTTIIEPTSGNTGIGLAMVAAAKGYRFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 92 LIMPDNMSKERINLLKAYGAEVVLTPAEQR--MPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTALEIYEQMDGE 169
Cdd:cd01561 81 IVMPETMSEEKRKLLRALGAEVILTPEAEAdgMKGAIAKARELAAETPNAFWLNQFENPANPEAHYETTAPEIWEQLDGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 170 LDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEIIQIADEEAL 249
Cdd:cd01561 161 VDAFVAGVGTGGTITGVARYLKEKNPNVRIVGVDPVGSVLFSGGPPGPHKIEGIGAGFIPENLDRSLIDEVVRVSDEEAF 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 446684939 250 TTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVLCIAPDTGERYLS 300
Cdd:cd01561 241 AMARRLAREEGLLVGGSSGAAVAAALKLAKRLGPGKTIVTILPDSGERYLS 291
|
|
| PLN02565 |
PLN02565 |
cysteine synthase |
3-305 |
1.98e-103 |
|
cysteine synthase
Pssm-ID: 166206 Cd Length: 322 Bit Score: 305.31 E-value: 1.98e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 3 LCENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTI-IEPTSGNTGIGLAM 81
Cdd:PLN02565 5 IAKDVTELIGKTPLVYLNNVVDGCVARIAAKLEMMEPCSSVKDRIGYSMITDAEEKGLIKPGESVlIEPTSGNTGIGLAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 82 NAAAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTALE 161
Cdd:PLN02565 85 MAAAKGYKLIITMPASMSLERRIILLAFGAELVLTDPAKGMKGAVQKAEEILAKTPNSYILQQFENPANPKIHYETTGPE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 162 IYEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEII 241
Cdd:PLN02565 165 IWKGTGGKVDAFVSGIGTGGTITGAGKYLKEQNPDIKLYGVEPVESAVLSGGKPGPHKIQGIGAGFIPGVLDVDLLDEVV 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446684939 242 QIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKR-LGAGKKVLCIAPDTGERYLSMGLFE 305
Cdd:PLN02565 245 QVSSDEAIETAKLLALKEGLLVGISSGAAAAAAIKIAKRpENAGKLIVVIFPSFGERYLSSVLFE 309
|
|
| PRK10717 |
PRK10717 |
cysteine synthase A; Provisional |
1-300 |
2.49e-101 |
|
cysteine synthase A; Provisional
Pssm-ID: 182672 [Multi-domain] Cd Length: 330 Bit Score: 299.85 E-value: 2.49e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 1 MKLCENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLA 80
Cdd:PRK10717 1 MKIFEDVSDTIGNTPLIRLNRASEATGCEILGKAEFLNPGGSVKDRAALNIIWDAEKRGLLKPGGTIVEGTAGNTGIGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 81 MNAAAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPA------EQRMPGAIAKALELQKQIPNSFI-PQQFENPANPNI 153
Cdd:PRK10717 81 LVAAARGYKTVIVMPETQSQEKKDLLRALGAELVLVPAapyanpNNYVKGAGRLAEELVASEPNGAIwANQFDNPANREA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 154 HRYTTALEIYEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSP----VLSG--GVPGPHKLVGTSPGF 227
Cdd:PRK10717 161 HYETTGPEIWEQTDGKVDGFVCAVGTGGTLAGVSRYLKETNPKVKIVLADPTGSAlysyYKTGelKAEGSSITEGIGQGR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446684939 228 IPKNLNTEVYNEIIQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVLCIAPDTGERYLS 300
Cdd:PRK10717 241 ITANLEGAPIDDAIRIPDEEALSTAYRLLEEEGLCLGGSSGINVAAALRLARELGPGHTIVTILCDSGERYQS 313
|
|
| PLN00011 |
PLN00011 |
cysteine synthase |
5-305 |
2.45e-95 |
|
cysteine synthase
Pssm-ID: 177651 Cd Length: 323 Bit Score: 284.59 E-value: 2.45e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 5 ENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPG-DTIIEPTSGNTGIGLAMNA 83
Cdd:PLN00011 9 NDVTELIGNTPMVYLNNIVDGCVARIAAKLEMMEPCSSVKDRIAYSMIKDAEDKGLITPGkSTLIEATAGNTGIGLACIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 84 AAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTALEIY 163
Cdd:PLN00011 89 AARGYKVILVMPSTMSLERRIILRALGAEVHLTDQSIGLKGMLEKAEEILSKTPGGYIPQQFENPANPEIHYRTTGPEIW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 164 EQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEIIQI 243
Cdd:PLN00011 169 RDSAGKVDILVAGVGTGGTATGVGKFLKEKNKDIKVCVVEPVESAVLSGGQPGPHLIQGIGSGIIPFNLDLTIVDEIIQV 248
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446684939 244 ADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKR-LGAGKKVLCIAPDTGERYLSMGLFE 305
Cdd:PLN00011 249 TGEEAIETAKLLALKEGLLVGISSGAAAAAALKVAKRpENAGKLIVVIFPSGGERYLSTKLFE 311
|
|
| cysta_beta |
TIGR01137 |
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but ... |
5-300 |
1.89e-89 |
|
cystathionine beta-synthase; Members of this family closely resemble cysteine synthase but contain an additional C-terminal CBS domain. The function of any bacterial member included in this family is proposed but not proven. [Amino acid biosynthesis, Serine family]
Pssm-ID: 273464 [Multi-domain] Cd Length: 455 Bit Score: 273.98 E-value: 1.89e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 5 ENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAA 84
Cdd:TIGR01137 3 DNILDLIGNTPLVRLNKVSKGLKCELLAKCEFFNPGGSVKDRIALRMIEDAEASGRLKPGDTIIEPTSGNTGIGLALVAA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 85 AKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRM--PGA-IAKALELQKQIPNSFIPQQFENPANPNIHRYTTALE 161
Cdd:TIGR01137 83 IKGYKCIIVLPEKMSSEKVDVLRALGAEIVRTPTAAAFdsPEShIGVAKRLVREIPGAHILDQYRNPSNPLAHYDTTGPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 162 IYEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSpVLSGGVP------GPHKLVGTSPGFIPKNLNTE 235
Cdd:TIGR01137 163 ILEQCEGKLDMFVAGVGTGGTITGIARYLKESCPGCRIVGADPEGS-ILAQPEElnqtgrTPYKVEGIGYDFIPTVLDRK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446684939 236 VYNEIIQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGA-GKKVLCIAPDTGERYLS 300
Cdd:TIGR01137 242 VVDEWIKTDDKESFTMARRLIKEEGLLVGGSSGSAVVAALKAAEDELQeGQRCVVLLPDSIRNYMT 307
|
|
| PLN03013 |
PLN03013 |
cysteine synthase |
1-305 |
4.49e-89 |
|
cysteine synthase
Pssm-ID: 178587 [Multi-domain] Cd Length: 429 Bit Score: 272.42 E-value: 4.49e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 1 MKLCENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTI-IEPTSGNTGIGL 79
