|
Name |
Accession |
Description |
Interval |
E-value |
| PRK06939 |
PRK06939 |
2-amino-3-ketobutyrate coenzyme A ligase; Provisional |
1-399 |
0e+00 |
|
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
Pssm-ID: 235893 [Multi-domain] Cd Length: 397 Bit Score: 782.07 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 1 MRDAFLAHVRGTLDQIRADGFYKTEREIASPQAADVKLADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVR 80
Cdd:PRK06939 1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 81 FICGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQD 160
Cdd:PRK06939 81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 161 LEAKLREADEAGARFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTG 240
Cdd:PRK06939 161 LEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 241 TLGKALGGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLELLasDEGARLRRRVRENGAHFRRRMSEAGF 320
Cdd:PRK06939 241 TLGKALGGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELL--EESDELRDRLWENARYFREGMTAAGF 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738096527 321 TLVPGEHPIIPVMLGDAQVATRMADALLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGKSLGVI 399
Cdd:PRK06939 319 TLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
|
|
| 2am3keto_CoA |
TIGR01822 |
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ... |
5-399 |
0e+00 |
|
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and bacterial (almost exclusively Proteobacterial) 2-amino-3-ketobutyrate--CoA ligase, now called glycine C-acetyltransferase. This enzyme can act in threonine catabolism. The closest homolog from Bacillus subtilis, and sequences like it, may be functionally equivalent but were not included in the model because of difficulty in finding reports of function. [Energy metabolism, Amino acids and amines]
Pssm-ID: 130881 [Multi-domain] Cd Length: 393 Bit Score: 621.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 5 FLAHVRGTLDQIRADGFYKTEREIASPQAADVKLADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICG 84
Cdd:TIGR01822 1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVADGREVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFICG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 85 TQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAK 164
Cdd:TIGR01822 81 TQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 165 LREADEAGARFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTGTLGK 244
Cdd:TIGR01822 161 LKEARAAGARHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTLGK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 245 ALGGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLELLasDEGARLRRRVRENGAHFRRRMSEAGFTLVP 324
Cdd:TIGR01822 241 ALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEML--EASNELRDRLWANTRYFRERMEAAGFDIKP 318
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738096527 325 GEHPIIPVMLGDAQVATRMADALLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGKSLGVI 399
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
|
|
| BioF |
COG0156 |
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ... |
5-394 |
0e+00 |
|
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; 7-keto-8-aminopelargonate synthetase or related enzyme is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439926 [Multi-domain] Cd Length: 385 Bit Score: 558.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 5 FLAHVRGTLDQIRADGFYKTEREIASPQAADVKLaDGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICG 84
Cdd:COG0156 1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTI-DGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 85 TQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAK 164
Cdd:COG0156 80 TTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 165 LREADEagARFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTGTLGK 244
Cdd:COG0156 160 LKKARA--ARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 245 ALgGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLELLASDEgaRLRRRVRENGAHFRRRMSEAGFTLVP 324
Cdd:COG0156 238 AL-GSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKELGFDLGP 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 325 GEHPIIPVMLGDAQVATRMADALLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGK 394
Cdd:COG0156 315 SESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
|
|
| KBL_like |
cd06454 |
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ... |
44-393 |
4.24e-160 |
|
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to serine palmitoyltransferase (SPT), 5-aminolevulinate synthase (ALAS), 8-amino-7-oxononanoate synthase (AONS), and 2-amino-3-ketobutyrate CoA ligase (KBL). SPT is responsible for the condensation of L-serine with palmitoyl-CoA to produce 3-ketodihydrospingosine, the reaction of the first step in sphingolipid biosynthesis. ALAS is involved in heme biosynthesis; it catalyzes the synthesis of 5-aminolevulinic acid from glycine and succinyl-coenzyme A. AONS catalyses the decarboxylative condensation of l-alanine and pimeloyl-CoA in the first committed step of biotin biosynthesis. KBL catalyzes the second reaction step of the metabolic degradation pathway for threonine converting 2-amino-3-ketobutyrate, to glycine and acetyl-CoA. The members of this CD are widely found in all three forms of life.
