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Conserved domains on  [gi|66730435|ref|NP_001019448|]
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2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial [Rattus norvegicus]

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) ...
 24-415 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 TIGR01822:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 393  Bit Score: 699.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    24 LRCVLDRELEGIRGAGTWKSERVITSRQGPCIRV-EGisGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   103 CGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   183 AKLKEAQKH--RLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   261 GKALGGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730435   341 ADHPICPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHGAL 415
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 24-415 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: 699.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    24 LRCVLDRELEGIRGAGTWKSERVITSRQGPCIRV-EGisGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   103 CGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   183 AKLKEAQKH--RLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   261 GKALGGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730435   341 ADHPICPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHGAL 415
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 28-415 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 654.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   28 LDRELEGIRGAGTWKSERVITSRQGPCIRVEGiSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQS 107
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  108 IHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  188 AQK--HRLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 265
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  266 GASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPI 345
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  346 CPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHGAL 415
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 28-410 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: 540.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  28 LDRELEGIRGAGTWKSERVITSRQGPCIRVEGisGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQS 107
Cdd:COG0156   5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 108 IHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:COG0156  83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 188 AQKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 267
Cdd:COG0156 163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 268 SGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICP 347
Cdd:COG0156 242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730435 348 VMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGK 410
Cdd:COG0156 322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 64-409 2.73e-156

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: 444.70  E-value: 2.73e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  64 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEALL 143
Cdd:cd06454   3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 144 TPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKEA-QKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYG 222
Cdd:cd06454  83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 223 ALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGC 302
Cdd:cd06454 163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 303 ASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGF-TISGADHPICPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKG 381
Cdd:cd06454 242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321

                       330       340
                ....*....|....*....|....*...
gi 66730435 382 KARIRVQISAVHSEEDIDRCVEAFVEVG 409
Cdd:cd06454 322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
64-405 2.37e-65

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 212.55  E-value: 2.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    64 ILNFCANNYLGLSShPEVIQAGLQALEefgaglISTRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCFDAN 135
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   136 -TGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYR-------HLDMADLEAKLKEAQKhrlrLVATDGAFSMDGD 207
Cdd:pfam00155  76 iEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   208 VAPLQEICRLAA---QYGALVFVDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPEPLISL 281
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   282 MRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICPVMLGDARLSSQMAE 361
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 66730435   362 DMLK-KGIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 405
Cdd:pfam00155 311 VLLEeVGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 24-415 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: 699.25  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    24 LRCVLDRELEGIRGAGTWKSERVITSRQGPCIRV-EGisGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   103 CGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   183 AKLKEAQKH--RLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   261 GKALGGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 66730435   341 ADHPICPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHGAL 415
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 28-415 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 654.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   28 LDRELEGIRGAGTWKSERVITSRQGPCIRVEGiSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQS 107
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  108 IHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  188 AQK--HRLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 265
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  266 GASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPI 345
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  346 CPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHGAL 415
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 28-410 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: 540.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  28 LDRELEGIRGAGTWKSERVITSRQGPCIRVEGisGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQS 107
Cdd:COG0156   5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 108 IHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:COG0156  83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 188 AQKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 267
Cdd:COG0156 163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 268 SGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICP 347
Cdd:COG0156 242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730435 348 VMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGK 410
Cdd:COG0156 322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 64-409 2.73e-156

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: 444.70  E-value: 2.73e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  64 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEALL 143
Cdd:cd06454   3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 144 TPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKEA-QKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYG 222
Cdd:cd06454  83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 223 ALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGC 302
Cdd:cd06454 163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 303 ASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGF-TISGADHPICPVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKG 381
Cdd:cd06454 242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321

                       330       340
                ....*....|....*....|....*...
gi 66730435 382 KARIRVQISAVHSEEDIDRCVEAFVEVG 409
Cdd:cd06454 322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 45-405 5.91e-134

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: 388.55  E-value: 5.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    45 RVITSRQGPCIRVEGISggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQRED 124
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRR--LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   125 AILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSM 204
Cdd:TIGR00858  79 ALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   205 DGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPEPLISLMR 283
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   284 QRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICPVMLGDARLSSQMAEDM 363
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 66730435   364 LKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 405
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 28-409 6.62e-122

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 358.70  E-value: 6.62e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   28 LDRELEGIRGAGTWKSERVITSRQGPCIRVEGISggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQS 107
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRR--MLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  108 IHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK05958  85 AHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  188 AQKHRlRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgG 266
Cdd:PRK05958 165 WRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVGTLGKAL-G 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  267 ASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPIC 346
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQ 322

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 66730435  347 PVMLGDARLSSQMAEDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 409
Cdd:PRK05958 323 PLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 67-409 8.21e-103

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: 310.89  E-value: 8.21e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    67 FCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDAN-TGLFE-ALLT 144
Cdd:TIGR01821  50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   145 PEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYGAL 224
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   225 VFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCAS 304
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   305 KALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICPVMLGDARLSSQMAEDMLKK-GIFVIGFSYPVVPKGKA 383
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTE 368

                         330       340
                  ....*....|....*....|....*.
gi 66730435   384 RIRVQISAVHSEEDIDRCVEAFVEVG 409
Cdd:TIGR01821 369 RLRITPTPAHTDKMIDDLVEALLLVW 394
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 67-408 3.55e-91

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 281.36  E-value: 3.55e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   67 FCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEAL--LT 144
Cdd:PRK13392  51 WCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLL 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  145 PEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYGAL 224
Cdd:PRK13392 131 PGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNAL 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  225 VFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCAS 304
Cdd:PRK13392 211 TYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGAT 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  305 KALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICPVMLGDARLSSQMAEDMLKK-GIFVIGFSYPVVPKGKA 383
Cdd:PRK13392 290 AAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPRGTE 369

                        330       340
                 ....*....|....*....|....*
gi 66730435  384 RIRVQISAVHSEEDIDRCVEAFVEV 408
Cdd:PRK13392 370 RLRITPTPLHDDEDIDALVAALVAI 394
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
64-405 2.37e-65

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 212.55  E-value: 2.37e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    64 ILNFCANNYLGLSShPEVIQAGLQALEefgaglISTRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCFDAN 135
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   136 -TGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYR-------HLDMADLEAKLKEAQKhrlrLVATDGAFSMDGD 207
Cdd:pfam00155  76 iEALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   208 VAPLQEICRLAA---QYGALVFVDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPEPLISL 281
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   282 MRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHPICPVMLGDARLSSQMAE 361
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 66730435   362 DMLK-KGIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 405
Cdd:pfam00155 311 VLLEeVGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 65-413 2.23e-63

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 211.54  E-value: 2.23e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   65 LNFCANNYLGLSSH-----PEVIQAglqaLEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLF 139
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  140 EALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLKEA------QKHRLR---LVATDGAFSMDGDVAP 210
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEGIYSMEGELCK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  211 LQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPEPLISLMRQRSRPY 289
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAH 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  290 LFSNSLPPAVVGCASKALDLLM---ESNTIVQSMAA---KTRRFRSKMEAAGFTISGA-DHPICPVMLGDARLSSQMAED 362
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILgedGTNRGAQKLAQireNSNFFRSELQKMGFEVLGDnDSPVMPIMLYNPAKIPAFSRE 417

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 66730435  363 MLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHG 413
Cdd:PLN02483 418 CLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 59-405 3.12e-62

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 207.99  E-value: 3.12e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   59 GISGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGL 138
Cdd:PLN02955  99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  139 FEAL-------------LTPED-AVLSDELNHASVIDGIRLCK----AHKYRYRHLDMADLEAKLKEAQKHRlRLVATDG 200
Cdd:PLN02955 179 MVAIgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  201 AFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPEPLIS 280
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQ 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  281 LMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRskmEAAGFTISGadhPICPVMLGDARLSSQMA 360
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDISS---PIISLVVGNQEKALKAS 410

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 66730435  361 EDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 405
Cdd:PLN02955 411 RYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
PLN02822 PLN02822
serine palmitoyltransferase
 46-411 1.15e-52

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 183.02  E-value: 1.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   46 VITSRQGPCIRVEGISggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDA 125
Cdd:PLN02822  95 VLESAAGPHTIINGKD--VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDS 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  126 ILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKL-------KEAQKHRlRLVAT 198
Cdd:PLN02822 173 ILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLekltaenKRKKKLR-RYIVV 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  199 DGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALGGAsGGYTTGPEP 277
Cdd:PLN02822 252 EAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSAR 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  278 LISLMRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIV----QSMAAKTRRFRSkmeAAGFTISGadHPICPVML--- 350
Cdd:PLN02822 331 VVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGLSD---IPGLSIGS--NTLSPIVFlhl 405

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 66730435  351 --------GDARLSSQMAEDMLKK-GIFVIGFSYPVVPKGK--ARIRVQISAVHSEEDIDRCVEAFVEVGKL 411
Cdd:PLN02822 406 ekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRVAAS 477
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
44-408 2.28e-50

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 174.81  E-value: 2.28e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   44 ERVITSRQGPCIRVEGISG-GILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLI-STRFICGTQSIHKnLEAKIARFHQ 121
Cdd:PRK07179  35 ERVNKNWNGKHLVLGKTPGpDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVmSAVFLHDDSPKPQ-FEKKLAAFTG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  122 REDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEaklKEAQKHRLRLVATDGA 201
Cdd:PRK07179 114 FESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLR---RQIERHGPGIIVVDSV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  202 FSMDGDVAPLQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGaSGGYTTGPEPLISL 281
Cdd:PRK07179 191 YSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAEY 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  282 MRQRSRPYLFSNSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRSKMEAAGFTISGADHpICPVMLGDARLSSQMAE 361
Cdd:PRK07179 270 VPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGSERNTEVLRD 348

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 66730435  362 DMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR----CVEAFVEV 408
Cdd:PRK07179 349 ALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRvlevCREARDEV 399
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 65-404 6.37e-46

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 162.77  E-value: 6.37e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   65 LNFCANNYLGLSSHPEVIQAGLQALEEFGAGLISTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDANTGLFEALLT 144
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  145 PEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADL----------EAKLKEAQKHRLRLVATDGAFSMDGDVAPLQEI 214
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  215 CRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPEPLISLMRQRSRPYLFS 292
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  293 NSLPPAVVGCASKALDLLMESNTIVQSMAAKTRRFRS-----------KMEAAGFTISGADHPICPVMLGDARLSS---- 357
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnsshpyalKLRNRLVITSDPISPIIYLRLSDQEATRrtde 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 66730435  358 -----QMAEDMLKKGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 404
Cdd:PLN03227 320 tlildQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
PRK07505 PRK07505
hypothetical protein; Provisional
 64-414 5.07e-43

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 155.14  E-value: 5.07e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   64 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLIST-RFICGTQsIHKNLEAKIARFHQREdAILYPSCFDANTGLFEAL 142
Cdd:PRK07505  48 FVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSsRTRVRSQ-ILKDLEEALSELFGAS-VLTFTSCSAAHLGILPLL 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  143 ----LTPEDAVLS--DELNHAS--VIDGIrlCkAHKYRYRHLDMADLEAkLKE-AQKHRLRLVATDGAFSMdGDVAPLQE 213
Cdd:PRK07505 126 asghLTGGVPPHMvfDKNAHASlnILKGI--C-ADETEVETIDHNDLDA-LEDiCKTNKTVAYVADGVYSM-GGIAPVKE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  214 ICRLAAQYGALVFVDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPEPLISLMRQRSRPYLF 291
Cdd:PRK07505 201 LLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAF 280

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  292 SNSLPPAVVGC--ASKALDLLMESNTIVQSMAAKTRRFRSKMEAagfTISGADHPICPVMLGDARLSSQMAEDMLKKGIF 369
Cdd:PRK07505 281 SQSLNVAALGAilASAEIHLSEELDQLQQKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFY 357

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 66730435  370 VIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGKLHGA 414
Cdd:PRK07505 358 TSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 65-399 1.90e-28

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 114.88  E-value: 1.90e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   65 LNFCANNYLGLSSHPEV---IQAGLQAL------EEFGAGliSTRFICGTQSIHKNLEAKIARFHQREDAILYPSCFDAN 135
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLvheVEKRYRLYcrqfphAQLGYG--GSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  136 TGLFEALLTPEDAVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAKLkeaQKHRLR-----LVATDGAFSMDGDVAP 210
Cdd:PRK05937  85 LGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL---ESCRQRsfgriFIFVCSVYSFKGTLAP 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  211 LQEICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGGASGGYTTGPEPLISLMrQRSRPYL 290
Cdd:PRK05937 162 LEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALGSMGAALLSSSEVKQDLM-LNSPPLR 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  291 FSNSLPPAVVGCASKALDLLMESNTIvqsmaAKTRRFRSKMEAAGFTISGADHPICPVMLGDarLSSQMAEDMLKKGIFV 370
Cdd:PRK05937 240 YSTGLPPHLLISIQVAYDFLSQEGEL-----ARKQLFRLKEYFAQKFSSAAPGCVQPIFLPG--ISEQELYSKLVETGIR 312

