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Conserved domains on  [gi|7657118|ref|NP_055106|]
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2-amino-3-ketobutyrate coenzyme A ligase, mitochondrial isoform 2 precursor [Homo sapiens]

Protein Classification

2am3keto_CoA family protein( domain architecture ID 10797558)

2am3keto_CoA family protein

Graphical summary

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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 ...
27-418 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: 724.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISG 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7657118    344 ASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
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 ...
27-418 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: 724.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISG 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7657118    344 ASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
31-418 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 654.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   191 AQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 268
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   269 GASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPI 348
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   349 CPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
31-413 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: 542.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:COG0156   5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:COG0156  83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  191 AQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 270
Cdd:COG0156 163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  271 SGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICP 350
Cdd:COG0156 242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657118  351 VMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 413
Cdd:COG0156 322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
67-412 2.63e-158

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: 450.09  E-value: 2.63e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   67 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 146
Cdd:cd06454   3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  147 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASRYG 225
Cdd:cd06454  83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  226 ALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 305
Cdd:cd06454 163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  306 ASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKG 384
Cdd:cd06454 242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321
                       330       340
                ....*....|....*....|....*...
gi 7657118  385 KARIRVQISAVHSEEDIDRCVEAFVEVG 412
Cdd:cd06454 322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
67-408 1.67e-59

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 197.53  E-value: 1.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     67 ILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYDAN 138
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    139 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMDGD 210
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    211 IAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLVSL 284
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    285 LRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMAD 364
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 7657118    365 DMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 408
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 ...
27-418 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: 724.67  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     27 LRGILEGELEGIRGAGTWKSERVITSRQGPHIRV-DGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFI 105
Cdd:TIGR01822   1 FYAQLAAELESIREAGLFKSERIITSPQGADIRVaDG--REVLNFCANNYLGLSSHPDLIQAAKDALDEHGFGMSSVRFI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    106 CGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLE 185
Cdd:TIGR01822  79 CGTQDIHKELEAKIAAFLGTEDTILYASCFDANGGLFETLLGAEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLE 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    186 AKLQEAQKH--RLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTL 263
Cdd:TIGR01822 159 AQLKEARAAgaRHRLIATDGVFSMDGVIAPLDEICDLADKYDALVMVDECHATGFLGPTGRGSHELCGVMGRVDIITGTL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    264 GKALGGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISG 343
Cdd:TIGR01822 239 GKALGGASGGFTTARKEVVELLRQRSRPYLFSNSLPPAVVGASIKVLEMLEASNELRDRLWANTRYFRERMEAAGFDIKP 318
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 7657118    344 ASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:TIGR01822 319 ADHPIIPVMLYDAVLAQRFARRLLEEGIYVTGFFYPVVPKGQARIRVQISAAHTEEQLDRAVEAFTRIGRELGVI 393
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
31-418 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 654.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK06939   9 LREELEEIKAEGLYKEERVITSPQGADITVAD-GKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK06939  88 LHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKE 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   191 AQK--HRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALG 268
Cdd:PRK06939 168 AKEagARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALG 247
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   269 GASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPI 348
Cdd:PRK06939 248 GASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFTLGPGEHPI 327
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   349 CPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGAL 418
Cdd:PRK06939 328 IPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
31-413 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: 542.72  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGvsGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:COG0156   5 LEAELAALKAAGLYRYLRVLESPQGPRVTIDG--REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGTTP 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:COG0156  83 LHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKK 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  191 AQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGA 270
Cdd:COG0156 163 ARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLSKAL-GS 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  271 SGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICP 350
Cdd:COG0156 242 SGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSESPIVP 321
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657118  351 VMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGR 413
Cdd:COG0156 322 VIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGK 384
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
67-412 2.63e-158