Cdd:PLN03013 111 LNIADNVSQLIGKTPMVYLNSIAKGCVANIAAKLEIMEPCCSVKDRIGYSMVTDAEQKGFISPGKSVlVEPTSGNTGIGL 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 80 AMNAAAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTA 159
Cdd:PLN03013 191 AFIAASRGYRLILTMPASMSMERRVLLKAFGAELVLTDPAKGMTGAVQKAEEILKNTPDAYMLQQFDNPANPKIHYETTG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 160 LEIYEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNE 239
Cdd:PLN03013 271 PEIWDDTKGKVDIFVAGIGTGGTITGVGRFIKEKNPKTQVIGVEPTESDILSGGKPGPHKIQGIGAGFIPKNLDQKIMDE 350
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446684939 240 IIQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKR-LGAGKKVLCIAPDTGeRYLSMGLFE 305
Cdd:PLN03013 351 VIAISSEEAIETAKQLALKEGLMVGISSGAAAAAAIKVAKRpENAGKLIAVSLFASG-RDIYTPRCS 416
|
|
| cysM |
PRK11761 |
cysteine synthase CysM; |
9-305 |
8.41e-89 |
|
cysteine synthase CysM;
Pssm-ID: 236972 Cd Length: 296 Bit Score: 266.74 E-value: 8.41e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 9 ELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAKGY 88
Cdd:PRK11761 8 DTIGNTPLVKLQRLPPDRGNTILAKLEGNNPAGSVKDRPALSMIVQAEKRGEIKPGDTLIEATSGNTGIALAMIAAIKGY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 89 KAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQiPNSFIPQQFENPANPNIHRYTTALEIYEQMDG 168
Cdd:PRK11761 88 RMKLIMPENMSQERRAAMRAYGAELILVPKEQGMEGARDLALQMQAE-GEGKVLDQFANPDNPLAHYETTGPEIWRQTEG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 169 ELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPK-GSpvlsgGVPGPHKLvgtSPGFIPKNLNTEVYNEIIQIADEE 247
Cdd:PRK11761 167 RITHFVSSMGTTGTIMGVSRYLKEQNPAVQIVGLQPEeGS-----SIPGIRRW---PEEYLPKIFDASRVDRVLDVSQQE 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 446684939 248 ALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLgAGKKVLCIAPDTGERYLSMGLFE 305
Cdd:PRK11761 239 AENTMRRLAREEGIFCGVSSGGAVAAALRIAREN-PNAVIVAIICDRGDRYLSTGVFP 295
|
|
| PLN02556 |
PLN02556 |
cysteine synthase/L-3-cyanoalanine synthase |
2-305 |
2.12e-84 |
|
cysteine synthase/L-3-cyanoalanine synthase
Pssm-ID: 178171 [Multi-domain] Cd Length: 368 Bit Score: 258.35 E-value: 2.12e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 2 KLCENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDT-IIEPTSGNTGIGLA 80
Cdd:PLN02556 48 KIKTDASQLIGKTPLVYLNKVTEGCGAYIAAKQEMFQPTSSIKDRPALAMIEDAEKKNLITPGKTtLIEPTSGNMGISLA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 81 MNAAAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTAL 160
Cdd:PLN02556 128 FMAAMKGYKMILTMPSYTSLERRVTMRAFGAELVLTDPTKGMGGTVKKAYELLESTPDAFMLQQFSNPANTQVHFETTGP 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 161 EIYEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEI 240
Cdd:PLN02556 208 EIWEDTLGQVDIFVMGIGSGGTVSGVGKYLKSKNPNVKIYGVEPAESNVLNGGKPGPHHITGNGVGFKPDILDMDVMEKV 287
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446684939 241 IQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRL-GAGKKVLCIAPDTGERYLSMGLFE 305
Cdd:PLN02556 288 LEVSSEDAVNMARELALKEGLMVGISSGANTVAALRLAKMPeNKGKLIVTVHPSFGERYLSSVLFQ 353
|
|
| cysM |
TIGR01138 |
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of ... |
7-304 |
4.57e-82 |
|
cysteine synthase B; CysM differs from CysK in that it can also use thiosulfate instead of sulfide, to produce cysteine thiosulfonate instead of cysteine. Alternate name: O-acetylserine (thiol)-lyase [Amino acid biosynthesis, Serine family]
Pssm-ID: 130208 [Multi-domain] Cd Length: 290 Bit Score: 249.83 E-value: 4.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 7 VTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAK 86
Cdd:TIGR01138 2 IEQTVGNTPLVRLQRMGPENGSEVWLKLEGNNPAGSVKDRPALSMIVEAEKRGEIKPGDVLIEATSGNTGIALAMIAALK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 87 GYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQIPNSFIpQQFENPANPNIHRYTTALEIYEQM 166
Cdd:TIGR01138 82 GYRMKLLMPDNMSQERKAAMRAYGAELILVTKEEGMEGARDLALELANRGEGKLL-DQFNNPDNPYAHYTSTGPEIWQQT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 167 DGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEP-KGSpvlsgGVPGPHKLvgtSPGFIPKNLNTEVYNEIIQIAD 245
Cdd:TIGR01138 161 GGRITHFVSSMGTTGTIMGVSRFLKEQNPPVQIVGLQPeEGS-----SIPGIRRW---PTEYLPGIFDASLVDRVLDIHQ 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 446684939 246 EEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGkKVLCIAPDTGERYLSMGLF 304
Cdd:TIGR01138 233 RDAENTMRELAVREGIFCGVSSGGAVAAALRLARELPDA-VVVAIICDRGDRYLSTGVF 290
|
|
| Trp-synth-beta_II |
cd00640 |
Tryptophan synthase beta superfamily (fold type II); this family of pyridoxal phosphate (PLP) ... |
14-293 |
2.52e-78 |
|
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: 238.18 E-value: 2.52e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIkPGDTIIEPTSGNTGIGLAMNAAAKGYKAILI 93
Cdd:cd00640 1 TPLVRLKRLSKLGGANIYLKLEFLNPTGSFKDRGALNLILLAEEEGKL-PKGVIIESTGGNTGIALAAAAARLGLKCTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 94 MPDNMSKERINLLKAYGAEVVLTPAEqrMPGAIAKALELQKQIPNSFIPQQFENPANPNIHrYTTALEIYEQMDGE-LDA 172
Cdd:cd00640 80 MPEGASPEKVAQMRALGAEVVLVPGD--FDDAIALAKELAEEDPGAYYVNQFDNPANIAGQ-GTIGLEILEQLGGQkPDA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 173 FVatagtggtitgtgetlkeklpnlyiavvepkgSPVLSGGVPGphklvGTSPGFIPKNLNTEVY---NEIIQIADEEAL 249
Cdd:cd00640 157 VV--------------------------------VPVGGGGNIA-----GIARALKELLPNVKVIgvePEVVTVSDEEAL 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446684939 250 TTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVLCIAPD 293
Cdd:cd00640 200 EAIRLLAREEGILVEPSSAAALAAALKLAKKLGKGKTVVVILTG 243
|
|
| PLP_SbnA_fam |
TIGR03945 |
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a ... |
7-299 |
6.11e-78 |
|
2,3-diaminopropionate biosynthesis protein SbnA; Members of this family include SbnA, a protein of the staphyloferrin B biosynthesis operon of Staphylococcus aureus. SbnA and SbnB together appear to synthesize 2,3-diaminopropionate, a precursor of certain siderophores and other secondary metabolites. SbnA is a pyridoxal phosphate-dependent enzyme. [Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274872 [Multi-domain] Cd Length: 304 Bit Score: 239.41 E-value: 6.11e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 7 VTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAK 86
