NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|81895983|sp|Q8BG54|]
View 

RecName: Full=Serine palmitoyltransferase 3; AltName: Full=Long chain base biosynthesis protein 2b; Short=LCB2b; AltName: Full=Long chain base biosynthesis protein 3; Short=LCB 3; AltName: Full=Serine-palmityl-CoA transferase 3; Short=SPT 3

Protein Classification

PLP-dependent aminotransferase family protein( domain architecture ID 139552)

PLP-dependent aminotransferase family protein may combine pyridoxal phosphate with an alpha-amino acid to form a Schiff base or aldimine intermediate, which then acts as the substrate in a reaction such as a transamination, racemization, or decarboxylation

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 56-535 0e+00

Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).


The actual alignment was detected with superfamily member PLN02483:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 489  Bit Score: 591.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   56 QEAPLYVYVLTYMGYGIGILFGYLRDFMRNwgIEKCnaaVEREEQKDFVPLYQDFENFYKRNLYMRIRDSWSHTVCSAPE 135
Cdd:PLN02483   2 ITIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  136 PYMNVMEKVTDDYNWTFRHTGKViENIINMASYNYLGLAGKYDDSMVRVKDTLEKYGVGVASTRNEMGTLDIHKELEDLM 215
Cdd:PLN02483  77 AWFDVVERVSNDNNKTLKRTTKT-RRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  216 AEFLNVEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIIRGQPGT 295
Cdd:PLN02483 156 ARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  296 GRAWKKILIVVEGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDPEDIDVYMGTFTKSFSG 375
Cdd:PLN02483 236 HRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGS 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  376 SGGYIGGKKEIVDYLRMQSHSTTYATSMSPVVAAQLIRSLKITMGYEGNIGGMERIQQLKENIKYFRRRLKEMGFIIYGN 455
Cdd:PLN02483 316 CGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGD 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  456 DFSPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELGDLLNVKYFPLK 535
Cdd:PLN02483 396 NDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAE 475
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 56-535 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 591.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   56 QEAPLYVYVLTYMGYGIGILFGYLRDFMRNwgIEKCnaaVEREEQKDFVPLYQDFENFYKRNLYMRIRDSWSHTVCSAPE 135
Cdd:PLN02483   2 ITIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  136 PYMNVMEKVTDDYNWTFRHTGKViENIINMASYNYLGLAGKYDDSMVRVKDTLEKYGVGVASTRNEMGTLDIHKELEDLM 215
Cdd:PLN02483  77 AWFDVVERVSNDNNKTLKRTTKT-RRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  216 AEFLNVEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIIRGQPGT 295
Cdd:PLN02483 156 ARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  296 GRAWKKILIVVEGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDPEDIDVYMGTFTKSFSG 375
Cdd:PLN02483 236 HRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGS 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  376 SGGYIGGKKEIVDYLRMQSHSTTYATSMSPVVAAQLIRSLKITMGYEGNIGGMERIQQLKENIKYFRRRLKEMGFIIYGN 455
Cdd:PLN02483 316 CGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGD 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  456 DFSPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELGDLLNVKYFPLK 535
Cdd:PLN02483 396 NDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAE 475
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 160-524 6.89e-156

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: 449.70  E-value: 6.89e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 160 ENIINMASYNYLGLAgkyDDSMV--RVKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMN 237
Cdd:cd06454   1 KKVLNFCSNDYLGLA---NHPEVieAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 238 IPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIirgqpgtgRAWKKILIVVEGVYSMEGSIV 317
Cdd:cd06454  78 LSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 318 NLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRElFGLDPEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHST 397
Cdd:cd06454 150 PLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEE-FGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGF 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 398 TYATSMSPVVAAQLIRSLKITMgyegniGGMERIQQLKENIKYFRRRLKEMGFIIYGNDFSPVIPVLLYMPAKVSAFSRF 477
Cdd:cd06454 229 IFSTSLPPAVAAAALAALEVLQ------GGPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDA 302

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 81895983 478 LLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELG 524
Cdd:cd06454 303 LLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 162-525 1.62e-127

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: 378.63  E-value: 1.62e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 162 IINMASYNYLGLAgkyDDSMVR--VKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMNIP 239
Cdd:COG0156  39 VLNFSSNDYLGLA---NHPRVIeaAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 240 VFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAiirgqpgtgRAWKKILIVVEGVYSMEGSIVNL 319
Cdd:COG0156 116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMDGDIAPL 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 320 AQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDpEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHSTTY 399
Cdd:COG0156 187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 400 ATSMSPVVAAQLIRSLKItMGYEGniggmERIQQLKENIKYFRRRLKEMGFIIYGNDfSPVIPVLLYMPAKVSAFSRFLL 479
Cdd:COG0156 266 STALPPAVAAAALAALEI-LREEP-----ELRERLWENIAYFREGLKELGFDLGPSE-SPIVPVIVGDAERALALADALL 338