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: 450.09  E-value: 2.63e-158
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   67 ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALL 146
Cdd:cd06454   3 VLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLSTLA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  147 TPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA-QKHRLRLVATDGAFSMDGDIAPLQEICCLASRYG 225
Cdd:cd06454  83 GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLAKKYG 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  226 ALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGC 305
Cdd:cd06454 163 AILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAF-GAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAVAAA 241
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  306 ASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHPICPVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKG 384
Cdd:cd06454 242 ALAALEVLQGGPERRERLQENVRYLRRGLKELGFpVGGSPSHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTVPRG 321
                       330       340
                ....*....|....*....|....*...
gi 7657118  385 KARIRVQISAVHSEEDIDRCVEAFVEVG 412
Cdd:cd06454 322 TARLRISLSAAHTKEDIDRLLEALKEVG 349
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
48-408 5.39e-133

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: 386.24  E-value: 5.39e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     48 RVITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQRED 127
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRR--LLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    128 AILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSM 207
Cdd:TIGR00858  79 ALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    208 DGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVM-DQVTIINSTLGKALGGAsGGYTTGPGPLVSLLR 286
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKpEPVDIQVGTLSKALGSY-GAYVAGSQALIDYLI 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    287 QRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDM 366
Cdd:TIGR00858 238 NRARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEEL 317
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 7657118    367 LKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 408
Cdd:TIGR00858 318 QQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
31-412 2.74e-121

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 357.16  E-value: 2.74e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    31 LEGELEGIRGAGTWKSERVITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQS 110
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRR--MLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   111 IHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE 190
Cdd:PRK05958  85 AHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   191 AQKHRlRLVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgG 269
Cdd:PRK05958 165 WRAGR-ALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLaGEPDVILVGTLGKAL-G 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   270 ASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPIC 349
Cdd:PRK05958 243 SSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMDSQSAIQ 322
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 7657118   350 PVMLGDARLASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVG 412
Cdd:PRK05958 323 PLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
70-413 1.69e-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: 312.43  E-value: 1.69e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     70 FCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN-AGLFE-ALLT 147
Cdd:TIGR01821  50 WCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANdATLATlAKII 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    148 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEICCLASRYGAL 227
Cdd:TIGR01821 130 PGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGAL 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    228 VFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAS 307
Cdd:TIGR01821 210 TYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAF-GVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGAT 288
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    308 KALDLLMGSNTIVQSMAAKTQRFRSKMEAAGF-TISGASHpICPVMLGDARLASRMADDML-KRGIFVIGFSYPVVPKGK 385
Cdd:TIGR01821 289 ASIRHLKESQDLRRAHQENVKRLKNLLEALGIpVIPNPSH-IVPVIIGDAALCKKVSDLLLnKHGIYVQPINYPTVPRGT 367
                         330       340
                  ....*....|....*....|....*...
gi 7657118    386 ARIRVQISAVHSEEDIDRCVEAFVEVGR 413
Cdd:TIGR01821 368 ERLRITPTPAHTDKMIDDLVEALLLVWD 395
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
53-411 2.36e-92

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 284.44  E-value: 2.36e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    53 RQGPHIRVDGVSGG--ILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAIL 130
Cdd:PRK13392  32 GRFPRARDHGPDGPrrVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   131 YPSCYDANAGLFEAL--LTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLRLVATDGAFSMD 208
Cdd:PRK13392 112 FTSGYVSNDAALSTLgkLLPGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRPKLIAFESVYSMD 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   209 GDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQR 288
Cdd:PRK13392 192 GDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAF-GCLGGYIAASADLIDFVRSF 270
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   289 ARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMADDMLK 368
Cdd:PRK13392 271 APGFIFTTALPPAVAAGATAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMS 350
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....
gi 7657118   369 R-GIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEV 411
Cdd:PRK13392 351 EhGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAI 394
PLN02483 PLN02483
serine palmitoyltransferase
68-416 2.64e-65

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 216.55  E-value: 2.64e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    68 LNFCANNYLGLSSH-----PEVIQAglqaLEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLF 142
Cdd:PLN02483 103 LNLGSYNYLGFAAAdeyctPRVIES----LKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTII 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   143 EALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEA------QKHRLR---LVATDGAFSMDGDIAP 213
Cdd:PLN02483 179 PALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegqpRTHRPWkkiIVIVEGIYSMEGELCK 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   214 LQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALgGASGGYTTGPGPLVSLLRQRARPY 292
Cdd:PLN02483 259 LPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSF-GSCGGYIAGSKELIQYLKRTCPAH 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   293 LFSNSLPPAVVGCASKALDLLM---GSNTIVQSMAA---KTQRFRSKMEAAGFTISGAS-HPICPVML-GDARLA--SRm 362
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILgedGTNRGAQKLAQireNSNFFRSELQKMGFEVLGDNdSPVMPIMLyNPAKIPafSR- 416
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 7657118   363 adDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHG 416
Cdd:PLN02483 417 --ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVG 468
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
62-408 3.67e-60

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 202.60  E-value: 3.67e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    62 GVSGGILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGL 141
Cdd:PLN02955  99 GRFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   142 FEAL-------------LTPED-AVLSDELNHASIIDGIRLCK----AHKYRYRHLDMADLEAKLQEAQKHRlRLVATDG 203
Cdd:PLN02955 179 MVAIgsvasllaasgkpLKNEKvAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKR-KVVVTDS 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   204 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKAlGGASGGYTTGPGPLVS 283
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKA-AGCHGGFIACSKKWKQ 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   284 LLRQRARPYLFSNSLPPAVVGCASKAldLLMGSNTIVQSMAAkTQRFRSKMEAAGFTISGashPICPVMLGDARLASRMA 363
Cdd:PLN02955 337 LIQSRGRSFIFSTAIPVPMAAAAYAA--VVVARKEKWRRKAI-WERVKEFKALSGVDISS---PIISLVVGNQEKALKAS 410
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 7657118   364 DDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAF 408
Cdd:PLN02955 411 RYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
67-408 1.67e-59

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 197.53  E-value: 1.67e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118     67 ILNFCANNYLGLSShPEVIQAGLQALEefgaglSSVRFICGTQSIHKNLEAKIARFH--------QREDAILYPSCYDAN 138
Cdd:pfam00155   3 KINLGSNEYLGDTL-PAVAKAEKDALA------GGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAGAN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    139 AGLFEALL-TPEDAVLSDELNHASIIDGIRLCKAHKYRYR-------HLDMADLEAKLQEAQKhrlrLVATDGAFSMDGD 210
Cdd:pfam00155  76 IEALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK----VVLHTSPHNPTGT 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    211 IAPLQEICCLAS---RYGALVFMDECHATGFLGPTGRGTDeLLGVMDQV-TIINSTLGKALG--GASGGYTTGPGPLVSL 284
Cdd:pfam00155 152 VATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVAT-RALLAEGPnLLVVGSFSKAFGlaGWRVGYILGNAAVISQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    285 LRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHPICPVMLGDARLASRMAD 364
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 7657118    365 DMLKR-GIFVIGFSYPVVPkgkARIRVQISAvHSEEDIDRCVEAF 408
Cdd:pfam00155 311 VLLEEvGVYVTPGSSPGVP---GWLRITVAG-GTEEELEELLEAI 351
PLN02822 PLN02822
serine palmitoyltransferase
49-411 2.20e-54

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 187.64  E-value: 2.20e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    49 VITSRQGPHIRVDGVSggILNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDA 128
Cdd:PLN02822  95 VLESAAGPHTIINGKD--VVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   129 ILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQE-------AQKHRlRLVAT 201
Cdd:PLN02822 173 ILYSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKltaenkrKKKLR-RYIVV 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   202 DGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGV-MDQVTIINSTLGKALGGAsGGYTTGPGP 280
Cdd:PLN02822 252 EAIYQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATE-GGFCTGSAR 330
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   281 LVSLLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIV----QSMAAKTQRFRSKMEaagftISGASHPICPVML--- 353
Cdd:PLN02822 331 VVDHQRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLaklkENIALLHKGLSDIPG-----LSIGSNTLSPIVFlhl 405
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 7657118   354 --------GDARLASRMADDMLKR-GIFVIGFSYPVVPKGK--ARIRVQISAVHSEEDIDRCVEAFVEV 411
Cdd:PLN02822 406 ekstgsakEDLSLLEHIADRMLKEdSVLVVVSKRSTLDKCRlpVGIRLFVSAGHTESDILKASESLKRV 474
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
47-411 4.78e-52

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 179.43  E-value: 4.78e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    47 ERVITSRQGPHIRVDGVSG-GILNFCANNYLGLSSHPEVIQAGLQALEEFGAGL--SSVrFICGTQSIHKnLEAKIARFH 123
Cdd:PRK07179  35 ERVNKNWNGKHLVLGKTPGpDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLvmSAV-FLHDDSPKPQ-FEKKLAAFT 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   124 QREDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEaqkHRLRLVATDG 203
Cdd:PRK07179 113 GFESCLLCQSGWAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER---HGPGIIVVDS 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   204 AFSMDGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRGTDELLGVMDQVTIINSTLGKALGGaSGGYTTGPGPLVS 283
Cdd:PRK07179 190 VYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAG-RAGIITCPRELAE 268
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   284 LLRQRARPYLFSNSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRSKMEAAGFTISGASHpICPVMLGDARLASRMA 363
Cdd:PRK07179 269 YVPFVSYPAIFSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIRSESQ-IIALETGSERNTEVLR 347
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|..
gi 7657118   364 DDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDR----CVEAFVEV 411
Cdd:PRK07179 348 DALEERNVFGAVFCAPATPKNRNLIRLSLNADLTASDLDRvlevCREARDEV 399
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
68-407 6.22e-43

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 155.06  E-value: 6.22e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    68 LNFCANNYLGLSSHPEVIQAGLQALEEFGAGLSSVRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDANAGLFEALLT 147
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   148 PEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADL----------EAKLQEAQKHRLRLVATDGAFSMDGDIAPLQEI 217
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKEL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   218 CCLASRYGALVFMDECHATGFLGPTGRGTDELLGV--MDQVTIINSTLGKALGGAsGGYTTGPGPLVSLLRQRARPYLFS 295
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSV-GGMTVGSEEVVDHQRLSGSGYCFS 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   296 NSLPPAVVGCASKALDLLMGSNTIVQSMAAKTQRFRS-----------KMEAAGFTISGASHPICPVMLGDAR------- 357
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGPQLLNRLHDSIANLYStltnsshpyalKLRNRLVITSDPISPIIYLRLSDQEatrrtde 319
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 7657118   358 --LASRMADDMLKRGIFVI--GFSYPVVPKGKAR--IRVQISAVHSEEDIDRCVEA 407
Cdd:PLN03227 320 tlILDQIAHHSLSEGVAVVstGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTV 375
PRK07505 PRK07505
hypothetical protein; Provisional
50-417 8.81e-43

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 154.75  E-value: 8.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    50 ITSRQGPHIRVDGVSGG-ILNFCANNYLGLSSHPEVIQAGLQALEEFGA-GLSSVRFICGTQsIHKNLEAKIARFHQREd 127
Cdd:PRK07505  30 LTVGEREGILITLADGHtFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSlHLSSSRTRVRSQ-ILKDLEEALSELFGAS- 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   128 AILYPSCYDANAGLFEAL----LTPEDAVLS--DELNHASIIDGIRLCkAHKYRYRHLDMADLEAKLQEAQKHRLRLVAT 201
Cdd:PRK07505 108 VLTFTSCSAAHLGILPLLasghLTGGVPPHMvfDKNAHASLNILKGIC-ADETEVETIDHNDLDALEDICKTNKTVAYVA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   202 DGAFSMdGDIAPLQEICCLASRYGALVFMDECHATGFLGPTGRG--TDELLGVMDQVTIINSTLGKALGGASGGYTTGPG 279
Cdd:PRK07505 187 DGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMLGDA 265
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   280 PLVSLLRQRARPYLFSNSLPPAVVGCASKALDL-LMGSNTIVQ-SMAAKTQRFRSKMEAagfTISGASHPICPVMLGDAR 357
Cdd:PRK07505 266 EQIELILRYAGPLAFSQSLNVAALGAILASAEIhLSEELDQLQqKLQNNIALFDSLIPT---EQSGSFLPIRLIYIGDED 342
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   358 LASRMADDMLKRGIFVIGFSYPVVPKGKARIRVQISAVHSEEDIDRCVEAFVEVGRLHGA 417
Cdd:PRK07505 343 TAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKEILDEGLA 402
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
68-402 3.39e-24

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 102.94  E-value: 3.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    68 LNFCANNYLGLSSHPEV---IQAGLQAL------EEFGAGLSsvRFICGTQSIHKNLEAKIARFHQREDAILYPSCYDAN 138
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLvheVEKRYRLYcrqfphAQLGYGGS--RAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   139 AGLFEALLTPEDAVLSDELNHASIIDGIRLCKAHKYRYRHLDMADLEAKLQEAQKHRLR--LVATDGAFSMDGDIAPLQE 216
Cdd:PRK05937  85 LGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFGriFIFVCSVYSFKGTLAPLEQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   217 ICCLASRYGALVFMDECHATGFLGPTGRGTDELLGvMDQVTIINSTLGKALGgasggyTTGPGPLVSL-----LRQRARP 291
Cdd:PRK05937 165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLG-YENFYAVLVTYSKALG------SMGAALLSSSevkqdLMLNSPP 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   292 YLFSNSLPPAVVGCASKALDLLMGSNTIvqsmaAKTQRFRSKMEAAGFTISGASHPICPVMLGDarLASRMADDMLKRGI 371
Cdd:PRK05937 238 LRYSTGLPPHLLISIQVAYDFLSQEGEL-----ARKQLFRLKEYFAQKFSSAAPGCVQPIFLPG--ISEQELYSKLVETG 310
                        330       340       350
                 ....*....|....*....|....*....|.
gi 7657118   372 FVIGFsypVVPKGKARIRVQISAVHSEEDID 402
Cdd:PRK05937 311 IRVGV---VCFPTGPFLRVNLHAFNTEDEVD 338
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
112-277 2.52e-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: 2.52e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  112 HKNLEAKIARFHQ--REDAILYPSCYDANAGLFEALLTPEDAVLSDELNHAS---IIDGIRLCKAHKYRYRHLDMADLEA 186
Cdd:cd01494   2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrywVAAELAGAKPVPVPVDDAGYGGLDV 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  187 KLQEAQKHRLR--LVATDGAFSMDGDIAPLQEICCLASRYGALVFMDECHATGflgptGRGTDELLGVMDQVTIINSTLG 264
Cdd:cd01494  82 AILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLH 156
                       170
                ....*....|...
gi 7657118  265 KALGGASGGYTTG 277
Cdd:cd01494 157 KNLGGEGGGVVIV 169
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
76-411 1.02e-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: 1.02e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118   76 LGLSSHPEVIQAGLQALEEFGAGLSSVRF-ICGTQSIhknlEA--KIARFHQREDAILypSCYDANAG-LFEAL-LTPED 150
Cdd:cd00610  73 LGFFYNEPAVELAELLLALTPEGLDKVFFvNSGTEAV----EAalKLARAYTGRKKII--SFEGAYHGrTLGALsLTGSK 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  151 A---VLSDELNHASIIDGirlckAHKYRYRHLDMADLEAkLQEAQKHRLRLVAtdgAFSMD------GDIAP----LQEI 217
Cdd:cd00610 147 KyrgGFGPLLPGVLHVPY-----PYRYRPPAELADDLEA-LEEALEEHPEEVA---AVIVEpiqgegGVIVPppgyLKAL 217
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  218 CCLASRYGALVFMDEChATGFlGPTGR-GTDELLGVM-DqvtIInsTLGKALGGAS--GGYTTGPGPLVSLlrqRARPYL 293
Cdd:cd00610 218 RELCRKHGILLIADEV-QTGF-GRTGKmFAFEHFGVEpD---IV--TLGKGLGGGLplGAVLGREEIMDAF---PAGPGL 287
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  294 FSNSL---PpavVGCA--SKALDLLMgSNTIVQSMAAKTQRFRSKMEAAgftisgASHPICPV-------MLG------- 354
Cdd:cd00610 288 HGGTFggnP---LACAaaLAVLEVLE-EEGLLENAAELGEYLRERLREL------AEKHPLVGdvrgrglMIGielvkdr 357
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657118  355 -----DARLASRMADDMLKRGIFVIgfsypvvPKGKARIRVQISAVHSEEDIDRCVEAFVEV 411
Cdd:cd00610 358 atkppDKELAAKIIKAALERGLLLR-------PSGGNVIRLLPPLIITEEEIDEGLDALDEA 412
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
115-410 1.06e-10