Cdd:TIGR03945 1 ILSLIGNTPLVKLERLFPDAPFRLFAKLEGFNPGGSIKDRPALYILEAAIKRGRITPGTTIIESSSGNLGIALAMICAYK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 87 GYKAILIMPDNMSKERINLLKAYGAEV--VLTPAEQR--MPGAIAKALELQKQIPNSFIPQQFENPANPNIHRYTTALEI 162
Cdd:TIGR03945 81 GLRFICVVDPNISPQNLKLLRAYGAEVekVTEPDETGgyLGTRIARVRELLASIPDAYWPNQYANPDNPRAHYHGTGREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 163 YEQMDgELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSpVLSGGVPGPHKLVGTSPGFIPKNLNTEVYNEIIQ 242
Cdd:TIGR03945 161 ARAFP-TLDYLFVGVSTTGTLMGCSRRLRERGPNTKVIAVDAVGS-VIFGGPPGRRHIPGLGASVVPELLDESLIDDVVH 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 446684939 243 IADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVLCIAPDTGERYL 299
Cdd:TIGR03945 239 VPEYDTVAGCRRLARREGILAGGSSGTVVAAIKRLLPRIPEGSTVVAILPDRGERYL 295
|
|
| PALP |
pfam00291 |
Pyridoxal-phosphate dependent enzyme; Members of this family are all pyridoxal-phosphate ... |
7-293 |
1.18e-69 |
|
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: 217.95 E-value: 1.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 7 VTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNgliKPGDTIIEPTSGNTGIGLAMNAAAK 86
Cdd:pfam00291 1 ISLGIGPTPLVRLPRLSKELGVDVYLKLESLNPTGSFKDRGALNLLLRLKEG---EGGKTVVEASSGNHGRALAAAAARL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 87 GYKAILIMPDNMSKERINLLKAYGAEVVLTPAEqrMPGAIAKALELQKQIPNSFIPQQFENPANPNIHRyTTALEIYEQM 166
Cdd:pfam00291 78 GLKVTIVVPEDAPPGKLLLMRALGAEVVLVGGD--YDEAVAAARELAAEGPGAYYINQYDNPLNIEGYG-TIGLEILEQL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 167 DGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGG---------VPGPHKLVGTSPGFIPKNLNTEVY 237
Cdd:pfam00291 155 GGDPDAVVVPVGGGGLIAGIARGLKELGPDVRVIGVEPEGAPALARSlaagrpvpvPVADTIADGLGVGDEPGALALDLL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446684939 238 NE----IIQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMI-AKRLGAGKKVLCIAPD 293
Cdd:pfam00291 235 DEyvgeVVTVSDEEALEAMRLLARREGIVVEPSSAAALAALKLAlAGELKGGDRVVVVLTG 295
|
|
| PLN02356 |
PLN02356 |
phosphateglycerate kinase |
9-300 |
5.99e-32 |
|
phosphateglycerate kinase
Pssm-ID: 215204 Cd Length: 423 Bit Score: 122.79 E-value: 5.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 9 ELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAKGY 88
Cdd:PLN02356 49 DAIGNTPLIRINSLSEATGCEILGKCEFLNPGGSVKDRVAVKIIEEALESGQLFPGGVVTEGSAGSTAISLATVAPAYGC 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 89 KAILIMPDNMSKERINLLKAYGAE------VVLTPAEQRMPGAIAKALE------------------------------- 131
Cdd:PLN02356 129 KCHVVIPDDVAIEKSQILEALGATvervrpVSITHKDHYVNIARRRALEanelaskrrkgsetdgihlektngciseeek 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 132 ----LQKQIPNSFIPQQFENPANPNIHRYTTALEIYEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGS 207
Cdd:PLN02356 209 enslFSSSCTGGFFADQFENLANFRAHYEGTGPEIWEQTQGNLDAFVAAAGTGGTLAGVSRFLQEKNPNIKCFLIDPPGS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 208 PVLSGGVPG---------------PHKLVGTSPGF--IPKNLNTEVYNEIIQIADEEALTTMRNLARQEGLLVGPSSGAS 270
Cdd:PLN02356 289 GLFNKVTRGvmytreeaegrrlknPFDTITEGIGInrLTQNFLMAKLDGAFRGTDKEAVEMSRYLLKNDGLFVGSSSAMN 368
|
330 340 350
....*....|....*....|....*....|
gi 446684939 271 VYAAIMIAKRLGAGKKVLCIAPDTGERYLS 300
Cdd:PLN02356 369 CVGAVRVAQSLGPGHTIVTILCDSGMRHLS 398
|
|
| Thr-dehyd |
cd01562 |
Threonine dehydratase: The first step in amino acid degradation is the removal of nitrogen. ... |
14-290 |
2.27e-24 |
|
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: 99.87 E-value: 2.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPgdtIIEPTSGNTGIGLAMNAAAKGYKAILI 93
Cdd:cd01562 18 TPLLTSPTLSELLGAEVYLKCENLQKTGSFKIRGAYNKLLSLSEEERAKG---VVAASAGNHAQGVAYAAKLLGIPATIV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 94 MPDNMSKERINLLKAYGAEVVLTpaEQRMPGAIAKALELQKQIPNSFIPqqfenPANpniHRY------TTALEIYEQMd 167
Cdd:cd01562 95 MPETAPAAKVDATRAYGAEVVLY--GEDFDEAEAKARELAEEEGLTFIH-----PFD---DPDviagqgTIGLEILEQV- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 168 GELDA-FV------------AtagtggtitgtgeTLKEKLPNLYIAVVEPKGSPVLS----GGVPGPHKLVGT------- 223
Cdd:cd01562 164 PDLDAvFVpvggggliagiaT-------------AVKALSPNTKVIGVEPEGAPAMAqslaAGKPVTLPEVDTiadglav 230
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446684939 224 -SPGFIPKNLNTEVYNEIIQIADEEALTTMRNLARQEGLLVGPSSGASVyAAIMIAKRLGAGKKVLCI 290
Cdd:cd01562 231 kRPGELTFEIIRKLVDDVVTVSEDEIAAAMLLLFEREKLVAEPAGALAL-AALLSGKLDLKGKKVVVV 297
|
|
| ThrC |
COG0498 |
Threonine synthase [Amino acid transport and metabolism]; Threonine synthase is part of the ... |
12-295 |
1.51e-23 |
|
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: 99.12 E-value: 1.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIkpgdTIIEPTSGNTGIGLAMNAAAKGYKAI 91
Cdd:COG0498 65 GGTPLVKAPRLADELGKNLYVKEEGHNPTGSFKDRAMQVAVSLALERGAK----TIVCASSGNGSAALAAYAARAGIEVF 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 92 LIMP-DNMSKERINLLKAYGAEVVLtpaeqrMPGAIAKALELQKQIpnsfipqqFEN----PANpNIHRY------TTAL 160
Cdd:COG0498 141 VFVPeGKVSPGQLAQMLTYGAHVIA------VDGNFDDAQRLVKEL--------AADeglyAVN-SINPArlegqkTYAF 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 161 EIYEQMDGELDAFVATagtggtitgtgeT--------------------LKEKLPNLYIAVVEPKgSPVL---SGGVPGP 217
Cdd:COG0498 206 EIAEQLGRVPDWVVVP------------TgnggnilagykafkelkelgLIDRLPRLIAVQATGC-NPILtafETGRDEY 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 218 HKLVG--TSPG-FIPKNLNTE-VYNEI-------IQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKR--LGAG 284
Cdd:COG0498 273 EPERPetIAPSmDIGNPSNGErALFALresggtaVAVSDEEILEAIRLLARREGIFVEPATAVAVAGLRKLREEgeIDPD 352
|
330
....*....|.
