|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-295 |
0e+00 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 517.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 2 ARDLKGVMPALLTPFDNQQRLDIESLRRLVRFNIG-QGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHV 80
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 81 GTVSTEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGlPMVVYNIPALSGVKLTLDQINTLVTLPG 160
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFTLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 161 VGALKQTSGDLYQMEQIRRAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECN 240
Cdd:PRK04147 160 VIGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489925453 241 KVIDLLIKVGVFRGLKTVLHYMDvVSVPLCRKPFAPVDEHYLPELKALANQLLAE 295
Cdd:PRK04147 240 DVIDLLIKNGVYPGLKEILHYMG-VDAGLCRKPFKPVDEKYLPALKALAAKYLKE 293
|
|
| nanA |
TIGR00683 |
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid ... |
5-296 |
1.13e-178 |
|
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273217 Cd Length: 293 Bit Score: 494.47 E-value: 1.13e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 5 LKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTVS 84
Cdd:TIGR00683 1 LRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 85 TEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGAL 164
Cdd:TIGR00683 81 TAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 165 KQTSGDLYQMEQIRRAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKVID 244
Cdd:TIGR00683 161 KQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVID 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489925453 245 LLIKVGVFRGLKTVLHYMDVVSVPLCRKPFAPVDEHYLPELKALANQLLAEK 296
Cdd:TIGR00683 241 LLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQER 292
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-291 |
1.43e-143 |
|
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.
Pssm-ID: 188641 [Multi-domain] Cd Length: 288 Bit Score: 405.15 E-value: 1.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 5 LKGVMPALLTPFDNQQRLDIESLRRLVRFNIG-QGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTV 83
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 84 STEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 163
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 164 LKQTSGDLYQMEQIRRAHP-DLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKV 242
Cdd:cd00954 161 VKFTATDLYDLERIRAASPeDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489925453 243 IDLLIKVGVFRGLKTVLHYMDvVSVPLCRKPFAPVDEHYLPELKALANQ 291
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMG-LDAGPCRLPLRKVTEKALAKAKELAAK 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
4-292 |
3.69e-138 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 391.73 E-value: 3.69e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 4 DLKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTV 83
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 84 STEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIdSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 163
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIA-EATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 164 LKQTSGDLYQMEQIRR-AHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKV 242
Cdd:pfam00701 160 IKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489925453 243 IDLLIKVGVFRGLKTVLHYMDVVSVPLCRKPFAPVDEHYLPELKALANQL 292
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
4-292 |
4.37e-97 |
|
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440098 [Multi-domain] Cd Length: 291 Bit Score: 287.43 E-value: 4.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 4 DLKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTV 83
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 84 STEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 163
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 164 LKQTSGDLYQMEQIRRAHP-DLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKV 242
Cdd:COG0329 160 IKEASGDLDRIAELIRATGdDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489925453 243 IDLLIKVGVFRGLKTVLHYMDVVSvPLCRKPFAPVDEHYLPELKALANQL 292
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPS-GPVRLPLLPLSEEERAELRAALKEL 288
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK04147 |
PRK04147 |
N-acetylneuraminate lyase; Provisional |
2-295 |
0e+00 |
|
N-acetylneuraminate lyase; Provisional
