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Conserved domains on  [gi|1560964891|gb|QAT14843|]
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5-aminolevulinate synthase [Brevundimonas diminuta]

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 2-404 0e+00

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).


The actual alignment was detected with superfamily member TIGR01821:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 402  Bit Score: 647.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   2 FDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGAQqDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGA 81
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDGAK-DVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  82 GGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIFR 161
Cdd:TIGR01821  80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 162 HNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGID 241
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 242 IVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAG 321
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 322 IPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNV 401
Cdd:TIGR01821 320 IPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399


                  ...
gi 1560964891 402 ARQ 404
Cdd:TIGR01821 400 PLS 402
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 2-404 0e+00

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: 647.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   2 FDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGAQqDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGA 81
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDGAK-DVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  82 GGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIFR 161
Cdd:TIGR01821  80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 162 HNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGID 241
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 242 IVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAG 321
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 322 IPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNV 401
Cdd:TIGR01821 320 IPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399


                  ...
gi 1560964891 402 ARQ 404
Cdd:TIGR01821 400 PLS 402
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 1-408 0e+00

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 578.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   1 MFDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGaQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAG 80
Cdd:PRK13392    1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPDG-PRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  81 AGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIF 160
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 161 RHNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGI 240
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 241 DIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEA 320
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNAN 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 321 GIPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCN 400
Cdd:PRK13392  320 GIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLE 399


                  ....*...
gi 1560964891 401 VARQPAAA 408
Cdd:PRK13392  400 LPRWREAA 407
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 4-398 2.43e-178

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: 501.89  E-value: 2.43e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   4 YKSAFQNSVDQVRSEGRYRVFADLKRVRGqfPRAVRrreDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGG 83
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQG--PRVTI---DG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  84 TRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHN 163
Cdd:COG0156    74 SRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRHN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 164 DLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIV 243
Cdd:COG0156   152 DMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDII 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 244 ECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:COG0156   232 MGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFD 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560964891 324 VLPSVSHIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSH 398
Cdd:COG0156   312 LGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 47-396 3.38e-172

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: 484.76  E-value: 3.38e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  47 QDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLST 126
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 127 LqkILPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEEL-LAAAPAAAPKLVAFESVYSMDGDIADIAGTIALA 205
Cdd:cd06454    81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLlREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 206 KKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPAL 285
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 286 TAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVG-NPVHCKLISDMLLeEHGIYVQPINYPT 364
Cdd:cd06454   239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRYPT 317

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1560964891 365 VPKGTERLRFTPSPDHDDAMIDKLVEAMDKLW 396
Cdd:cd06454   318 VPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
48-391 6.47e-73

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 231.81  E-value: 6.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  48 DVVVWCSNDYLGMgqhpVVIDAMQAEIEktgAGAGGTRNISGTTRSAVDLEAELASWH--------QKEAALLFTSGYVA 119
Cdd:pfam00155   2 DKINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 120 NEATLSTLqKILPGLIIFSDALNHASMIAGIRNGGGERHIFR-------HNDLEHLEELLAAAPaaapKLVAFESVYSMD 192
Cdd:pfam00155  75 NIEALIFL-LANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP----KVVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 193 GDIADIAG--TIA-LAKKYGALTYLDEVHAVGLYGETGAgVAERDGVLDGIDIVEC-TLGKAIGVMG---GYIAADAVIV 265
Cdd:pfam00155 150 GTVATLEEleKLLdLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 266 DAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVGNPVHCKLI 345
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1560964891 346 SDMLLEEHGIYVQPINYPTVPkgtERLRFTPSpDHDDAMIDKLVEA 391
Cdd:pfam00155 309 AQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEA 350
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 2-404 0e+00

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: 647.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   2 FDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGAQqDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGA 81
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDGAK-DVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  82 GGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIFR 161
Cdd:TIGR01821  80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 162 HNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGID 241
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 242 IVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAG 321
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQDLRRAHQENVKRLKNLLEALG 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 322 IPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNV 401
Cdd:TIGR01821 320 IPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRLGL 399