gi 446684939 285 KKVLCIApdTG 295
Cdd:COG0498 353 EPVVVLS--TG 361
|
|
| IlvA |
COG1171 |
Threonine deaminase [Amino acid transport and metabolism]; Threonine deaminase is part of the ... |
14-290 |
2.57e-23 |
|
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: 97.41 E-value: 2.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYN-LLHVAEKngliKPGDTIIEPTSGNTGIGLAMNAAAKGYKAIL 92
Cdd:COG1171 25 TPLLRSPTLSERLGAEVYLKLENLQPTGSFKLRGAYNaLASLSEE----ERARGVVAASAGNHAQGVAYAARLLGIPATI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 93 IMPDNMSKERINLLKAYGAEVVLTPAEQrmPGAIAKALELQKQIPNSFIPqqfenPANPN--IHRYTT-ALEIYEQMdGE 169
Cdd:COG1171 101 VMPETAPAVKVAATRAYGAEVVLHGDTY--DDAEAAAAELAEEEGATFVH-----PFDDPdvIAGQGTiALEILEQL-PD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 170 LDAF------------VATagtggtitgtgeTLKEKLPNLYIAVVEPKGSPVL-----SGG---VPGPHKLV----GTSP 225
Cdd:COG1171 173 LDAVfvpvggggliagVAA------------ALKALSPDIRVIGVEPEGAAAMyrslaAGEpvtLPGVDTIAdglaVGRP 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446684939 226 GFIPKNLNTEVYNEIIQIADEEALTTMRNLARQEGLLVGPSSGASVyAAIMIAKRLGAGKKVLCI 290
Cdd:COG1171 241 GELTFEILRDLVDDIVTVSEDEIAAAMRLLLERTKIVVEPAGAAAL-AALLAGKERLKGKRVVVV 304
|
|
| Thr-synth_1 |
cd01563 |
Threonine synthase is a pyridoxal phosphate (PLP) dependent enzyme that catalyses the last ... |
12-290 |
1.02e-20 |
|
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: 90.35 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRLSKFIPE-DAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLikpgDTIIEPTSGNTGIGLAMNAAAKGYKA 90
Cdd:cd01563 21 GNTPLVRAPRLGERlGGKNLYVKDEGLNPTGSFKDRGMTVAVSKAKELGV----KAVACASTGNTSASLAAYAARAGIKC 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 91 ILIMPDNMSKERINLLKAYGAEVVltpaeqRMPGAIAKALELQKQIPNSFIPQqfenpANPNIHRY------TTALEIYE 164
Cdd:cd01563 97 VVFLPAGKALGKLAQALAYGATVL------AVEGNFDDALRLVRELAEENWIY-----LSNSLNPYrlegqkTIAFEIAE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 165 QMDGEL-DAFVATAGTGGTITGTGETLKE--------KLPNLYiaVVEPKG-SPVLSGGVPG---------PHKL----- 220
Cdd:cd01563 166 QLGWEVpDYVVVPVGNGGNITAIWKGFKElkelglidRLPRMV--GVQAEGaAPIVRAFKEGkddiepvenPETIatair 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446684939 221 VGtSPGFIPKNLNT--EVYNEIIQIADEEALTTMRNLARQEGLLVGPSSGASVyAAIMIAKRLG---AGKKVLCI 290
Cdd:cd01563 244 IG-NPASGPKALRAvrESGGTAVAVSDEEILEAQKLLARTEGIFVEPASAASL-AGLKKLREEGiidKGERVVVV 316
|
|
| PRK06450 |
PRK06450 |
threonine synthase; Validated |
12-274 |
1.47e-14 |
|
threonine synthase; Validated
Pssm-ID: 180565 [Multi-domain] Cd Length: 338 Bit Score: 72.85 E-value: 1.47e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRlskfipedAADVYVKLEMFNPSRSVKDRAAYNLL-HVAEKNglIKpgdTIIEPTSGNTGIGLAMNAAAKGYKA 90
Cdd:PRK06450 57 GRTPLIK--------KGNIWFKLDFLNPTGSYKDRGSVTLIsYLAEKG--IK---QISEDSSGNAGASIAAYGAAAGIEV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 91 ILIMPDNMSKERINLLKAYGAEVVltpaeqRMPGAIAkalELQKQIPNS--FIPQQFENPANPNIHRyTTALEIYEQMDG 168
Cdd:PRK06450 124 KIFVPETASGGKLKQIESYGAEVV------RVRGSRE---DVAKAAENSgyYYASHVLQPQFRDGIR-TLAYEIAKDLDW 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 169 ELDAFV-ATAGTGGTITGTGETLK--------EKLPNLyIAVVEPKGSPV---LSGGVPGPHK--------LVGTSPGFI 228
Cdd:PRK06450 194 KIPNYVfIPVSAGTLLLGVYSGFKhlldsgviSEMPKI-VAVQTEQVSPLcakFKGISYTPPDkvtsiadaLVSTRPFLL 272
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 446684939 229 PKNLNT-EVYNEIIQIADEEALTTMRNLARQeGLLVGPSSgASVYAA 274
Cdd:PRK06450 273 DYMVKAlSEYGECIVVSDNEIVEAWKELAKK-GLLVEYSS-ATVYAA 317
|
|
| PRK06381 |
PRK06381 |
threonine synthase; Validated |
12-117 |
1.21e-13 |
|
threonine synthase; Validated
Pssm-ID: 235789 Cd Length: 319 Bit Score: 70.12 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRLSKfIPE--DAADVYVKLEMFNPSRSVKDRAAYNllHV--AEKNGLikpgDTIIEPTSGNTGIGLAMNAAAKG 87
Cdd:PRK06381 14 GGTPLLRARK-LEEelGLRKIYLKFEGANPTGTQKDRIAEA--HVrrAMRLGY----SGITVGTCGNYGASIAYFARLYG 86
|
90 100 110
....*....|....*....|....*....|
gi 446684939 88 YKAILIMPDNMSKERINLLKAYGAEVVLTP 117
Cdd:PRK06381 87 LKAVIFIPRSYSNSRVKEMEKYGAEIIYVD 116
|
|
| PRK06608 |
PRK06608 |
serine/threonine dehydratase; |
29-172 |
8.62e-13 |
|
serine/threonine dehydratase;
Pssm-ID: 235842 [Multi-domain] Cd Length: 338 Bit Score: 67.87 E-value: 8.62e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 29 DVYVKLEMFNPSRSVKDRAAYN-LLHVAEKNgliKPGDTIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERINLLK 107
Cdd:PRK06608 39 EIFFKVESLQKTGAFKVRGVLNhLLELKEQG---KLPDKIVAYSTGNHGQAVAYASKLFGIKTRIYLPLNTSKVKQQAAL 115
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446684939 108 AYGAEVVLTPAEQRmpgAIAKALELQKQ----IPNSFIPQQFENPAnpnihryTTALEIYEQMDGELDA 172
Cdd:PRK06608 116 YYGGEVILTNTRQE---AEEKAKEDEEQgfyyIHPSDSDSTIAGAG-------TLCYEALQQLGFSPDA 174
|
|
| PRK06815 |
PRK06815 |
threonine/serine dehydratase; |
28-289 |
1.71e-12 |
|
threonine/serine dehydratase;
Pssm-ID: 180709 [Multi-domain] Cd Length: 317 Bit Score: 66.64 E-value: 1.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 28 ADVYVKLEMFNPSRSVKDRAAYNLL----HVAEKNGlikpgdtIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERI 103
Cdd:PRK06815 35 CEVYLKCEHLQHTGSFKFRGASNKLrllnEAQRQQG-------VITASSGNHGQGVALAAKLAGIPVTVYAPEQASAIKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 104 NLLKAYGAEVVLTP-----AEQrmpgAIAKALELQKQIpnsFIPqqfenPAN-PNI--HRYTTALEIYEQMDGeLDAFVA 175