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 81895983 480 KKKISVVVVGFPATslPEGRA--RFSMSSAHTREMLDTVLEVVDELGD 525
Cdd:COG0156 339 ERGIYVSAIRPPTV--PKGTArlRITLSAAHTEEDIDRLLEALAEVGK 384
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
160-520 2.36e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.63  E-value: 2.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   160 ENIINMASYNYLGlagkydDSMVRVKDTLEKygVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMS--------FGMGF 231
Cdd:pfam00155   1 TDKINLGSNEYLG------DTLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGRSPVLKldreaavvFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   232 ATNAMNIP-VFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFK-------HNNAENLEKLLREAIIrgqpgtgrawkkiL 303
Cdd:pfam00155  73 GANIEALIfLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   304 IVVEGVYSMEGSIVNLAQ---IVALKKKYKAYLYIDEAHSIGCTGPTGRgVRELFGLDPEDIDVYMGTFTKSFSGSG--- 377
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   378 GYIGGKKEIVDYLRMQSHSTTYATSMSPVVAAQLIRSLKITMGYEgniggmERIQQLKENIKYFRRRLKEMGFIIYGNDf 457
Cdd:pfam00155 219 GYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELE------EMRQRIKERRDYLRDGLQAAGLSVLPSQ- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81895983   458 SPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATSlpEGRARFSMsSAHTREMLDTVLEVV 520
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPGV--PGWLRITV-AGGTEEELEELLEAI 351
 
Name Accession Description Interval E-value
PLN02483 PLN02483
serine palmitoyltransferase
 56-535 0e+00

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 591.74  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   56 QEAPLYVYVLTYMGYGIGILFGYLRDFMRNwgIEKCnaaVEREEQKDFVPLYQDFENFYKRNLYMRIRDSWSHTVCSAPE 135
Cdd:PLN02483   2 ITIPYLTALTTYFSYGLLFAFGQLRDFFRA--ILDW---WKTSNLQGYAPICLGLEDFYIRRLYLRIQDCFNRPIASAPD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  136 PYMNVMEKVTDDYNWTFRHTGKViENIINMASYNYLGLAGKYDDSMVRVKDTLEKYGVGVASTRNEMGTLDIHKELEDLM 215
Cdd:PLN02483  77 AWFDVVERVSNDNNKTLKRTTKT-RRCLNLGSYNYLGFAAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  216 AEFLNVEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIIRGQPGT 295
Cdd:PLN02483 156 ARFVGKPAAIVFGMGYATNSTIIPALIGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQIAEGQPRT 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  296 GRAWKKILIVVEGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDPEDIDVYMGTFTKSFSG 375
Cdd:PLN02483 236 HRPWKKIIVIVEGIYSMEGELCKLPEIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPADVDIMMGTFTKSFGS 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  376 SGGYIGGKKEIVDYLRMQSHSTTYATSMSPVVAAQLIRSLKITMGYEGNIGGMERIQQLKENIKYFRRRLKEMGFIIYGN 455
Cdd:PLN02483 316 CGGYIAGSKELIQYLKRTCPAHLYATSMSPPAVQQVISAIKVILGEDGTNRGAQKLAQIRENSNFFRSELQKMGFEVLGD 395

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  456 DFSPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELGDLLNVKYFPLK 535
Cdd:PLN02483 396 NDSPVMPIMLYNPAKIPAFSRECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAE 475
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 160-524 6.89e-156

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: 449.70  E-value: 6.89e-156
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 160 ENIINMASYNYLGLAgkyDDSMV--RVKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMN 237
Cdd:cd06454   1 KKVLNFCSNDYLGLA---NHPEVieAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGV 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 238 IPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIirgqpgtgRAWKKILIVVEGVYSMEGSIV 317
Cdd:cd06454  78 LSTLAGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREAR--------RPYGKKLIVTEGVYSMDGDIA 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 318 NLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRElFGLDPEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHST 397
Cdd:cd06454 150 PLPELVDLAKKYGAILFVDEAHSVGVYGPHGRGVEE-FGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGF 228

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 398 TYATSMSPVVAAQLIRSLKITMgyegniGGMERIQQLKENIKYFRRRLKEMGFIIYGNDFSPVIPVLLYMPAKVSAFSRF 477
Cdd:cd06454 229 IFSTSLPPAVAAAALAALEVLQ------GGPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDDPAKAVAFSDA 302

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*..
gi 81895983 478 LLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELG 524
Cdd:cd06454 303 LLERGIYVQAIRYPTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 162-525 1.62e-127

