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Conserved domains on  [gi|446172969|ref|WP_000250824|]
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MULTISPECIES: glycine C-acetyltransferase [Staphylococcus]

Protein Classification

PLP-dependent aminotransferase family protein; bifunctional SDR family oxidoreductase/aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 10797561)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation| bifunctional extended SDR (short-chain dehydrogenase/reductase) family NAD(P)-dependent oxidoreductase/aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 9-395 0e+00

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: 688.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969    9 LEENINYLKENGLYNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLH 88
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   89 DELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAV 168
Cdd:TIGR01825  81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRENP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  169 EsgqYNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMG-KGAGTVKHFGLQDKIDFQIGTLSKAIGV 247
Cdd:TIGR01825 161 S---YGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGeAGRGTVHHFGLEDKVDIQVGTLSKAIGV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  248 VGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITP 327
Cdd:TIGR01825 238 VGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITP 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969  328 VIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKLI 395
Cdd:TIGR01825 318 VVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVGKELGLI 385
 
Name Accession Description Interval E-value
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 9-395 0e+00

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: 688.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969    9 LEENINYLKENGLYNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLH 88
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   89 DELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAV 168
Cdd:TIGR01825  81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRENP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  169 EsgqYNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMG-KGAGTVKHFGLQDKIDFQIGTLSKAIGV 247
Cdd:TIGR01825 161 S---YGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGeAGRGTVHHFGLEDKVDIQVGTLSKAIGV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  248 VGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITP 327
Cdd:TIGR01825 238 VGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITP 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969  328 VIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKLI 395
Cdd:TIGR01825 318 VVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVGKELGLI 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 1-395 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 675.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   1 MVQSLHEFLEENINYLKENGLYNEIDTIEGANGPEIKI-NGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVR 79
Cdd:PRK06939   1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVaDGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  80 TINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDD 159
Cdd:PRK06939  81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 160 LRAKAKEAVESGQyNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQI 238
Cdd:PRK06939 161 LEAQLKEAKEAGA-RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEnGRGTVEHFGVMDRVDIIT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 239 GTLSKAI-GVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYD 317
Cdd:PRK06939 240 GTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFT 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969 318 TGESETPITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKLI 395
Cdd:PRK06939 320 LGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 5-391 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: 576.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   5 LHEFLEENINYLKENGLYNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGT 84
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  85 LDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKA 164
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 165 KEAvesGQYNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIGTLSK 243
Cdd:COG0156  161 KKA---RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGEtGRGLVEHFGLEDRVDIIMGTLSK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 244 AIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESET 323
Cdd:COG0156  238 ALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969 324 PITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKE 391
Cdd:COG0156  318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 41-389 1.49e-172

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: 485.14  E-value: 1.49e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  41 KSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISA 120
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 121 VMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAveSGQYNKVMYITDGVFSMDGDVAKLPEIVEIA 200
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--RRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 201 EEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIGTLSKAIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGD 279
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPhGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 280 TKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESE-TPITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTV 358
Cdd:cd06454  239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318

                        330       340       350
                 ....*....|....*....|....*....|.
gi 446172969 359 PRGTGRVRNMPTAAHTKDMLDEAIAAYEKVG 389
Cdd:cd06454  319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
44-384 1.99e-64

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 209.47  E-value: 1.99e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   44 INLSSNNYLGLatneDLKSAAKAAIDthgVGAGAVRTINGTLDLHDELEETLAKFKGT--------EAAIAYQSGFNCNM 115
Cdd:pfam00155   4 INLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGANI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  116 AAISAVM-NKNDAILSDELNHASIIDGCRLSKAKIIRVN-------HSDMDDLRAKAKEAVesgqynKVMYITdGVFSMD 187
Cdd:pfam00155  77 EALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP------KVVLHT-SPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  188 GDVAKLPEIVEIAE---EFGLLTYVDDAHGSGVMGKGAGTVKHFGLQDKIDFQI-GTLSKAIGVVG---GYVAGTKELID 260
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVvGSFSKAFGLAGwrvGYILGNAAVIS 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  261 WLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITPVIIGDEKTTQEFS 340
Cdd:pfam00155 230 QLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELA 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 446172969  341 KRLKDE-GVYVKSIVFPTVPrGTGRVrNMptAAHTKDMLDEAIAA 384
Cdd:pfam00155 310 QVLLEEvGVYVTPGSSPGVP-GWLRI-TV--AGGTEEELEELLEA 350
 