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 62.74  E-value: 1.06e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  115 LEAKIARFHQR--------EDAILYPSCYDANAGLFEALLTPEDAVLSDELNHASIIDGIRLCKAhKYRYRHLD----MA 182
Cdd:cd00609  41 LREAIAEWLGRrggvdvppEEIVVTNGAQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGA-EVVPVPLDeeggFL 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  183 DLEAKLQEAQKHRLRLVA-------TDGAFSMDGdiapLQEICCLASRYGALVFMDECHatGFLGPTGRGTDELLGV-MD 254
Cdd:cd00609 120 LDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLdAY 193
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  255 QVTIINSTLGKALGGAS--GGYTTGPGPLVSLLRQRARPYLFSNSLPPAVVGCAsKALDLLMGS-NTIVQSMAAKTQRFR 331
Cdd:cd00609 194 ERVIVLRSFSKTFGLPGlrIGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAA-AALDDGEEHlEELRERYRRRRDALL 272
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  332 SKMEAAGFTI----SGASHpicpVMLG-----DARLASRMAddmLKRGIFVIGFSYPvVPKGKARIRvqISAVHSEEDID 402
Cdd:cd00609 273 EALKELGPLVvvkpSGGFF----LWLDlpegdDEEFLERLL---LEAGVVVRPGSAF-GEGGEGFVR--LSFATPEEELE 342

                ....*...
gi 7657118  403 RCVEAFVE 410
Cdd:cd00609 343 EALERLAE 350
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
144-237 9.38e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 47.44  E-value: 9.38e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118  144 ALLTPEDAVLSDELNHASIIDGIR-LCKAHKYRYR--------HLDMADLEAKLQEaqkhRLRLVATDGAFSMDGDIAPL 214
Cdd:COG0520  98 GRLKPGDEILITEMEHHSNIVPWQeLAERTGAEVRvipldedgELDLEALEALLTP----RTKLVAVTHVSNVTGTVNPV 173
                        90       100
                ....*....|....*....|...
gi 7657118  215 QEICCLASRYGALVFMDECHATG 237
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
146-403 1.42e-05

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: 46.86  E-value: 1.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    146 LTPEDAVLSDELNHASIIDGI-RLCKAHKYRYR--------HLDMADLEAKLqeaqKHRLRLVATDGAFSMDGDIAPLQE 216
Cdd:pfam00266  85 LKPGDEIVITEMEHHANLVPWqELAKRTGARVRvlpldedgLLDLDELEKLI----TPKTKLVAITHVSNVTGTIQPVPE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    217 ICCLASRYGALVFMDECHATG--------------------FLGPTGRG----TDELLGVMDqvtiinstlgKALGGasG 272
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIGvlygRRDLLEKMP----------PLLGG--G 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7657118    273 GYTTGPGplVSLLRQRARPYLFSNSLPP--AVVGCAsKALDLLM--GSNTIVQSMAAKTQRFRSKMEAAGFTisgashpi 348
Cdd:pfam00266 229 GMIETVS--LQESTFADAPWKFEAGTPNiaGIIGLG-AALEYLSeiGLEAIEKHEHELAQYLYERLLSLPGI-------- 297
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7657118    349 cpVMLGDARLASRM---------ADDML---KRGIFVIGFSYPVVPKGKAR-----IRVQISAVHSEEDIDR 403
Cdd:pfam00266 298 --RLYGPERRASIIsfnfkgvhpHDVATlldESGIAVRSGHHCAQPLMVRLglggtVRASFYIYNTQEDVDR 367
 
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.
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