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: 378.63  E-value: 1.62e-127
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 162 IINMASYNYLGLAgkyDDSMVR--VKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMNIP 239
Cdd:COG0156  39 VLNFSSNDYLGLA---NHPRVIeaAAEALDRYGTGSGGSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVIS 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 240 VFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAiirgqpgtgRAWKKILIVVEGVYSMEGSIVNL 319
Cdd:COG0156 116 ALAGRGDLIFSDELNHASIIDGARLSGAKVVRFRHNDMDDLERLLKKA---------RAARRKLIVTDGVFSMDGDIAPL 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 320 AQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDpEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHSTTY 399
Cdd:COG0156 187 PEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLE-DRVDIIMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIF 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 400 ATSMSPVVAAQLIRSLKItMGYEGniggmERIQQLKENIKYFRRRLKEMGFIIYGNDfSPVIPVLLYMPAKVSAFSRFLL 479
Cdd:COG0156 266 STALPPAVAAAALAALEI-LREEP-----ELRERLWENIAYFREGLKELGFDLGPSE-SPIVPVIVGDAERALALADALL 338

                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 81895983 480 KKKISVVVVGFPATslPEGRA--RFSMSSAHTREMLDTVLEVVDELGD 525
Cdd:COG0156 339 ERGIYVSAIRPPTV--PKGTArlRITLSAAHTEEDIDRLLEALAEVGK 384
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 160-529 1.36e-95

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 297.11  E-value: 1.36e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  160 ENIINMASYNYLGLAgkyDDSMVR--VKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMN 237
Cdd:PRK06939  42 KEVINFCANNYLGLA---NHPELIaaAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  238 IPVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLREAIIRGQpgtgrawKKILIVVEGVYSMEGSIV 317
Cdd:PRK06939 119 FETLLGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGA-------RHKLIATDGVFSMDGDIA 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  318 NLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDpEDIDVYMGTFTKSFSG-SGGYIGGKKEIVDYLRMQSHS 396
Cdd:PRK06939 192 PLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVM-DRVDIITGTLGKALGGaSGGYTAGRKEVIDWLRQRSRP 270

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  397 TTYATSMSPVVAAQLIRSLKITMgyegniGGMERIQQLKENIKYFRRRLKEMGFIIYGNDfSPVIPVLLYMPAKVSAFSR 476
Cdd:PRK06939 271 YLFSNSLAPAIVAASIKVLELLE------ESDELRDRLWENARYFREGMTAAGFTLGPGE-HPIIPVMLGDAKLAQEFAD 343

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 81895983  477 FLLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELGDLLNV 529
Cdd:PRK06939 344 RLLEEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGV 396
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 160-524 1.72e-83

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 265.10  E-value: 1.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  160 ENIINMASYNYLGLAGkyDDSMVR-VKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMNI 238
Cdd:PRK05958  39 RRMLNFASNDYLGLAR--HPRLIAaAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVL 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  239 PVFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLReaiirgQPGTGRAWkkilIVVEGVYSMEGSIVN 318
Cdd:PRK05958 117 TALAGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLA------KWRAGRAL----IVTESVFSMDGDLAP 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  319 LAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDPEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHSTT 398
Cdd:PRK05958 187 LAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFI 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  399 YATSMSPVVAAQLIRSLKITMGYEgniggmERIQQLKENIKYFRRRLKEMGFIIyGNDFSPVIPVLLYMPAKVSAFSRFL 478
Cdd:PRK05958 267 FTTALPPAQAAAARAALRILRREP------ERRERLAALIARLRAGLRALGFQL-MDSQSAIQPLIVGDNERALALAAAL 339

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 81895983  479 LKKKISVVVVGFPatSLPEG--RARFSMSSAHTREMLDTVLEVVDELG 524
Cdd:PRK05958 340 QEQGFWVGAIRPP--TVPAGtsRLRITLTAAHTEADIDRLLEALAEAL 385
PLN02822 PLN02822
serine palmitoyltransferase
 162-468 1.00e-54

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 192.26  E-value: 1.00e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  162 IINMASYNYLGLAG--KYDDSMVrvkDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMNIP 239
Cdd:PLN02822 111 VVNFASANYLGLIGneKIKESCT---SALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIP 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  240 VFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLrEAIIRGQpgtgRAWKKI--LIVVEGVYSMEGSIV 317
Cdd:PLN02822 188 AFCKKGDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTL-EKLTAEN----KRKKKLrrYIVVEAIYQNSGQIA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  318 NLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDPEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHST 397
Cdd:PLN02822 263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81895983  398 TYATSMSPVVAAQLIRSLKItmgYEGNIGGMERiqqLKENIKYFRRRLKEM-GFIIYGNDFSPVIPVLLYMP 468
Cdd:PLN02822 343 VFSASLPPYLASAAITAIDV---LEDNPSVLAK---LKENIALLHKGLSDIpGLSIGSNTLSPIVFLHLEKS 408
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 152-525 9.16e-51

