NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|240120119|ref|NP_001155184|]
View 

2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial isoform b [Mus musculus]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 24-371 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: 611.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   24 LRCILDSELEGIRGAGTWKSERVITSRQGPSIRV-DGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  183 AKLKEAQKH--RLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  261 GKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350
                  ....*....|....*....|....*....|.
gi 240120119  341 ADHPICPVMLGDARLSSQMADDMLKKGKWLT 371
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVT 349
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 24-371 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: 611.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   24 LRCILDSELEGIRGAGTWKSERVITSRQGPSIRV-DGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  183 AKLKEAQKH--RLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  261 GKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350
                  ....*....|....*....|....*....|.
gi 240120119  341 ADHPICPVMLGDARLSSQMADDMLKKGKWLT 371
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVT 349
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 28-367 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 569.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGiSGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 188 AQK--HRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 265
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 266 GASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPI 345
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327

                        330       340
                 ....*....|....*....|..
gi 240120119 346 CPVMLGDARLSSQMADDMLKKG 367
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 28-367 3.79e-166

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: 469.92  E-value: 3.79e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:COG0156   83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 188 AQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 267
Cdd:COG0156  163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 268 SGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICP 347
Cdd:COG0156  242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321

                        330       340
                 ....*....|....*....|
gi 240120119 348 VMLGDARLSSQMADDMLKKG 367
Cdd:COG0156  322 VIVGDAERALALADALLERG 341
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 64-371 5.25e-135

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: 389.61  E-value: 5.25e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  64 ILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALL 143
Cdd:cd06454    3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 144 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEA-QKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYG 222
Cdd:cd06454   83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 223 ALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGC 302
Cdd:cd06454  163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 303 ASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGA-DHPICPVMLGDARLSSQMADDMLKKGKWLT 371
Cdd:cd06454  242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQ 311
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
64-368 1.65e-58

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 193.68  E-value: 1.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   64 ILNFCANNYLGLSShPAVIQAGLQtleefgAGLSSTRFICGTQSIHKNLEAKIAHFH--------QREDAILYPSCFDAN 135
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  136 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLKEAQKhrlrLVATDGAFSMDGD 207
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  208 IAPLQDICRLAA---QYGALVFVDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPEPLVSL 281
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  282 LRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMAD 361
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310


                  ....*..
gi 240120119  362 DMLKKGK 368
Cdd:pfam00155 311 VLLEEVG 317
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 24-371 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: 611.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   24 LRCILDSELEGIRGAGTWKSERVITSRQGPSIRV-DGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  183 AKLKEAQKH--RLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  261 GKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350
                  ....*....|....*....|....*....|.
gi 240120119  341 ADHPICPVMLGDARLSSQMADDMLKKGKWLT 371
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVT 349
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 28-367 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 569.83  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGiSGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 188 AQK--HRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 265
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 266 GASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPI 345
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327

                        330       340
                 ....*....|....*....|..
gi 240120119 346 CPVMLGDARLSSQMADDMLKKG 367
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 28-367 3.79e-166

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: 469.92  E-value: 3.79e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:COG0156   83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 188 AQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 267
Cdd:COG0156  163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 268 SGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICP 347
Cdd:COG0156  242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321

                        330       340
                 ....*....|....*....|
gi 240120119 348 VMLGDARLSSQMADDMLKKG 367
Cdd:COG0156  322 VIVGDAERALALADALLERG 341
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 64-371 5.25e-135

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: 389.61  E-value: 5.25e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  64 ILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALL 143
Cdd:cd06454    3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 144 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEA-QKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYG 222
Cdd:cd06454   83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 223 ALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGC 302
Cdd:cd06454  163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 303 ASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGA-DHPICPVMLGDARLSSQMADDMLKKGKWLT 371
Cdd:cd06454  242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQ 311
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 45-369 1.34e-115

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: 340.40  E-value: 1.34e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   45 RVITSRQGPSIRVDGISggILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQRED 124
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRR--LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  125 AILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSM 204
Cdd:TIGR00858  79 ALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  205 DGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPEPLVSLLR 283
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  284 QRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDM 363
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317


                  ....*.
gi 240120119  364 LKKGKW 369
Cdd:TIGR00858 318 QQQGIF 323
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 28-371 1.03e-103

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 310.94  E-value: 1.03e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGISggILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRR--MLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK05958  85 AHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 188 AQKHRlRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgG 266
Cdd:PRK05958 165 WRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVGTLGKAL-G 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 267 ASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPIC 346
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQ 322