Cdd:PRK06815 108 DAIRALGAEVRLYGgdalnAEL----AARRAAEQQGKV---YIS-----PYNdPQViaGQGTIGMELVEQQPD-LDAVFV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 176 TAGTGGTITGTGETLKEKLPNLYI------------------AVVEPKGSPVLSGGVPGphklvGTSPGFIPKNLNTEVY 237
Cdd:PRK06815 175 AVGGGGLISGIATYLKTLSPKTEIigcwpanspslytsleagEIVEVAEQPTLSDGTAG-----GVEPGAITFPLCQQLI 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446684939 238 NEIIQIADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLgAGKKV---LC 289
Cdd:PRK06815 250 DQKVLVSEEEIKEAMRLIAETDRWLIEGAAGVALAAALKLAPRY-QGKKVavvLC 303
|
|
| PRK12483 |
PRK12483 |
threonine dehydratase; Reviewed |
30-174 |
7.08e-12 |
|
threonine dehydratase; Reviewed
Pssm-ID: 237111 [Multi-domain] Cd Length: 521 Bit Score: 65.59 E-value: 7.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 30 VYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLikpGDTIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERINLLKAY 109
Cdd:PRK12483 54 VLLKREDLQPVFSFKIRGAYNKMARLPAEQL---ARGVITASAGNHAQGVALAAARLGVKAVIVMPRTTPQLKVDGVRAH 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446684939 110 GAEVVLtpAEQRMPGAIAKALELQKQIPNSFIPqQFENPaNPNIHRYTTALEIYEQMDGELDA-FV 174
Cdd:PRK12483 131 GGEVVL--HGESFPDALAHALKLAEEEGLTFVP-PFDDP-DVIAGQGTVAMEILRQHPGPLDAiFV 192
|
|
| PRK08329 |
PRK08329 |
threonine synthase; Validated |
14-166 |
8.39e-12 |
|
threonine synthase; Validated
Pssm-ID: 236244 [Multi-domain] Cd Length: 347 Bit Score: 64.85 E-value: 8.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKfipedaaDVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLikpgDTIIEPTSGNTGIGLAMNAAAKGYKAILI 93
Cdd:PRK08329 65 TPTVKRSI-------KVYFKLDYLQPTGSFKDRGTYVTVAKLKEEGI----NEVVIDSSGNAALSLALYSLSEGIKVHVF 133
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446684939 94 MPDNMSKERINLLKAYGAEVVLTPAEqRMPgAIAKALELQKQIPNSFIPQQFenpaNPNIHRYT--TALEIYEQM 166
Cdd:PRK08329 134 VSYNASKEKISLLSRLGAELHFVEGD-RME-VHEEAVKFSKRNNIPYVSHWL----NPYFLEGTktIAYEIYEQI 202
|
|
| PRK05638 |
PRK05638 |
threonine synthase; Validated |
12-278 |
1.49e-09 |
|
threonine synthase; Validated
Pssm-ID: 235539 [Multi-domain] Cd Length: 442 Bit Score: 58.28 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRlSKFIPEDAADVYVKLEMFNPSRSVKDRAAYnllhVAEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAKGYKAI 91
Cdd:PRK05638 65 GGTPLIR-ARISEKLGENVYIKDETRNPTGSFRDRLAT----VAVSYGLPYAANGFIVASDGNAAASVAAYSARAGKEAF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 92 LIMPDNMSKERINLLKAYGAEVVLTpaEQRMPGAIAKALELQKQipNSFIPQQFENpanpNI----HRYTTALEIYEQMD 167
Cdd:PRK05638 140 VVVPRKVDKGKLIQMIAFGAKIIRY--GESVDEAIEYAEELARL--NGLYNVTPEY----NIigleGQKTIAFELWEEIN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 168 GEldAFVATAGTGGTITGTGETLKE--------KLPNLyIAVVEPKGSPVLSGGVPGPHKLVGT-SPGFIPKN-LNTEVY 237
Cdd:PRK05638 212 PT--HVIVPTGSGSYLYSIYKGFKElleigvieEIPKL-IAVQTERCNPIASEILGNKTKCNETkALGLYVKNpVMKEYV 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446684939 238 NEIIQ-------IADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIA 278
Cdd:PRK05638 289 SEAIKesggtavVVNEEEIMAGEKLLAKEGIFAELSSAVVMPALLKLG 336
|
|
| thrC |
TIGR00260 |
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction ... |
3-290 |
1.47e-08 |
|
threonine synthase; Involved in threonine biosynthesis it catalyses the reaction O-PHOSPHO-L-HOMOSERINE + H(2)O = L-THREONINE + ORTHOPHOSPHATE using pyridoxal phosphate as a cofactor. the enzyme is distantly related to the serine/threonine dehydratases which are also pyridoxal-phosphate dependent enzymes. the pyridoxal-phosphate binding site is a Lys (K) residues present at residue 70 of the model. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 272986 [Multi-domain] Cd Length: 327 Bit Score: 55.08 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 3 LCENVTELIgDTPvvRLSKFIPEDaaDVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLikpgDTIIEPTSGNTGIGLAMN 82
Cdd:TIGR00260 18 LGEGVTPLF-RAP--ALAANVGIK--NLYVKELGHNPTLSFKDRGMAVALTKALELGN----DTVLCASTGNTGAAAAAY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 83 AAAKGYKAILIMP-DNMSKERINLLKAYGAEVVltpaeqRMPGAIAKALELQKQIPNSFiPQQFENPANPNIHRY----T 157
Cdd:TIGR00260 89 AGKAGLKVVVLYPaGKISLGKLAQALGYNAEVV------AIDGNFDDAQRLVKQLFEDK-PALGLNSANSIPYRLegqkT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 158 TALEIYEQMDGEL-DAFVATAGTGGTITGTGETLKEK-------LPNLyIAVVEPKGSPV----LSGGVPGPHKLVGT-- 223
Cdd:TIGR00260 162 YAFEAVEQLGWEApDKVVVPVPNSGNFGAIWKGFKEKkmlgldsLPVK-RGIQAEGAADIvrafLEGGQWEPIETPETls 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446684939 224 ------SPGFIPKNLN-TEVYNEIIQ-IADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAK--RLGAGKKVLCI 290
Cdd:TIGR00260 241 tamdigNPANWPRALEaFRRSNGYAEdLSDEEILEAIKLLAREEGYFVEPHSAVAVAALLKLVEkgTADPAERVVCA 317
|
|
| PRK08246 |
PRK08246 |
serine/threonine dehydratase; |
14-119 |
1.76e-08 |
|
serine/threonine dehydratase;
Pssm-ID: 181319 [Multi-domain] Cd Length: 310 Bit Score: 54.58 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAAdVYVKLEMFNPSRSVKDRAAYNLLHVAEKnglikPGDTIIEPTSGNTGIGLAMNAAAKGYKAILI 93
Cdd:PRK08246 24 TPVLEADGAGFGPAP-VWLKLEHLQHTGSFKARGAFNRLLAAPV-----PAAGVVAASGGNAGLAVAYAAAALGVPATVF 97
|
90 100
....*....|....*....|....*.