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 179.66  E-value: 9.16e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  152 FRHTGKVIENIINMASYNYLGLaGKYDDSMVRVKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGF 231
Cdd:PRK13392  38 RDHGPDGPRRVTIWCSNDYLGM-GQHPDVIGAMVDALDRYGAGAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  232 ATNAMNIPVFVGK--GCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLLrEAIIRGQPGtgrawkkiLIVVEGV 309
Cdd:PRK13392 117 VSNDAALSTLGKLlpGCVILSDALNHASMIEGIRRSGAEKQVFRHNDLADLEEQL-ASVDPDRPK--------LIAFESV 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  310 YSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLdPEDIDVYMGTFTKSFSGSGGYIGGKKEIVDY 389
Cdd:PRK13392 188 YSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGL-MDRIDMIQGTLAKAFGCLGGYIAASADLIDF 266

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  390 LRMQSHSTTYATSMSPVVAAQL---IRSLKITmgyegnigGMERiQQLKENIKYFRRRLKEMGFIIYGNDfSPVIPVLLY 466
Cdd:PRK13392 267 VRSFAPGFIFTTALPPAVAAGAtaaIRHLKTS--------QTER-DAHQDRVAALKAKLNANGIPVMPSP-SHIVPVMVG 336

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 81895983  467 MPAKVSAFSRFLLKKK-ISVVVVGFPatSLPEG--RARFSMSSAHTREMLDTVLEVVDELGD 525
Cdd:PRK13392 337 DPTLCKAISDRLMSEHgIYIQPINYP--TVPRGteRLRITPTPLHDDEDIDALVAALVAIWD 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
160-520 2.36e-45

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 163.63  E-value: 2.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   160 ENIINMASYNYLGlagkydDSMVRVKDTLEKygVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMS--------FGMGF 231
Cdd:pfam00155   1 TDKINLGSNEYLG------DTLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGRSPVLKldreaavvFGSGA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   232 ATNAMNIP-VFVGKGCLILSDEFNHTSVILGSRLSGAVIRPFK-------HNNAENLEKLLREAIIrgqpgtgrawkkiL 303
Cdd:pfam00155  73 GANIEALIfLLANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEKPK-------------V 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   304 IVVEGVYSMEGSIVNLAQ---IVALKKKYKAYLYIDEAHSIGCTGPTGRgVRELFGLDPEDIDVYMGTFTKSFSGSG--- 377
Cdd:pfam00155 140 VLHTSPHNPTGTVATLEElekLLDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVVGSFSKAFGLAGwrv 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   378 GYIGGKKEIVDYLRMQSHSTTYATSMSPVVAAQLIRSLKITMGYEgniggmERIQQLKENIKYFRRRLKEMGFIIYGNDf 457
Cdd:pfam00155 219 GYILGNAAVISQLRKLARPFYSSTHLQAAAAAALSDPLLVASELE------EMRQRIKERRDYLRDGLQAAGLSVLPSQ- 291

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81895983   458 SPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATSlpEGRARFSMsSAHTREMLDTVLEVV 520
Cdd:pfam00155 292 AGFFLLTGLDPETAKELAQVLLEEVGVYVTPGSSPGV--PGWLRITV-AGGTEEELEELLEAI 351
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 163-522 1.08e-44

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 162.77  E-value: 1.08e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  163 INMASYNYLGLAgkyDDSMVR--VKDTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNAMNIPV 240
Cdd:PLN03227   1 LNFATHDFLSTS---SSPTLRqtALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  241 FVGKGCLILSDEFNHTSVILGSRLSGAVIRPFKHNNAENLEKLL-----REAIIRGQPGTGRAWkkilIVVEGVYSMEGS 315
Cdd:PLN03227  78 FAKRGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraQDVALKRKPTDQRRF----LVVEGLYKNTGT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  316 IVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDP-EDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQS 394
Cdd:PLN03227 154 LAPLKELVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSG 233

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  395 HSTTYATSMSPVVAAQLIRSLkitmgyEGNIGGMERIQQLKENIKYFRRRLK----------EMGFIIYGNDFSPVIPVL 464
Cdd:PLN03227 234 SGYCFSASAPPFLAKADATAT------AGELAGPQLLNRLHDSIANLYSTLTnsshpyalklRNRLVITSDPISPIIYLR 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 81895983  465 LY-MPAK--------VSAFSRFLLKKKISVVVVGFPATSLPEGRA----RFSMSSAHTREMLDTVLEVVDE 522
Cdd:PLN03227 308 LSdQEATrrtdetliLDQIAHHSLSEGVAVVSTGGHVKKFLQLVPppclRVVANASHTREDIDKLLTVLGE 378
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
141-533 1.09e-37