                        330       340
                 ....*....|....*....|....*....
gi 66730435  371 IGFsypVVPKGKARIRVQISAVHSEEDID 399
Cdd:PRK05937 313 VGV---VCFPTGPFLRVNLHAFNTEDEVD 338
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 109-274 7.56e-19

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: 83.20  E-value: 7.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 109 HKNLEAKIARFHQ--REDAILYPSCFDANTGLFEALLTPEDAVLSDELNHAS---VIDGIRLCKAHKYRYRHLDMADLEA 183
Cdd:cd01494   2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 184 KLKEAQKHRLR--LVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGflgptGRGTDELLGVMDQVTIINSTLG 261
Cdd:cd01494  82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156

                       170
                ....*....|...
gi 66730435 262 KALGGASGGYTTG 274
Cdd:cd01494 157 KNLGGEGGGVVIV 169
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 112-407 6.27e-12

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: 66.21  E-value: 6.27e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 112 LEAKIARFHQR--------EDAILYPSCFDANTGLFEALLTPEDAVLSDELNHASVIDGIRLCKAhKYRYRHLD----MA 179
Cdd:cd00609  41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 180 DLEAKLKEAQKHRLRLVA-------TDGAFSMDGdvapLQEICRLAAQYGALVFVDECHatGFLGPTGRGTDELLGV-MD 251
Cdd:cd00609 120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 252 QVTIINSTLGKALGGAS--GGYTTGPEPLISLMRQRSRPYLFSNSLPPAVVGCAsKALDLLMES-NTIVQSMAAKTRRFR 328
Cdd:cd00609 194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDDGEEHlEELRERYRRRRDALL 272

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 329 SKMEAAGFTI----SGA-----DHPIcpvmLGDARLSSQMAEdmlKKGIFVIGFSYPvVPKGKARIRvqISAVHSEEDID 399
Cdd:cd00609 273 EALKELGPLVvvkpSGGfflwlDLPE----GDDEEFLERLLL---EAGVVVRPGSAF-GEGGEGFVR--LSFATPEEELE 342


                ....*...
gi 66730435 400 RCVEAFVE 407
Cdd:cd00609 343 EALERLAE 350
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 169-408 1.85e-11

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: 65.28  E-value: 1.85e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 169 HKYRYRHLDMADLEAkLKEAQKHRLRLVAtdgAFSMD------GDVAP----LQEICRLAAQYGALVFVDEChATGFlGP 238
Cdd:cd00610 166 YRYRPPAELADDLEA-LEEALEEHPEEVA---AVIVEpiqgegGVIVPppgyLKALRELCRKHGILLIADEV-QTGF-GR 239

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 239 TGR-GTDELLGVM-DqvtIInsTLGKALGGAS--GGYTTGPEplisLMRQ-RSRPYLFSNSL---PpavVGCA--SKALD 308
Cdd:cd00610 240 TGKmFAFEHFGVEpD---IV--TLGKGLGGGLplGAVLGREE----IMDAfPAGPGLHGGTFggnP---LACAaaLAVLE 307

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 309 LLMESNtIVQSMAAKTRRFRSKMEAAgftisgADHPICPV-------MLG------------DARLSSQMAEDMLKKGIF 369
Cdd:cd00610 308 VLEEEG-LLENAAELGEYLRERLREL------AEKHPLVGdvrgrglMIGielvkdratkppDKELAAKIIKAALERGLL 380

                       250       260       270
                ....*....|....*....|....*....|....*....
gi 66730435 370 VIgfsypvvPKGKARIRVQISAVHSEEDIDRCVEAFVEV 408
Cdd:cd00610 381 LR-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
141-234 9.22e-09

Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 56.69  E-value: 9.22e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 141 ALLTPEDAVLSDELNHASVIDGIR-LCKAHKYRYR--------HLDMADLEAKLKEaqkhRLRLVATDGAFSMDGDVAPL 211
Cdd:COG0520  98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173

                        90       100
                ....*....|....*....|...
gi 66730435 212 QEICRLAAQYGALVFVDECHATG 234
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 79-400 4.02e-08