Name Accession Description Interval E-value
gly_Cac_T_rel TIGR01825
pyridoxal phosphate-dependent acyltransferase, putative; This model represents an enzyme ...
 9-395 0e+00

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: 688.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969    9 LEENINYLKENGLYNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLH 88
Cdd:TIGR01825   1 LRQDLNGLKENGLYISIRVLESAQGPRVRVNGKEVINLSSNNYLGFADHPRLKEAAAQAIQQYGVGAGAVRTIAGTLRLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   89 DELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAV 168
Cdd:TIGR01825  81 EELEEKLAKFKKTEAALVFQSGFNTNQGVLSALLRKGDIVLSDELNHASIIDGLRLTKATKKIYKHADMDDLDRVLRENP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  169 EsgqYNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMG-KGAGTVKHFGLQDKIDFQIGTLSKAIGV 247
Cdd:TIGR01825 161 S---YGKKLIVTDGVFSMDGDVAPLPEIVELAERYGAVTYVDDAHGSGVMGeAGRGTVHHFGLEDKVDIQVGTLSKAIGV 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  248 VGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITP 327
Cdd:TIGR01825 238 VGGYAAGHKELIEYLKNRARPFLFSTAQPPAVVAALAAAVDELQRSPELMERLWDNTRFFKAGLGKLGYDTGGSETPITP 317

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969  328 VIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKLI 395
Cdd:TIGR01825 318 VVIGDEKAAQEFSRRLFDEGIFAQSIVFPTVPRGTARIRNIPTAEHTKDDLDQALDAYEKVGKELGLI 385
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 1-395 0e+00

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 675.37  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   1 MVQSLHEFLEENINYLKENGLYNEIDTIEGANGPEIKI-NGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVR 79
Cdd:PRK06939   1 MSGAFYAQLREELEEIKAEGLYKEERVITSPQGADITVaDGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  80 TINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDD 159
Cdd:PRK06939  81 FICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMAD 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 160 LRAKAKEAVESGQyNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQI 238
Cdd:PRK06939 161 LEAQLKEAKEAGA-RHKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGEnGRGTVEHFGVMDRVDIIT 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 239 GTLSKAI-GVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYD 317
Cdd:PRK06939 240 GTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLEESDELRDRLWENARYFREGMTAAGFT 319

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969 318 TGESETPITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKLI 395
Cdd:PRK06939 320 LGPGEHPIIPVMLGDAKLAQEFADRLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGVI 397
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 5-391 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: 576.23  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   5 LHEFLEENINYLKENGLYNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGT 84
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGGSRLVSGT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  85 LDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKA 164
Cdd:COG0156   81 TPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 165 KEAvesGQYNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIGTLSK 243
Cdd:COG0156  161 KKA---RAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGEtGRGLVEHFGLEDRVDIIMGTLSK 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 244 AIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESET 323
Cdd:COG0156  238 ALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPELRERLWENIAYFREGLKELGFDLGPSES 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446172969 324 PITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKE 391
Cdd:COG0156  318 PIVPVIVGDAERALALADALLERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 41-389 1.49e-172

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: 485.14  E-value: 1.49e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  41 KSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISA 120
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 121 VMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAveSGQYNKVMYITDGVFSMDGDVAKLPEIVEIA 200
Cdd:cd06454   81 LAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREA--RRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 201 EEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIGTLSKAIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGD 279
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPhGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 280 TKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESE-TPITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTV 358
Cdd:cd06454  239 AAAALAALEVLQGGPERRERLQENVRYLRRGLKELGFPVGGSPsHIIPPLIGDDPAKAVAFSDALLERGIYVQAIRYPTV 318

                        330       340       350
                 ....*....|....*....|....*....|.
gi 446172969 359 PRGTGRVRNMPTAAHTKDMLDEAIAAYEKVG 389
Cdd:cd06454  319 PRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 3-384 6.83e-143

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 411.47  E-value: 6.83e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   3 QSLHEFLEENINYLKENGLYNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTIN 82
Cdd:PRK05958   1 MSWLDRLEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  83 GTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRA 162
Cdd:PRK05958  81 GNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 163 KAKEAVEsgqyNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKID-FQIGT 240
Cdd:PRK05958 161 LLAKWRA----GRALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPqGRGLAAEAGLAGEPDvILVGT 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 241 LSKAIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGE 320
Cdd:PRK05958 237 LGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPERRERLAALIARLRAGLRALGFQLMD 316