                  ...
gi 1560964891 402 ARQ 404
Cdd:TIGR01821 400 PLS 402
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 1-408 0e+00

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 578.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   1 MFDYKSAFQNSVDQVRSEGRYRVFADLKRVRGQFPRAVRRREDGaQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAG 80
Cdd:PRK13392    1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPDG-PRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  81 AGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKILPGLIIFSDALNHASMIAGIRNGGGERHIF 160
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 161 RHNDLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGI 240
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 241 DIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEA 320
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNAN 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 321 GIPVLPSVSHIVPVHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCN 400
Cdd:PRK13392  320 GIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRLE 399


                  ....*...
gi 1560964891 401 VARQPAAA 408
Cdd:PRK13392  400 LPRWREAA 407
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 4-398 2.43e-178

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: 501.89  E-value: 2.43e-178
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   4 YKSAFQNSVDQVRSEGRYRVFADLKRVRGqfPRAVRrreDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGG 83
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQG--PRVTI---DG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  84 TRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHN 163
Cdd:COG0156    74 SRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRHN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 164 DLEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIV 243
Cdd:COG0156   152 DMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDII 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 244 ECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:COG0156   232 MGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFD 311

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1560964891 324 VLPSVSHIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSH 398
Cdd:COG0156   312 LGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 47-396 3.38e-172

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: 484.76  E-value: 3.38e-172
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  47 QDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLST 126
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 127 LqkILPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEEL-LAAAPAAAPKLVAFESVYSMDGDIADIAGTIALA 205
Cdd:cd06454    81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLlREARRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 206 KKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPAL 285
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 286 TAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVG-NPVHCKLISDMLLeEHGIYVQPINYPT 364
Cdd:cd06454   239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRYPT 317

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1560964891 365 VPKGTERLRFTPSPDHDDAMIDKLVEAMDKLW 396
Cdd:cd06454   318 VPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 5-391 1.62e-115

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 342.14  E-value: 1.62e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   5 KSAFQNSVDQVRSEGRYRVFadlkRVRGQFPRAVRRREDgaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGT 84
Cdd:PRK05958    4 LDRLEAALAQRRAAGLYRSL----RPREGGAGRWLVVDG---RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  85 RNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLqkILPGLIIFSDALNHASMIAGIRNGGGERHIFRHND 164
Cdd:PRK05958   77 RLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHND 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 165 LEHLEELLAAAPAAApKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVE 244
Cdd:PRK05958  155 VDALEALLAKWRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIL 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 245 C-TLGKAIGVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:PRK05958  234 VgTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQ 313

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1560964891 324 VLPSVSHIVPVHVGNPVHCKLISDMLLeEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEA 391
Cdd:PRK05958  314 LMDSQSAIQPLIVGDNERALALAAALQ-EQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEA 380
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 29-393 6.00e-109

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: 324.61  E-value: 6.00e-109
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  29 RVRGQFPRAVRRREDgaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKE 108
Cdd:TIGR00858   1 RPLDRGPGPEVVRDG---RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 109 AALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAAPKLVAFESV 188
Cdd:TIGR00858  78 AALLFSSGYLANVGVISALVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 189 YSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVL-DGIDIVECTLGKAIGVMGGYIAADAVIVDA 267
Cdd:TIGR00858 156 FSMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSYGAYVAGSQALIDY 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 268 VRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVGNPVHCKLISD 347
Cdd:TIGR00858 236 LINRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAE 315

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1560964891 348 MLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMD 393
Cdd:TIGR00858 316 ELQQQ-GIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 1-391 1.12e-97