gi 446684939 94 MPDNMSKERINLLKAYGAEVVLTPAE 119
Cdd:PRK08246 98 VPETAPPAKVARLRALGAEVVVVGAE 123
|
|
| PRK08197 |
PRK08197 |
threonine synthase; Validated |
12-298 |
1.02e-07 |
|
threonine synthase; Validated
Pssm-ID: 181283 [Multi-domain] Cd Length: 394 Bit Score: 52.70 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 12 GDTPVVRLSKFIPE-DAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKpgdtIIEPTSGNTGIGLAMNAAAKGYKA 90
Cdd:PRK08197 78 GMTPLLPLPRLGKAlGIGRLWVKDEGLNPTGSFKARGLAVGVSRAKELGVKH----LAMPTNGNAGAAWAAYAARAGIRA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 91 ILIMPdnMSKERINLL--KAYGAEVVLTPAEQRMPGAI-AKALELQKQIPNSFI--PQQFENpanpnihRYTTALEIYEQ 165
Cdd:PRK08197 154 TIFMP--ADAPEITRLecALAGAELYLVDGLISDAGKIvAEAVAEYGWFDVSTLkePYRIEG-------KKTMGLELAEQ 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 166 MDGEL-DAFVATAGTGGTITGTGETLKE---------KLPNLYiaVVEPKG-SPVL---------SGGVPGPHKLvgtSP 225
Cdd:PRK08197 225 LGWRLpDVILYPTGGGVGLIGIWKAFDElealgwiggKRPRLV--AVQAEGcAPIVkaweegkeeSEFWEDAHTV---AF 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 226 GF-IPKNLNTE-----VYNE---IIQIADEEALTTMRNLARQEGLLVGPsSGASVYAAIMIAK---RLGAGKKVLCIAPD 293
Cdd:PRK08197 300 GIrVPKALGDFlvldaVRETggcAIAVSDDAILAAQRELAREEGLFACP-EGAATFAAARQLResgWLKGDERVVLFNTG 378
|
....*
gi 446684939 294 TGERY 298
Cdd:PRK08197 379 SGLKY 383
|
|
| PRK08638 |
PRK08638 |
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB; |
14-142 |
2.28e-07 |
|
bifunctional threonine ammonia-lyase/L-serine ammonia-lyase TdcB;
Pssm-ID: 236317 [Multi-domain] Cd Length: 333 Bit Score: 51.27 E-value: 2.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRlSKFIPEDA-ADVYVKLEMFNPSRSVKDRAAYN-LLHVAEKNGliKPGdtIIEPTSGNTGIGLAMNAAAKGYKAI 91
Cdd:PRK08638 28 TPLPR-SNYLSERCkGEIFLKLENMQRTGSFKIRGAFNkLSSLTDAEK--RKG--VVACSAGNHAQGVALSCALLGIDGK 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 446684939 92 LIMPDNMSKERINLLKAYGAEVVLtpAEQRMPGAIAKALELQKQIPNSFIP 142
Cdd:PRK08638 103 VVMPKGAPKSKVAATCGYGAEVVL--HGDNFNDTIAKVEEIVEEEGRTFIP 151
|
|
| PRK09224 |
PRK09224 |
threonine ammonia-lyase IlvA; |
29-174 |
6.76e-07 |
|
threonine ammonia-lyase IlvA;
Pssm-ID: 236417 [Multi-domain] Cd Length: 504 Bit Score: 50.52 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 29 DVYVKLEMFNPSRSVKDRAAYNL---LHVAEKN-GlikpgdtIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERIN 104
Cdd:PRK09224 36 QVLLKREDLQPVFSFKLRGAYNKmaqLTEEQLArG-------VITASAGNHAQGVALSAARLGIKAVIVMPVTTPDIKVD 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446684939 105 LLKAYGAEVVLtpAEQRMPGAIAKALELQKQIPNSFIPqQFENP---ANPNihryTTALEIYEQMDGELDA-FV 174
Cdd:PRK09224 109 AVRAFGGEVVL--HGDSFDEAYAHAIELAEEEGLTFIH-PFDDPdviAGQG----TIAMEILQQHPHPLDAvFV 175
|
|
| PRK07048 |
PRK07048 |
threo-3-hydroxy-L-aspartate ammonia-lyase; |
14-287 |
7.53e-07 |
|
threo-3-hydroxy-L-aspartate ammonia-lyase;
Pssm-ID: 235918 [Multi-domain] Cd Length: 321 Bit Score: 49.63 E-value: 7.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYN-LLHVAE---KNGlikpgdtIIEPTSGNTGIGLAMNAAAKGYK 89
Cdd:PRK07048 25 TPVLTSRTADARTGAQVFFKCENFQRMGAFKFRGAYNaLSQFSPeqrRAG-------VVTFSSGNHAQAIALSARLLGIP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 90 AILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKalELQKQIPNSFIPqqfenpanPNIHRY------TTALEIY 163
Cdd:PRK07048 98 ATIVMPQDAPAAKVAATRGYGGEVVTYDRYTEDREEIGR--RLAEERGLTLIP--------PYDHPHviagqgTAAKELF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 164 EQMdGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPK----GSPVLSGG----VPGPHKL----VGTSPGFIPKN 231
Cdd:PRK07048 168 EEV-GPLDALFVCLGGGGLLSGCALAARALSPGCKVYGVEPEagndGQQSFRSGeivhIDTPRTIadgaQTQHLGNYTFP 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446684939 232 LNTEVYNEIIQIADEEALTTMRNLARQEGLLVGPsSGASVYAAIMIAKRLGAGKKV 287
Cdd:PRK07048 247 IIRRLVDDIVTVSDAELVDAMRFFAERMKIVVEP-TGCLGAAAALRGKVPLKGKRV 301
|
|
| L-Ser-dehyd |
cd06448 |
Serine dehydratase is a pyridoxal phosphate (PLP)-dependent enzyme which catalyzes the ... |
14-274 |
7.28e-06 |
|
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: 46.91 E-value: 7.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPgDTIIEPTSGNTGIGLAMNAAAKGYKAILI 93
Cdd:cd06448 2 TPLIESTALSKTAGCNVFLKLENLQPSGSFKIRGIGHLCQKSAKQGLNEC-VHVVCSSGGNAGLAAAYAARKLGVPCTIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 94 MPDNMSKERINLLKAYGAEVVLTpAEQRMPGAIAKALELQKQIPNS-FIPqQFENPANPNIHRyTTALEIYEQMD--GEL 170
Cdd:cd06448 81 VPESTKPRVVEKLRDEGATVVVH-GKVWWEADNYLREELAENDPGPvYVH-PFDDPLIWEGHS-SMVDEIAQQLQsqEKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 171 DAFVATAGTGGTITGTGETLKE----KLPnlyIAVVEPKGSPVLSGGVPG--PHKL-----VGTSPG-----------FI 228
Cdd:cd06448 158 DAIVCSVGGGGLLNGIVQGLERngwgDIP---VVAVETEGAHSLNASLKAgkLVTLpkitsVATSLGaktvssqaleyAQ 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446684939 229 PKNLNTEVyneiiqIADEEALTTMRNLARQEGLLVGPSSGASVYAA 274
Cdd:cd06448 235 EHNIKSEV------VSDRDAVQACLRFADDERILVEPACGAALAVV 274
|
|
| PLN02550 |
PLN02550 |
threonine dehydratase |
3-204 |
1.27e-05 |
|
threonine dehydratase
Pssm-ID: 178165 [Multi-domain] Cd Length: 591 Bit Score: 46.45 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 3 LCENVTELIGDTPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKpgdTIIEPTSGNTGIGLAMN 82
Cdd:PLN02550 99 LSAKVYDVAIESPLQLAKKLSERLGVKVLLKREDLQPVFSFKLRGAYNMMAKLPKEQLDK---GVICSSAGNHAQGVALS 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 83 AAAKGYKAILIMPDNMSKERINLLKAYGAEVVLTPAEQRMPGAIAKALELQKQipNSFIPqQFENPaNPNIHRYTTALEI 162
Cdd:PLN02550 176 AQRLGCDAVIAMPVTTPEIKWQSVERLGATVVLVGDSYDEAQAYAKQRALEEG--RTFIP-PFDHP-DVIAGQGTVGMEI 251
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446684939 163 YEQMDGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEP 204
Cdd:PLN02550 252 VRQHQGPLHAIFVPVGGGGLIAGIAAYVKRVRPEVKIIGVEP 293
|
|
| PRK08206 |
PRK08206 |
diaminopropionate ammonia-lyase; Provisional |
66-116 |
2.17e-05 |
|
diaminopropionate ammonia-lyase; Provisional
Pssm-ID: 236186 Cd Length: 399 Bit Score: 45.64 E-value: 2.17e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 446684939 66 TIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERINLLKAYGAEVVLT 116
Cdd:PRK08206 118 TFATATDGNHGRGVAWAAQQLGQKAVIYMPKGSSEERVDAIRALGAECIIT 168
|
|
| ETR |
cd08290 |
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the ... |
48-125 |
3.80e-05 |
|
2-enoyl thioester reductase (ETR); 2-enoyl thioester reductase (ETR) catalyzes the NADPH-dependent conversion of trans-2-enoyl acyl carrier protein/coenzyme A (ACP/CoA) to acyl-(ACP/CoA) in fatty acid synthesis. 2-enoyl thioester reductase activity has been linked in Candida tropicalis as essential in maintaining mitiochondrial respiratory function. This ETR family is a part of the medium chain dehydrogenase/reductase family, but lack the zinc coordination sites characteristic of the alcohol dehydrogenases in this family. NAD(P)(H)-dependent oxidoreductases are the major enzymes in the interconversion of alcohols and aldehydes, or ketones. Alcohol dehydrogenase in the liver converts ethanol and NAD+ to acetaldehyde and NADH, while in yeast and some other microorganisms ADH catalyzes the conversion acetaldehyde to ethanol in alcoholic fermentation. ADH is a member of the medium chain alcohol dehydrogenase family (MDR), which has a NAD(P)(H)-binding domain in a Rossmann fold of a beta-alpha form. The NAD(H)-binding region is comprised of 2 structurally similar halves, each of which contacts a mononucleotide. The N-terminal catalytic domain has a distant homology to GroES. These proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site, and a structural zinc in a lobe of the catalytic domain. NAD(H) binding occurs in the cleft between the catalytic and coenzyme-binding domains, at the active site, and coenzyme binding induces a conformational closing of this cleft. Coenzyme binding typically precedes and contributes to substrate binding. Candida tropicalis enoyl thioester reductase (Etr1p) catalyzes the NADPH-dependent reduction of trans-2-enoyl thioesters in mitochondrial fatty acid synthesis. Etr1p forms homodimers, with each subunit containing a nucleotide-binding Rossmann fold domain and a catalytic domain.
Pssm-ID: 176250 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 48 AYNLLHVAEKnglIKPGDTIIEpTSGNTGIGLAMN--AAAKGYKAILIMPDNMSKERI-NLLKAYGAEVVLTPAEQRMPG 124
Cdd:cd08290 134 AYRLLEDFVK---LQPGDWVIQ-NGANSAVGQAVIqlAKLLGIKTINVVRDRPDLEELkERLKALGADHVLTEEELRSLL 209
|
.
gi 446684939 125 A 125
Cdd:cd08290 210 A 210
|
|
| PLN02970 |
PLN02970 |
serine racemase |
14-207 |
9.59e-05 |
|
serine racemase
Pssm-ID: 215524 [Multi-domain] Cd Length: 328 Bit Score: 43.51 E-value: 9.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 14 TPVVRLSKFIPEDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKpgdTIIEPTSGNTGIGLAMNAAAKGYKAILI 93
Cdd:PLN02970 28 TPVLTSSSLDALAGRSLFFKCECFQKGGAFKFRGACNAIFSLSDDQAEK---GVVTHSSGNHAAALALAAKLRGIPAYIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 94 MPDNMSKERINLLKAYGAEVVLTpaEQRMPGAIAKALELQKQIPNSFIPqqfenPANpniHRY------TTALEIYEQMD 167
Cdd:PLN02970 105 VPKNAPACKVDAVIRYGGIITWC--EPTVESREAVAARVQQETGAVLIH-----PYN---DGRvisgqgTIALEFLEQVP 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446684939 168 gELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGS 207
Cdd:PLN02970 175 -ELDVIIVPISGGGLISGIALAAKAIKPSIKIIAAEPKGA 213
|
|
| PRK08639 |
PRK08639 |
threonine dehydratase; Validated |
28-290 |
1.17e-04 |
|
threonine dehydratase; Validated
Pssm-ID: 236318 [Multi-domain] Cd Length: 420 Bit Score: 43.26 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 28 ADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLikpGDTIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERINLLK 107
Cdd:PRK08639 40 ANVYLKREDLQPVRSYKLRGAYNAISQLSDEEL---AAGVVCASAGNHAQGVAYACRHLGIPGVIFMPVTTPQQKIDQVR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 108 AYGAEVVltpaEQRMPG-----AIAKALELQKQIPNSFIPqqfenpanPNIHRY------TTALEIYEQMD--GELDAFV 174
Cdd:PRK08639 117 FFGGEFV----EIVLVGdtfddSAAAAQEYAEETGATFIP--------PFDDPDviagqgTVAVEILEQLEkeGSPDYVF 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 175 ATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSP----VLSGGvpGPHKL--------------VGTSPGFIPKnlntEV 236
Cdd:PRK08639 185 VPVGGGGLISGVTTYLKERSPKTKIIGVEPAGAAsmkaALEAG--KPVTLekidkfvdgaavarVGDLTFEILK----DV 258
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446684939 237 YNEIIQIaDEEAL-TTMRNLARQEGLLVGPSSGASVyAAIMIAKRLGAGKKVLCI 290
Cdd:PRK08639 259 VDDVVLV-PEGAVcTTILELYNKEGIVAEPAGALSI-AALELYKDEIKGKTVVCV 311
|
|
| PRK07334 |
PRK07334 |
threonine dehydratase; Provisional |
13-287 |
1.27e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 235994 [Multi-domain] Cd Length: 403 Bit Score: 43.34 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 13 DTPVVR---LSKFIpedAADVYVKLEMFNPSRSVKDRAAYN---LLHVAEKngliKPGdtIIEPTSGNTGIGLAMNAAAK 86
Cdd:PRK07334 23 RTPCVHsrtLSQIT---GAEVWLKFENLQFTASFKERGALNkllLLTEEER----ARG--VIAMSAGNHAQGVAYHAQRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 87 GYKAILIMPDNMSKERINLLKAYGAEVVL---TPAEqrmpgAIAKALELQKQIPNSFIpqqfenpanpniHRY------- 156
Cdd:PRK07334 94 GIPATIVMPRFTPTVKVERTRGFGAEVVLhgeTLDE-----ARAHARELAEEEGLTFV------------HPYddpavia 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 157 ---TTALEIYEQMdGELDAFVATAGTGGTITGTGETLKEKLPNLYIAVVEPKGSPVLSGGVPGPHKLVGTS--------- 224
Cdd:PRK07334 157 gqgTVALEMLEDA-PDLDTLVVPIGGGGLISGMATAAKALKPDIEIIGVQTELYPSMYAAIKGVALPCGGStiaegiavk 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446684939 225 -PGFIPKNLNTEVYNEIIQIAD---EEALTTMRNLARQ--EGllvgpsSGASVYAAIMIAKRLGAGKKV 287
Cdd:PRK07334 236 qPGQLTLEIVRRLVDDILLVSEadiEQAVSLLLEIEKTvvEG------AGAAGLAALLAYPERFRGRKV 298
|
|
| PRK06110 |
PRK06110 |
threonine dehydratase; |
28-114 |
2.62e-04 |
|
threonine dehydratase;
Pssm-ID: 235699 Cd Length: 322 Bit Score: 41.90 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 28 ADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPGdtIIEPTSGNTGIGLAMNAAAKGYKAILIMPDNMSKERINLLK 107
Cdd:PRK06110 36 CEVWVKHENHTPTGAFKVRGGLVYFDRLARRGPRVRG--VISATRGNHGQSVAFAARRHGLAATIVVPHGNSVEKNAAMR 113
|
....*..