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 143.61  E-value: 1.09e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  141 MEKVTDDYnWTFRHTGKVI-------ENIINMASYNYLGLAGKYDDSMVRVkDTLEKYGVGVAstrneMGTLDIHKE--- 210
Cdd:PRK07179  29 LDKYIEER-VNKNWNGKHLvlgktpgPDAIILQSNDYLNLSGHPDIIKAQI-AALQEEGDSLV-----MSAVFLHDDspk 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  211 --LEDLMAEFLNVEAVMSFGMGFATN--------AMNIPVFVgkgclilsDEFNHTSVILGSRLSGAVIRPFKHNNAENL 280
Cdd:PRK07179 102 pqFEKKLAAFTGFESCLLCQSGWAANvgllqtiaDPNTPVYI--------DFFAHMSLWEGVRAAGAQAHPFRHNDVDHL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  281 EKLLReaiiRGQPGtgrawkkiLIVVEGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRG-VRELfGLDp 359
Cdd:PRK07179 174 RRQIE----RHGPG--------IIVVDSVYSTTGTIAPLADIVDIAEEFGCVLVVDESHSLGTHGPQGAGlVAEL-GLT- 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  360 EDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHSTTYATSMSPVVAAQLIRSLKITmgyegnIGGMERIQQLKENIK 439
Cdd:PRK07179 240 SRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATLEVI------ESADDRRARLHANAR 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  440 YFRRRLKEMGFIIYGNdfSPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATslPEGRA--RFSMSSAHTREMLDTVL 517
Cdd:PRK07179 314 FLREGLSELGYNIRSE--SQIIALETGSERNTEVLRDALEERNVFGAVFCAPAT--PKNRNliRLSLNADLTASDLDRVL 389

                        410
                 ....*....|....*.
gi 81895983  518 EVVDELGDLLNVKYFP 533
Cdd:PRK07179 390 EVCREARDEVDLWFWK 405
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 169-530 4.25e-25

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 108.61  E-value: 4.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  169 NYLGLAGKYDDSMVRVKdTLEKYGVGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNaMNIPVFVG----- 243
Cdd:PLN02955 111 DYLGLSSHPTISNAAAN-AAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAAN-MAAMVAIGsvasl 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  244 ----------KGCLILSDEFNHTSVILGSRLS----GAVIRPFKHNNAENLEKLLREAIIrgqpgtgrawKKILIVVEGV 309
Cdd:PLN02955 189 laasgkplknEKVAIFSDALNHASIIDGVRLAerqgNVEVFVYRHCDMYHLNSLLSSCKM----------KRKVVVTDSL 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  310 YSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGVRELFGLDpEDIDVYMGTFTKSFSGSGGYIGGKKEIVDY 389
Cdd:PLN02955 259 FSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCE-ADVDLCVGTLSKAAGCHGGFIACSKKWKQL 337

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  390 LRMQSHSTTYATSMS-PVVAAQLIRSLKITMGYEGNIGGMERIQQLKEnikyfrrrlkemgfiIYGNDF-SPVIPVLLYM 467
Cdd:PLN02955 338 IQSRGRSFIFSTAIPvPMAAAAYAAVVVARKEKWRRKAIWERVKEFKA---------------LSGVDIsSPIISLVVGN 402

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 81895983  468 PAKVSAFSRFLLKKKISVVVVGFPATSLPEGRARFSMSSAHTREMLDTVLEVVDELGDLLNVK 530
Cdd:PLN02955 403 QEKALKASRYLLKSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALSSCLDFDNTA 465
PRK07505 PRK07505
hypothetical protein; Provisional
 143-525 2.76e-23

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 101.98  E-value: 2.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  143 KVTDDYNWTFRHT-GKvieNIINMASYNYLGLagKYDDSMVR-VKDTLEKYGVGVAST-RNEMgTLDIHKELEDLMAEFL 219
Cdd:PRK07505  31 TVGEREGILITLAdGH---TFVNFVSCSYLGL--DTHPAIIEgAVDALKRTGSLHLSSsRTRV-RSQILKDLEEALSELF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  220 NVEaVMSFGMGFATNAMNIPVFV------GKGCLILSDEFNHTS--VILGS-RLSGAVIRpFKHNNAENLEKLLREaiir 290
Cdd:PRK07505 105 GAS-VLTFTSCSAAHLGILPLLAsghltgGVPPHMVFDKNAHASlnILKGIcADETEVET-IDHNDLDALEDICKT---- 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  291 gqpgtgraWKKILIVVEGVYSMeGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRG-VRELFG--LDPEDIDVymG 367
Cdd:PRK07505 179 --------NKTVAYVADGVYSM-GGIAPVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyVRSELDyrLNERTIIA--A 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  368 TFTKSFSGSGGYIG-GKKEIVDYLRmqSHSTTYATSMSPVVA--------AQLIRSLKITmgyegniggmERIQQLKENI 438
Cdd:PRK07505 248 SLGKAFGASGGVIMlGDAEQIELIL--RYAGPLAFSQSLNVAalgailasAEIHLSEELD----------QLQQKLQNNI 315