2-amino-3-ketobutyrate coenzyme A ligase; Provisional


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 297.11  E-value: 1.12e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891   1 MFDYKSAFQNSVDQVRSEGRYRVfadlKRVRGQFPRAVRRREDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAG 80
Cdd:PRK06939    2 SGAFYAQLREELEEIKAEGLYKE----ERVITSPQGADITVADG--KEVINFCANNYLGLANHPELIAAAKAALDSHGFG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  81 AGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLqkILPGLIIFSDALNHASMIAGIRNGGGERHIF 160
Cdd:PRK06939   76 MASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 161 RHNDLE--HLEELLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLD 238
Cdd:PRK06939  154 ANNDMAdlEAQLKEAKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMD 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 239 GIDIVECTLGKAI-GVMGGYIAADAVIVDAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRL 317
Cdd:PRK06939  234 RVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGM 313

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1560964891 318 SEAGIPVLPSVSHIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEA 391
Cdd:PRK06939  314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDA 386
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
48-391 6.47e-73

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 231.81  E-value: 6.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  48 DVVVWCSNDYLGMgqhpVVIDAMQAEIEktgAGAGGTRNISGTTRSAVDLEAELASWH--------QKEAALLFTSGYVA 119
Cdd:pfam00155   2 DKINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGA 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 120 NEATLSTLqKILPGLIIFSDALNHASMIAGIRNGGGERHIFR-------HNDLEHLEELLAAAPaaapKLVAFESVYSMD 192
Cdd:pfam00155  75 NIEALIFL-LANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP----KVVLHTSPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 193 GDIADIAG--TIA-LAKKYGALTYLDEVHAVGLYGETGAgVAERDGVLDGIDIVEC-TLGKAIGVMG---GYIAADAVIV 265
Cdd:pfam00155 150 GTVATLEEleKLLdLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVgSFSKAFGLAGwrvGYILGNAAVI 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 266 DAVRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPVLPSVSHIVPVHVGNPVHCKLI 345
Cdd:pfam00155 229 SQLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1560964891 346 SDMLLEEHGIYVQPINYPTVPkgtERLRFTPSpDHDDAMIDKLVEA 391
Cdd:pfam00155 309 AQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEA 350
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 44-392 1.91e-52

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 182.18  E-value: 1.91e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  44 GAQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEAT 123
Cdd:PLN02955   99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 124 ----------LSTLQKILPG--LIIFSDALNHASMIAGIR----NGGGERHIFRHNDLEHLEELLAAAPAAApKLVAFES 187
Cdd:PLN02955  179 mvaigsvaslLAASGKPLKNekVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 188 VYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDA 267
Cdd:PLN02955  258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQL 337

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 268 VRSWASGFIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKrrlSEAGIPVlpsVSHIVPVHVGNPVHCKLISD 347
Cdd:PLN02955  338 IQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDI---SSPIISLVVGNQEKALKASR 411

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1560964891 348 MLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAM 392
Cdd:PLN02955  412 YLLKS-GFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
PLN02483 PLN02483
serine palmitoyltransferase
 54-406 5.94e-50

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 175.72  E-value: 5.94e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  54 SNDYLGMGQH-----PVVIDAMQaeieKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLq 128
Cdd:PLN02483  107 SYNYLGFAAAdeyctPRVIESLK----KYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL- 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 129 kILPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAAPK---------LVAFESVYSMDGDIADIA 199
Cdd:PLN02483  182 -IGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPrthrpwkkiIVIVEGIYSMEGELCKLP 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 200 GTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVlD--GIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIF 277
Cdd:PLN02483  261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGV-DpaDVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLY 339

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 278 TTSLPPALTAGALASV----------RHLKAHPELRDahqeRAATLKRRLSEAGIPVLPSV-SHIVPVHVGNPVHCKLIS 346
Cdd:PLN02483  340 ATSMSPPAVQQVISAIkvilgedgtnRGAQKLAQIRE----NSNFFRSELQKMGFEVLGDNdSPVMPIMLYNPAKIPAFS 415

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 347 DMLLEEHGIYVQpINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAMDKLWSHCNVARQPA 406
Cdd:PLN02483  416 RECLKQNVAVVV-VGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPA 474
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
45-391 4.84e-41

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 149.77  E-value: 4.84e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  45 AQQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGagaggtrniSGTTRSAV---------DLEAELASWHQKEAALLFTS 115
Cdd:PRK07179   52 PGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEG---------DSLVMSAVflhddspkpQFEKKLAAFTGFESCLLCQS 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 116 GYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAapkLVAFESVYSMDGDI 195
Cdd:PRK07179  123 GWAANVGLLQTIAD--PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTI 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 196 ADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGVLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGF 275
Cdd:PRK07179  198 APLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPA 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 276 IFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIPvLPSVSHIVPVHVGNPVHCKLISDMlLEEHGI 355
Cdd:PRK07179  278 IFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYN-IRSESQIIALETGSERNTEVLRDA-LEERNV 355

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1560964891 356 YVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEA 391
Cdd:PRK07179  356 FGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEV 391
PLN02822 PLN02822
serine palmitoyltransferase
 47-395 9.10e-37

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 139.88  E-value: 9.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  47 QDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGyvaneatLST 126
Cdd:PLN02822  109 KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYG-------LST 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 127 LQKILP-----GLIIFSDALNHASMIAGIRNGGGERHIFRHNDLE------HLEELLAAAPAAAPKLVAFESVYSMDGDI 195
Cdd:PLN02822  182 IFSVIPafckkGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMEslrntlEKLTAENKRKKKLRRYIVVEAIYQNSGQI 261

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 196 ADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGV-LDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASG 274
Cdd:PLN02822  262 APLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSG 341

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 275 FIFTTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSeaGIPVLPSVSH----IVPVHVGNP---VHCKL--- 344
Cdd:PLN02822  342 YVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLS--DIPGLSIGSNtlspIVFLHLEKStgsAKEDLsll 419

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1560964891 345 --ISDMLLEEHGIYVQPINYPTV-----PKGterLRFTPSPDHDDAMIDKLVEAMDKL 395
Cdd:PLN02822  420 ehIADRMLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESLKRV 474
PRK07505 PRK07505
hypothetical protein; Provisional
 38-392 1.38e-31

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 123.94  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  38 VRRREDGaqQDVVVWCSNDYLGMGQHPVVIDAMQAEIEKTGagaggTRNISgTTRSAV------DLEAELASWHQKEAaL 111
Cdd:PRK07505   39 LITLADG--HTFVNFVSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELFGASV-L 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 112 LFTSGYVANEATLSTLQK-ILPG----LIIFsDALNHASMIA--GIRNGGGERHIFRHNDLEhleelLAAAPAAAPKLVA 184
Cdd:PRK07505  110 TFTSCSAAHLGILPLLASgHLTGgvppHMVF-DKNAHASLNIlkGICADETEVETIDHNDLD-----ALEDICKTNKTVA 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 185 F--ESVYSMdGDIADIAGTIALAKKYGALTYLDEVHAVGLYGETGAGVA--ERDGVLDGIDIVECTLGKAIGVMGGYIA- 259
Cdd:PRK07505  184 YvaDGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGYVrsELDYRLNERTIIAASLGKAFGASGGVIMl 262

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 260 ADAVIVDAVRSWASGFIFTTSLPPALTAGALASVR-HLKahPELrDAHQERaatLKRRL---------SEAGIPvLPsvs 329
Cdd:PRK07505  263 GDAEQIELILRYAGPLAFSQSLNVAALGAILASAEiHLS--EEL-DQLQQK---LQNNIalfdsliptEQSGSF-LP--- 332

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1560964891 330 hIVPVHVGNPVHCKLISDMLLEEhGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVEAM 392
Cdd:PRK07505  333 -IRLIYIGDEDTAIKAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 47-302 3.55e-27