Pssm-ID: 179749 [Multi-domain] Cd Length: 293 Bit Score: 517.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 2 ARDLKGVMPALLTPFDNQQRLDIESLRRLVRFNIG-QGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHV 80
Cdd:PRK04147 1 AKNLKGVYAALLTPFDEDGQIDEQGLRRLVRFNIEkQGIDGLYVGGSTGEAFLLSTEEKKQVLEIVAEEAKGKVKLIAQV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 81 GTVSTEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGlPMVVYNIPALSGVKLTLDQINTLVTLPG 160
Cdd:PRK04147 81 GSVNTAEAQELAKYATELGYDAISAVTPFYYPFSFEEICDYYREIIDSADN-PMIVYNIPALTGVNLSLDQFNELFTLPK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 161 VGALKQTSGDLYQMEQIRRAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECN 240
Cdd:PRK04147 160 VIGVKQTAGDLYQLERIRKAFPDKLIYNGFDEMFASGLLAGADGAIGSTYNVNGWRARQIFEAAKAGDIQEAQELQHECN 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 489925453 241 KVIDLLIKVGVFRGLKTVLHYMDvVSVPLCRKPFAPVDEHYLPELKALANQLLAE 295
Cdd:PRK04147 240 DVIDLLIKNGVYPGLKEILHYMG-VDAGLCRKPFKPVDEKYLPALKALAAKYLKE 293
|
|
| nanA |
TIGR00683 |
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid ... |
5-296 |
1.13e-178 |
|
N-acetylneuraminate lyase; N-acetylneuraminate lyase is also known as N-acetylneuraminic acid aldolase, sialic acid aldolase, or sialate lyase. It is an intracellular enzyme. The structure of this homotetrameric enzyme related to dihydrodipicolinate synthase is known. In Clostridium tertium, the enzyme appears to be in an operon with a secreted sialidase that releases sialic acid from host sialoglycoconjugates. In several E. coli strains, however, this enzyme is responsible for N-acetyl-D-neuraminic acid synthesis for capsule production by condensing N-acetyl-D-mannosamine and pyruvate. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Central intermediary metabolism, Amino sugars]
Pssm-ID: 273217 Cd Length: 293 Bit Score: 494.47 E-value: 1.13e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 5 LKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTVS 84
Cdd:TIGR00683 1 LRGVMAALLTPFDQQQALDKASLRRLVQFNIQQGIDGLYVGGSTGEAFVQSLSEREQVLEIVAEEAKGKIKLIAHVGCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 85 TEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGAL 164
Cdd:TIGR00683 81 TAESQQLAASAKRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 165 KQTSGDLYQMEQIRRAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKVID 244
Cdd:TIGR00683 161 KQTSGDLYQMEQIRREHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIQTAQKLQTECNKVID 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489925453 245 LLIKVGVFRGLKTVLHYMDVVSVPLCRKPFAPVDEHYLPELKALANQLLAEK 296
Cdd:TIGR00683 241 LLIKTGVFRGLKTVLHYMDVVSVPLCRKPFGPVDEKYLPELKALAQQLMQER 292
|
|
| NAL |
cd00954 |
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); ... |
5-291 |
1.43e-143 |
|
N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL); N-Acetylneuraminic acid aldolase, also called N-acetylneuraminate lyase (NAL), which catalyses the reversible aldol reaction of N-acetyl-D-mannosamine and pyruvate to give N-acetyl-D-neuraminic acid (D-sialic acid). It has a widespread application as biocatalyst for the synthesis of sialic acid and its derivatives. This enzyme has been shown to be quite specific for pyruvate as the donor, but flexible to a variety of D- and, to some extent, L-hexoses and pentoses as acceptor substrates. NAL is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases.
Pssm-ID: 188641 [Multi-domain] Cd Length: 288 Bit Score: 405.15 E-value: 1.43e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 5 LKGVMPALLTPFDNQQRLDIESLRRLVRFNIG-QGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTV 83
Cdd:cd00954 1 LKGLIAALLTPFDENGEINEDVLRAIVDYLIEkQGVDGLYVNGSTGEGFLLSVEERKQIAEIVAEAAKGKVTLIAHVGSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 84 STEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 163
Cdd:cd00954 81 NLKESQELAKHAEELGYDAISAITPFYYKFSFEEIKDYYREIIAAAASLPMIIYHIPALTGVNLTLEQFLELFEIPNVIG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 164 LKQTSGDLYQMEQIRRAHP-DLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKV 242
Cdd:cd00954 161 VKFTATDLYDLERIRAASPeDKLVLNGFDEMLLSALALGADGAIGSTYNVNGKRYRKIFEAFNAGDIDTARELQHVINDV 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 489925453 243 IDLLIKVGVFRGLKTVLHYMDvVSVPLCRKPFAPVDEHYLPELKALANQ 291
Cdd:cd00954 241 ITVLIKNGLYPTLKAILRLMG-LDAGPCRLPLRKVTEKALAKAKELAAK 288
|
|
| DHDPS |
pfam00701 |
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure. |
4-292 |
3.69e-138 |
|
Dihydrodipicolinate synthetase family; This family has a TIM barrel structure.
