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Conserved domains on  [gi|981909219|ref|WP_060093325|]
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8-amino-7-oxononanoate synthase [Burkholderia vietnamiensis]

Protein Classification

8-amino-7-oxononanoate synthase( domain architecture ID 10012622)

8-amino-7-oxononanoate synthase catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide in the biosynthesis of biotin

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
12-398 6.66e-162

8-amino-7-oxononanoate synthase; Reviewed


:

Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 460.01  E-value: 6.66e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  12 LLDTLQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGH 91
Cdd:PRK05958   3 WLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  92 SRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHAL 171
Cdd:PRK05958  83 SPAHEALEEELAEWFG----AERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 172 GALLDASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGR-GALAAAALRSPNLVYVGTLG 250
Cdd:PRK05958 159 EALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVGTLG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 251 KAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIGGDegDARRAHLAALIERTRALLRATRWQPVD 330
Cdd:PRK05958 239 KALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMD 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981909219 331 SHTAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIAA 398
Cdd:PRK05958 317 SQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
 
Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
12-398 6.66e-162

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 460.01  E-value: 6.66e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  12 LLDTLQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGH 91
Cdd:PRK05958   3 WLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  92 SRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHAL 171
Cdd:PRK05958  83 SPAHEALEEELAEWFG----AERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 172 GALLDASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGR-GALAAAALRSPNLVYVGTLG 250
Cdd:PRK05958 159 EALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVGTLG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 251 KAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIGGDegDARRAHLAALIERTRALLRATRWQPVD 330
Cdd:PRK05958 239 KALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMD 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981909219 331 SHTAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIAA 398
Cdd:PRK05958 317 SQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
12-401 1.61e-151

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: 433.71  E-value: 1.61e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  12 LLDTLQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGH 91
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  92 SRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHAL 171
Cdd:COG0156   81 TPLHEELEEELAEFLG----KEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 172 GALL-DASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLG 250
Cdd:COG0156  157 ERLLkKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 251 KAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVD 330
Cdd:COG0156  237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEIL--REEPELRERLWENIAYFREGLKELGFDLGP 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981909219 331 SHTAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIAASEA 401
Cdd:COG0156  315 SESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
33-395 3.62e-126

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: 368.13  E-value: 3.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   33 RTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdA 112
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKG----T 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  113 PRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDAP-TKLIVSDTVF 191
Cdd:TIGR00858  77 EAALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGErRKLIVTDGVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  192 SMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGR-GALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEWM 270
Cdd:TIGR00858 157 SMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRgTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  271 IQRARSYIFTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVDSHTAVQPLVIGSNDATLAAM 350
Cdd:TIGR00858 237 INRARTLIFSTALPPAVAAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALA 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 981909219  351 RALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:TIGR00858 315 EELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
48-395 2.37e-115

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: 340.31  E-value: 2.37e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  48 RDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLA 127
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHG----KEAALVFSSGYAANDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 128 AMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDAP--TKLIVSDTVFSMDGDLAPLAELVA 205
Cdd:cd06454   77 VLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPygKKLIVTEGVYSMDGDIAPLPELVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 206 LAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPP 285
Cdd:cd06454  157 LAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 286 AVAHAVSASLKVIGGdeGDARRAHLAALIERTRALLRATRWQPVDSH-TAVQPLVIGSNDATLAAMRALDARGLWVPAIR 364
Cdd:cd06454  237 AVAAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIR 314
                        330       340       350
                 ....*....|....*....|....*....|.
gi 981909219 365 PPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:cd06454  315 YPTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
48-395 7.66e-50

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 171.72  E-value: 7.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   48 RDIVGFASNDYLGLAAHPALVAAFAEGAQRygsgsggSHLLGGHSRAHARLEDELAGFAGGF----SDAPRALYFSTGYM 123
Cdd:pfam00155   1 TDKINLGSNEYLGDTLPAVAKAEKDALAGG-------TRNLYGPTDGHPELREALAKFLGRSpvlkLDREAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  124 ANL-AAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYP-------HADMHALGALLDAsdaPTKLIVSDTVFSMDG 195
Cdd:pfam00155  74 ANIeALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE---KPKVVLHTSPHNPTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  196 DLAPLAELVALAE---RHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAG---AFVVAHETVIEW 269
Cdd:pfam00155 151 TVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  270 MIQRARSYIFTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVDSHTAVQPLVIGSNDATLAA 349
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 981909219  350 MRAL-DARGLWVPAIRPPTVPagtSRLRISLsAAHSFDDLARLEAAL 395
Cdd:pfam00155 309 AQVLlEEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
12-398 6.66e-162