Pssm-ID: 99747 [Multi-domain] Cd Length: 349 Bit Score: 453.94 E-value: 4.24e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 44 VLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLL 123
Cdd:cd06454 3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 124 GEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAKLREADEaGARFKLIATDGVFSMDGIIADLKGVCDLADRY 203
Cdd:cd06454 83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARR-PYGKKLIVTEGVYSMDGDIAPLPELVDLAKKY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 204 GALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTGTLGKALgGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAE 283
Cdd:cd06454 162 GAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 284 ASLAVLELLASdeGARLRRRVRENGAHFRRRMSEAGFTLVPGE-HPIIPVMLGDAQVATRMADALLAEGVYVIGFSFPVV 362
Cdd:cd06454 241 AALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318
|
330 340 350
....*....|....*....|....*....|.
gi 738096527 363 PRGRARIRTQMSAAHTPEQIDRAVDAFVRVG 393
Cdd:cd06454 319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
|
|
| PRK05958 |
PRK05958 |
8-amino-7-oxononanoate synthase; Reviewed |
4-393 |
2.33e-130 |
|
8-amino-7-oxononanoate synthase; Reviewed
Pssm-ID: 235655 [Multi-domain] Cd Length: 385 Bit Score: 379.50 E-value: 2.33e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 4 AFLAHVRGTLDQIRADGFYKTEREIASPQAADVKLaDGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFIC 83
Cdd:PRK05958 2 SWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVV-DGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 84 GTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEA 163
Cdd:PRK05958 81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 164 KLREADeagARFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVD-IVTGTL 242
Cdd:PRK05958 161 LLAKWR---AGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDvILVGTL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 243 GKALgGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLELLASDEGarLRRRVRENGAHFRRRMSEAGFTL 322
Cdd:PRK05958 238 GKAL-GSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE--RRERLAALIARLRAGLRALGFQL 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 738096527 323 VPGEHPIIPVMLGDAQVATRMADALLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVG 393
Cdd:PRK05958 315 MDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
|
|
| bioF |
TIGR00858 |
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ... |
28-389 |
5.46e-128 |
|
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. This model represents 8-amino-7-oxononanoate synthase, the BioF protein of biotin biosynthesis. This model is based on a careful phylogenetic analysis to separate members of this family from 2-amino-3-ketobutyrate and other related pyridoxal phosphate-dependent enzymes. In several species, including Staphylococcus and Coxiella, a candidate 8-amino-7-oxononanoate synthase is confirmed by location in the midst of a biotin biosynthesis operon but scores below the trusted cutoff of this model. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]
Pssm-ID: 273303 [Multi-domain] Cd Length: 360 Bit Score: 372.76 E-value: 5.46e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 28 IASPQAADVKLADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICGTQTVHKQLEAALSRFLGTDDTIL 107
Cdd:TIGR00858 2 PLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 108 YSSCFDANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAKLREADeaGARFKLIATDGVFSMD 187
Cdd:TIGR00858 82 FSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNR--GERRKLIVTDGVFSMD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 188 GIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVA-DRVDIVTGTLGKALGGAsGGYVSARKEIVELLRQ 266
Cdd:TIGR00858 160 GDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLIN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 267 RSRPYLFSNTLAPSIAEASLAVLELLAsdEGARLRRRVRENGAHFRRRMSEAGFTLVPGEHPIIPVMLGDAQVATRMADA 346
Cdd:TIGR00858 239 RARTLIFSTALPPAVAAAALAALELIQ--EEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEE 316
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 738096527 347 LLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAF 389
Cdd:TIGR00858 317 LQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
|
|
| 5aminolev_synth |
TIGR01821 |
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ... |
8-398 |
7.56e-97 |
|
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]
Pssm-ID: 273820 [Multi-domain] Cd Length: 402 Bit Score: 294.71 E-value: 7.56e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 8 HVRGTLDQIRADGFYKTEREI-----ASPQAADVKLADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFI 82
Cdd:TIGR01821 6 FFNKEIDKLHLEGRYRVFADLerqagEFPFAQWHRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 83 CGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETL--LGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQD 160
Cdd:TIGR01821 86 SGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLakIIPGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAH 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 161 LEAKLREADEAgaRFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTG 240
Cdd:TIGR01821 166 LEKLLQSVDPN--RPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 241 TLGKALgGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLELLASDEgaRLRRRVRENGAHFRRRMSEAGF 320
Cdd:TIGR01821 244 TLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLEALGI 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738096527 321 TLVPGEHPIIPVMLGDAQVATRMADALLAE-GVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGKSLGV 398
Cdd:TIGR01821 321 PVIPNPSHIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399
|
|
| PRK13392 |
PRK13392 |
5-aminolevulinate synthase; Provisional |
5-398 |
5.12e-81 |
|
5-aminolevulinate synthase; Provisional
Pssm-ID: 184023 [Multi-domain] Cd Length: 410 Bit Score: 254.39 E-value: 5.12e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 5 FLAHVRGTLDQIRADGFYKT----EREIAS-PQAADVKLADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASV 79
Cdd:PRK13392 4 YDSYFDAALAQLHQEGRYRVfadlEREAGRfPRARDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 80 RFICGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETL--LGEEDAIISDELNHASIIDGVRLSKAKRFRYKNND 157
Cdd:PRK13392 84 RNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 158 MQDLEAKLREADEAgaRFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDI 237
Cdd:PRK13392 164 LADLEEQLASVDPD--RPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 238 VTGTLGKALgGASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLELLASDEGARLRRRVREngAHFRRRMSE 317
Cdd:PRK13392 242 IQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRV--AALKAKLNA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 318 AGFTLVPGEHPIIPVMLGDAQVATRMADALLAE-GVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGKSL 396
Cdd:PRK13392 319 NGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRL 398
|
..