Pssm-ID: 395570 [Multi-domain] Cd Length: 289 Bit Score: 391.73 E-value: 3.69e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 4 DLKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTV 83
Cdd:pfam00701 1 KFSGIITALVTPFDTDGTLDFAALRQLIDFLINKGVDGLVVGGTTGESFTLSTEEREQLVEITVNEAKGRIPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 84 STEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIdSADGLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 163
Cdd:pfam00701 81 STSEAIHLAQLAEEYGADGALAVTPYYNKPSQEGLYQHFKAIA-EATDLPMILYNVPSRTGVDLTPETVGRLATNPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 164 LKQTSGDLYQMEQIRR-AHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKV 242
Cdd:pfam00701 160 IKEASGDLDRMINIKKeAGPDFVILSGDDETMLPALSLGADGVISVTSNIAGHRMRQMYKALKNGDLATAALINHKLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489925453 243 IDLLIKVGVFRGLKTVLHYMDVVSVPLCRKPFAPVDEHYLPELKALANQL 292
Cdd:pfam00701 240 IKILFAEPNPIPIKTALELLGLVVGPTCRLPLTPLSEEERPELEAILKAA 289
|
|
| DapA |
COG0329 |
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and ... |
4-292 |
4.37e-97 |
|
4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase [Amino acid transport and metabolism, Cell wall/membrane/envelope biogenesis]; 4-hydroxy-tetrahydrodipicolinate synthase/N-acetylneuraminate lyase is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440098 [Multi-domain] Cd Length: 291 Bit Score: 287.43 E-value: 4.37e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 4 DLKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTV 83
Cdd:COG0329 1 KFRGVIPALVTPFDADGSVDEEALRRLVEFLIDAGVDGLVVLGTTGESATLTDEERKRVLEAVVEAAAGRVPVIAGVGSN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 84 STEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNIPALSGVKLTLDQINTLVTLPGVGA 163
Cdd:COG0329 81 STAEAIELARHAEEAGADAVLVVPPYYNKPTQEGLYAHFKAIAEAVD-LPIILYNIPGRTGVDLSPETLARLAEIPNIVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 164 LKQTSGDLYQMEQIRRAHP-DLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKV 242
Cdd:COG0329 160 IKEASGDLDRIAELIRATGdDFAVLSGDDALALPALALGADGVISVTANVAPELMVALYEAALAGDLAEARALQDRLLPL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489925453 243 IDLLIKVGVFRGLKTVLHYMDVVSvPLCRKPFAPVDEHYLPELKALANQL 292
Cdd:COG0329 240 IRALFAEGNPAPVKAALALLGLPS-GPVRLPLLPLSEEERAELRAALKEL 288
|
|
| DHDPS-like |
cd00408 |
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the ... |
8-288 |
9.41e-91 |
|
Dihydrodipicolinate synthase family; Dihydrodipicolinate synthase family. A member of the class I aldolases, which use an active-site lysine which stabilizes a reaction intermediate via Schiff base formation, and have TIM beta/alpha barrel fold. The dihydrodipicolinate synthase family comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways and includes such proteins as N-acetylneuraminate lyase, MosA protein, 5-keto-4-deoxy-glucarate dehydratase, trans-o-hydroxybenzylidenepyruvate hydratase-aldolase, trans-2'-carboxybenzalpyruvate hydratase-aldolase, and 2-keto-3-deoxy- gluconate aldolase. The family is also referred to as the N-acetylneuraminate lyase (NAL) family.