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: 54.95  E-value: 4.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435    79 PEVIQAGLQALEEFGAGLISTRFICGTQSIHK--NLEAKIARFHQREDA--ILypscFDANTGlfEAL----------LT 144
Cdd:pfam00266  13 QEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAyeEAREKVAEFINAPSNdeII----FTSGTT--EAInlvalslgrsLK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   145 PEDAVLSDELNHASVIDGI-RLCKAHKYRYR--------HLDMADLEAKLKEaqkhRLRLVATDGAFSMDGDVAPLQEIC 215
Cdd:pfam00266  87 PGDEIVITEMEHHANLVPWqELAKRTGARVRvlpldedgLLDLDELEKLITP----KTKLVAITHVSNVTGTIQPVPEIG 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   216 RLAAQYGALVFVDECHATG--------------------FLGPTGRGtdellgvmdqVTIINSTLGKALGGASGGYTTGP 275
Cdd:pfam00266 163 KLAHQYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIG----------VLYGRRDLLEKMPPLLGGGGMIE 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435   276 EPLISLMRQRSRPYLFSNSLPP--AVVGCAsKALDLLMEsntivQSMAAKTRRFRSKMEAAGFTISGADHPICpvmLGDA 353
Cdd:pfam00266 233 TVSLQESTFADAPWKFEAGTPNiaGIIGLG-AALEYLSE-----IGLEAIEKHEHELAQYLYERLLSLPGIRL---YGPE 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 66730435   354 RLSSQM--------AEDML----KKGIFVIGFSYPVVPKGKAR-----IRVQISAVHSEEDIDR 400
Cdd:pfam00266 304 RRASIIsfnfkgvhPHDVAtlldESGIAVRSGHHCAQPLMVRLglggtVRASFYIYNTQEDVDR 367
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 145-236 3.52e-04

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 42.45  E-value: 3.52e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 145 PEDAVLSDELNHASVIdgI---RLCKAHKYRYRH--------LDMADLEAKLKEaqkhRLRLVATDGAFSMDGDVAPLQE 213
Cdd:cd06453  87 PGDEIVTSVMEHHSNI--VpwqQLAERTGAKLKVvpvdddgqLDLEALEKLLTE----RTKLVAVTHVSNVLGTINPVKE 160

                        90       100
                ....*....|....*....|...
gi 66730435 214 ICRLAAQYGALVFVDECHATGFL 236
Cdd:cd06453 161 IGEIAHEAGVPVLVDGAQSAGHM 183
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
209-338 9.66e-04

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 41.18  E-value: 9.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435  209 APLQEICRLAAQYGALVFVDEC--HATgFLGPTGRGTDELLGvMDQVTIINSTLGK--ALGGASGGYTTGPEPLISLMRq 284
Cdd:PRK07777 179 AELAAIAELAVEHDLLVITDEVyeHLV-FDGARHLPLATLPG-MRERTVTISSAAKtfNVTGWKIGWACGPAPLIAAVR- 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 66730435  285 RSRPYL-FSNSLP--PAVvgcaSKALDLLME-SNTIVQSMAAKTRRFRSKMEAAGFTI 338
Cdd:PRK07777 256 AAKQYLtYVGGAPfqPAV----AHALDHEDAwVAALRDSLQAKRDRLAAGLAEAGFEV 309
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 109-236 1.30e-03

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: 40.65  E-value: 1.30e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 109 HKNLEAKIARFHQREDAILYPSCFDANTGLFEALLTPED-AVLSDELNHASVIDGIRLCKAHKYRYRHLDMADLEAkLKE 187
Cdd:cd00614  42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDhVVASDDLYGGTYRLFERLLPKLGIEVTFVDPDDPEA-LEA 120

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 66730435 188 AQKHRLRLVATDGAFSMDGDVAPLQEICRLAAQYGALVFVDECHATGFL 236
Cdd:cd00614 121 AIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYL 169
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 141-231 1.46e-03

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: 40.31  E-value: 1.46e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 66730435 141 ALLTPEDAVLSDELNHASVIDGIRLCKAH-KY------RYRHL----DMADLEAKLKEAQKHRLrLVATDGAFsmDGDVA 209
Cdd:cd00615  94 AVCGPGDKILIDRNCHKSVINGLVLSGAVpVYlkpernPYYGIaggiPPETFKKALIEHPDAKA-AVITNPTY--YGICY 170

                        90       100
                ....*....|....*....|..
gi 66730435 210 PLQEICRLAAQYGALVFVDECH 231
Cdd:cd00615 171 NLRKIVEEAHHRGLPVLVDEAH 192
 
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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