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 111.03  E-value: 3.55e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  47 QDVVVWCSNDYLGMGQHPVVIDAMQAE-----IEKTGA--GAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVA 119
Cdd:PRK05937    4 SLSIDFVTNDFLGFSRSDTLVHEVEKRyrlycRQFPHAqlGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 120 NEATLSTLQKILPglIIFSDALNHASMIAGIRNGGGERHIFRHNDLEHLEELLAAAPAAAPK--LVAFESVYSMDGDIAD 197
Cdd:PRK05937   84 NLGLCAHLSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLAP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 198 IAGTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGvLDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIF 277
Cdd:PRK05937  162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRY 240

                         250       260
                  ....*....|....*....|....*
gi 1560964891 278 TTSLPPALTAGALASVRHLKAHPEL 302
Cdd:PRK05937  241 STGLPPHLLISIQVAYDFLSQEGEL 265
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 50-323 3.78e-27

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 111.53  E-value: 3.78e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  50 VVWCSNDYLGMGQHPVVIDAMQAEIEKTGAGAGGTRNISGTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQK 129
Cdd:PLN03227    1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 130 ilPGLIIFSDALNHASMIAGIRNGGGERHIFRHND----------LEHLEELLAAAPAAAPKLVAFESVYSMDGDIADIA 199
Cdd:PLN03227   81 --RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDmkdlrrvleqVRAQDVALKRKPTDQRRFLVVEGLYKNTGTLAPLK 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 200 GTIALAKKYGALTYLDEVHAVGLYGETGAGVAERDGV--LDGIDIVECTLGKAIGVMGGYIAADAVIVDAVRSWASGFIF 277
Cdd:PLN03227  159 ELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCF 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1560964891 278 TTSLPPALTAGALASVRHLKAHPELRDAHQERAATLKRRLSEAGIP 323
Cdd:PLN03227  239 SASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNSSHP 284
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 203-394 6.24e-09

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: 57.58  E-value: 6.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 203 ALAKKYGALTYLDEVhAVGLyGETGAGVA-ERDGVLdgIDIVecTLGKAIG---VMGGYIAADAviVDAVRSWASGFIFT 278
Cdd:cd00610   219 ELCRKHGILLIADEV-QTGF-GRTGKMFAfEHFGVE--PDIV--TLGKGLGgglPLGAVLGREE--IMDAFPAGPGLHGG 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 279 T--SLPPALTAGaLASVRHLKAHPELRDAhQERAATLKRRLSEAgIPVLPSVSHI-----------VPVHVGNPVHCKLI 345
Cdd:cd00610   291 TfgGNPLACAAA-LAVLEVLEEEGLLENA-AELGEYLRERLREL-AEKHPLVGDVrgrglmigielVKDRATKPPDKELA 367

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1560964891 346 SDMLLE--EHGIYVQPInyptvpkGTERLRFTPSPDHDDAMIDKLVEAMDK 394
Cdd:cd00610   368 AKIIKAalERGLLLRPS-------GGNVIRLLPPLIITEEEIDEGLDALDE 411
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 187-390 1.23e-08

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: 56.20  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 187 SVYSMDgDIADIAgtiALAKKYGALTYLDEVHavGLYGETGAGVAERDGVLDGIDIVEC-TLGKAIGVMG---GYIAA-D 261
Cdd:cd00609   147 AVLSEE-ELEELA---ELAKKHGILIISDEAY--AELVYDGEPPPALALLDAYERVIVLrSFSKTFGLPGlriGYLIApP 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 262 AVIVDAVRSWASgfiFTTSLPPALTAGALASV-----RHLKahpELRDAHQERAATLKRRLSEAGIPVLPSVS---HIVp 333
Cdd:cd00609   221 EELLERLKKLLP---YTTSGPSTLSQAAAAAAlddgeEHLE---ELRERYRRRRDALLEALKELGPLVVVKPSggfFLW- 293

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1560964891 334 VHVGNPVHCKLISDMLLEEHGIYVQPINYPTVPKGTERLRFTPSPDHDDAMIDKLVE 390
Cdd:cd00609   294 LDLPEGDDEEFLERLLLEAGVVVRPGSAFGEGGEGFVRLSFATPEEELEEALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 106-256 1.58e-07