gi 446684939 108 AYGAEVV 114
Cdd:PRK06110 114 ALGAELI 120
|
|
| MDR |
cd05188 |
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; ... |
52-119 |
2.78e-04 |
|
Medium chain reductase/dehydrogenase (MDR)/zinc-dependent alcohol dehydrogenase-like family; The medium chain reductase/dehydrogenases (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH) , quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit, a catalytic zinc at the active site and a structural zinc in a lobe of the catalytic domain. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines. Other MDR members have only a catalytic zinc, and some contain no coordinated zinc.
Pssm-ID: 176178 [Multi-domain] Cd Length: 271 Bit Score: 41.54 E-value: 2.78e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446684939 52 LHVAEKNGLIKPGDTIIepTSGNTGIGLAMNAAAKGYKAILIMPDnMSKERINLLKAYGAEVVLTPAE 119
Cdd:cd05188 123 YHALRRAGVLKPGDTVL--VLGAGGVGLLAAQLAKAAGARVIVTD-RSDEKLELAKELGADHVIDYKE 187
|
|
| PRK08813 |
PRK08813 |
threonine dehydratase; Provisional |
18-148 |
4.65e-04 |
|
threonine dehydratase; Provisional
Pssm-ID: 236339 [Multi-domain] Cd Length: 349 Bit Score: 41.15 E-value: 4.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684939 18 RLSKFIP------EDAADVYVKLEMFNPSRSVKDRAAYNLLHVAEKNGLIKPgdtIIEPTSGNTGIGLAMNAAAKGYKAI 91
Cdd:PRK08813 32 RLRRYLSptplhyAERFGVWLKLENLQRTGSYKVRGALNALLAGLERGDERP---VICASAGNHAQGVAWSAYRLGVQAI 108
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446684939 92 LIMPDNMSKERINLLKAYGAEVvltpaeqRMPG-----AIAKALELQKQIPNSFIpQQFENP 148
Cdd:PRK08813 109 TVMPHGAPQTKIAGVAHWGATV-------RQHGnsydeAYAFARELADQNGYRFL-SAFDDP 162
|
|
| Zn_ADH2 |
cd08256 |
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and ... |
52-119 |
5.23e-04 |
|
Alcohol dehydrogenases of the MDR family; This group has the characteristic catalytic and structural zinc-binding sites of the zinc-dependent alcohol dehydrogenases of the MDR family. The medium chain dehydrogenases/reductase (MDR)/zinc-dependent alcohol dehydrogenase-like family, which contains the zinc-dependent alcohol dehydrogenase (ADH-Zn) and related proteins, is a diverse group of proteins related to the first identified member, class I mammalian ADH. MDRs display a broad range of activities and are distinguished from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P)-binding Rossmann fold domain of a beta-alpha form and an N-terminal catalytic domain with distant homology to GroES. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability.
Pssm-ID: 176218 [Multi-domain] Cd Length: 350 Bit Score: 41.24 E-value: 5.23e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446684939 52 LHVAEKnGLIKPGDTIIEPTSGNTGIGLAMNAAAKGYKAILIMpdNMSKERINLLKAYGAEVVLTPAE 119
Cdd:cd08256 164 LHAVDR-ANIKFDDVVVLAGAGPLGLGMIGAARLKNPKKLIVL--DLKDERLALARKFGADVVLNPPE 228
|
|
| RlmE |
COG0293 |
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and ... |
29-68 |
7.85e-03 |
|
23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ [Translation, ribosomal structure and biogenesis]; 23S rRNA U2552 (ribose-2'-O)-methylase RlmE/FtsJ is part of the Pathway/BioSystem: 23S rRNA modification
Pssm-ID: 440062 [Multi-domain] Cd Length: 208 Bit Score: 36.97 E-value: 7.85e-03
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 446684939 29 DVYVKL---EMFnpsRSvkdRAAYNLLHVAEKNGLIKPGDTII 68
Cdd:COG0293 19 DPYVKRakkEGY---RS---RAAYKLLEIDEKDKLIKPGMRVV 55
|
|
| Trp-synth_B |
cd06446 |
Tryptophan synthase-beta: Tryptophan synthase is a bifunctional enzyme that catalyses the ... |
243-288 |
8.87e-03 |
|
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: 37.52 E-value: 8.87e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 446684939 243 IADEEALTTMRNLARQEGLLVGPSSGASVYAAIMIAKRLGAGKKVL 288
Cdd:cd06446 306 VTDEEALEAFKLLARTEGIIPALESSHAIAYAIKLAKKLGKEKVIV 351
|
|
| iditol_2_DH_like |
cd08235 |
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some ... |
55-120 |
9.00e-03 |
|
L-iditol 2-dehydrogenase; Putative L-iditol 2-dehydrogenase based on annotation of some members in this subgroup. L-iditol 2-dehydrogenase catalyzes the NAD+-dependent conversion of L-iditol to L-sorbose in fructose and mannose metabolism. This enzyme is related to sorbitol dehydrogenase, alcohol dehydrogenase, and other medium chain dehydrogenase/reductases. The zinc-dependent alcohol dehydrogenase (ADH-Zn)-like family of proteins is a diverse group of proteins related to the first identified member, class I mammalian ADH. This group is also called the medium chain dehydrogenases/reductase family (MDR) to highlight its broad range of activities and to distinguish from the smaller short chain dehydrogenases (~ 250 amino acids vs. the ~ 350 amino acids of the MDR). The MDR proteins have 2 domains: a C-terminal NAD(P) binding-Rossmann fold domain of a beta-alpha form and an N-terminal GroES-like catalytic domain. The MDR group contains a host of activities, including the founding alcohol dehydrogenase (ADH), quinone reductase, sorbitol dehydrogenase, formaldehyde dehydrogenase, butanediol DH, ketose reductase, cinnamyl reductase, and numerous others. The zinc-dependent alcohol dehydrogenases (ADHs) catalyze the NAD(P)(H)-dependent interconversion of alcohols to aldehydes or ketones. Active site zinc has a catalytic role, while structural zinc aids in stability. ADH-like proteins typically form dimers (typically higher plants, mammals) or tetramers (yeast, bacteria), and generally have 2 tightly bound zinc atoms per subunit. The active site zinc is coordinated by a histidine, two cysteines, and a water molecule. The second zinc seems to play a structural role, affects subunit interactions, and is typically coordinated by 4 cysteines.
Pssm-ID: 176197 [Multi-domain] Cd Length: 343 Bit Score: 37.19 E-value: 9.00e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446684939 55 AEKNGLIKPGDTIIEPTSGNTGIGLAMNAAAKGYKAIlIMPDnMSKERINLLKAYGAEVVLTPAEQ 120
Cdd:cd08235 157 AQRKAGIKPGDTVLVIGAGPIGLLHAMLAKASGARKV-IVSD-LNEFRLEFAKKLGADYTIDAAEE 220
|
|
| |