gi 738096527 397 GV 398
Cdd:PRK13392 399 EL 400
|
|
| PLN02483 |
PLN02483 |
serine palmitoyltransferase |
45-398 |
1.14e-68 |
|
serine palmitoyltransferase
Pssm-ID: 178101 [Multi-domain] Cd Length: 489 Bit Score: 224.64 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 45 LNFCANNYLGLAN-DRRLVAAAAAGLERDGFGMASVRFICGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLL 123
Cdd:PLN02483 103 LNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALI 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 124 GEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAKLREADEAGA-----RFK--LIATDGVFSMDGIIADLKGV 196
Cdd:PLN02483 183 GKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrPWKkiIVIVEGIYSMEGELCKLPEI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 197 CDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGV--ADrVDIVTGTLGKALgGASGGYVSARKEIVELLRQRSRPYLFS 274
Cdd:PLN02483 263 VAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdpAD-VDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAHLYA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 275 NTLAPSIAEASLAVLELL----ASDEGARLRRRVRENGAHFRRRMSEAGFTlVPGEH--PIIPVMLGDAQVATRMADALL 348
Cdd:PLN02483 341 TSMSPPAVQQVISAIKVIlgedGTNRGAQKLAQIRENSNFFRSELQKMGFE-VLGDNdsPVMPIMLYNPAKIPAFSRECL 419
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 738096527 349 AEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGKSLGV 398
Cdd:PLN02483 420 KQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
42-389 |
3.16e-63 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 206.39 E-value: 3.16e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 42 AGVLNFCANNYLGLAndrrLVAAAAAGLErdgFGMASVRFICGTQTVHKQLEAALSRFLGT--------DDTILYSSCFD 113
Cdd:pfam00155 1 TDKINLGSNEYLGDT----LPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 114 ANGGLFETLLGE-EDAIISDELNHASIIDGVRLSKAKRFRYK-------NNDMQDLEAKLREADeagarfKLIATDGVFS 185
Cdd:pfam00155 74 ANIEALIFLLANpGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP------KVVLHTSPHN 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 186 MDGIIADLKGVCDLAD---RYGALVMVDDSHAVGFIGEHGRgTPEHCGVADRVD-IVTGTLGKALG--GASGGYVSARKE 259
Cdd:pfam00155 148 PTGTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGlaGWRVGYILGNAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 260 IVELLRQRSRPYLFSNTLAPSIAEASLAvlELLASDEGARLRRRVRENGAHFRRRMSEAGFTLVPGEHPIIPVMLGDAQV 339
Cdd:pfam00155 227 VISQLRKLARPFYSSTHLQAAAAAALSD--PLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPET 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 738096527 340 ATRMADALLAE-GVYVIGFSFPVVPrgrARIRTQMsAAHTPEQIDRAVDAF 389
Cdd:pfam00155 305 AKELAQVLLEEvGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
|
|
| PLN02955 |
PLN02955 |
8-amino-7-oxononanoate synthase |
27-389 |
6.46e-55 |
|
8-amino-7-oxononanoate synthase
Pssm-ID: 178541 [Multi-domain] Cd Length: 476 Bit Score: 188.34 E-value: 6.46e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 27 EIASPQA-ADVKLADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICGTQTVHKQLEAALSRFLGTDDT 105
Cdd:PLN02955 86 EIFSGDAlAEERKGRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDC 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 106 ILYSSCFDANGGLF--------------ETLLGEEDAIISDELNHASIIDGVRLSK----AKRFRYKNNDMQDLEAKLRE 167