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  439 KYFrrrlKEMGFIIYGNDFSPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPAtsLPEGRA--RFSMSSAHTREMLDTV 516
Cdd:PRK07505 316 ALF----DSLIPTEQSGSFLPIRLIYIGDEDTAIKAAKQLLDRGFYTSPVFFPV--VAKGRAglRIMFRASHTNDEIKRL 389


                 ....*....
gi 81895983  517 LEVVDELGD 525
Cdd:PRK07505 390 CSLLKEILD 398
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 193-405 1.27e-19

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 90.61  E-value: 1.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  193 VGVASTRNEMGTLDIHKELEDLMAEFLNVEAVMSFGMGFATNaMNIPVFVGKGC-LILSDEFNHTSVILGSRLSGAVIRP 271
Cdd:PRK05937  43 LGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN-LGLCAHLSSVTdYVLWDEQVHISVVYSLSVISGWHQS 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983  272 FKHNNAENLEKLLREAIIRGQpgtgrawKKILIVVEGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTGRGV 351
Cdd:PRK05937 122 FRHNDLDHLESLLESCRQRSF-------GRIFIFVCSVYSFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGF 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 81895983  352 RELFGLdpEDIDVYMGTFTKSFSGSGGYIGGKKEIVDYLRMQSHSTTYATSMSP 405
Cdd:PRK05937 195 CHSLGY--ENFYAVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPP 246
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 309-522 1.13e-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: 63.13  E-value: 1.13e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 309 VYSMEgsivNLAQIVALKKKYKAYLYIDEAHSigCTGPTGRGVRELFGLDPEDIDVYMGTFTKSFSGSG---GY-IGGKK 384
Cdd:cd00609 148 VLSEE----ELEELAELAKKHGILIISDEAYA--ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPE 221

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 385 EIVDYLRMQShstTYATSMSPVVAAQLIRSLkitmgYEGNIGGMERI-QQLKENIKYFRRRLKEMGFIIygndfsPVIP- 462
Cdd:cd00609 222 ELLERLKKLL---PYTTSGPSTLSQAAAAAA-----LDDGEEHLEELrERYRRRRDALLEALKELGPLV------VVKPs 287

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 81895983 463 ----VLLYMPAKVSA--FSRFLLKKKIsVVVVGFPATSLPEGRARFSMssAHTREMLDTVLEVVDE 522
Cdd:cd00609 288 ggffLWLDLPEGDDEefLERLLLEAGV-VVRPGSAFGEGGEGFVRLSF--ATPEEELEEALERLAE 350
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 208-383 1.04e-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: 57.78  E-value: 1.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 208 HKELEDLMAEFLN--VEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHTSVIL-GSRLSGAVIRPFKHNNAEnlekll 284
Cdd:cd01494   2 LEELEEKLARLLQpgNDKAVFVPSGTGANEAALLALLGPGDEVIVDANGHGSRYWvAAELAGAKPVPVPVDDAG------ 75

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 285 rEAIIRGQPGTGRAWKKI--LIVVEGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGctgptGRGVRELFGLDpEDI 362
Cdd:cd01494  76 -YGGLDVAILEELKAKPNvaLIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG-----ASPAPGVLIPE-GGA 148

                       170       180
                ....*....|....*....|..
gi 81895983 363 DVYMGTFTKSFSGSG-GYIGGK 383
Cdd:cd01494 149 DVVTFSLHKNLGGEGgGVVIVK 170
Beta_elim_lyase pfam01212
Beta-eliminating lyase;
210-452 5.03e-06

Beta-eliminating lyase;


Pssm-ID: 426128 [Multi-domain]  Cd Length: 288  Bit Score: 48.37  E-value: 5.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   210 ELEDLMAEFLNVEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHT------SVILgsrLSGAVIRPFKHNNA-----E 278
Cdd:pfam01212  36 RLEDRVAELFGKEAALFVPSGTAANQLALMAHCQRGDEVICGEPAHIhfdetgGHAE---LGGVQPRPLDGDEAgnmdlE 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   279 NLEKLLREAIIRGQPGTGrawkkiLIVVE--------GVYSMEgsivNLAQIVALKKKYKAYLYIDEAH------SIGCT 344
Cdd:pfam01212 113 DLEAAIREVGADIFPPTG------LISLEnthnsaggQVVSLE----NLREIAALAREHGIPVHLDGARfanaavALGVI 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   345 gptgrgVRELFgldpEDIDVYMGTFTKSFSGS-GGYIGGKKEIVDYLRMQSHstTYATSM--SPVVAAQLIRSLKItmgy 421
Cdd:pfam01212 183 ------VKEIT----SYADSVTMCLSKGLGAPvGSVLAGSDDFIAKAIRQRK--YLGGGLrqAGVLAAAGLRALEE---- 246