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 460.01  E-value: 6.66e-162
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  12 LLDTLQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGH 91
Cdd:PRK05958   3 WLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  92 SRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHAL 171
Cdd:PRK05958  83 SPAHEALEEELAEWFG----AERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDAL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 172 GALLDASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGR-GALAAAALRSPNLVYVGTLG 250
Cdd:PRK05958 159 EALLAKWRAGRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVGTLG 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 251 KAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIGGDegDARRAHLAALIERTRALLRATRWQPVD 330
Cdd:PRK05958 239 KALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRRE--PERRERLAALIARLRAGLRALGFQLMD 316
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981909219 331 SHTAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIAA 398
Cdd:PRK05958 317 SQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEA 384
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
12-401 1.61e-151

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: 433.71  E-value: 1.61e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  12 LLDTLQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGH 91
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  92 SRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHAL 171
Cdd:COG0156   81 TPLHEELEEELAEFLG----KEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 172 GALL-DASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLG 250
Cdd:COG0156  157 ERLLkKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDIIMGTLS 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 251 KAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVD 330
Cdd:COG0156  237 KALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEIL--REEPELRERLWENIAYFREGLKELGFDLGP 314
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 981909219 331 SHTAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIAASEA 401
Cdd:COG0156  315 SESPIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
33-395 3.62e-126

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: 368.13  E-value: 3.62e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   33 RTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdA 112
Cdd:TIGR00858   1 RPLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKG----T 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  113 PRALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDAP-TKLIVSDTVF 191
Cdd:TIGR00858  77 EAALLFSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGErRKLIVTDGVF 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  192 SMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGR-GALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEWM 270
Cdd:TIGR00858 157 SMDGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEDGRgTLEHFGLKPEPVDIQVGTLSKALGSYGAYVAGSQALIDYL 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  271 IQRARSYIFTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVDSHTAVQPLVIGSNDATLAAM 350
Cdd:TIGR00858 237 INRARTLIFSTALPPAVAAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALA 314
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 981909219  351 RALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:TIGR00858 315 EELQQQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
48-395 2.37e-115

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: 340.31  E-value: 2.37e-115
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  48 RDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLA 127
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHG----KEAALVFSSGYAANDG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 128 AMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDAP--TKLIVSDTVFSMDGDLAPLAELVA 205
Cdd:cd06454   77 VLSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARRPygKKLIVTEGVYSMDGDIAPLPELVD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 206 LAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAPP 285
Cdd:cd06454  157 LAKKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPP 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 286 AVAHAVSASLKVIGGdeGDARRAHLAALIERTRALLRATRWQPVDSH-TAVQPLVIGSNDATLAAMRALDARGLWVPAIR 364
Cdd:cd06454  237 AVAAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIR 314
                        330       340       350
                 ....*....|....*....|....*....|.
gi 981909219 365 PPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:cd06454  315 YPTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
16-388 3.10e-78

pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme subfamily related to three known enzymes; it appears closest to glycine C-acteyltransferase, shows no overlap with it in species distribution, and may share that function. The three closely related enzymes are glycine C-acetyltransferase (2-amino-3-ketobutyrate coenzyme A ligase), 5-aminolevulinic acid synthase, and 8-amino-7-oxononanoate synthase. All transfer the R-group (acetyl, succinyl, or 6-carboxyhexanoyl) from coenzyme A to an amino acid (Gly, Gly, Ala, respectively), with release of CO2 for the latter two reactions.


