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Conserved domains on  [gi|1697440459|ref|XP_029637260|]
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5-aminolevulinate synthase, nonspecific, mitochondrial isoform X1 [Octopus sinensis]

Protein Classification

Graphical summary

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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) ...
 182-585 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 TIGR01821:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 402  Bit Score: 625.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 182 FDYERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEeHHDLKQKKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGA 261
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQ-WHRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 262 GGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN 341
Cdd:TIGR01821  80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 342 HNDPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMD 421
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 422 LITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRndEGRMLRSKHQSNVKYLRDRLLE 501
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK--ESQDLRRAHQENVKRLKNLLEA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 502 IGIPAVQCPSHIIPIHIGDPKMATTICNELMSKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVWLSH 581
Cdd:TIGR01821 318 LGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRL 397


                  ....
gi 1697440459 582 DLPL 585
Cdd:TIGR01821 398 GLPL 401
Preseq_ALAS super family cl07589
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 7-83 1.31e-05

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


The actual alignment was detected with superfamily member pfam09029:

Pssm-ID: 462658  Cd Length: 114  Bit Score: 44.41  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459   7 CPFLTKFSVSYIRQHAPQVLSNINHCP--YAGSISHYSSSLQQQLESVTVGAAQAETV---------------VASKCPF 69
Cdd:pfam09029   7 CPFLSRVPQAFLQKARKSLLSYAQRCPvmMTRALSTSSANLQGEKEETPVAGPTAKQAkalplghpspqagqsVASKCPF 86

                          90
                  ....*....|....*
gi 1697440459  70 GAKE-DPPSSPKVRE 83
Cdd:pfam09029  87 LAAEmGQKNSNVVRK 101
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 182-585 0e+00

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 625.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 182 FDYERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEeHHDLKQKKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGA 261
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQ-WHRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 262 GGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN 341
Cdd:TIGR01821  80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 342 HNDPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMD 421
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 422 LITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRndEGRMLRSKHQSNVKYLRDRLLE 501
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK--ESQDLRRAHQENVKRLKNLLEA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 502 IGIPAVQCPSHIIPIHIGDPKMATTICNELMSKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVWLSH 581
Cdd:TIGR01821 318 LGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRL 397


                  ....
gi 1697440459 582 DLPL 585
Cdd:TIGR01821 398 GLPL 401
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 227-578 0e+00

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: 524.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCT 306
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 307 LGkhLPGVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKAD-PGIPKIVAFETVHSMSGAVCPLEELCDIA 385
Cdd:cd06454    81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 386 HKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTI 465
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 466 LAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGD-PKMATTICNELMsKHNIYVQAINY 544
Cdd:cd06454   239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1697440459 545 PTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVW 578
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 182-588 3.54e-177

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 507.08  E-value: 3.54e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 182 FDYERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEEHHDlKQKKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGA 261
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGP-DGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 262 GGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN 341
Cdd:PRK13392   81 GGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 342 HNDPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMD 421
Cdd:PRK13392  161 HNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRID 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 422 LITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLE 501
Cdd:PRK13392  241 MIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLNA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 502 IGIPAVQCPSHIIPIHIGDPKMATTICNELMSKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVWLSH 581
Cdd:PRK13392  319 NGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRL 398


                  ....*..
gi 1697440459 582 DLPLNPQ 588
Cdd:PRK13392  399 ELPRWRE 405
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 184-578 7.77e-165

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: 474.54  E-value: 7.77e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 184 YERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEEhhdlkqkKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGG 263
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG-------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 264 TRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKhlPGVQLFSDAGNHASMIQGIINSRAPKHIFNHN 343
Cdd:COG0156    74 SRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRHN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 344 DPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLI 423
Cdd:COG0156   152 DMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDII 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 424 TGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLEIG 503
Cdd:COG0156   232 MGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKELG 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1697440459 504 IPAVQCPSHIIPIHIGDPKMATTICNELMsKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVW 578
Cdd:COG0156   310 FDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
227-572 4.77e-64