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446172969 321 SETPITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAA 384
Cdd:PRK05958 317 SQSAIQPLIVGDNERALALAAALQEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEA 380
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 27-386 1.75e-142

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: 409.35  E-value: 1.75e-142
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   27 TIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIA 106
Cdd:TIGR00858   2 PLDRGPGPEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  107 YQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAVESGQynkVMYITDGVFSM 186
Cdd:TIGR00858  82 FSSGYLANVGVISALVGKGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERR---KLIVTDGVFSM 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  187 DGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGL-QDKIDFQIGTLSKAIGVVGGYVAGTKELIDWLKA 264
Cdd:TIGR00858 159 DGDIAPLPQLVALAERYGAWLMVDDAHGTGVLGEdGRGTLEHFGLkPEPVDIQVGTLSKALGSYGAYVAGSQALIDYLIN 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  265 QSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITPVIIGDEKTTQEFSKRLK 344
Cdd:TIGR00858 239 RARTLIFSTALPPAVAAAALAALELIQEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 446172969  345 DEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYE 386
Cdd:TIGR00858 319 QQGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
PLN02483 PLN02483
serine palmitoyltransferase
 44-394 2.63e-79

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 252.38  E-value: 2.63e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  44 INLSSNNYLGLAT-NEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVM 122
Cdd:PLN02483 103 LNLGSYNYLGFAAaDEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALI 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 123 NKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAVESGQ------YNKVMYITDGVFSMDGDVAKLPEI 196
Cdd:PLN02483 183 GKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQprthrpWKKIIVIVEGIYSMEGELCKLPEI 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 197 VEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDK-IDFQIGTLSKAIGVVGGYVAGTKELIDWLKAQSRPFLFSTS 274
Cdd:PLN02483 263 VAVCKKYKAYVYLDEAHSIGAVGKtGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATS 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 275 LAPGDTKAITEAVKKLM--DSTELH----DKLWNNAQYLKNGLSKLGYDT-GESETPITPVIIGDEKTTQEFSKRLKDEG 347
Cdd:PLN02483 343 MSPPAVQQVISAIKVILgeDGTNRGaqklAQIRENSNFFRSELQKMGFEVlGDNDSPVMPIMLYNPAKIPAFSRECLKQN 422

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 446172969 348 VYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKL 394
Cdd:PLN02483 423 VAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 48-384 1.97e-77

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 245.15  E-value: 1.97e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  48 SNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNK--N 125
Cdd:PRK13392  53 SNDYLGMGQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLlpG 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 126 DAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLrakaKEAVESGQYNKVMYIT-DGVFSMDGDVAKLPEIVEIAEEFG 204
Cdd:PRK13392 133 CVILSDALNHASMIEGIRRSGAEKQVFRHNDLADL----EEQLASVDPDRPKLIAfESVYSMDGDIAPIEAICDLADRYN 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 205 LLTYVDDAHGSGVMG-KGAGTVKHFGLQDKIDFQIGTLSKAIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAI 283
Cdd:PRK13392 209 ALTYVDEVHAVGLYGaRGGGIAERDGLMDRIDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGA 288

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 284 TEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITPVIIGDEKTTQEFSKRL-KDEGVYVKSIVFPTVPRGT 362
Cdd:PRK13392 289 TAAIRHLKTSQTERDAHQDRVAALKAKLNANGIPVMPSPSHIVPVMVGDPTLCKAISDRLmSEHGIYIQPINYPTVPRGT 368

                        330       340
                 ....*....|....*....|..
gi 446172969 363 GRVRNMPTAAHTKDMLDEAIAA 384
Cdd:PRK13392 369 ERLRITPTPLHDDEDIDALVAA 390
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
44-384 1.99e-64

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 209.47  E-value: 1.99e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   44 INLSSNNYLGLatneDLKSAAKAAIDthgVGAGAVRTINGTLDLHDELEETLAKFKGT--------EAAIAYQSGFNCNM 115
Cdd:pfam00155   4 INLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLGRspvlkldrEAAVVFGSGAGANI 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  116 AAISAVM-NKNDAILSDELNHASIIDGCRLSKAKIIRVN-------HSDMDDLRAKAKEAVesgqynKVMYITdGVFSMD 187
Cdd:pfam00155  77 EALIFLLaNPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKP------KVVLHT-SPHNPT 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  188 GDVAKLPEIVEIAE---EFGLLTYVDDAHGSGVMGKGAGTVKHFGLQDKIDFQI-GTLSKAIGVVG---GYVAGTKELID 260
Cdd:pfam00155 150 GTVATLEELEKLLDlakEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVvGSFSKAFGLAGwrvGYILGNAAVIS 229

