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Conserved domains on  [gi|240120117|ref|NP_038875|]
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2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial isoform a [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

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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: 699.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   24 LRCILDSELEGIRGAGTWKSERVITSRQGPSIRV-DGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  183 AKLKEAQKH--RLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  261 GKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240120117  341 ADHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 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: 699.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   24 LRCILDSELEGIRGAGTWKSERVITSRQGPSIRV-DGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  183 AKLKEAQKH--RLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  261 GKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240120117  341 ADHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 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: 655.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGiSGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 188 AQK--HRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 265
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 266 GASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPI 345
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 346 CPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 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 240120117  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:COG0156   83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 188 AQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 267
Cdd:COG0156  163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 268 SGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICP 347
Cdd:COG0156  242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240120117 348 VMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 410
Cdd:COG0156  322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 64-409 8.77e-157

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: 446.24  E-value: 8.77e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  64 ILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALL 143
Cdd:cd06454    3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 144 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEA-QKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYG 222
Cdd:cd06454   83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 223 ALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGC 302
Cdd:cd06454  163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 303 ASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGA-DHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKG 381
Cdd:cd06454  242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321

                        330       340
                 ....*....|....*....|....*...
gi 240120117 382 KARIRVQISAVHSEEDIDRCVEAFVEVG 409
Cdd:cd06454  322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
64-405 3.33e-65

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 212.17  E-value: 3.33e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   64 ILNFCANNYLGLSShPAVIQAGLQtleefgAGLSSTRFICGTQSIHKNLEAKIAHFH--------QREDAILYPSCFDAN 135
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  136 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLKEAQKhrlrLVATDGAFSMDGD 207
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  208 IAPLQDICRLAA---QYGALVFVDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPEPLVSL 281
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  282 LRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMAD 361
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 240120117  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: 699.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   24 LRCILDSELEGIRGAGTWKSERVITSRQGPSIRV-DGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 182
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  183 AKLKEAQKH--RLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  261 GKALGGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 240120117  341 ADHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 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: 655.73  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGiSGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 188 AQK--HRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 265
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 266 GASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPI 345
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 346 CPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 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 240120117  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGisGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:COG0156   83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 188 AQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 267
Cdd:COG0156  163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 268 SGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICP 347
Cdd:COG0156  242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240120117 348 VMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 410
Cdd:COG0156  322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 64-409 8.77e-157

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: 446.24  E-value: 8.77e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  64 ILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALL 143
Cdd:cd06454    3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 144 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEA-QKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYG 222
Cdd:cd06454   83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 223 ALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGC 302
Cdd:cd06454  163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 303 ASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGA-DHPICPVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKG 381
Cdd:cd06454  242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSpSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321

                        330       340
                 ....*....|....*....|....*...
gi 240120117 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 4.91e-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: 388.93  E-value: 4.91e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   45 RVITSRQGPSIRVDGISggILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQRED 124
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRR--LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  125 AILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSM 204
Cdd:TIGR00858  79 ALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  205 DGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPEPLVSLLR 283
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  284 QRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDM 363
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 240120117  364 LKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 405
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 28-409 7.90e-121

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 356.00  E-value: 7.90e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  28 LDSELEGIRGAGTWKSERVITSRQGPSIRVDGISggILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQS 107
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRR--MLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 108 IHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKE 187
Cdd:PRK05958  85 AHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 188 AQKHRlRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgG 266
Cdd:PRK05958 165 WRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVGTLGKAL-G 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 267 ASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPIC 346
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQ 322

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 240120117 347 PVMLGDARLSSQMADDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 409
Cdd:PRK05958 323 PLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 67-410 2.31e-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: 312.05  E-value: 2.31e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   67 FCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDAN-AGLFE-ALLT 144
Cdd:TIGR01821  50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  145 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGAL 224
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  225 VFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCAS 304
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  305 KALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMADDMLKK-GIFVIGFSYPVVPKGKA 383
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKhGIYVQPINYPTVPRGTE 368

                         330       340
                  ....*....|....*....|....*..
gi 240120117  384 RIRVQISAVHSEEDIDRCVEAFVEVGR 410
Cdd:TIGR01821 369 RLRITPTPAHTDKMIDDLVEALLLVWD 395
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 29-408 1.92e-91

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 281.74  E-value: 1.92e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  29 DSELEGIRGAGTWKS----ERviTSRQGPSIRVDGISGG--ILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFI 102
Cdd:PRK13392   9 DAALAQLHQEGRYRVfadlER--EAGRFPRARDHGPDGPrrVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 103 CGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEAL--LTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMAD 180
Cdd:PRK13392  87 SGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLAD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 181 LEAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 260
Cdd:PRK13392 167 LEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTL 246

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 261 GKALgGASGGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSG 340
Cdd:PRK13392 247 AKAF-GCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMP 325

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240120117 341 ADHPICPVMLGDARLSSQMADDMLKK-GIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEV 408
Cdd:PRK13392 326 SPSHIVPVMVGDPTLCKAISDRLMSEhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAI 394
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
64-405 3.33e-65

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 212.17  E-value: 3.33e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   64 ILNFCANNYLGLSShPAVIQAGLQtleefgAGLSSTRFICGTQSIHKNLEAKIAHFH--------QREDAILYPSCFDAN 135
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  136 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLKEAQKhrlrLVATDGAFSMDGD 207
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  208 IAPLQDICRLAA---QYGALVFVDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPEPLVSL 281
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  282 LRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHPICPVMLGDARLSSQMAD 361
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 240120117  362 DMLK-KGIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 405
Cdd:pfam00155 311 VLLEeVGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 65-413 1.84e-63

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 211.54  E-value: 1.84e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  65 LNFCANNYLGLSSH-----PAVIQaglqTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLF 139
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIE----SLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 140 EALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLKEA------QKHRLR---LVATDGAFSMDGDIAP 210
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEGIYSMEGELCK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 211 LQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPEPLVSLLRQRSRPY 289
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAH 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 290 LFSNSLPPAVVGCASKALDLLMESNAI------IQSMAAKTRRFRSKMEAAGFTVSGA-DHPICPVMLGDARLSSQMADD 362
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILGEDGTnrgaqkLAQIRENSNFFRSELQKMGFEVLGDnDSPVMPIMLYNPAKIPAFSRE 417

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 240120117 363 MLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHG 413
Cdd:PLN02483 418 CLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 59-405 3.30e-61

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 205.29  E-value: 3.30e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  59 GISGGILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGL 138
Cdd:PLN02955  99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 139 FEAL-------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLKEAQKHRlRLVATDG 200
Cdd:PLN02955 179 MVAIgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 201 AFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPEPLVS 280
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQ 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 281 LLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRskmEAAGFTVSGadhPICPVMLGDARLSSQMA 360
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK---ALSGVDISS---PIISLVVGNQEKALKAS 410

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 240120117 361 DDMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 405
Cdd:PLN02955 411 RYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
PLN02822 PLN02822
serine palmitoyltransferase
 46-408 1.19e-52

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 183.02  E-value: 1.19e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  46 VITSRQGPSIRVDGISggILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDA 125
Cdd:PLN02822  95 VLESAAGPHTIINGKD--VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDS 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 126 ILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKL-------KEAQKHRlRLVAT 198
Cdd:PLN02822 173 ILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLekltaenKRKKKLR-RYIVV 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 199 DGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPEP 277
Cdd:PLN02822 252 EAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHAL-ATEGGFCTGSAR 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 278 LVSLLRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAII----QSMAAKTRRFRSkmeAAGFTVSGadHPICPVML--- 350
Cdd:PLN02822 331 VVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGLSD---IPGLSIGS--NTLSPIVFlhl 405

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 240120117 351 --------GDARLSSQMADDMLKK-GIFVIGFSYPVVPKGK--ARIRVQISAVHSEEDIDRCVEAFVEV 408
Cdd:PLN02822 406 ekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRV 474
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
44-408 6.55e-49

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 170.96  E-value: 6.55e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  44 ERVITSRQGPSIRVDGISG-GILNFCANNYLGLSSHPAVIQAGLQTLEEFGAGL-SSTRFICGTQSIHKnLEAKIAHFHQ 121
Cdd:PRK07179  35 ERVNKNWNGKHLVLGKTPGpDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLvMSAVFLHDDSPKPQ-FEKKLAAFTG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 122 REDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEaklKEAQKHRLRLVATDGA 201
Cdd:PRK07179 114 FESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLR---RQIERHGPGIIVVDSV 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 202 FSMDGDIAPLQDICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGaSGGYTTGPEPLVSL 281
Cdd:PRK07179 191 YSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAEY 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 282 LRQRSRPYLFSNSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRSKMEAAGFTVSGADHpICPVMLGDARLSSQMAD 361
Cdd:PRK07179 270 VPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGSERNTEVLRD 348

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|.
gi 240120117 362 DMLKKGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR----CVEAFVEV 408
Cdd:PRK07179 349 ALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRvlevCREARDEV 399
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 65-404 1.66e-45

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 161.61  E-value: 1.66e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  65 LNFCANNYLGLSSHPAVIQAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLT 144
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 145 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLKEAQKHRLRLVATDGAFSMDGDIAPLQDI 214
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 215 CRLAAQYGALVFVDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPEPLVSLLRQRSRPYLFS 292
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 293 NSLPPAVVGCASKALDLLMESNAIIQSMAAKTRRFRS-----------KMEAAGFTVSGADHPICPVMLGDARLSS---- 357
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnsshpyalKLRNRLVITSDPISPIIYLRLSDQEATRrtde 319

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 240120117 358 -----QMADDMLKKGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 404
Cdd:PLN03227 320 tlildQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
PRK07505 PRK07505
hypothetical protein; Provisional
 64-414 1.18e-42

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 154.37  E-value: 1.18e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  64 ILNFCANNYLGLSSHPAVIQAGLQTLEEFGA-GLSSTRFICGTQsIHKNLEAKIA-HFHQRedAILYPSCFDANAGLFEA 141
Cdd:PRK07505  48 FVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSeLFGAS--VLTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 142 L----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAkLKE-AQKHRLRLVATDGAFSMdGDIAPLQDI 214
Cdd:PRK07505 125 LasghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDA-LEDiCKTNKTVAYVADGVYSM-GGIAPVKEL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 215 CRLAAQYGALVFVDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLRQRSRPYLFS 292
Cdd:PRK07505 202 LRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDAEQIELILRYAGPLAFS 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 293 NSLPPAVVGC--ASKALDLLMESNAIIQSMAAKTRRFRSKMEAagfTVSGADHPICPVMLGDARLSSQMADDMLKKGIFV 370
Cdd:PRK07505 282 QSLNVAALGAilASAEIHLSEELDQLQQKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYT 358

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 240120117 371 IGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGA 414
Cdd:PRK07505 359 SPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 65-399 2.07e-27

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 111.80  E-value: 2.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  65 LNFCANNYLGLSSHPAVI-------QAGLQTLEEFGAGLSSTRFICGTQSIHKNLEAKIAHFHQREDAILYPSCFDANAG 137
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLVhevekryRLYCRQFPHAQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 138 LFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLkeaQKHRLR-----LVATDGAFSMDGDIAPLQ 212
Cdd:PRK05937  87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLL---ESCRQRsfgriFIFVCSVYSFKGTLAPLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 213 DICRLAAQYGALVFVDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGGASGGYTTGPEPLVSLLrQRSRPYLFS 292
Cdd:PRK05937 164 QIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALGSMGAALLSSSEVKQDLM-LNSPPLRYS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 293 NSLPPAVVGCASKALDLLMESNAIiqsmaAKTRRFRSKMEAAGFTVSGADHPICPVMLGDarLSSQMADDMLKKGIFVIG 372
Cdd:PRK05937 242 TGLPPHLLISIQVAYDFLSQEGEL-----ARKQLFRLKEYFAQKFSSAAPGCVQPIFLPG--ISEQELYSKLVETGIRVG 314

                        330       340
                 ....*....|....*....|....*..
gi 240120117 373 FsypVVPKGKARIRVQISAVHSEEDID 399
Cdd:PRK05937 315 V---VCFPTGPFLRVNLHAFNTEDEVD 338
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 109-274 3.76e-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: 78.58  E-value: 3.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 109 HKNLEAKIAHFHQ--REDAILYPSCFDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 183
Cdd:cd01494    2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 184 KLKEAQKHRLR--LVATDGAFSMDGDIAPLQDICRLAAQYGALVFVDECHATGflgptGRGTDELLGVMDQVTIINSTLG 261
Cdd:cd01494   82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156

                        170
                 ....*....|...
gi 240120117 262 KALGGASGGYTTG 274
Cdd:cd01494  157 KNLGGEGGGVVIV 169
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 112-407 7.18e-13

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: 69.29  E-value: 7.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 112 LEAKIAHFHQR--------EDAILYPSCFDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 179
Cdd:cd00609   41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 180 DLEAKLKEAQKHRLRLVA-------TDGAFSMDGdiapLQDICRLAAQYGALVFVDECHatGFLGPTGRGTDELLGV-MD 251
Cdd:cd00609  120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 252 QVTIINSTLGKALGGAS--GGYTTGPEPLVSLLRQRSRPYLFSNSLPPAVVGCAsKALDLLMES-NAIIQSMAAKTRRFR 328
Cdd:cd00609  194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDDGEEHlEELRERYRRRRDALL 272

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 329 SKMEAAGFTV----SGA-----DHPIcpvmLGDARLSSQMAddmLKKGIFVIGFSYPvVPKGKARIRvqISAVHSEEDID 399
Cdd:cd00609  273 EALKELGPLVvvkpSGGfflwlDLPE----GDDEEFLERLL---LEAGVVVRPGSAF-GEGGEGFVR--LSFATPEEELE 342


                 ....*...
gi 240120117 400 RCVEAFVE 407
Cdd:cd00609  343 EALERLAE 350
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 169-408 1.10e-10

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: 62.97  E-value: 1.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 169 HKYRYRHLDMADLEAkLKEAQKHRLRLVAtdgAFSMD------GDIAP----LQDICRLAAQYGALVFVDEChATGFlGP 238
Cdd:cd00610  166 YRYRPPAELADDLEA-LEEALEEHPEEVA---AVIVEpiqgegGVIVPppgyLKALRELCRKHGILLIADEV-QTGF-GR 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 239 TGR-GTDELLGVM-DqvtIInsTLGKALGGAS--GGYTTGPEPLVSLlrqRSRPYLFSNSL---PpavVGCA--SKALDL 309
Cdd:cd00610  240 TGKmFAFEHFGVEpD---IV--TLGKGLGGGLplGAVLGREEIMDAF---PAGPGLHGGTFggnP---LACAaaLAVLEV 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 310 LMESNaIIQSMAAKTRRFRSKMEAAgftvsgADHPICPV-------MLG------------DARLSSQMADDMLKKGIFV 370
Cdd:cd00610  309 LEEEG-LLENAAELGEYLRERLREL------AEKHPLVGdvrgrglMIGielvkdratkppDKELAAKIIKAALERGLLL 381

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 240120117 371 IgfsypvvPKGKARIRVQISAVHSEEDIDRCVEAFVEV 408
Cdd:cd00610  382 R-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
141-234 6.46e-08

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 54.37  E-value: 6.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 141 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLKEaqkhRLRLVATDGAFSMDGDIAPL 211
Cdd:COG0520   98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173

                         90       100
                 ....*....|....*....|...
gi 240120117 212 QDICRLAAQYGALVFVDECHATG 234
Cdd:COG0520  174 KEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 79-400 1.01e-07

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: 53.40  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117   79 PAVIQAGLQTLEEFGAGLSSTRFICGTQSIHK--NLEAKIAHFHQREDA--ILYPSC----FDANAGLFEALLTPEDAVL 150
Cdd:pfam00266  13 QEVLDAIQEYYTDYNGNVHRGVHTLGKEATQAyeEAREKVAEFINAPSNdeIIFTSGtteaINLVALSLGRSLKPGDEIV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  151 SDELNHASIIDGI-RLCKAHKYRYR--------HLDMADLEAKLKEaqkhRLRLVATDGAFSMDGDIAPLQDICRLAAQY 221
Cdd:pfam00266  93 ITEMEHHANLVPWqELAKRTGARVRvlpldedgLLDLDELEKLITP----KTKLVAITHVSNVTGTIQPVPEIGKLAHQY 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  222 GALVFVDECHATG--------------------FLGPTGRGtdellgvmdqVTIINSTLGKALGGASGGYTTGPEPLVSL 281
Cdd:pfam00266 169 GALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIG----------VLYGRRDLLEKMPPLLGGGGMIETVSLQE 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117  282 LRQRSRPYLFSNSLPP--AVVGCAsKALDLLME--SNAIIQSMAAKTRRFRSKMEAAGFTV---SGADHPICPVMLGDAr 354
Cdd:pfam00266 239 STFADAPWKFEAGTPNiaGIIGLG-AALEYLSEigLEAIEKHEHELAQYLYERLLSLPGIRlygPERRASIISFNFKGV- 316

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 240120117  355 lssQMADDML---KKGIFVIGFSYPVVPKGKAR-----IRVQISAVHSEEDIDR 400
Cdd:pfam00266 317 ---HPHDVATlldESGIAVRSGHHCAQPLMVRLglggtVRASFYIYNTQEDVDR 367
PRK07777 PRK07777
putative succinyldiaminopimelate transaminase DapC;
209-338 1.85e-04

putative succinyldiaminopimelate transaminase DapC;


Pssm-ID: 236095 [Multi-domain]  Cd Length: 387  Bit Score: 43.49  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 209 APLQDICRLAAQYGALVFVDEC--HATgFLGPTGRGTDELLGvMDQVTIINSTLGK--ALGGASGGYTTGPEPLVSLLRq 284
Cdd:PRK07777 179 AELAAIAELAVEHDLLVITDEVyeHLV-FDGARHLPLATLPG-MRERTVTISSAAKtfNVTGWKIGWACGPAPLIAAVR- 255

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 240120117 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 1.63e-03

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: 40.53  E-value: 1.63e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 145 PEDAVLSDELNHAS-IIDGIRLCKAHKYRYRH--------LDMADLEAKLKEaqkhRLRLVATDGAFSMDGDIAPLQDIC 215
Cdd:cd06453   87 PGDEIVTSVMEHHSnIVPWQQLAERTGAKLKVvpvdddgqLDLEALEKLLTE----RTKLVAVTHVSNVLGTINPVKEIG 162

                         90       100
                 ....*....|....*....|.
gi 240120117 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 5.06e-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: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 141 ALLTPEDAVLSDELNHASIIDGIRLCKA---------HKYR--YRHLDMADLEAKLKEAQKHRLrLVATDGAFsmDGDIA 209
Cdd:cd00615   94 AVCGPGDKILIDRNCHKSVINGLVLSGAvpvylkperNPYYgiAGGIPPETFKKALIEHPDAKA-AVITNPTY--YGICY 170

                         90       100
                 ....*....|....*....|..
gi 240120117 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 8.85e-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: 37.95  E-value: 8.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 240120117 109 HKNLEAKIAHFHQREDAILYPSCFDANAGLFEALLTPED-AVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAkLKE 187
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKAGDhVVASDDLYGGTYRLFERLLPKLGIEVTFVDPDDPEA-LEA 120

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 240120117 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.
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