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 214.09  E-value: 4.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMswhpVVKKAVREALEkhgAGAGGTRNISGNSPLHELLEKEIASLH--------NKEAALLFTSCYV 298
Cdd:pfam00155   1 TDKINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 299 ANDSTLCTLgKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN-------HNDPLHLEQLLRKAdpgiPKIVAFETVHSM 371
Cdd:pfam00155  74 ANIEALIFL-LANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 372 SGAVCPLEELCDIA---HKYGALTFVDEVHAVGLYGENGAgIGERDGVMHKMDLIT-GTLGKAFGNIG---GYVASTAQA 444
Cdd:pfam00155 149 TGTVATLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVvGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 445 IDMIRSYASGFIFTTSLPPTILAGATAAIriLRNDEGRMLRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGDPKMA 524
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDPL--LVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1697440459 525 TTICNELMSKHNIYVQAINYPTVPqgeEKLRVAPTpHHSRDMMDNFVD 572
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLE 349
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 7-83 1.31e-05

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 44.41  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459   7 CPFLTKFSVSYIRQHAPQVLSNINHCP--YAGSISHYSSSLQQQLESVTVGAAQAETV---------------VASKCPF 69
Cdd:pfam09029   7 CPFLSRVPQAFLQKARKSLLSYAQRCPvmMTRALSTSSANLQGEKEETPVAGPTAKQAkalplghpspqagqsVASKCPF 86

                          90
                  ....*....|....*
gi 1697440459  70 GAKE-DPPSSPKVRE 83
Cdd:pfam09029  87 LAAEmGQKNSNVVRK 101
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 182-585 0e+00

5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an enzyme for one of two routes to the heme precursor 5-aminolevulinate. The protein is a pyridoxal phosphate-dependent enzyme related to 2-amino-3-ketobutyrate CoA tranferase and 8-amino-7-oxononanoate synthase. This enzyme appears restricted to the alpha Proteobacteria and mitochondrial derivatives. [Biosynthesis of cofactors, prosthetic groups, and carriers, Heme, porphyrin, and cobalamin]


Pssm-ID: 273820 [Multi-domain]  Cd Length: 402  Bit Score: 625.60  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 182 FDYERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEeHHDLKQKKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGA 261
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQ-WHRPDGAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAGA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 262 GGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN 341
Cdd:TIGR01821  80 GGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIFR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 342 HNDPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMD 421
Cdd:TIGR01821 160 HNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRID 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 422 LITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRndEGRMLRSKHQSNVKYLRDRLLE 501
Cdd:TIGR01821 240 IIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLK--ESQDLRRAHQENVKRLKNLLEA 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 502 IGIPAVQCPSHIIPIHIGDPKMATTICNELMSKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVWLSH 581
Cdd:TIGR01821 318 LGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDRL 397


                  ....
gi 1697440459 582 DLPL 585
Cdd:TIGR01821 398 GLPL 401
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 227-578 0e+00

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: 524.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCT 306
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 307 LGkhLPGVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKAD-PGIPKIVAFETVHSMSGAVCPLEELCDIA 385
Cdd:cd06454    81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 386 HKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTI 465
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 466 LAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGD-PKMATTICNELMsKHNIYVQAINY 544
Cdd:cd06454   239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1697440459 545 PTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVW 578
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 182-588 3.54e-177

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 507.08  E-value: 3.54e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 182 FDYERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEEHHDlKQKKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGA 261
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGP-DGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAGA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 262 GGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN 341
Cdd:PRK13392   81 GGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVFR 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 342 HNDPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMD 421
Cdd:PRK13392  161 HNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRID 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 422 LITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLE 501
Cdd:PRK13392  241 MIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLNA 318

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 502 IGIPAVQCPSHIIPIHIGDPKMATTICNELMSKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVWLSH 581
Cdd:PRK13392  319 NGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDRL 398


                  ....*..
gi 1697440459 582 DLPLNPQ 588
Cdd:PRK13392  399 ELPRWRE 405
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 184-578 7.77e-165