                        330       340
                 ....*....|....*....|....*
gi 240120119 347 PVMLGDARLSSQMADDMLKKGKWLT 371
Cdd:PRK05958 323 PLIVGDNERALALAAALQEQGFWVG 347
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 67-366 2.09e-91

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: 280.08  E-value: 2.09e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   67 FCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDAN-AGLFE-ALLT 144
Cdd:TIGR01821  50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  145 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGAL 224
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  225 VFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCAS 304
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 240120119  305 KALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDMLKK 366
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNK 350
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 29-364 1.93e-77

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 244.76  E-value: 1.93e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  29 DSELEGIRGAGTWKS----ERviTSRQGPSIRVDGISGG--ILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:PRK13392   9 DAALAQLHQEGRYRVfadlER--EAGRFPRARDHGPDGPrrVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEAL--LTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMAD 180
Cdd:PRK13392  87 SGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLAD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 181 LEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:PRK13392 167 LEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 261 GKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:PRK13392 247 AKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMP 325

                        330       340
                 ....*....|....*....|....
gi 240120119 341 ADHPICPVMLGDARLSSQMADDML 364
Cdd:PRK13392 326 SPSHIVPVMVGDPTLCKAISDRLM 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
64-368 1.65e-58

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 193.68  E-value: 1.65e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   64 ILNFCANNYLGLSShPAVIQAGLQtleefgAGLSSTRFICGTQSIHKNLEAKIAHFH--------QREDAILYPSCFDAN 135
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  136 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLKEAQKhrlrLVATDGAFSMDGD 207
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  208 IAPLQDICRLAA---QYGALVFVDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPEPLVSL 281
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  282 LRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMAD 361
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310


                  ....*..
gi 240120119  362 DMLKKGK 368
Cdd:pfam00155 311 VLLEEVG 317
PLN02483 PLN02483
serine palmitoyltransferase
 65-350 5.14e-52

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 180.34  E-value: 5.14e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  65 LNFCANNYLGLSSH-----PAVIQaglqTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLF 139
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIE----SLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 140 EALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEA------QKHRLR---LVATDGAFSMDGDIAP 210
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEGIYSMEGELCK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 211 LQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPY 289
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAH 337

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 240120119 290 LFSNSLPPAVVGCASKALDLLMESNAI------IQSMAAKTRRFRSKMEAAGFTVSGA-DHPICPVML 350
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILGEDGTnrgaqkLAQIRENSNFFRSELQKMGFEVLGDnDSPVMPIML 405
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 59-367 1.11e-50

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 176.40  E-value: 1.11e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  59 GISGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGL 138
Cdd:PLN02955  99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 139 FEAL-------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLKEAQKHRlRLVATDG 200
Cdd:PLN02955 179 MVAIgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 201 AFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPEPLVS 280
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQ 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 281 LLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRskmEAAGFTVSGadhPICPVMLGDARLSSQMA 360
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDISS---PIISLVVGNQEKALKAS 410


                 ....*..
gi 240120119 361 DDMLKKG 367
Cdd:PLN02955 411 RYLLKSG 417
PLN02822 PLN02822
serine palmitoyltransferase
 46-376 2.76e-48

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 170.31  E-value: 2.76e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  46 VITSRQGPSIRVDGISggILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDA 125
Cdd:PLN02822  95 VLESAAGPHTIINGKD--VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDS 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 126 ILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKL-------KEAQKHRlRLVAT 198
Cdd:PLN02822 173 ILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLekltaenKRKKKLR-RYIVV 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 199 DGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALGGAsGGYTTGPEP 277
Cdd:PLN02822 252 EAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSAR 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 278 LVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAII----QSMAAKTRRFRSkmeAAGFTVSGadHPICPVML--- 350
Cdd:PLN02822 331 VVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGLSD---IPGLSIGS--NTLSPIVFlhl 405

                        330       340       350
                 ....*....|....*....|....*....|....
gi 240120119 351 --------GDARLSSQMADDMLKKGKWLTSRTFR 376
Cdd:PLN02822 406 ekstgsakEDLSLLEHIADRMLKEDSVLVVVSKR 439
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 65-364 5.91e-42

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 151.21  E-value: 5.91e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  65 LNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLT 144
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 145 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDI 214
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 215 CRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPEPLVSLLRQRSRPYLFS 292
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 293 NSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRS-----------KMEAAGFTVSGADHPICPVMLGDARLSSQMAD 361
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnsshpyalKLRNRLVITSDPISPIIYLRLSDQEATRRTDE 319


                 ...
gi 240120119 362 DML 364
Cdd:PLN03227 320 TLI 322
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
44-340 3.75e-40