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  261 WLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGESETPITPVIIGDEKTTQEFS 340
Cdd:pfam00155 230 QLRKLARPFYSSTHLQAAAAAALSDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELA 309

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 446172969  341 KRLKDE-GVYVKSIVFPTVPrGTGRVrNMptAAHTKDMLDEAIAA 384
Cdd:pfam00155 310 QVLLEEvGVYVTPGSSPGVP-GWLRI-TV--AGGTEEELEELLEA 350
PLN02822 PLN02822
serine palmitoyltransferase
 27-393 2.49e-57

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 194.57  E-value: 2.49e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  27 TIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIA 106
Cdd:PLN02822  95 VLESAAGPHTIINGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSIL 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 107 YQSGFNCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAVESGQYNKVM--YI-TDGV 183
Cdd:PLN02822 175 YSYGLSTIFSVIPAFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAENKRKKKLrrYIvVEAI 254

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 184 FSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQ-DKIDFQIGTLSKAIGVVGGYVAGTKELIDW 261
Cdd:PLN02822 255 YQNSGQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKsGRGLSEHFGVPiEKIDIITAAMGHALATEGGFCTGSARVVDH 334

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 262 LKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKL-GYD-TGESETPItpVIIGDEKTTQEF 339
Cdd:PLN02822 335 QRLSSSGYVFSASLPPYLASAAITAIDVLEDNPSVLAKLKENIALLHKGLSDIpGLSiGSNTLSPI--VFLHLEKSTGSA 412

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 340 S-----------KRLKDEGVYVKSIVFPTV-----PRGtgrVRNMPTAAHTKDMLDEAIAAYEKVGKEMK 393
Cdd:PLN02822 413 KedlsllehiadRMLKEDSVLVVVSKRSTLdkcrlPVG---IRLFVSAGHTESDILKASESLKRVAASVL 479
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 46-384 1.64e-56

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 192.58  E-value: 1.64e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  46 LSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAV---- 121
Cdd:PLN02955 107 FSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVAIgsva 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 122 ----------MNKNDAILSDELNHASIIDGCRLSK----AKIIRVNHSDMDDLrakaKEAVESGQYNKVMYITDGVFSMD 187
Cdd:PLN02955 187 sllaasgkplKNEKVAIFSDALNHASIIDGVRLAErqgnVEVFVYRHCDMYHL----NSLLSSCKMKRKVVVTDSLFSMD 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 188 GDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIGTLSKAIGVVGGYVAGTKELIDWLKAQS 266
Cdd:PLN02955 263 GDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGEnGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQSRG 342

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 267 RPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKnGLSklGYDTGeseTPITPVIIGDEKTTQEFSKRLKDE 346
Cdd:PLN02955 343 RSFIFSTAIPVPMAAAAYAAVVVARKEKWRRKAIWERVKEFK-ALS--GVDIS---SPIISLVVGNQEKALKASRYLLKS 416

                        330       340       350
                 ....*....|....*....|....*....|....*...
gi 446172969 347 GVYVKSIVFPTVPRGTGRVRNMPTAAHTKDMLDEAIAA 384
Cdd:PLN02955 417 GFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITA 454
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
37-394 1.18e-48

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 169.80  E-value: 1.18e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  37 KINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGagavrTINGTLDLHDE-----LEETLAKFKGTEAAIAYQSGF 111
Cdd:PRK07179  50 KTPGPDAIILQSNDYLNLSGHPDIIKAQIAALQEEGDS-----LVMSAVFLHDDspkpqFEKKLAAFTGFESCLLCQSGW 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 112 NCNMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEavesgqYNKVMYITDGVFSMDGDVA 191
Cdd:PRK07179 125 AANVGLLQTIADPNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIER------HGPGIIVVDSVYSTTGTIA 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 192 KLPEIVEIAEEFGLLTYVDDAHGSGVMG-KGAGTVKHFGLQDKIDFQIGTLSKAIGVVGGYVAGTKELIDWLKAQSRPFL 270
Cdd:PRK07179 199 PLADIVDIAEEFGCVLVVDESHSLGTHGpQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAI 278