Pssm-ID: 188630 [Multi-domain] Cd Length: 281 Bit Score: 270.96 E-value: 9.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 8 VMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTVSTEE 87
Cdd:cd00408 1 VIPALVTPFTADGEVDLDALRRLVEFLIEAGVDGLVVLGTTGEAPTLTDEERKEVIEAVVEAVAGRVPVIAGVGANSTRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 88 SQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQT 167
Cdd:cd00408 81 AIELARHAEEAGADGVLVVPPYYNKPSQEGIVAHFKAVADASD-LPVILYNIPGRTGVDLSPETIARLAEHPNIVGIKDS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 168 SGDLYQMEQIRRA-HPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKVIDLL 246
Cdd:cd00408 160 SGDLDRLTRLIALlGPDFAVLSGDDDLLLPALALGADGAISGAANVAPKLAVALYEAARAGDLEEARALQDRLLPLIEAL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 489925453 247 IKVGVFRGLKTVLHYMDVVSVPlCRKPFAPVDEHYLPELKAL 288
Cdd:cd00408 240 FKEGNPAPVKAALALLGLDAGP-VRLPLVPLSEEERAKLEAL 280
|
|
| DHDPS |
cd00950 |
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in ... |
5-288 |
2.00e-62 |
|
Dihydrodipicolinate synthase (DHDPS); Dihydrodipicolinate synthase (DHDPS) is a key enzyme in lysine biosynthesis. It catalyzes the aldol condensation of L-aspartate-beta- semialdehyde and pyruvate to dihydropicolinic acid via a Schiff base formation between pyruvate and a lysine residue. The functional enzyme is a homotetramer consisting of a dimer of dimers. DHDPS is member of dihydrodipicolinate synthase family that comprises several pyruvate-dependent class I aldolases that use the same catalytic step to catalyze different reactions in different pathways.
Pssm-ID: 188637 [Multi-domain] Cd Length: 284 Bit Score: 198.87 E-value: 2.00e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 5 LKGVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTVS 84
Cdd:cd00950 1 FGGSITALVTPFKDDGSVDFDALERLIEFQIENGTDGLVVCGTTGESPTLSDEEHEAVIEAVVEAVNGRVPVIAGTGSNN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 85 TEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNIPALSGVKLTLDQINTLVTLPGVGAL 164
Cdd:cd00950 81 TAEAIELTKRAEKAGADAALVVTPYYNKPSQEGLYAHFKAIAEATD-LPVILYNVPGRTGVNIEPETVLRLAEHPNIVGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 165 KQTSGDLYQMEQIR-RAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKVI 243
Cdd:cd00950 160 KEATGDLDRVSELIaLCPDDFAVLSGDDALTLPFLALGGVGVISVAANVAPKLMAEMVRAALAGDLEKARELHRKLLPLI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 489925453 244 DLLikvgvFR-----GLKTVLHYMDVVSvPLCRKPFAPVDEHYLPELKAL 288
Cdd:cd00950 240 KAL-----FAepnpiPVKAALALLGLIS-GELRLPLVPLSEELRAKLRAA 283
|
|
| dapA |
TIGR00674 |
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are ... |
7-292 |
5.65e-45 |
|
4-hydroxy-tetrahydrodipicolinate synthase; Members of this family are 4-hydroxy-tetrahydrodipicolinate synthase, previously (incorrectly) called dihydrodipicolinate synthase. It is a homotetrameric enzyme of lysine biosynthesis. E. coli has several paralogs closely related to dihydrodipicoline synthase (DapA), as well as the more distant N-acetylneuraminate lyase. In Pyrococcus horikoshii, the bidirectional best hit with E. coli is to an uncharacterized paralog of DapA, not DapA itself, and it is omitted from the seed. The putative members from the Chlamydias (pathogens with a parasitic metabolism) are easily the most divergent members of the multiple alignment. [Amino acid biosynthesis, Aspartate family]