Pssm-ID: 130884 [Multi-domain]  Cd Length: 385  Bit Score: 246.66  E-value: 3.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   16 LQRGLAELDAQGLRRVRRTADTACDAHMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAH 95
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   96 ARLEDELAGFAGGFSdaprALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALL 175
Cdd:TIGR01825  81 EELEEKLAKFKKTEA----ALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  176 -DASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAG 254
Cdd:TIGR01825 157 rENPSYGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGEAGRGTVHHFGLEDKVDIQVGTLSKAIG 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  255 VAGAFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSASLKVIGGDEgdarrAHLAALIERTR---ALLRATRWQPVDS 331
Cdd:TIGR01825 237 VVGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSP-----ELMERLWDNTRffkAGLGKLGYDTGGS 311
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 981909219  332 HTAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDL 388
Cdd:TIGR01825 312 ETPITPVVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDL 368
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
12-398 9.05e-78

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 245.49  E-value: 9.05e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  12 LLDTLQRGLAELDAQGLRRVRRTADTACDAHMRV-DGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGG 90
Cdd:PRK06939   5 FYAQLREELEEIKAEGLYKEERVITSPQGADITVaDGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  91 HSRAHARLEDELAGFAGgfSDAprALYFSTGYMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHA 170
Cdd:PRK06939  85 TQDLHKELEEKLAKFLG--TED--AILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 171 LGALL---DASDAPTKLIVSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQgrgalaaaALRSPNL---- 243
Cdd:PRK06939 161 LEAQLkeaKEAGARHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEN--------GRGTVEHfgvm 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 244 ----VYVGTLGKA-AGVAGAFVVAHETVIEWMIQRARSYIFTTaapPAVAHAVSASLKVIGG-DEGDARRAHLAALIERT 317
Cdd:PRK06939 233 drvdIITGTLGKAlGGASGGYTAGRKEVIDWLRQRSRPYLFSN---SLAPAIVAASIKVLELlEESDELRDRLWENARYF 309
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 318 RALLRATRWQPVDSHTAVQPLVIGsnDATLAA--MRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:PRK06939 310 REGMTAAGFTLGPGEHPIIPVMLG--DAKLAQefADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAF 387

                 ...
gi 981909219 396 IAA 398
Cdd:PRK06939 388 EKV 390
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
48-395 8.30e-67

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 219.55  E-value: 8.30e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  48 RDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFaggfSDAPRALYFSTGYMANLA 127
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADL----KKKEDCLVCPTGFAANMA 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 128 AMTA--------------LTGKQATIFSDALNHASLIDGIRLSR----ANVQIYPHADMHALGALLDASDAPTKLIVSDT 189
Cdd:PLN02955 178 AMVAigsvasllaasgkpLKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHLNSLLSSCKMKRKVVVTDS 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 190 VFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEW 269
Cdd:PLN02955 258 LFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQL 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 270 MIQRARSYIFTTAAPPAVAHAVSASlkVIGGDEGDARRahlAALIERTRALLRATrwqPVDSHTAVQPLVIGSNDATLAA 349
Cdd:PLN02955 338 IQSRGRSFIFSTAIPVPMAAAAYAA--VVVARKEKWRR---KAIWERVKEFKALS---GVDISSPIISLVVGNQEKALKA 409
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 981909219 350 MRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:PLN02955 410 SRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITAL 455
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
46-398 2.80e-61

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: 203.04  E-value: 2.80e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   46 DGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGGFSdaprALYFSTGYMAN 125
Cdd:TIGR01821  43 GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGAGGTRNISGTNIPHVELEAELADLHGKES----ALVFTSGYVAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  126 LAAMTALTGK--QATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASD-APTKLIVSDTVFSMDGDLAPLAE 202
Cdd:TIGR01821 119 DATLATLAKIipGCVIFSDELNHASMIEGIRHSGAEKFIFRHNDVAHLEKLLQSVDpNRPKIIAFESVYSMDGDIAPIEE 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  203 LVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEWMIQRARSYIFTTA 282
Cdd:TIGR01821 199 ICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRIDIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTS 278
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  283 APPAVAHAVSASLKVIGGDEgDARRAHlAALIERTRALLRATRWQPVDSHTAVQPLVIGSNDATLAAMRALDAR-GLWVP 361
Cdd:TIGR01821 279 LPPAIAAGATASIRHLKESQ-DLRRAH-QENVKRLKNLLEALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKhGIYVQ 356
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 981909219  362 AIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIAA 398
Cdd:TIGR01821 357 PINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLV 393
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
48-397 2.58e-55

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 187.75  E-value: 2.58e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  48 RDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGGFSdaprALYFSTGYMANLA 127
Cdd:PRK13392  46 RRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKES----ALLFTSGYVSNDA 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 128 AMTALTGK--QATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDAPT-KLIVSDTVFSMDGDLAPLAELV 204
Cdd:PRK13392 122 ALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQLASVDPDRpKLIAFESVYSMDGDIAPIEAIC 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 205 ALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAGAFVVAHETVIEWMIQRARSYIFTTAAP 284
Cdd:PRK13392 202 DLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALP 281
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 285 PAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVDSHTAVQPLVIGsnDATL---AAMRALDARGLWVP 361
Cdd:PRK13392 282 PAVAAGATAAIRHL--KTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVG--DPTLckaISDRLMSEHGIYIQ 357
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 981909219 362 AIRPPTVPAGTSRLRISLSAAHSFDDLARLEAALIA 397
Cdd:PRK13392 358 PINYPTVPRGTERLRITPTPLHDDEDIDALVAALVA 393
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
48-395 7.66e-50

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 171.72  E-value: 7.66e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   48 RDIVGFASNDYLGLAAHPALVAAFAEGAQRygsgsggSHLLGGHSRAHARLEDELAGFAGGF----SDAPRALYFSTGYM 123
Cdd:pfam00155   1 TDKINLGSNEYLGDTLPAVAKAEKDALAGG-------TRNLYGPTDGHPELREALAKFLGRSpvlkLDREAAVVFGSGAG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  124 ANL-AAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYP-------HADMHALGALLDAsdaPTKLIVSDTVFSMDG 195
Cdd:pfam00155  74 ANIeALIFLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKE---KPKVVLHTSPHNPTG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  196 DLAPLAELVALAE---RHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKAAGVAG---AFVVAHETVIEW 269
Cdd:pfam00155 151 TVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQ 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  270 MIQRARSYIFTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWQPVDSHTAVQPLVIGSNDATLAA 349
Cdd:pfam00155 231 LRKLARPFYSSTHLQAAAAAALSDPLLVA--SELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKEL 308
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 981909219  350 MRAL-DARGLWVPAIRPPTVPagtSRLRISLsAAHSFDDLARLEAAL 395
Cdd:pfam00155 309 AQVLlEEVGVYVTPGSSPGVP---GWLRITV-AGGTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
54-390 4.19e-33

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 129.50  E-value: 4.19e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  54 ASNDYLGLAAH-----PALVaafaEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdAPRALYFSTGYMANLAA 128
Cdd:PLN02483 106 GSYNYLGFAAAdeyctPRVI----ESLKKYSASTCSSRVDGGTTKLHRELEELVARFVG----KPAAIVFGMGYATNSTI 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 129 MTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDA--------PTK--LIVSDTVFSMDGDLA 198
Cdd:PLN02483 178 IPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAegqprthrPWKkiIVIVEGIYSMEGELC 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 199 PLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNL-VYVGTLGKAAGVAGAFVVAHETVIEWMIQRARSY 277
Cdd:PLN02483 258 KLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVdIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAH 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 278 IFTTAAPPAVAHAVSASLKVIGGDEGDARRAH-LAALIER---TRALLRATRWQPV-DSHTAVQPLVIgSNDATLAAM-R 351
Cdd:PLN02483 338 LYATSMSPPAVQQVISAIKVILGEDGTNRGAQkLAQIRENsnfFRSELQKMGFEVLgDNDSPVMPIML-YNPAKIPAFsR 416
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 981909219 352 ALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLAR 390
Cdd:PLN02483 417 ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIK 455
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
42-395 2.54e-30

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 120.50  E-value: 2.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  42 HMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdAPRALYFSTG 121
Cdd:PRK07179  48 LGKTPGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTG----FESCLLCQSG 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 122 YMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRAnvQIYP--HADMHALGALLdASDAPtKLIVSDTVFSMDGDLAP 199
Cdd:PRK07179 124 WAANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGA--QAHPfrHNDVDHLRRQI-ERHGP-GIIVVDSVYSTTGTIAP 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 200 LAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLGKA-AGVAGAFVVAHEtVIEWMIQRARSYI 278
Cdd:PRK07179 200 LADIVDIAEEFGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAfAGRAGIITCPRE-LAEYVPFVSYPAI 278
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 279 FTTAAPPAVAHAVSASLKVIggDEGDARRAHLAALIERTRALLRATRWqPVDSHTAVQPLVIGSNDATLAAMRALDARGL 358
Cdd:PRK07179 279 FSSTLLPHEIAGLEATLEVI--ESADDRRARLHANARFLREGLSELGY-NIRSESQIIALETGSERNTEVLRDALEERNV 355
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 981909219 359 WVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:PRK07179 356 FGAVFCAPATPKNRNLIRLSLNADLTASDLDRVLEVC 392
PRK07505 PRK07505
hypothetical protein; Provisional
8-395 4.80e-25

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 105.45  E-value: 4.80e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219   8 IATPLLD-TLQRGLAELDAQGLRRVRRTADtacdahmrvDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSH 86
Cdd:PRK07505  14 RAEKFWDaAYDEGLNGLTVGEREGILITLA---------DGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSS 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  87 LLGGHSRAHARLEDELAG-FAGGFSDAPRALYFSTGYMANLAAMTALTGKQATIFSDALNHASL--IDGIRLSRANVQIY 163
Cdd:PRK07505  85 RTRVRSQILKDLEEALSElFGASVLTFTSCSAAHLGILPLLASGHLTGGVPPHMVFDKNAHASLniLKGICADETEVETI 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 164 PHADMHALGALldASDAPTKLIVSDTVFSMdGDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGR--GALAAAALRSP 241
Cdd:PRK07505 165 DHNDLDALEDI--CKTNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEgyVRSELDYRLNE 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 242 NLVYVGTLGKAAGVAGAFVVAHETVIEWMIQR-ARSYIFTTAAPPAVAHAVSASLKVIGGDEGDARRAHLAALIERTRAL 320
Cdd:PRK07505 242 RTIIAASLGKAFGASGGVIMLGDAEQIELILRyAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSL 321
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 981909219 321 LrATRWQPVDShtAVQPLVIGSNDATLAAMRALDARGLWVPAIRPPTVPAGTSRLRISLSAAHSFDDLARLEAAL 395
Cdd:PRK07505 322 I-PTEQSGSFL--PIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
47-402 4.30e-22

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 96.77  E-value: 4.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  47 GRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRA---HARLEDELAGFAGGFSDAPRALYFSTGYM 123
Cdd:PRK05937   3 ESLSIDFVTNDFLGFSRSDTLVHEVEKRYRLYCRQFPHAQLGYGGSRAilgPSSLLDDLEHKIAHFHGAPEAFIVPSGYM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 124 ANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLDASDAPTK---LIVSDTVFSMDGDLAPL 200
Cdd:PRK05937  83 ANLGLCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQRSFgriFIFVCSVYSFKGTLAPL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 201 AELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVgTLGKAAGVAGAFVVAHETVIEWMIQRARSYIFT 280
Cdd:PRK05937 163 EQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 281 TAAPPAVAHAVSASLKviggdegdarraHLAALIERTRALLRATR---WQPVDSHTA--VQPLVI-GSNDATLAAMraLD 354
Cdd:PRK05937 242 TGLPPHLLISIQVAYD------------FLSQEGELARKQLFRLKeyfAQKFSSAAPgcVQPIFLpGISEQELYSK--LV 307
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 981909219 355 ARGLWVPAIRPPTVPAgtsrLRISLSAAHSFDDLARLEAALIAASEAS 402
Cdd:PRK05937 308 ETGIRVGVVCFPTGPF----LRVNLHAFNTEDEVDILVSVLATYLEKY 351
PLN02822 PLN02822
serine palmitoyltransferase
42-395 6.26e-21

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 94.42  E-value: 6.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  42 HMRVDGRDIVGFASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGgfsdAPRALYFSTG 121
Cdd:PLN02822 103 HTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLG----TPDSILYSYG 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 122 YMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLD-------ASDAPTKLIVSDTVFSMD 194
Cdd:PLN02822 179 LSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVVEAIYQNS 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 195 GDLAPLAELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNL-VYVGTLGKAAGVAGAFVVAHETVIEWmiQR 273
Cdd:PLN02822 259 GQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIdIITAAMGHALATEGGFCTGSARVVDH--QR 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 274 ARS--YIFTTAAPPAVAHAVSASLKVIGGD-EGDARRAHLAALIERTralLRATRWQPVDSHTaVQPLVI-------GSN 343
Cdd:PLN02822 337 LSSsgYVFSASLPPYLASAAITAIDVLEDNpSVLAKLKENIALLHKG---LSDIPGLSIGSNT-LSPIVFlhlekstGSA 412
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981909219 344 DATLA-----AMRALDARGLWVPAIRPPTV-----PAGtsrLRISLSAAHSFDDLARLEAAL 395
Cdd:PLN02822 413 KEDLSllehiADRMLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESL 471
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
53-401 2.15e-20

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 91.89  E-value: 2.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  53 FASNDYLGLAAHPALVAAFAEGAQRYGSGSGGSHLLGGHSRAHARLEDELAGFAGGFSdaprALYFSTGYMANLAAMTAL 132
Cdd:PLN03227   3 FATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTES----AILYSDGASTTSSTVAAF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 133 TGKQATIFSDALNHASLIDGIRLSRANVQIYPHADMHALGALLD---ASDAPTKL--------IVSDTVFSMDGDLAPLA 201
Cdd:PLN03227  79 AKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEqvrAQDVALKRkptdqrrfLVVEGLYKNTGTLAPLK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 202 ELVALAERHGAWLVVDDAHGFGVLGPQGRGALAAAALRSPNLVYVGTLG--KAAGVAGAFVVAHETVIEWMIQRARSYIF 279
Cdd:PLN03227 159 ELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPMVHAEIVTFSleNAFGSVGGMTVGSEEVVDHQRLSGSGYCF 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 280 TTAAPPAVAHAVSASLKVIGGDE------GDARRAHLAALIERTRALLRATRWQPVDSHTAVQPLVI---------GSND 344
Cdd:PLN03227 239 SASAPPFLAKADATATAGELAGPqllnrlHDSIANLYSTLTNSSHPYALKLRNRLVITSDPISPIIYlrlsdqeatRRTD 318
                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981909219 345 ATL-----AAMRALDARGLWVPAIRPPTVPAGTSR--LRISLSAAHSFDDLARLEAALIAASEA 401
Cdd:PLN03227 319 ETLildqiAHHSLSEGVAVVSTGGHVKKFLQLVPPpcLRVVANASHTREDIDKLLTVLGEAVEA 382
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
95-395 3.33e-10

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 61.20  E-value: 3.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219  95 HARLEDELAGFAG---GFSDAPRALYFSTG-YMANLAAMTALTGKQATIFSDALNHASLIDGIRLSRANVQIYP----HA 166
Cdd:cd00609   38 LPELREAIAEWLGrrgGVDVPPEEIVVTNGaQEALSLLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVPldeeGG 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 167 DMHALGALLDASDAPTKLIV-------SDTVFSMDGdlapLAELVALAERHGAWLVVDDAHGfGVLGPQGRGALAAAALR 239
Cdd:cd00609  118 FLLDLELLEAAKTPKTKLLYlnnpnnpTGAVLSEEE----LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDA 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 240 SPNLVYVGTLGKAAGVAG---AFVVAHETVIEWMIQRARSYIFTTAAPPAVAHAVSAsLKviggDEGDARRAHLAALIER 316
Cdd:cd00609  193 YERVIVLRSFSKTFGLPGlriGYLIAPPEELLERLKKLLPYTTSGPSTLSQAAAAAA-LD----DGEEHLEELRERYRRR 267
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 317 TRALLRA-TRWQPVDSHTAVQPLVI-----GSNDATLAAMRALDARGLWVPAIRPPtvPAGTSRLRISLsaAHSFDDLAR 390
Cdd:cd00609  268 RDALLEAlKELGPLVVVKPSGGFFLwldlpEGDDEEFLERLLLEAGVVVRPGSAFG--EGGEGFVRLSF--ATPEEELEE 343

                 ....*
gi 981909219 391 LEAAL 395
Cdd:cd00609  344 ALERL 348
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
112-263 1.07e-09

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: 57.01  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981909219 112 APRALYFSTGYMANLAAMTALTGKQATIFSDALNHAS-LIDGIRLSRANVQIYPH---ADMHALGALLDASDA--PTKLI 185
Cdd:cd01494   17 NDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSrYWVAAELAGAKPVPVPVddaGYGGLDVAILEELKAkpNVALI 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981909219 186 VSDTVFSMDGDLAPLAELVALAERHGAWLVVDDAHGFGvlgpqGRGALAAAALRSPNLVYVGTLGKAAGVAGAFVVAH 263
Cdd:cd01494   97 VITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPEGGADVVTFSLHKNLGGEGGGVVIV 169
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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