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: 474.54  E-value: 7.77e-165
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 184 YERFFEQQIEKKKQNHSYRVFKKVLRKGEDFPFAEEhhdlkqkKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGG 263
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG-------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSGG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 264 TRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKhlPGVQLFSDAGNHASMIQGIINSRAPKHIFNHN 343
Cdd:COG0156    74 SRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRHN 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 344 DPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLI 423
Cdd:COG0156   152 DMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDII 231

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 424 TGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLEIG 503
Cdd:COG0156   232 MGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKELG 309

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1697440459 504 IPAVQCPSHIIPIHIGDPKMATTICNELMsKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINVW 578
Cdd:COG0156   310 FDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVG 383
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 233-578 4.59e-104

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 319.41  E-value: 4.59e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 233 CSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKhlP 312
Cdd:PRK05958   45 ASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAG--K 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 313 GVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKADPGiPKIVAFETVHSMSGAVCPLEELCDIAHKYGALT 392
Cdd:PRK05958  123 GDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 393 FVDEVHAVGLYGENGAGIGERDGVMHKMDLI-TGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATA 471
Cdd:PRK05958  202 LVDEAHGTGVLGPQGRGLAAEAGLAGEPDVIlVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARA 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 472 AIRILRNDEGRmlRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGDPKMATTICNELmSKHNIYVQAINYPTVPQGE 551
Cdd:PRK05958  282 ALRILRREPER--RERLAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAAAL-QEQGFWVGAIRPPTVPAGT 358

                         330       340
                  ....*....|....*....|....*..
gi 1697440459 552 EKLRVAPTPHHSRDMMDNFVDCLINVW 578
Cdd:PRK05958  359 SRLRITLTAAHTEADIDRLLEALAEAL 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 227-574 5.57e-101

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: 310.35  E-value: 5.57e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCT 306
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 307 LGKhlPGVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAH 386
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 387 KYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLI-TGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTI 465
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIqVGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 466 LAGATAAIRILRNDEGRmlRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGDPKMATTICNELMsKHNIYVQAINYP 545
Cdd:TIGR00858 254 AAAALAALELIQEEPWR--REKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ-QQGIFVGAIRPP 330

                         330       340
                  ....*....|....*....|....*....
gi 1697440459 546 TVPQGEEKLRVAPTPHHSRDMMDNFVDCL 574
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 225-577 5.01e-96

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 299.03  E-value: 5.01e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 225 QKKDITVW--------CSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSC 296
Cdd:PRK06939   32 QGADITVAdgkevinfCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSC 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 297 YVAND---STLctLGKHlpgVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKADPGIP--KIVAFETVHSM 371
Cdd:PRK06939  112 FDANGglfETL--LGKE---DAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGArhKLIATDGVFSM 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 372 SGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLITGTLGKAFGN-IGGYVASTAQAIDMIRS 450
Cdd:PRK06939  187 DGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALGGaSGGYTAGRKEVIDWLRQ 266

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 451 YASGFIFTTSLPPTILAGATAAIRILrnDEGRMLRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGDPKMATTICNE 530
Cdd:PRK06939  267 RSRPYLFSNSLAPAIVAASIKVLELL--EESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADR 344

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1697440459 531 LMsKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDNFVDCLINV 577
Cdd:PRK06939  345 LL-EEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLDRAIDAFEKV 390
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
227-572 4.77e-64

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 214.09  E-value: 4.77e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMswhpVVKKAVREALEkhgAGAGGTRNISGNSPLHELLEKEIASLH--------NKEAALLFTSCYV 298
Cdd:pfam00155   1 TDKINLGSNEYLGD----TLPAVAKAEKD---ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 299 ANDSTLCTLgKHLPGVQLFSDAGNHASMIQGIINSRAPKHIFN-------HNDPLHLEQLLRKAdpgiPKIVAFETVHSM 371
Cdd:pfam00155  74 ANIEALIFL-LANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 372 SGAVCPLEELCDIA---HKYGALTFVDEVHAVGLYGENGAgIGERDGVMHKMDLIT-GTLGKAFGNIG---GYVASTAQA 444
Cdd:pfam00155 149 TGTVATLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNLLVvGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 445 IDMIRSYASGFIFTTSLPPTILAGATAAIriLRNDEGRMLRSKHQSNVKYLRDRLLEIGIPAVQCPSHIIPIHIGDPKMA 524
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDPL--LVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1697440459 525 TTICNELMSKHNIYVQAINYPTVPqgeEKLRVAPTpHHSRDMMDNFVD 572
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLE 349
PLN02483 PLN02483
serine palmitoyltransferase
 234-569 3.09e-51

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 183.42  E-value: 3.09e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 234 SNDYVGM-SWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTL-GKhl 311
Cdd:PLN02483  107 SYNYLGFaAADEYCTPRVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALiGK-- 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 312 pGVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKA-DPGIPK--------IVAFETVHSMSGAVCPLEELC 382
Cdd:PLN02483  185 -GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiAEGQPRthrpwkkiIVIVEGIYSMEGELCKLPEIV 263

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 383 DIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHK-MDLITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSL 461
Cdd:PLN02483  264 AVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSM 343

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 462 PPTILAGATAAIRILRNDEG------RMLRSKHQSNvkYLRDRLLEIGIPAV-QCPSHIIPIHIGDPKMATTICNELMsK 534
Cdd:PLN02483  344 SPPAVQQVISAIKVILGEDGtnrgaqKLAQIRENSN--FFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECL-K 420

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1697440459 535 HNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDN 569
Cdd:PLN02483  421 QNVAVVVVGFPATPLLLARARICISASHSREDLIK 455
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 227-574 4.78e-50

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 179.87  E-value: 4.78e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCT 306
Cdd:PLN02955  102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 307 LG----------KHLPG--VQLFSDAGNHASMIQGII----NSRAPKHIFNHNDPLHLEQLLRKADPGiPKIVAFETVHS 370
Cdd:PLN02955  182 IGsvasllaasgKPLKNekVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 371 MSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLITGTLGKAFGNIGGYVASTAQAIDMIRS 450
Cdd:PLN02955  261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 451 YASGFIFTTSLPPTILAGATAAIRILRNDEGRmlRSKHQSNVKYLRDrlleigIPAVQCPSHIIPIHIGDPKMATTICNE 530
Cdd:PLN02955  341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKA------LSGVDISSPIISLVVGNQEKALKASRY 412

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1697440459 531 LMsKHNIYVQAINYPTVPQGEEKLRVAPTPHHS----RDMMDNFVDCL 574
Cdd:PLN02955  413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTtedvKKLITALSSCL 459
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
234-520 6.58e-48

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 172.50  E-value: 6.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 234 SNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKhlPG 313
Cdd:PRK07179   61 SNDYLNLSGHPDIIKAQIAALQEEGDSLVMSAVFLHDDSPKPQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAD--PN 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 314 VQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKADPGIpkiVAFETVHSMSGAVCPLEELCDIAHKYGALTF 393
Cdd:PRK07179  139 TPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPGI---IVVDSVYSTTGTIAPLADIVDIAEEFGCVLV 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 394 VDEVHAVGLYGENGAGIGERDGVMHKMDLITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTSLPPTILAGATAAI 473
Cdd:PRK07179  216 VDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPFVSYPAIFSSTLLPHEIAGLEATL 295

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1697440459 474 RILRNDEGRmlRSKHQSNVKYLRDRLLEIGIPaVQCPSHIIPIHIGD 520
Cdd:PRK07179  296 EVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIALETGS 339
PRK07505 PRK07505
hypothetical protein; Provisional
 197-577 3.86e-44

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 162.07  E-value: 3.86e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 197 QNHSYRVFKKVLRKGEDF-PFAEEHH--------------DLKQKKDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGA 261
Cdd:PRK07505    1 MQHKYRNNKKRINRAEKFwDAAYDEGlngltvgeregiliTLADGHTFVNFVSCSYLGLDTHPAIIEGAVDALKRTGSLH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 262 GGTRNISGNSPLHELLEKEIASLHNKEAaLLFTSCYVANDSTLCTLGK-HLPG----VQLFsDAGNHASM--IQGIINSR 334
Cdd:PRK07505   81 LSSSRTRVRSQILKDLEEALSELFGASV-LTFTSCSAAHLGILPLLASgHLTGgvppHMVF-DKNAHASLniLKGICADE 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 335 APKHIFNHNDPLHLEQLLRKAdpgipKIVAF--ETVHSMSGAVcPLEELCDIAHKYGALTFVDEVHAVGLYGENGAG--I 410
Cdd:PRK07505  159 TEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSMGGIA-PVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 411 GERDGVMHKMDLITGTLGKAFGNIGGYVA-STAQAIDMIRSYASGFIFTTSLPPTILAGATAAIRILRNDEGRMLRSKHQ 489
Cdd:PRK07505  233 SELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQ 312