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 146.69  E-value: 3.75e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  44 ERVITSRQGPSIRVDGISG-GILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGL-SSTRFICGTQSIHKnLEAKIAHFHQ 121
Cdd:PRK07179  35 ERVNKNWNGKHLVLGKTPGpDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLvMSAVFLHDDSPKPQ-FEKKLAAFTG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 122 REDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEaklKEAQKHRLRLVATDGA 201
Cdd:PRK07179 114 FESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLR---RQIERHGPGIIVVDSV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 202 FSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGaSGGYTTGPEPLVSL 281
Cdd:PRK07179 191 YSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAEY 269

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 240120119 282 LRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:PRK07179 270 VPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRS 328
PRK07505 PRK07505
hypothetical protein; Provisional
 64-381 2.05e-28

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 114.69  E-value: 2.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  64 ILNFCANNYLGLSSHPAVIQAGLQTLEEFGA-GLSSTRFICGTQsIHKNLEAKIA-HFHQRedAILYPSCFDANAGLFEA 141
Cdd:PRK07505  48 FVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSeLFGAS--VLTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 142 L----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAkLKE-AQKHRLRLVATDGAFSMdGDIAPLQDI 214
Cdd:PRK07505 125 LasghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDA-LEDiCKTNKTVAYVADGVYSM-GGIAPVKEL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 215 CRLAAQYGALVFVDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLRQRSRPYLFS 292
Cdd:PRK07505 202 LRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAFS 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 293 NSLPPAVVGC--ASKALDLLMESNAIIQSMAAKTRRFRSKMEAagfTVSGADHPICPVMLGDARLSSQMADDMLKKGKWL 370
Cdd:PRK07505 282 QSLNVAALGAilASAEIHLSEELDQLQQKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYT 358

                        330
                 ....*....|.
gi 240120119 371 TSRTFRWTAQG 381
Cdd:PRK07505 359 SPVFFPVVAKG 369
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 65-330 3.17e-26

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 107.94  E-value: 3.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  65 LNFCANNYLGLSSHPAVI-------QAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAG 137
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLVhevekryRLYCRQFPHAQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 138 LFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLkeaQKHRLR-----LVATDGAFSMDGDIAPLQ 212
Cdd:PRK05937  87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL---ESCRQRsfgriFIFVCSVYSFKGTLAPLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 213 DICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLrQRSRPYLFS 292
Cdd:PRK05937 164 QIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALGSMGAALLSSSEVKQDLM-LNSPPLRYS 241

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 240120119 293 NSLPPAVVGCASKALDLLMESNAIiqsmaAKTRRFRSK 330
Cdd:PRK05937 242 TGLPPHLLISIQVAYDFLSQEGEL-----ARKQLFRLK 274
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 109-274 1.17e-17

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: 79.73  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 109 HKNLEAKIAHFHQ--REDAILYPSCFDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 183
Cdd:cd01494    2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 184 KLKEAQKHRLR--LVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGflgptGRGTDELLGVMDQVTIINSTLG 261
Cdd:cd01494   82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156

                        170
                 ....*....|...
gi 240120119 262 KALGGASGGYTTG 274
Cdd:cd01494  157 KNLGGEGGGVVIV 169
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 112-338 2.41e-10

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: 61.20  E-value: 2.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 112 LEAKIAHFHQR--------EDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 179
Cdd:cd00609   41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 180 DLEAKLKEAQKHRLRLVA-------TDGAFSMDGdiapLQDICRLAAQYGALVFVDECHatGFLGPTGRGTDELLGV-MD 251
Cdd:cd00609  120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 252 QVTIINSTLGKALGGAS--GGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCAsKALDLLMES-NAIIQSMAAKTRRFR 328
Cdd:cd00609  194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDDGEEHlEELRERYRRRRDALL 272

                        250
                 ....*....|
gi 240120119 329 SKMEAAGFTV 338
Cdd:cd00609  273 EALKELGPLV 282
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
141-234 3.89e-08

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 54.76  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 141 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLKEaqkhRLRLVATDGAFSMDGDIAPL 211
Cdd:COG0520   98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173