Cdd:PLN02955 166 LVCPTGFAANMAAMvaigsvasllaasgKPLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSS 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 168 ADeagARFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTGTLGKAlG 247
Cdd:PLN02955 246 CK---MKRKVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-A 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 248 GASGGYVSARKEIVELLRQRSRPYLFSNTLAPSIAEASLAVLeLLASDEGARlRRRVRENGAHFRRrmseagFTLVPGEH 327
Cdd:PLN02955 322 GCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAV-VVARKEKWR-RKAIWERVKEFKA------LSGVDISS 393
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738096527 328 PIIPVMLGDAQVATRMADALLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAF 389
Cdd:PLN02955 394 PIISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
|
|
| PLN02822 |
PLN02822 |
serine palmitoyltransferase |
40-396 |
1.40e-52 |
|
serine palmitoyltransferase
Pssm-ID: 178417 [Multi-domain] Cd Length: 481 Bit Score: 182.25 E-value: 1.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 40 DGAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLF 119
Cdd:PLN02822 107 NGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVI 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 120 ETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEA---KLREADEAGARF-KLIATDGVFSMDGIIADLKG 195
Cdd:PLN02822 187 PAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNtleKLTAENKRKKKLrRYIVVEAIYQNSGQIAPLDE 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 196 VCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVA-DRVDIVTGTLGKALgGASGGYVSARKEIVELLRQRSRPYLFS 274
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPiEKIDIITAAMGHAL-ATEGGFCTGSARVVDHQRLSSSGYVFS 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 275 NTLAPSIAEASLAVLELLasDEGARLRRRVRENGAHFRRRMSEAGFTLVpGEHPIIPVML-----------GDAQVATRM 343
Cdd:PLN02822 346 ASLPPYLASAAITAIDVL--EDNPSVLAKLKENIALLHKGLSDIPGLSI-GSNTLSPIVFlhlekstgsakEDLSLLEHI 422
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 738096527 344 ADALLAE-GVYVIGFSFPVVPRGR--ARIRTQMSAAHTPEQIDRAVDAFVRVGKSL 396
Cdd:PLN02822 423 ADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRVAASV 478
|
|
| PRK07179 |
PRK07179 |
quorum-sensing autoinducer synthase; |
41-384 |
6.28e-48 |
|
quorum-sensing autoinducer synthase;
Pssm-ID: 180866 [Multi-domain] Cd Length: 407 Bit Score: 167.88 E-value: 6.28e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 41 GAGVLNFCANNYLGLANDRRLVAAAAAGLERDGFG--MASVrFICGTQTVHkQLEAALSRFLGTDDTILYSSCFDANGGL 118
Cdd:PRK07179 53 GPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSlvMSAV-FLHDDSPKP-QFEKKLAAFTGFESCLLCQSGWAANVGL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 119 FETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAKLREADEAgarfkLIATDGVFSMDGIIADLKGVCD 198
Cdd:PRK07179 131 LQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG-----IIVVDSVYSTTGTIAPLADIVD 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 199 LADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVADRVDIVTGTLGKALGGaSGGYVSARKEIVELLRQRSRPYLFSNTLA 278
Cdd:PRK07179 206 IAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAEYVPFVSYPAIFSSTLL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 279 P-SIA--EASLAVLEllASDEGarlRRRVRENGAHFRRRMSEAGFTlVPGEHPIIPVMLGDAQVATRMADALLAEGVYVI 355
Cdd:PRK07179 285 PhEIAglEATLEVIE--SADDR---RARLHANARFLREGLSELGYN-IRSESQIIALETGSERNTEVLRDALEERNVFGA 358
|
330 340
....*....|....*....|....*....