Pssm-ID: 129757 [Multi-domain] Cd Length: 285 Bit Score: 154.02 E-value: 5.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 7 GVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTVSTE 86
Cdd:TIGR00674 1 GVITALITPFKEDGSVDFAALEKLIDFQIENGTDAIVVVGTTGESPTLSHEEHKKVIEFVVDLVNGRVPVIAGTGSNATE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 87 ESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQ 166
Cdd:TIGR00674 81 EAISLTKFAEDVGADGFLVVTPYYNKPTQEGLYQHFKAIAEEVD-LPIILYNVPSRTGVSLYPETVKRLAEEPNIVAIKE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 167 TSGDLYQMEQIRRAHP-DLVLYNGYDEIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTAQKLQTECNKVIDL 245
Cdd:TIGR00674 160 ATGNLERISEIKAIAPdDFVVLSGDDALTLPMMALGGKGVISVTANVAPKLMKEMVNNALEGDFAEAREIHQKLMPLHKA 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489925453 246 LIKVGVFRGLKTVLHYMDVVSVPLcRKPFAPVDEHYLPELKALANQL 292
Cdd:TIGR00674 240 LFIETNPIPVKTALALLGLIEGEL-RLPLTELSEEHRNKLRDVLKDL 285
|
|
| PLN02417 |
PLN02417 |
dihydrodipicolinate synthase |
7-291 |
1.00e-34 |
|
dihydrodipicolinate synthase
Pssm-ID: 178038 Cd Length: 280 Bit Score: 127.07 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 7 GVMPALLTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTVSTE 86
Cdd:PLN02417 4 RLITAIKTPYLPDGRFDLEAYDSLVNMQIENGAEGLIVGGTTGEGQLMSWDEHIMLIGHTVNCFGGKIKVIGNTGSNSTR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 87 ESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSAdglPMVVYNIPALSGVKLTLDQINTLVTLPGVGALKQ 166
Cdd:PLN02417 84 EAIHATEQGFAVGMHAALHINPYYGKTSQEGLIKHFETVLDMG---PTIIYNVPGRTGQDIPPEVIFKIAQHPNFAGVKE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 167 TSGDlyqmEQIRR-AHPDLVLYNGYD-EIFASGLLAGADGGIGSTYNIMGWRYQGIVKALKEGDIRTA-----QKLQTEC 239
Cdd:PLN02417 161 CTGN----DRVKQyTEKGILLWSGNDdECHDARWDYGADGVISVTSNLVPGLMHKLMFAGKNKELNDKllplmDWLFCEP 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 489925453 240 NKVidllikvgvfrGLKTVLHYMDVVSvPLCRKPFAPVDEHYLPELKALANQ 291
Cdd:PLN02417 237 NPI-----------GLNTALAQLGLIR-PVFRLPYVPLDLAKRAEFVALVKA 276
|
|
| KDG_aldolase |
cd00953 |
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) ... |
12-280 |
5.32e-28 |
|
KDG (2-keto-3-deoxygluconate) aldolases found in archaea; KDG (2-keto-3-deoxygluconate) aldolases found in archaea. This subfamily of enzymes is adapted for high thermostability and shows specificity for non-phosphorylated substrates. The enzyme catalyses the reversible aldol cleavage of 2-keto-3-dexoygluconate to pyruvate and glyceraldehyde, the third step of a modified non-phosphorylated Entner-Doudoroff pathway of glucose oxidation. KDG aldolase shows no significant sequence similarity to microbial 2-keto-3-deoxyphosphogluconate (KDPG) aldolases, and the enzyme shows no activity with glyceraldehyde 3-phosphate as substrate. The enzyme is a tetramer and a member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188640 Cd Length: 279 Bit Score: 109.01 E-value: 5.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 12 LLTPFDNQqRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKgkvTLIAHVGTVSTEESQQL 91