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 271 FSTSLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSKLGYDTGeSETPITPVIIGDEKTTQEFSKRLKDEGVYv 350
Cdd:PRK07179 279 FSSTLLPHEIAGLEATLEVIESADDRRARLHANARFLREGLSELGYNIR-SESQIIALETGSERNTEVLRDALEERNVF- 356

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 446172969 351 kSIVF--PTVPRGTGRVRNMPTAAHTKDMLDEAIAAYEKVGKEMKL 394
Cdd:PRK07179 357 -GAVFcaPATPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDL 401
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 44-387 6.64e-48

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 167.39  E-value: 6.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  44 INLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMN 123
Cdd:PLN03227   1 LNFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 124 KNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRAKAKEAVESGQYNKV-------MYITDGVFSMDGDVAKLPEI 196
Cdd:PLN03227  81 RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQVRAQDVALKRkptdqrrFLVVEGLYKNTGTLAPLKEL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 197 VEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIGTLS--KAIGVVGGYVAGTKELIDWLKAQSRPFLFST 273
Cdd:PLN03227 161 VALKEEFHYRLILDESFSFGTLGKsGRGSLEHAGLKPMVHAEIVTFSleNAFGSVGGMTVGSEEVVDHQRLSGSGYCFSA 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 274 SLAPGDTKAITEAVKKLMDSTELHDKLWNNAQYLKNGLSK-----------LGYDTGESETPITPVIIGDEKTTqefskR 342
Cdd:PLN03227 241 SAPPFLAKADATATAGELAGPQLLNRLHDSIANLYSTLTNsshpyalklrnRLVITSDPISPIIYLRLSDQEAT-----R 315

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446172969 343 LKDEGVYVKSIVFPTVPRGTGRV------------------RNMPTAAHTKDMLDEAIAAYEK 387
Cdd:PLN03227 316 RTDETLILDQIAHHSLSEGVAVVstgghvkkflqlvpppclRVVANASHTREDIDKLLTVLGE 378
PRK07505 PRK07505
hypothetical protein; Provisional
 18-376 3.09e-43

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 155.14  E-value: 3.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  18 ENGLyNEIDTIEGANGPEIKINGKSYINLSSNNYLGLATNEDLKSAAKAAIDTHGVGAGAVRTINGTLDLHDELEETLAK 97
Cdd:PRK07505  24 DEGL-NGLTVGEREGILITLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLHLSSSRTRVRSQILKDLEEALSE 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  98 FKGTEAaIAYQSGFNCNMAAI----SAVMNKNDAILS--DELNHAS--IIDGCRLSKAKIIRVNHSDMDDLRAKAKeave 169
Cdd:PRK07505 103 LFGASV-LTFTSCSAAHLGILpllaSGHLTGGVPPHMvfDKNAHASlnILKGICADETEVETIDHNDLDALEDICK---- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 170 sgQYNKVMYITDGVFSMdGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTV-KHFGLQ-DKIDFQIGTLSKAIG 246
Cdd:PRK07505 178 --TNKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKnGEGYVrSELDYRlNERTIIAASLGKAFG 254

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 247 VVGGYVA-GTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDS--TELHDKLWNNAQYLKnglSKLGYDTGESET 323
Cdd:PRK07505 255 ASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSEelDQLQQKLQNNIALFD---SLIPTEQSGSFL 331

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 446172969 324 PITPVIIGDEKTTQEFSKRLKDEGVYVKSIVFPTVPRGTGRVRNMPTAAHTKD 376
Cdd:PRK07505 332 PIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 44-359 1.44e-18

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 86.37  E-value: 1.44e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  44 INLSSNNYLGLATNEDLKSAAKAAIDTH-------GVGAGAVRTINGTLDLHDELEETLAKFKGTEAAIAYQSGFNCNMA 116
Cdd:PRK05937   7 IDFVTNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 117 AISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVNHSDMDDLRA--KAKEAVESGqynKVMYITDGVFSMDGDVAKLP 194
Cdd:PRK05937  87 LCAHLSSVTDYVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESllESCRQRSFG---RIFIFVCSVYSFKGTLAPLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 195 EIVEIAEEFGLLTYVDDAHGSGVMGK-GAGTVKHFGLQDKIDFQIgTLSKAIGVVGGYVAGTKELIDWLKAQSRPFLFST 273
Cdd:PRK05937 164 QIIALSKKYHAHLIVDEAHAMGIFGDdGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYST 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 274 SLAPGDTKAITEAVKKLMDSTEL-HDKLWNNAQYL--KNGLSKLGYdtgesetpITPVIIGDeKTTQEFSKRLKDEGVYV 350
Cdd:PRK05937 243 GLPPHLLISIQVAYDFLSQEGELaRKQLFRLKEYFaqKFSSAAPGC--------VQPIFLPG-ISEQELYSKLVETGIRV 313