gi 738096527 356 GFSFPVVPRGRARIRTQMSAAHTPEQIDR 384
Cdd:PRK07179 359 VFCAPATPKNRNLIRLSLNADLTASDLDR 387
|
|
| PRK07505 |
PRK07505 |
hypothetical protein; Provisional |
38-397 |
7.53e-43 |
|
hypothetical protein; Provisional
Pssm-ID: 181006 [Multi-domain] Cd Length: 402 Bit Score: 154.37 E-value: 7.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 38 LADGAGVLNFCANNYLGLANDRRLVAAAAAGLERDG-FGMASVRFICGTQtVHKQLEAALSRFLGTDdTILYSSCFDANG 116
Cdd:PRK07505 42 LADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGsLHLSSSRTRVRSQ-ILKDLEEALSELFGAS-VLTFTSCSAAHL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 117 GLFETLL------GEEDAIISDELNHAS--IIDGVRLSKAKRFRYKNNDMQDLEAKLREadeaGARFKLIAtDGVFSMDG 188
Cdd:PRK07505 120 GILPLLAsghltgGVPPHMVFDKNAHASlnILKGICADETEVETIDHNDLDALEDICKT----NKTVAYVA-DGVYSMGG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 189 IiADLKGVCDLADRYGALVMVDDSHAVGFIGEHGRG-TPEHCGVA--DRVdIVTGTLGKALGGASGGYVSARKEIVELLR 265
Cdd:PRK07505 195 I-APVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDYRlnERT-IIAASLGKAFGASGGVIMLGDAEQIELIL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 266 QRSRPYLFSNTLAPSIAEASLAVLELLASDEGARLRRRVRENGAHFRRRM--SEAGFTLvpgehPIIPVMLGDAQVATRM 343
Cdd:PRK07505 273 RYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIptEQSGSFL-----PIRLIYIGDEDTAIKA 347
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 738096527 344 ADALLAEGVYVIGFSFPVVPRGRARIRTQMSAAHTPEQIDRAVDAFVRVGKSLG 397
Cdd:PRK07505 348 AKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGL 401
|
|
| PLN03227 |
PLN03227 |
serine palmitoyltransferase-like protein; Provisional |
45-388 |
2.94e-42 |
|
serine palmitoyltransferase-like protein; Provisional
Pssm-ID: 178766 [Multi-domain] Cd Length: 392 Bit Score: 152.75 E-value: 2.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 45 LNFCANNYLGLANDRRLVAAAAAGLERDGFGMASVRFICGTQTVHKQLEAALSRFLGTDDTILYSSCFDANGGLFETLLG 124
Cdd:PLN03227 1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 125 EEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLE---AKLREADEA-----GARFKLIATDGVFSMDGIIADLKGV 196
Cdd:PLN03227 81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRrvlEQVRAQDVAlkrkpTDQRRFLVVEGLYKNTGTLAPLKEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 197 CDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGV--ADRVDIVTGTLGKALGGAsGGYVSARKEIVELLRQRSRPYLFS 274
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 275 NTLAPSIAEASLAVLELLASDEG--ARL---RRRVRE---NGAH-FRRRMSEAGFTLVPGEHPIIPVMLGDaQVATRMAD 345
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQllNRLhdsIANLYStltNSSHpYALKLRNRLVITSDPISPIIYLRLSD-QEATRRTD 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 738096527 346 A----------LLAEGVYVI--GFSFPVVPRGRAR--IRTQMSAAHTPEQIDRAVDA 388
Cdd:PLN03227 319 EtlildqiahhSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
89-257 |
6.48e-28 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 107.85 E-value: 6.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 89 HKQLEAALSRFLGT--DDTILYSSCFDANGGLFETLLGEEDAIISDELNHASII-DGVRLSKAK--RFRYKNNDMQDLEA 163
Cdd:cd01494 2 LEELEEKLARLLQPgnDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYwVAAELAGAKpvPVPVDDAGYGGLDV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 164 KLREADEAGARFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGfigehGRGTPEHCGVADRVDIVTGTLG 243
Cdd:cd01494 82 AILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156
|
170
....*....|....
gi 738096527 244 KALGGASGGYVSAR 257
Cdd:cd01494 157 KNLGGEGGGVVIVK 170
|
|
| PRK05937 |
PRK05937 |
8-amino-7-oxononanoate synthase; Provisional |
41-383 |
1.10e-22 |
|
8-amino-7-oxononanoate synthase; Provisional
Pssm-ID: 102071 [Multi-domain] Cd Length: 370 Bit Score: 98.31 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 41 GAGVLNFCANNYLGLANDRRLVAAAAAGLER-------DGFGMASVRFICGTQTVHKQLEAALSRFLGTDDTILYSSCFD 113
Cdd:PRK05937 3 ESLSIDFVTNDFLGFSRSDTLVHEVEKRYRLycrqfphAQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 114 ANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNNDMQDLEAKLREADEAGARFKLIATDGVFSMDGIIADL 193
Cdd:PRK05937 83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGRIFIFVCSVYSFKGTLAPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 194 KGVCDLADRYGALVMVDDSHAVGFIGEHGRGTPEHCGVaDRVDIVTGTLGKALGGASGGYVSARKEIVELLrQRSRPYLF 273
Cdd:PRK05937 163 EQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGY-ENFYAVLVTYSKALGSMGAALLSSSEVKQDLM-LNSPPLRY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 274 SNTLAPSIAEASLAVLELLASdEGARLRRRVRENGAHFRRRMSEAGFTLVPgehpiiPVMLGD--AQVATRMadaLLAEG 351
Cdd:PRK05937 241 STGLPPHLLISIQVAYDFLSQ-EGELARKQLFRLKEYFAQKFSSAAPGCVQ------PIFLPGisEQELYSK---LVETG 310
|
330 340 350
....*....|....*....|....*....|..
gi 738096527 352 VYVIGFSFPVVPrgraRIRTQMSAAHTPEQID 383
Cdd:PRK05937 311 IRVGVVCFPTGP----FLRVNLHAFNTEDEVD 338
|
|
| OAT_like |
cd00610 |
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ... |
193-392 |
9.50e-18 |
|
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.