                         90       100
                 ....*....|....*....|...
gi 240120119 212 QDICRLAAQYGALVFVDECHATG 234
Cdd:COG0520  174 KEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 79-334 6.31e-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: 53.79  E-value: 6.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119   79 PAVIQAGLQTLEEFGAGLSSTRFICGTQSIHK--NLEAKIAHFHQREDA--ILYPSC----FDANAGLFEALLTPEDAVL 150
Cdd:pfam00266  13 QEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAyeEAREKVAEFINAPSNdeIIFTSGtteaINLVALSLGRSLKPGDEIV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  151 SDELNHASIIDGI-RLCKAHKYRYR--------HLDMADLEAKLKEaqkhRLRLVATDGAFSMDGDIAPLQDICRLAAQY 221
Cdd:pfam00266  93 ITEMEHHANLVPWqELAKRTGARVRvlpldedgLLDLDELEKLITP----KTKLVAITHVSNVTGTIQPVPEIGKLAHQY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119  222 GALVFVDECHATG--------------------FLGPTGRGtdellgvmdqVTIINSTLGKALGGASGGYTTGPEPLVSL 281
Cdd:pfam00266 169 GALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIG----------VLYGRRDLLEKMPPLLGGGGMIETVSLQE 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 240120119  282 LRQRSRPYLFSNSLPP--AVVGCAsKALDLLMEsnaiiQSMAAKTRRFRSKMEAA 334
Cdd:pfam00266 239 STFADAPWKFEAGTPNiaGIIGLG-AALEYLSE-----IGLEAIEKHEHELAQYL 287
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 169-334 9.86e-05

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: 44.10  E-value: 9.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 169 HKYRYRHLDMADLEAkLKEAQKHRLRLVAtdgAFSMD------GDIAP----LQDICRLAAQYGALVFVDEChATGFlGP 238
Cdd:cd00610  166 YRYRPPAELADDLEA-LEEALEEHPEEVA---AVIVEpiqgegGVIVPppgyLKALRELCRKHGILLIADEV-QTGF-GR 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 239 TGR-GTDELLGVM-DqvtIInsTLGKALGGAS--GGYTTGPEPLVSLlrqRSRPYLFSNSL---PpavVGCA--SKALDL 309
Cdd:cd00610  240 TGKmFAFEHFGVEpD---IV--TLGKGLGGGLplGAVLGREEIMDAF---PAGPGLHGGTFggnP---LACAaaLAVLEV 308

                        170       180
                 ....*....|....*....|....*
gi 240120119 310 LMESNaIIQSMAAKTRRFRSKMEAA 334
Cdd:cd00610  309 LEEEG-LLENAAELGEYLRERLREL 332
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
209-338 1.40e-04

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 43.49  E-value: 1.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 209 APLQDICRLAAQYGALVFVDEC--HATgFLGPTGRGTDELLGvMDQVTIINSTLGK--ALGGASGGYTTGPEPLVSLLRq 284
Cdd:PRK07777 179 AELAAIAELAVEHDLLVITDEVyeHLV-FDGARHLPLATLPG-MRERTVTISSAAKtfNVTGWKIGWACGPAPLIAAVR- 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 240120119 285 RSRPYL-FSNSLP--PAVvgcaSKALDLLME-SNAIIQSMAAKTRRFRSKMEAAGFTV 338
Cdd:PRK07777 256 AAKQYLtYVGGAPfqPAV----AHALDHEDAwVAALRDSLQAKRDRLAAGLAEAGFEV 309
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 145-236 9.94e-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: 40.91  E-value: 9.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 145 PEDAVLSDELNHAS-IIDGIRLCKAHKYRYRH--------LDMADLEAKLKEaqkhRLRLVATDGAFSMDGDIAPLQDIC 215
Cdd:cd06453   87 PGDEIVTSVMEHHSnIVPWQQLAERTGAKLKVvpvdddgqLDLEALEKLLTE----RTKLVAVTHVSNVLGTINPVKEIG 162

                         90       100
                 ....*....|....*....|.
gi 240120119 216 RLAAQYGALVFVDECHATGFL 236
Cdd:cd06453  163 EIAHEAGVPVLVDGAQSAGHM 183
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 141-231 3.55e-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: 38.77  E-value: 3.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 141 ALLTPEDAVLSDELNHASIIDGIRLCKAH-KY------RYRHL----DMADLEAKLKEAQKHRLrLVATDGAFsmDGDIA 209
Cdd:cd00615   94 AVCGPGDKILIDRNCHKSVINGLVLSGAVpVYlkpernPYYGIaggiPPETFKKALIEHPDAKA-AVITNPTY--YGICY 170

                         90       100
                 ....*....|....*....|..
gi 240120119 210 PLQDICRLAAQYGALVFVDECH 231
Cdd:cd00615  171 NLRKIVEEAHHRGLPVLVDEAH 192
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 109-236 6.15e-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: 38.34  E-value: 6.15e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120119 109 HKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPED-AVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAkLKE 187
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDhVVASDDLYGGTYRLFERLLPKLGIEVTFVDPDDPEA-LEA 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 240120119 188 AQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFL 236
Cdd:cd00614  121 AIKPETKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYL 169
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH