NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530419684|ref|XP_005261468|]
View 

2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial isoform X7 [Homo sapiens]

Protein Classification

2am3keto_CoA family protein( domain architecture ID 10797558)

2am3keto_CoA family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 27-432 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: 715.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetw 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRY-------------- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  344 FRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFV 423
Cdd:TIGR01822 305 FRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFT 384


                  ....*....
gi 530419684  424 EVGRLHGAL 432
Cdd:TIGR01822 385 RIGRELGVI 393
 
Name Accession Description Interval E-value
2am3keto_CoA TIGR01822
glycine C-acetyltransferase; This model represents a narrowly defined clade of animal and ...
 27-432 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: 715.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetw 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRY-------------- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  344 FRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFV 423
Cdd:TIGR01822 305 FRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFT 384


                  ....*....
gi 530419684  424 EVGRLHGAL 432
Cdd:TIGR01822 385 RIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 31-432 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 646.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 191 AQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 268
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 269 GASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKM 348
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARY--------------FREGM 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 349 EAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRL 428
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKE 393


                 ....
gi 530419684 429 HGAL 432
Cdd:PRK06939 394 LGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 31-427 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: 534.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:COG0156   83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 191 AQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 270
Cdd:COG0156  163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 271 SGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEA 350
Cdd:COG0156  242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAY--------------FREGLKE 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530419684 351 AGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 427
Cdd:COG0156  308 LGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 67-426 5.68e-155

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: 442.38  E-value: 5.68e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  67 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 146
Cdd:cd06454    3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 147 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASRYG 225
Cdd:cd06454   83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 226 ALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 305
Cdd:cd06454  163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 306 ASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRG 384
Cdd:cd06454  242 ALAALEVLQGGPERRERLQENVRY--------------LRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERG 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 530419684 385 IFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 426
Cdd:cd06454  308 IYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
67-422 3.79e-56

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 189.05  E-value: 3.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   67 ILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYDAN 138
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  139 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMDGD 210
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  211 IAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLVSL 284
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  285 LRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICP 364
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDY--------------LRDGLQAAGLSVLPSQAGFFL 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530419684  365 VMLGDARLASRMADDMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 422
Cdd:pfam00155 297 LTGLDPETAKELAQVLLEEvGVYVTPGSSPGVP---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 ...
 27-432 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: 715.81  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetw 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRY-------------- 304

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  344 FRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFV 423
Cdd:TIGR01822 305 FRERMEAAGFDIKPADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFT 384


                  ....*....
gi 530419684  424 EVGRLHGAL 432
Cdd:TIGR01822 385 RIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 31-432 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 646.10  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 191 AQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 268
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 269 GASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKM 348
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARY--------------FREGM 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 349 EAAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRL 428
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKE 393


                 ....
gi 530419684 429 HGAL 432
Cdd:PRK06939 394 LGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 31-427 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: 534.63  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:COG0156    5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:COG0156   83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 191 AQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 270
Cdd:COG0156  163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 271 SGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEA 350
Cdd:COG0156  242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAY--------------FREGLKE 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530419684 351 AGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 427
Cdd:COG0156  308 LGFDLGPSESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 67-426 5.68e-155

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: 442.38  E-value: 5.68e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  67 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 146
Cdd:cd06454    3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 147 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASRYG 225
Cdd:cd06454   83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 226 ALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 305
Cdd:cd06454  163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 306 ASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRG 384
Cdd:cd06454  242 ALAALEVLQGGPERRERLQENVRY--------------LRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERG 307

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|..
gi 530419684 385 IFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 426
Cdd:cd06454  308 IYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 48-422 2.11e-129

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: 377.76  E-value: 2.11e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   48 RVITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQRED 127
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRR--LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  128 AILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSM 207
Cdd:TIGR00858  79 ALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  208 DGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPGPLVSLLR 286
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  287 QRARPYLFSNSLPPAVVGCASKALDLLmgsntivQSMAAKTQrcdsqqgRLGGGETWFRSKMEAAGFTISGASHPICPVM 366
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELI-------QEEPWRRE-------KLLALIARLRAGLEALGFTLMPSCTPIVPVI 303

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530419684  367 LGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 422
Cdd:TIGR00858 304 IGDNASALALAEELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 31-426 5.72e-118

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 349.46  E-value: 5.72e-118
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRR--MLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK05958  85 AHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 191 AQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgG 269
Cdd:PRK05958 165 WRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVGTLGKAL-G 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 270 ASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLmgsntivqsmaaktQRCDSQQGRLGGGETWFRSKME 349
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRIL--------------RREPERRERLAALIARLRAGLR 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530419684 350 AAGFTISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 426
Cdd:PRK05958 309 ALGFQLMDSQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 70-427 2.98e-100

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: 304.73  E-value: 2.98e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   70 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN-AGLFE-ALLT 147
Cdd:TIGR01821  50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  148 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 227
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  228 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 307
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  308 KALDLLMGSntivqsmaaKTQRcDSQQGRLgggeTWFRSKMEAAGF-TISGASHpICPVMLGDARLASRMADDML-KRGI 385
Cdd:TIGR01821 289 ASIRHLKES---------QDLR-RAHQENV----KRLKNLLEALGIpVIPNPSH-IVPVIIGDAALCKKVSDLLLnKHGI 353

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 530419684  386 FVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 427
Cdd:TIGR01821 354 YVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWD 395
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 53-425 1.29e-88

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 275.19  E-value: 1.29e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  53 RQGPHIRVDGVSGG--ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAIL 130
Cdd:PRK13392  32 GRFPRARDHGPDGPrrVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 131 YPSCYDANAGLFEAL--LTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMD 208
Cdd:PRK13392 112 FTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMD 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 209 GDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQR 288
Cdd:PRK13392 192 GDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSF 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 289 ARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICPVMLG 368
Cdd:PRK13392 271 APGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAA--------------LKAKLNANGIPVMPSPSHIVPVMVG 336

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530419684 369 DARLASRMADDMLKR-GIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEV 425
Cdd:PRK13392 337 DPTLCKAISDRLMSEhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAI 394
PLN02483 PLN02483
serine palmitoyltransferase
 68-430 3.47e-64

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 214.24  E-value: 3.47e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  68 LNFCANNYLGLSSH-----PEVIQAglqaLEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLF 142
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 143 EALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA------QKHRLR---LVATDGAFSMDGDIAP 213
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEGIYSMEGELCK 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 214 LQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPY 292
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAH 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 293 LFSNSLPPAVVGCASKALDLLM---GSNTIVQSMAaktqrcdsqqgRLGGGETWFRSKMEAAGFTISGAS-HPICPVML- 367
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILgedGTNRGAQKLA-----------QIRENSNFFRSELQKMGFEVLGDNdSPVMPIMLy 406

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530419684 368 GDARLA--SRmadDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHG 430
Cdd:PLN02483 407 NPAKIPafSR---ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 62-422 5.82e-58

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 197.59  E-value: 5.82e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  62 GVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGL 141
Cdd:PLN02955  99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 142 FEAL-------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLQEAQKHRlRLVATDG 203
Cdd:PLN02955 179 MVAIgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 204 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPGPLVS 283
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQ 336

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 284 LLRQRARPYLFSNSLPPAVVGCASKAldllmgsntIVQSMAAKTQRCdsqqgrlgggETWFRSK--MEAAGFTISGashP 361
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAA---------VVVARKEKWRRK----------AIWERVKefKALSGVDISS---P 394

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530419684 362 ICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 422
Cdd:PLN02955 395 IISLVVGNQEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
67-422 3.79e-56

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 189.05  E-value: 3.79e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   67 ILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYDAN 138
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  139 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMDGD 210
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  211 IAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLVSL 284
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  285 LRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRcdsqqgrlgggetwFRSKMEAAGFTISGASHPICP 364
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDY--------------LRDGLQAAGLSVLPSQAGFFL 296

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 530419684  365 VMLGDARLASRMADDMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 422
Cdd:pfam00155 297 LTGLDPETAKELAQVLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
PLN02822 PLN02822
serine palmitoyltransferase
 49-425 1.14e-53

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 186.10  E-value: 1.14e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  49 VITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDA 128
Cdd:PLN02822  95 VLESAAGPHTIINGKD--VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDS 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 129 ILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE-------AQKHRlRLVAT 201
Cdd:PLN02822 173 ILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKltaenkrKKKLR-RYIVV 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 202 DGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALGGAsGGYTTGPGP 280
Cdd:PLN02822 252 EAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSAR 330

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 281 LVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIV----QSMAAKTQRCDSQQGrlgggetwfrskmeaagftIS 356
Cdd:PLN02822 331 VVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGLSDIPG-------------------LS 391

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 357 GASHPICPVML-----------GDARLASRMADDMLKR-GIFVIGFSYPVVPKGK--ARIRVQISAVHSEEDIDRCVEAF 422
Cdd:PLN02822 392 IGSNTLSPIVFlhlekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESL 471


                 ...
gi 530419684 423 VEV 425
Cdd:PLN02822 472 KRV 474
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
47-425 3.60e-49

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 172.12  E-value: 3.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  47 ERVITSRQGPHIRVDGVSG-GILNFCANNYLGLSSHPEVIQAGLQALEEFGAGL--SSVrFICGTQSIHKnLEAKIARFH 123
Cdd:PRK07179  35 ERVNKNWNGKHLVLGKTPGpDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLvmSAV-FLHDDSPKPQ-FEKKLAAFT 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 124 QREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEaqkHRLRLVATDG 203
Cdd:PRK07179 113 GFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPGIIVVDS 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 204 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGaSGGYTTGPGPLVS 283
Cdd:PRK07179 190 VYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAE 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 284 LLRQRARPYLFSNSLPPAVVGCASKALDLLmgsntivqsmaaktQRCDSQQGRLGGGETWFRSKMEAAGFTISGASHpIC 363
Cdd:PRK07179 269 YVPFVSYPAIFSSTLLPHEIAGLEATLEVI--------------ESADDRRARLHANARFLREGLSELGYNIRSESQ-II 333

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530419684 364 PVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR----CVEAFVEV 425
Cdd:PRK07179 334 ALETGSERNTEVLRDALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRvlevCREARDEV 399
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 68-421 1.38e-43

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 156.99  E-value: 1.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  68 LNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLT 147
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 148 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEI 217
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 218 CCLASRYGALVFMDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFS 295
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 296 NSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRCDSqqgRLGGGETWFRSKMEAAGFTISGASHPICPVMLGDAR---- 371
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYS---TLTNSSHPYALKLRNRLVITSDPISPIIYLRLSDQEatrr 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530419684 372 -----LASRMADDMLKRGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 421
Cdd:PLN03227 317 tdetlILDQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
PRK07505 PRK07505
hypothetical protein; Provisional
 50-431 3.56e-43

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 156.29  E-value: 3.56e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  50 ITSRQGPHIRVDGVSGG-ILNFCANNYLGLSSHPEVIQAGLQALEEFGA-GLSSVRFICGTQsIHKNLEAKIARFHQREd 127
Cdd:PRK07505  30 LTVGEREGILITLADGHtFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSELFGAS- 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 128 AILYPSCYDANAGLFEAL----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAKLQEAQKHRLRLVAT 201
Cdd:PRK07505 108 VLTFTSCSAAHLGILPLLasghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDALEDICKTNKTVAYVA 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 202 DGAFSMdGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPG 279
Cdd:PRK07505 187 DGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDA 265

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 280 PLVSLLRQRARPYLFSNSLPPAVVGCASKALDLlmgsntivqsmaAKTQRCDSQQGRLGGGETWFRSKMEAagfTISGAS 359
Cdd:PRK07505 266 EQIELILRYAGPLAFSQSLNVAALGAILASAEI------------HLSEELDQLQQKLQNNIALFDSLIPT---EQSGSF 330

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530419684 360 HPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGA 431
Cdd:PRK07505 331 LPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 68-313 1.78e-23

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 101.01  E-value: 1.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  68 LNFCANNYLGLSSHPEV---IQAGLQAL------EEFGAGLSsvRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN 138
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLvheVEKRYRLYcrqfphAQLGYGGS--RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 139 AGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLR--LVATDGAFSMDGDIAPLQE 216
Cdd:PRK05937  85 LGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLAPLEQ 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 217 ICCLASRYGALVFMDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGgasggyTTGPGPLVSL-----LRQRARP 291
Cdd:PRK05937 165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALG------SMGAALLSSSevkqdLMLNSPP 237

                        250       260
                 ....*....|....*....|..
gi 530419684 292 YLFSNSLPPAVVGCASKALDLL 313
Cdd:PRK05937 238 LRYSTGLPPHLLISIQVAYDFL 259
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 112-277 2.26e-16

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: 76.27  E-value: 2.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 112 HKNLEAKIARFHQ--REDAILYPSCYDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 186
Cdd:cd01494    2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 187 KLQEAQKHRLR--LVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGflgptGRGTDELLGVMDQVTIINSTLG 264
Cdd:cd01494   82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156

                        170
                 ....*....|...
gi 530419684 265 KALGGASGGYTTG 277
Cdd:cd01494  157 KNLGGEGGGVVIV 169
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 115-424 3.41e-08

Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 55.04  E-value: 3.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 115 LEAKIARFHQR--------EDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 182
Cdd:cd00609   41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 183 DLEAKLQEAQKHRLRLVA-------TDGAFSMDGdiapLQEICCLASRYGALVFMDECHatGFLGPTGRGTDELLGV-MD 254
Cdd:cd00609  120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 255 QVTIINSTLGKALGGAS--GGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAsKALDLlmGSNTIVQSMAAKTQRCDs 332
Cdd:cd00609  194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDD--GEEHLEELRERYRRRRD- 269

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 333 qqgrlgggetWFRSKMEAAGFTI----SGASHpicpVMLG-----DARLASRMAddmLKRGIFVIGFSYPvVPKGKARIR 403
Cdd:cd00609  270 ----------ALLEALKELGPLVvvkpSGGFF----LWLDlpegdDEEFLERLL---LEAGVVVRPGSAF-GEGGEGFVR 331

                        330       340
                 ....*....|....*....|.
gi 530419684 404 vqISAVHSEEDIDRCVEAFVE 424
Cdd:cd00609  332 --LSFATPEEELEEALERLAE 350
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
144-237 8.68e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 47.83  E-value: 8.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684 144 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLQEaqkhRLRLVATDGAFSMDGDIAPL 214
Cdd:COG0520   98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173

                         90       100
                 ....*....|....*....|...
gi 530419684 215 QEICCLASRYGALVFMDECHATG 237
Cdd:COG0520  174 KEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 82-330 2.63e-04

Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 43.00  E-value: 2.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684   82 PEVIQAGLQALEEF-GAGLSSV-RFicGTQSIHK--NLEAKIARFHQREDA--ILYPS-CYDANA----GLFEALLTPED 150
Cdd:pfam00266  13 QEVLDAIQEYYTDYnGNVHRGVhTL--GKEATQAyeEAREKVAEFINAPSNdeIIFTSgTTEAINlvalSLGRSLKPGDE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  151 AVLSDELNHASIIDGIRLCKAHKYRYR--------HLDMADLEAKLqeaqKHRLRLVATDGAFSMDGDIAPLQEICCLAS 222
Cdd:pfam00266  91 IVITEMEHHANLVPWQELAKRTGARVRvlpldedgLLDLDELEKLI----TPKTKLVAITHVSNVTGTIQPVPEIGKLAH 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530419684  223 RYGALVFMDECHATG--------------------FLGPTGRG----TDELLGVMDqvtiinstlgKALGGasGGYTTGP 278
Cdd:pfam00266 167 QYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIGvlygRRDLLEKMP----------PLLGG--GGMIETV 234

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530419684  279 GplVSLLRQRARPYLFSNSLPP--AVVGCAsKALDLLM--GSNTIVQSMAAKTQRC 330
Cdd:pfam00266 235 S--LQESTFADAPWKFEAGTPNiaGIIGLG-AALEYLSeiGLEAIEKHEHELAQYL 287
 
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