                         250       260       270
                  ....*....|....*....|....*....|.
gi 81895983   422 egnigGMERIQQLKENIKYFRRRLKEMGFII 452
Cdd:pfam01212 247 -----GVARLARDHATARRLAEGLELLRLAI 272
TA_like cd06502
Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP) ...
 210-523 3.47e-05

Low-specificity threonine aldolase (TA). This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). TA catalyzes the conversion of L-threonine or L-allo-threonine to glycine and acetaldehyde in a secondary glycine biosynthetic pathway.


Pssm-ID: 99748 [Multi-domain]  Cd Length: 338  Bit Score: 46.17  E-value: 3.47e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 210 ELEDLMAEFLNVEAVMSFGMGFATNAMNIPVFVGKGCLILSDEFNHTSVILG---SRLSGAVIRPFKHNNAENLEKLLRE 286
Cdd:cd06502  36 KLEARAAELFGKEAALFVPSGTAANQLALAAHTQPGGSVICHETAHIYTDEAgapEFLSGVKLLPVPGENGKLTPEDLEA 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 287 AIIRGQ----PGTGrawkkiLIVVE------GVYSMEgsivNLAQIVALKKKYKAYLYIDEAH------SIGCTgptgrg 350
Cdd:cd06502 116 AIRPRDdihfPPPS------LVSLEntteggTVYPLD----ELKAISALAKENGLPLHLDGARlanaaaALGVA------ 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 351 VRELfgldPEDIDVYMGTFTKSFSGSGGYI-GGKKEIV---DYLRMQSHSTtyaTSMSPVVAAQLIRSLKitmgyegNIG 426
Cdd:cd06502 180 LKTY----KSGVDSVSFCLSKGGGAPVGAVvVGNRDFIaraRRRRKQAGGG---MRQSGFLAAAGLAALE-------NDL 245

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 427 GMERIQQLKENIKYFRRRLKEMGfiiyGNDFSPVIPVLLYMPAKVSAFSRFLLKKKISVVVVGFPATSLPEGRARFSMSS 506
Cdd:cd06502 246 WLRRLRHDHEMARRLAEALEELG----GLESEVQTNIVLLDPVEANAVFVELSKEAIERRGEGVLFYAWGEGGVRFVTHW 321

                       330
                ....*....|....*..
gi 81895983 507 AHTREMLDTVLEVVDEL 523
Cdd:cd06502 322 DTTEEDVDELLSALKAV 338
Orn_deC_like cd00615
Ornithine decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 200-447 9.69e-05

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: 44.55  E-value: 9.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 200 NEMGTLD-------IHKELEDLMAEFLNVEAVmSFGMGFATNAMNIPV--FVGKGCLILSDEFNHTSVILGSRLSGAV-- 268
Cdd:cd00615  46 TELTGLDdlldptgPIKEAQELAARAFGAKHT-FFLVNGTSSSNKAVIlaVCGPGDKILIDRNCHKSVINGLVLSGAVpv 124

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 269 -IRPFKhNNAENL-----EKLLREAIIRGQpgtgraWKKILIVVEGVYsmEGSIVNLAQIVALKKKYKAYLYIDEAHsig 342
Cdd:cd00615 125 yLKPER-NPYYGIaggipPETFKKALIEHP------DAKAAVITNPTY--YGICYNLRKIVEEAHHRGLPVLVDEAH--- 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 343 ctgptgrGVRELFG--------LDPEDIDVY-----MGTFTKsfsgsGGYIGGKKEIVDYLRMQSHSTTYATSmSPVVaa 409
Cdd:cd00615 193 -------GAHFRFHpilpssaaMAGADIVVQsthktLPALTQ-----GSMIHVKGDLVNPDRVNEALNLHQST-SPSY-- 257

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 81895983 410 QLIRSLKITMGYEGNiGGMERIQQLKENIKYFRRRLKE 447
Cdd:cd00615 258 LILASLDVARAMMAL-EGKELVEELIELALYARQEINK 294
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
216-523 4.28e-04