Pssm-ID: 99735 [Multi-domain] Cd Length: 413 Bit Score: 84.16 E-value: 9.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 193 LKGVCDLADRYGALVMVDDShAVGFigehGR-GTP---EHCGVadRVDIVTgtLGKALGGAS--GGYVsARKEIVELLrq 266
Cdd:cd00610 214 LKALRELCRKHGILLIADEV-QTGF----GRtGKMfafEHFGV--EPDIVT--LGKGLGGGLplGAVL-GREEIMDAF-- 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 267 RSRPYLFSNTLA--PSIAEASLAVLELLASDegaRLRRRVRENGAHFRRRMSE-----------------AGFTLVPGEH 327
Cdd:cd00610 282 PAGPGLHGGTFGgnPLACAAALAVLEVLEEE---GLLENAAELGEYLRERLRElaekhplvgdvrgrglmIGIELVKDRA 358
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738096527 328 PIIPvmlgDAQVATRMADALLAEGVYVIGFsfpvvprGRARIRTQMSAAHTPEQIDRAVDAFVRV 392
Cdd:cd00610 359 TKPP----DKELAAKIIKAALERGLLLRPS-------GGNVIRLLPPLIITEEEIDEGLDALDEA 412
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
89-391 |
1.23e-11 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 65.44 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 89 HKQLEAALSRFLGT--------DDTILYSSCFDANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAK--RFRYKNNDM 158
Cdd:cd00609 38 LPELREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEvvPVPLDEEGG 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 159 QDLEAKLREAdEAGARFKLIA-------TDGVFSMDgiiaDLKGVCDLADRYGALVMVDDSHAvGFIGEHGRGTPEHCGV 231
Cdd:cd00609 118 FLLDLELLEA-AKTPKTKLLYlnnpnnpTGAVLSEE----ELEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 232 ADRVDIVTGTLGKALGGAS--GGYVSARKEIVELLRQRSRPYLFSNTlaPSIAEAslAVLELLASDEG--ARLRRRVREN 307
Cdd:cd00609 192 AYERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGP--STLSQA--AAAAALDDGEEhlEELRERYRRR 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 308 GAHFRRRMSEAGftlvpGEHPIIP-----VMLG-DAQVATRMADALLAE-GVYVI-GFSFPVVPRGRARIrtqmSAAHTP 379
Cdd:cd00609 268 RDALLEALKELG-----PLVVVKPsggffLWLDlPEGDDEEFLERLLLEaGVVVRpGSAFGEGGEGFVRL----SFATPE 338
|
330
....*....|..
gi 738096527 380 EQIDRAVDAFVR 391
Cdd:cd00609 339 EELEEALERLAE 350
|
|
| BioA |
COG0161 |
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]; ... |
193-392 |
5.36e-10 |
|
Adenosylmethionine-8-amino-7-oxononanoate aminotransferase [Coenzyme transport and metabolism]; Adenosylmethionine-8-amino-7-oxononanoate aminotransferase is part of the Pathway/BioSystem: Biotin biosynthesis
Pssm-ID: 439931 [Multi-domain] Cd Length: 446 Bit Score: 60.84 E-value: 5.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 193 LKGVCDLADRYGALvMVDDSHAVGFigehGR-GTP---EHCGVadRVDIVTgtLGKALggaSGGY-----VSARKEIVEL 263
Cdd:COG0161 236 LKRLREICDKYGIL-LIADEVITGF----GRtGKMfacEHAGV--TPDIIT--LAKGL---TGGYlplgaTLVSDEIYDA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 264 LRQRSRP------YLFS-NTLAPSIAeasLAVLELLASDEgarLRRRVRENGAHFRRRMSE----------------AGF 320
Cdd:COG0161 304 FLDGDEAgafmhgHTYSgHPLACAAA---LANLDILEEED---LLENVAAIGAYLRAGLAEladhplvgdvrglgliGAI 377
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 738096527 321 TLVPGEHPIIPvMLGDAQVATRMADALLAEGVYV------IGFSFPVVprgrarIrtqmsaahTPEQIDRAVDAFVRV 392
Cdd:COG0161 378 ELVADKATKEP-FDPEGRVGARVYAAALERGLILrplgdtIYLMPPLI------I--------TEEEIDELVDALREA 440
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