                 ....*....
gi 446172969 351 KSIVFPTVP 359
Cdd:PRK05937 314 GVVCFPTGP 322
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 87-256 1.63e-13

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: 68.18  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  87 LHDELEETLAKF--KGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHASII-DGCRLSKAKIIRVNHSDMDDLRAK 163
Cdd:cd01494    1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYwVAAELAGAKPVPVPVDDAGYGGLD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 164 AKEAVES-GQYNKVMYITDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGKGagtvKHFGLQDKIDFQIGTLS 242
Cdd:cd01494   81 VAILEELkAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAP----GVLIPEGGADVVTFSLH 156

                        170
                 ....*....|....
gi 446172969 243 KAIGVVGGYVAGTK 256
Cdd:cd01494  157 KNLGGEGGGVVIVK 170
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 116-384 7.61e-12

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: 65.83  E-value: 7.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 116 AAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRV--NHSDMDDLRAKAKEAVESGQyNKVMYI------TDGVFSMD 187
Cdd:cd00609   74 LLLRALLNPGDEVLVPDPTYPGYEAAARLAGAEVVPVplDEEGGFLLDLELLEAAKTPK-TKLLYLnnpnnpTGAVLSEE 152

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 188 gdvaKLPEIVEIAEEFGLLTYVDDAHGSGVMGKGAGTVKHFGLQDKIDFQIGTLSKAIGVVG---GYVAGTK-ELIDWLK 263
Cdd:cd00609  153 ----ELEELAELAKKHGILIISDEAYAELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPeELLERLK 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 264 AQSRPFLFSTSLapgdtkAITEAVKKLMDS-----TELHDKLWNNAQYLKNGLSKLGYdtgesETPITPVI-------IG 331
Cdd:cd00609  229 KLLPYTTSGPST------LSQAAAAAALDDgeehlEELRERYRRRRDALLEALKELGP-----LVVVKPSGgfflwldLP 297

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 446172969 332 DEKTTQEFSKRLKDEGVYV-KSIVFPTVPRGTGRVrnmpTAAHTKDMLDEAIAA 384
Cdd:cd00609  298 EGDDEEFLERLLLEAGVVVrPGSAFGEGGEGFVRL----SFATPEEELEEALER 347
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 88-259 2.16e-08

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 55.29  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  88 HDELEETLAKFKGTEAAIAYQSGfncnMAAISAVMN----KNDAILS-DELNHASIIDGCRLSKAKIIRVNHSDMDDlRA 162
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSG----MAAISTVLLallkAGDHVVAsDDLYGGTYRLFERLLPKLGIEVTFVDPDD-PE 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 163 KAKEAVESGqyNKVMYItDGVFSMDGDVAKLPEIVEIAEEFGLLTYVDDAHGSGVMGK----GAGTVKHfglqdkidfqi 238
Cdd:cd00614  117 ALEAAIKPE--TKLVYV-ESPTNPTLKVVDIEAIAELAHEHGALLVVDNTFATPYLQRplelGADIVVH----------- 182

                        170       180
                 ....*....|....*....|....*
gi 446172969 239 gTLSKAIG----VVGGYVAGTKELI 259
Cdd:cd00614  183 -SATKYIGghsdVIAGVVVGSGEAL 206
PRK05968 PRK05968
hypothetical protein; Provisional
 90-279 3.57e-08