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: 50.84  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 106 QKEAALLFTSGYVANEATLSTLQKilPGLIIFSDALNHASMIAGIRN-GGGERHIFRHNDLEHLEELLAAA----PAAAP 180
Cdd:cd01494    16 GNDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAElAGAKPVPVPVDDAGYGGLDVAILeelkAKPNV 93

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1560964891 181 KLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGlygetGAGVAERDGVLDGIDIVECTLGKAIGVMGG 256
Cdd:cd01494    94 ALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLHKNLGGEGG 164
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 91-331 6.20e-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: 41.80  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  91 TRSAvdLEAELASWHQKEAALLFTSGYVANEATLSTLQK----ILPGLIIFSDALNHASMIAgiRNGGGERHIFRHNDLE 166
Cdd:cd00614    41 TVDA--LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLYGGTYRLFERLL--PKLGIEVTFVDPDDPE 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 167 hleeLLAAAPAAAPKLVAFESVYSMDGDIADIAGTIALAKKYGALTYLDEVHAVGLYgetgagvaeRDGVLDGIDIVECT 246
Cdd:cd00614   117 ----ALEAAIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYL---------QRPLELGADIVVHS 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 247 LGKAIG----VMGGYIAA-DAVIVDAVRSWasGFIFTTSLPPALTAGALASVRHLkahpELR-DAHQERAATLKRRLSEa 320
Cdd:cd00614   184 ATKYIGghsdVIAGVVVGsGEALIQRLRFL--RLALGTILSPFDAWLLLRGLKTL----PLRmERHSENALKVAEFLEK- 256

                         250
                  ....*....|.
gi 1560964891 321 gipvLPSVSHI 331
Cdd:cd00614   257 ----HPKVERV 263
Aminotran_3 pfam00202
Aminotransferase class-III;
63-394 9.14e-04

Aminotransferase class-III;


Pssm-ID: 395148 [Multi-domain]  Cd Length: 397  Bit Score: 41.16  E-value: 9.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891  63 HPVVIDAMQAEIEKTGAGAGGTRnisgTTRSAVDLEAELASWHQKEAALLFTSGYVANEATLSTLQKIL--------PGL 134
Cdd:pfam00202  45 HPALVAAVKTQADKLSHVSFGAF----TNEPALDLAEKLLKLTPGDRVFLMNSGSEANETAVKLARKWYrekgatgrTKI 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 135 IIFSDALN---HASM-----IAGIRNGGG----ERHIFRHNDLEHLEELLAAAPAAAPKLVA--------FESVYSMDGD 194
Cdd:pfam00202 121 IAFSGAFHgrtMGALsvtgsKPKYKTGFGpflpGFPRLPYPDPEFLKEQRCLEELEALIAVKddevaaviVEPIQGEGGV 200

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 195 IAD----IAGTIALAKKYGALTYLDEVhAVGLyGETGAGVA-ERDGVLDgiDIVecTLGKAIGvmGGYIAAdAVIVDA-- 267
Cdd:pfam00202 201 NPPspgfLAGLRAICKKHGVLLIADEV-QTGF-GRTGKLFAhEHWGVPP--DIM--TFAKALT--GGFPLA-ATLGRAev 271

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1560964891 268 VRSWASGFIFTTSLP-PALTAGALASVRHLKAHPELRDAhQERAATLKRRLSEAG-----IPVLPSVSHIVPVHVGNPVH 341
Cdd:pfam00202 272 MQAFAPGSHGGTFGGnPLACAAALATLEIIEDEDLLQNA-ARLGAYLKEGLEDLQkkyevIKDVRGKGLMIGIELKEDVT 350

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1560964891 342 CKLISDMLLEEHGIYVQPINYPTVpkgterlRFTPSPDHDDAMIDKLVEAMDK 394
Cdd:pfam00202 351 VNPPILLAALEAGVLILPCGDNVI-------RLLPPLTITDEQIDEGLEIISK 396
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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