163-398 |
8.88e-09 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 56.64 E-value: 8.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 163 AKLREADEAGARFKLIA-------TdgvfsmdGIIADLKGVCDLADRYGALVMVDdshAVGFIGehgrGTPEHcgVAD-R 234
Cdd:COG0075 114 EEVEEALAADPDIKAVAvvhnetsT-------GVLNPLEEIGALAKEHGALLIVD---AVSSLG----GVPLD--MDEwG 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 235 VDIVTGTLGKALGGASG-GYVSARKEIVELLRQRSRP--YL-------------FSNTLAPSIAEASLAVLELLAsDEG- 297
Cdd:COG0075 178 IDVVVSGSQKCLMLPPGlAFVAVSERALEAIEARKLPsyYLdlklwlkywekgqTPYTPPVSLLYALREALDLIL-EEGl 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 298 -ARLRRRvRENGAHFRRRMSEAGFTLVPGEH---PII-PVMLGDAQVATRMADALLAEGVYVIGFSFPVVpRGRA-RIrt 371
Cdd:COG0075 257 eNRFARH-RRLAEALRAGLEALGLELFAEEEyrsPTVtAVRVPEGVDAAALRKRLKERYGIEIAGGLGPL-KGKIfRI-- 332
|
250 260 270
....*....|....*....|....*....|.
gi 738096527 372 qmsaAH----TPEQIDRAVDAFVRVGKSLGV 398
Cdd:COG0075 333 ----GHmgyvNPEDVLRTLAALEEALRELGV 359
|
|
| ArgD |
COG4992 |
Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and ... |
193-392 |
7.02e-08 |
|
Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase [Amino acid transport and metabolism]; Acetylornithine/succinyldiaminopimelate/putrescine aminotransferase is part of the Pathway/BioSystem: Arginine biosynthesis
Pssm-ID: 444016 [Multi-domain] Cd Length: 396 Bit Score: 53.89 E-value: 7.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 193 LKGVCDLADRYGALVMVDDshaV--GFigehGR-GTP---EHCGVadRVDIVTgtLGKALGgasGGY----VSARKEIVE 262
Cdd:COG4992 204 LKGLRELCDEHGALLILDE---VqtGM----GRtGKLfayEHYGV--EPDILT--LAKGLG---GGFpigaVLAREEVAD 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 263 LLrqrsRPYL----FS-NTLApsiAEASLAVLELLASDEgarLRRRVRENGAHFRRRMSEA-----GFTLVPGEHPIIPV 332
Cdd:COG4992 270 VF----TPGDhgstFGgNPLA---CAAALAVLDVLEEEG---LLENVAEKGAYLREGLEALaakypLVKEVRGRGLMIGI 339
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738096527 333 MLGDAqvATRMADALLAEGV-------YVIGFSFPVVprgrarIrtqmsaahTPEQIDRAVDAFVRV 392
Cdd:COG4992 340 ELDDP--AAEVVKALLEEGLlvnaagpNVIRLLPPLI------I--------TEEEIDEALAALEEA 390
|
|
| Orn_deC_like |
cd00615 |
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
88-317 |
1.82e-05 |
|
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.
Pssm-ID: 99739 [Multi-domain] Cd Length: 294 Bit Score: 46.09 E-value: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 88 VHKQLEAALSRFLGTDDTILY---SSCfdANGGLFETLLGEEDAIISDELNHASIIDGVRLSKAKRFRYKNN-------- 156
Cdd:cd00615 60 PIKEAQELAARAFGAKHTFFLvngTSS--SNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKPErnpyygia 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 157 ---DMQDLEAKLREADEAGArfkLIATDGVFsmDGIIADLKGVCDLADRYGALVMVDDSHaVGFIGEHGRgtPEHCGVAD 233
Cdd:cd00615 138 ggiPPETFKKALIEHPDAKA---AVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH-GAHFRFHPI--LPSSAAMA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 234 RVDIVTGTLGKALGGAS-GGYVSARKEIVELLRQRSRPYLFSNTlAPS-IAEASLAVLELLASDEGARLRRRVRENGAHF 311
Cdd:cd00615 210 GADIVVQSTHKTLPALTqGSMIHVKGDLVNPDRVNEALNLHQST-SPSyLILASLDVARAMMALEGKELVEELIELALYA 288
|
....*.