hypothetical protein; Provisional


Pssm-ID: 168320 [Multi-domain]  Cd Length: 389  Bit Score: 54.70  E-value: 3.57e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  90 ELEETLAKFKGTEAAIAYQSGfncnMAAIS----AVMNKNDAILSdeLNHAsIIDGCRL-------SKAKIIRVNHSDMD 158
Cdd:PRK05968  67 AFEEMLAKLEGAEDARGFASG----MAAISstvlSFVEPGDRIVA--VRHV-YPDAFRLfetilkrMGVEVDYVDGRDEE 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 159 DLRAKAKEAvesgqynKVMYI---TDGVFSMDgDVAKLpeiVEIAEEFGLLTYVDDAHGSGVMGKGagtvkhfgLQDKID 235
Cdd:PRK05968 140 AVAKALPGA-------KLLYLespTSWVFELQ-DVAAL---AALAKRHGVVTMIDNSWASPVFQRP--------ITLGVD 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 446172969 236 FQIGTLSKAIG----VVGGYVAGTKELIDWLKAQSRPFLfSTSLAPGD 279
Cdd:PRK05968 201 LVIHSASKYLGghsdTVAGVVAGSKEHIARINAEAYPYL-GAKLSPFE 247
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 86-214 6.42e-06

Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD corresponds to ornithine decarboxylase (ODC), arginine decarboxylase (ADC) and lysine decarboxylase (LDC). ODC is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. ADC catalyzes the decarboxylation of arginine and LDC catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life.


Pssm-ID: 99739 [Multi-domain]  Cd Length: 294  Bit Score: 47.63  E-value: 6.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  86 DLHD------ELEETLAKFKGTEAAIAYQSGFNC-NMAAISAVMNKNDAILSDELNHASIIDGCRLSKAKIIRVN---HS 155
Cdd:cd00615   53 DLLDptgpikEAQELAARAFGAKHTFFLVNGTSSsNKAVILAVCGPGDKILIDRNCHKSVINGLVLSGAVPVYLKperNP 132

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446172969 156 DMDDLRA----KAKEAVESGQYNKVMYITDGVFsmDGDVAKLPEIVEIAEEFGLLTYVDDAHG 214
Cdd:cd00615  133 YYGIAGGippeTFKKALIEHPDAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAHG 193
PRK06234 PRK06234
methionine gamma-lyase; Provisional
 90-313 1.56e-03

methionine gamma-lyase; Provisional


Pssm-ID: 168478 [Multi-domain]  Cd Length: 400  Bit Score: 40.20  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  90 ELEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDE---------LNHAsiidgcrLSK--AKIIRVNHSDMD 158
Cdd:PRK06234  68 EVENKLALLEGGEAAVVAASGMGAISSSLWSALKAGDHVVASDtlygctfalLNHG-------LTRygVEVTFVDTSNLE 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 159 DLRAKAKEAVE----SGQYNKVMYITDgvfsmdgdvakLPEIVEIAEEF--GLLTYVDDAHGSGVMGK----GAGTVKHF 228
Cdd:PRK06234 141 EVRNALKANTKvvylETPANPTLKVTD-----------IKAISNIAHENnkECLVFVDNTFCTPYIQRplqlGADVVVHS 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969 229 GLQdkidfqigTLSKAIGVVGGYVAGTKELIDWLKAQSRPFLFSTSLAPGDTKAITEAVKKLMDSTELHDKlwnNAQYLK 308
Cdd:PRK06234 210 ATK--------YLNGHGDVIAGFVVGKEEFINQVKLFGIKDMTGSVIGPFEAFLIIRGMKTLQIRMEKHCK---NAMKVA 278


                 ....*
gi 446172969 309 NGLSK 313
Cdd:PRK06234 279 KFLES 283
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
69-265 5.40e-03

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 38.35  E-value: 5.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969   69 DTHGVGAGAVRTINGTLDLHDE----------LEETLAKFKGTEAAIAYQSGFNCNMAAISAVMNKNDAILSDELNHaSI 138
Cdd:pfam01212   5 DTVTGPTPAMREAMAAAMVGDEvyggdptvnrLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAH-IH 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446172969  139 IDGCR----LSKAKIIRVNHS-----DMDDLRAKAKEAVESGQYN-KVMYITDGVFSMDGDVAKLPEIVEIAE---EFGL 205
Cdd:pfam01212  84 FDETGghaeLGGVQPRPLDGDeagnmDLEDLEAAIREVGADIFPPtGLISLENTHNSAGGQVVSLENLREIAAlarEHGI 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446172969  206 LTYVDDAH------GSGV----MGKGAGTVkhfglqdkidfQIGtLSKAIGV-VGGYVAGTKELIDWLKAQ 265
Cdd:pfam01212 164 PVHLDGARfanaavALGVivkeITSYADSV-----------TMC-LSKGLGApVGSVLAGSDDFIAKAIRQ 222
 
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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