Cdd:cd00953 8 VITPFTGN-KIDKEKFKKHCENLISKGIDYVFVAGTTGLGPSLSFQEKLELLKAYSDITD---KVIFQVGSLNLEESIEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 92 ASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSAdgLPMVVYNIPALSGVKLTLDQINTLVTLPG-VGALKQTSGD 170
Cdd:cd00953 84 ARAAKSFGIYAIASLPPYYFPGIPEEWLIKYFTDISSP--YPTFIYNYPKATGYDINARMAKEIKKAGGdIIGVKDTNED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 171 LYQMEQIRRAHPDLVLYNGYDEIFASGLLAGADGGIGSTYNIMgwrYQGIVKALKEGDIRTAQKLQTECNKVIDLLIKVG 250
Cdd:cd00953 162 ISHMLEYKRLVPDFKVYSGPDSLIFSALRSGLDGSVAAASNYL---PEVFVKIKDHVAIEDAFKLQFLINEVLDASRKYG 238
|
250 260 270
....*....|....*....|....*....|
gi 489925453 251 VFRGLKTVLHYMDVVSVPLCRKPFAPVDEH 280
Cdd:cd00953 239 SWSANYSLVKIFQGYDAGEPRPPFYPLDEE 268
|
|
| PRK03620 |
PRK03620 |
5-dehydro-4-deoxyglucarate dehydratase; Provisional |
3-200 |
1.07e-17 |
|
5-dehydro-4-deoxyglucarate dehydratase; Provisional
Pssm-ID: 235141 Cd Length: 303 Bit Score: 81.40 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 3 RDLKGVMPA-LL----TPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLI 77
Cdd:PRK03620 1 QELKQILGSgLLsfpvTPFDADGSFDEAAYREHLEWLAPYGAAALFAAGGTGEFFSLTPDEYSQVVRAAVETTAGRVPVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 78 AHVGTvSTEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNipaLSGVKLTLDQINTLVT 157
Cdd:PRK03620 81 AGAGG-GTAQAIEYAQAAERAGADGILLLPPYLTEAPQEGLAAHVEAVCKSTD-LGVIVYN---RDNAVLTADTLARLAE 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489925453 158 -LPGVGALKQTSGDLYQMEQIRRAHPDLVLY-NGYD--EIFASGLLA 200
Cdd:PRK03620 156 rCPNLVGFKDGVGDIELMQRIVRALGDRLLYlGGLPtaEVFAAAYLA 202
|
|
| KDGDH |
cd00951 |
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase ... |
13-200 |
2.30e-17 |
|
5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH); 5-dehydro-4-deoxyglucarate dehydratase, also called 5-keto-4-deoxy-glucarate dehydratase (KDGDH), which is member of dihydrodipicolinate synthase (DHDPS) family that comprises several pyruvate-dependent class I aldolases. The enzyme is involved in glucarate metabolism, and its mechanism presumbly involves a Schiff-base intermediate similar to members of DHDPS family. While in the case of Pseudomonas sp. 5-dehydro-4-deoxy-D-glucarate is degraded by KDGDH to 2,5-dioxopentanoate, in certain species of Enterobacteriaceae it is degraded instead to pyruvate and glycerate.
Pssm-ID: 188638 Cd Length: 289 Bit Score: 80.06 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 13 LTPFDNQQRLDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTLIAHVGTvSTEESQQLA 92
Cdd:cd00951 9 VTHFDADGSFDEDAYRAHVEWLLSYGAAALFAAGGTGEFFSLTPDEYAQVVRAAVEETAGRVPVLAGAGY-GTATAIAYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 93 SAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADgLPMVVYNipaLSGVKLTLDQINTLV-TLPGVGALKQTSGDL 171
Cdd:cd00951 88 QAAEKAGADGILLLPPYLTEAPQEGLYAHVEAVCKSTD-LGVIVYN---RANAVLTADSLARLAeRCPNLVGFKDGVGDI 163
|
170 180 190
....*....|....*....|....*....|..