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 42.82  E-value: 4.28e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 216 AEFLNVEA--VMSFGMGfATNAMNIPVF----VGKGCLILSDEFNHTSVILG----SRLSGAVIR--PFKHNNAENLEKL 283
Cdd:COG0520  69 ARFIGAASpdEIIFTRG-TTEAINLVAYglgrLKPGDEILITEMEHHSNIVPwqelAERTGAEVRviPLDEDGELDLEAL 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 284 lrEAIIRgqPGTgrawkKILIVVeGVYSMEGSIVNLAQIVALKKKYKAYLYIDEAHSIGCTGPTgrgVRELfgldpeDID 363
Cdd:COG0520 148 --EALLT--PRT-----KLVAVT-HVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPHLPVD---VQAL------GCD 208

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 364 VYmgtftkSFSG------SGgyIG---GKKEIVDYLR--MQSHSTTYATSMSPVVAAQLIRSLKI-TMGYEGNIG----- 426
Cdd:COG0520 209 FY------AFSGhklygpTG--IGvlyGKRELLEALPpfLGGGGMIEWVSFDGTTYADLPRRFEAgTPNIAGAIGlgaai 280

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 427 ------GMERIQQ-LKENIKYFRRRLKEM-GFIIYGN----DFSPVIPVLL--YMPAKVSAfsrFLLKKKISVVVVGFPA 492
Cdd:COG0520 281 dyleaiGMEAIEArERELTAYALEGLAAIpGVRILGPadpeDRSGIVSFNVdgVHPHDVAA---LLDDEGIAVRAGHHCA 357

                       330       340       350
                ....*....|....*....|....*....|....*.
gi 81895983 493 TSLP-----EGRARFSMSSAHTREMLDTVLEVVDEL 523
Cdd:COG0520 358 QPLMrrlgvPGTVRASFHLYNTEEEIDRLVEALKKL 393
OKR_DC_1 pfam01276
Orn/Lys/Arg decarboxylase, major domain;
195-465 8.94e-04

Orn/Lys/Arg decarboxylase, major domain;


Pssm-ID: 396025 [Multi-domain]  Cd Length: 417  Bit Score: 41.72  E-value: 8.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   195 VASTRNEMGTLDIH----KELEDLMAEFLNVEAVMSFGMGFATNAMNIPVFV-GKGCLILSDEFNHTSVILGSRLSGAV- 268
Cdd:pfam01276  51 VCIEDVELGDLLDHegaiKEAQKYAARVFGADKSYFVVNGTSGSNKTVGMAVcTPGDTILIDRNCHKSIHHALMLSGATp 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   269 --IRPfkHNNA----------ENLEKLLREAIIRGQPGTgraWKKILIVVEGVYsmEGSIVNLAQIVALKKKYKAYLYID 336
Cdd:pfam01276 131 vyLEP--SRNAygiiggiplhEFQEETLKEAIAEVPDAK---GPRLAVITNPTY--DGVLYNAKEIVDTLHHLSDPILFD 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983   337 EAHsIGCT--GPTGRGVRELFGLDPEDIDVYMGTFTKSFSGS---GGYIGGKKE-IVDYLRMQSHSTTYATSmSPVVAaq 410
Cdd:pfam01276 204 SAW-VGYEqfIPIYADASPMGGENENGPGIFVTQSVHKLLAAlsqASYIHKKEGhIVNHDRFNEAFMMHATT-SPSYP-- 279

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 81895983   411 LIRSLKITMGYEGNIGGMERIQQLKENIKYFRrrlKEMGFIIYGNDFSPVIPVLL 465
Cdd:pfam01276 280 IFASLDVAAKMLEGNSGRRLWNECVERAIEFR---KAIDTLNNCEFFRPWNPEIV 331
ARO8 COG1167
DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain ...
 354-486 1.16e-03

DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain [Transcription, Amino acid transport and metabolism]; DNA-binding transcriptional regulator, MocR family, contains an aminotransferase domain is part of the Pathway/BioSystem: Lysine biosynthesis


Pssm-ID: 440781 [Multi-domain]  Cd Length: 471  Bit Score: 41.74  E-value: 1.16e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 81895983 354 LFGLDPEDIDVYMGTFTKSFSGsG---GYIGGKKEIVDYLRMQSHSTTYATSMSP-VVAAQLIRSlkitmgyegniGGME 429
Cdd:COG1167 297 LAALDAPGRVIYIGSFSKTLAP-GlrlGYLVAPGRLIERLARLKRATDLGTSPLTqLALAEFLES-----------GHYD 364

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 81895983 430 RI-----QQLKENIKYFRRRLKEmgfiIYGNDFSPVIP-----VLLYMPAKVS--AFSRFLLKKKISVV 486
Cdd:COG1167 365 RHlrrlrREYRARRDLLLAALAR----HLPDGLRVTGPpgglhLWLELPEGVDaeALAAAALARGILVA 429
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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