gi 738096527 312 RRRMSE 317
Cdd:cd00615 289 RQEINK 294
|
|
| ARO8 |
COG1167 |
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ... |
198-392 |
2.68e-05 |
|
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 440781 [Multi-domain] Cd Length: 471 Bit Score: 45.98 E-value: 2.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 198 DLADRYGALVMVDDSHavGFIGEHGRGTP------EHcgvaDRVdIVTGTLGKALggASG---GYVSARKEIVELLRQrs 268
Cdd:COG1167 269 ELARRHGVPIIEDDYD--SELRYDGRPPPplaaldAP----GRV-IYIGSFSKTL--APGlrlGYLVAPGRLIERLAR-- 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 269 rpYLFSNTLAPSIAEAsLAVLELLASDEGARLRRRVRE----------------NGAHFRRRMSEAGFTLVpgehpiipV 332
Cdd:COG1167 338 --LKRATDLGTSPLTQ-LALAEFLESGHYDRHLRRLRReyrarrdlllaalarhLPDGLRVTGPPGGLHLW--------L 406
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 738096527 333 MLGDAQVATRMADALLAEGVYVI-GFSFPVVPRGRARIRtqMS-AAHTPEQIDRAVDAFVRV 392
Cdd:COG1167 407 ELPEGVDAEALAAAALARGILVApGSAFSADGPPRNGLR--LGfGAPSEEELEEALRRLAEL 466
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
123-216 |
2.19e-04 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 43.00 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 123 LGEEDAIISDELNHASIID---------GVRLSKAKRFRYKNNDMQDLEAKLREadeagaRFKLIATDGVFSMDGIIADL 193
Cdd:pfam00266 85 LKPGDEIVITEMEHHANLVpwqelakrtGARVRVLPLDEDGLLDLDELEKLITP------KTKLVAITHVSNVTGTIQPV 158
|
90 100
....*....|....*....|...
gi 738096527 194 KGVCDLADRYGALVMVDDSHAVG 216
Cdd:pfam00266 159 PEIGKLAHQYGALVLVDAAQAIG 181
|
|
| CGS_like |
cd00614 |
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ... |
92-266 |
3.43e-04 |
|
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.
Pssm-ID: 99738 [Multi-domain] Cd Length: 369 Bit Score: 42.57 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 92 LEAALSRFLGTDDTILYSSCFDANGGLFETLLGEEDAIISDE---------LNHASIIDGVRLSKAkrfryknnDMQDLE 162
Cdd:cd00614 45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDHVVASDdlyggtyrlFERLLPKLGIEVTFV--------DPDDPE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 163 AkLREADEAGArfKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDDSHAVGFIG---EHGrgtpehcgvadrVDIVT 239
Cdd:cd00614 117 A-LEAAIKPET--KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQrplELG------------ADIVV 181
|
170 180 190
....*....|....*....|....*....|.
gi 738096527 240 GTLGKALGGAS---GGYVSAR-KEIVELLRQ 266
Cdd:cd00614 182 HSATKYIGGHSdviAGVVVGSgEALIQRLRF 212
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
123-216 |
4.03e-04 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 42.05 E-value: 4.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 123 LGEEDAIISDELNHASIIDGVR-LSKAKRFRYK--------NNDMQDLEAKLREadeagaRFKLIATDGVFSMDGIIADL 193
Cdd:COG0520 100 LKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP------RTKLVAVTHVSNVTGTVNPV 173
|
90 100
....*....|....*....|...
gi 738096527 194 KGVCDLADRYGALVMVDDSHAVG 216
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVP 196
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
157-322 |
2.71e-03 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 39.58 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 157 DMQDLEAKLREADeagarFKLIATDGVFSMDGIIADLKGVCDLADRYGALVMVDdshAVGFIGehgrGTPEHcgvADR-- 234
Cdd:cd06451 112 SPEEIAEALEQHD-----IKAVTLTHNETSTGVLNPLEGIGALAKKHDALLIVD---AVSSLG----GEPFR---MDEwg 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738096527 235 VDI-VTGTlGKALGGASG-GYVSARKEIVELLRQRSRP---YLFSNTLAPSIAE--------------ASLAVLELLAsD 295
Cdd:cd06451 177 VDVaYTGS-QKALGAPPGlGPIAFSERALERIKKKTKPkgfYFDLLLLLKYWGEgysyphtppvnllyALREALDLIL-E 254
|
170 180
....*....|....*....|....*....
gi 738096527 296 EG--ARLRRRvRENGAHFRRRMSEAGFTL 322
Cdd:cd06451 255 EGleNRWARH-RRLAKALREGLEALGLKL 282
|
|
| |