gi 489925453 172 YQMEQIRRAHPDLVLY-NGYD--EIFASGLLA 200
Cdd:cd00951 164 ELMRRIVAKLGDRLLYlGGLPtaEVFALAYLA 195
|
|
| Aldolase_Class_I |
cd00945 |
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which ... |
8-208 |
3.27e-09 |
|
Class I aldolases; Class I aldolases. The class I aldolases use an active-site lysine which stabilizes a reaction intermediates via Schiff base formation, and have TIM beta/alpha barrel fold. The members of this family include 2-keto-3-deoxy-6-phosphogluconate (KDPG) and 2-keto-4-hydroxyglutarate (KHG) aldolases, transaldolase, dihydrodipicolinate synthase sub-family, Type I 3-dehydroquinate dehydratase, DeoC and DhnA proteins, and metal-independent fructose-1,6-bisphosphate aldolase. Although structurally similar, the class II aldolases use a different mechanism and are believed to have an independent evolutionary origin.
Pssm-ID: 188634 [Multi-domain] Cd Length: 201 Bit Score: 55.80 E-value: 3.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 8 VMPALLTPFDnqqrlDIESLRRLVRFNIGQGVDGLYVGGStgeafvqnrvereqVLEIVAEEAKG-KVTLIAHV----GT 82
Cdd:cd00945 1 IDLTLLHPDA-----TLEDIAKLCDEAIEYGFAAVCVNPG--------------YVRLAADALAGsDVPVIVVVgfptGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 83 VSTEESQQLASAAHRYGFDAVSAVTPFYYPFS--FEEHCDHYRAIIDSAD-GLPMVVYNIPA-LSGVKLTLDQINTLVTL 158
Cdd:cd00945 62 TTTEVKVAEVEEAIDLGADEIDVVINIGSLKEgdWEEVLEEIAAVVEAADgGLPLKVILETRgLKTADEIAKAARIAAEA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489925453 159 pGVGALKQTSG------DLYQMEQIRRAHPDLV-LYNGYD----EIFASGLLAGADGGIGS 208
Cdd:cd00945 142 -GADFIKTSTGfggggaTVEDVKLMKEAVGGRVgVKAAGGiktlEDALAAIEAGADGIGTS 201
|
|
| CHBPH_aldolase |
cd00952 |
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2 ... |
4-169 |
1.09e-08 |
|
Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA); Trans-o-hydroxybenzylidenepyruvate hydratase-aldolase (HBPHA) and trans-2'-carboxybenzalpyruvate hydratase-aldolase (CBPHA). HBPHA catalyzes HBP to salicyaldehyde and pyruvate. This reaction is part of the degradative pathways for naphthalene and naphthalenesulfonates by bacteria. CBPHA is homologous to HBPHA and catalyzes the cleavage of CBP to 2-carboxylbenzaldehyde and pyruvate during the degradation of phenanthrene. They are member of the DHDPS family of Schiff-base-dependent class I aldolases.
Pssm-ID: 188639 Cd Length: 309 Bit Score: 55.14 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 4 DLKGV---MPALLTPFDNQQR----LDIESLRRLVRFNIGQGVDGLYVGGSTGEAFVQNRVEREQVLEIVAEEAKGKVTL 76
Cdd:cd00952 1 DIKGVwaiVPTPSKPDASDWRatdtVDLDETARLVERLIAAGVDGILTMGTFGECATLTWEEKQAFVATVVETVAGRVPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489925453 77 IAHVGTVSTEESQQLASAAHRYGFDAVSAVTPFYYPFSFEEHCDHYRAIIDSADGLPMVVYNIPALSGVKLTLDQINTLV 156
Cdd:cd00952 81 FVGATTLNTRDTIARTRALLDLGADGTMLGRPMWLPLDVDTAVQFYRDVAEAVPEMAIAIYANPEAFKFDFPRAAWAELA 160
|
170
....*....|...
gi 489925453 157 TLPGVGALKQTSG 169
Cdd:cd00952 161 QIPQVVAAKYLGD 173
|
|
| |