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 490 SNVKYLrDRLLEIGIPAVQCPshIIPIHIGDPKMATTICNELMsKHNIYVQAINYPTVPQGEEKLRVAPTPHHSRDMMDN 569
Cdd:PRK07505  313 NNIALF-DSLIPTEQSGSFLP--IRLIYIGDEDTAIKAAKQLL-DRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKR 388


                  ....*...
gi 1697440459 570 FVDCLINV 577
Cdd:PRK07505  389 LCSLLKEI 396
PLN02822 PLN02822
serine palmitoyltransferase
 227-502 1.13e-33

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 134.10  E-value: 1.13e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 227 KDITVWCSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCT 306
Cdd:PLN02822  109 KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPA 188

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 307 LGKHlpGVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLLRKADPG------IPKIVAFETVHSMSGAVCPLEE 380
Cdd:PLN02822  189 FCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKLTAEnkrkkkLRRYIVVEAIYQNSGQIAPLDE 266

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 381 LCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGV-MHKMDLITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTT 459
Cdd:PLN02822  267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1697440459 460 SLPPTILAGATAAIRILRNDEGrmLRSKHQSNVKYLRDRLLEI 502
Cdd:PLN02822  347 SLPPYLASAAITAIDVLEDNPS--VLAKLKENIALLHKGLSDI 387
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 231-574 1.26e-32

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 129.64  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 231 VWCSNDYVGMSWHPVVKKAVREALEKHGAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTLGKH 310
Cdd:PLN03227    2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 311 lpGVQLFSDAGNHASMIQGIINSRAPKHIFNHNDPLHL----------EQLLRKADPGIPKIVAFETVHSMSGAVCPLEE 380
Cdd:PLN03227   82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLrrvleqvraqDVALKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 381 LCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGV--MHKMDLITGTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFT 458
Cdd:PLN03227  160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 459 TSLPPTILAGATAAIRILRNDEgRMLRSKHQsNVKYLRDRLLEIGIPAVQCP-----------SHIIPIHIGDpKMATTI 527
Cdd:PLN03227  240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSD-QEATRR 316

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 528 CNELMSKHNIY-----------VQAINYPTVPQG--EEKLRVAPTPHHSRDMMDNFVDCL 574
Cdd:PLN03227  317 TDETLILDQIAhhslsegvavvSTGGHVKKFLQLvpPPCLRVVANASHTREDIDKLLTVL 376
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 234-487 3.35e-27

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 113.34  E-value: 3.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 234 SNDYVGMSWHPVVKKAVREALEKH-------GAGAGGTRNISGNSPLHELLEKEIASLHNKEAALLFTSCYVANdSTLCT 306
Cdd:PRK05937   11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMAN-LGLCA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 307 lgkHLPGVQ--LFSDAGNHASMIQGIINSRAPKHIFNHNDPLHLEQLL---RKADPGipKIVAFE-TVHSMSGAVCPLEE 380
Cdd:PRK05937   90 ---HLSSVTdyVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLescRQRSFG--RIFIFVcSVYSFKGTLAPLEQ 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 381 LCDIAHKYGALTFVDEVHAVGLYGENGAGIGERDGVMHKMDLITgTLGKAFGNIGGYVASTAQAIDMIRSYASGFIFTTS 460
Cdd:PRK05937  165 IIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTG 243

                         250       260
                  ....*....|....*....|....*..
gi 1697440459 461 LPPTILAGATAAIRILrNDEGRMLRSK 487
Cdd:PRK05937  244 LPPHLLISIQVAYDFL-SQEGELARKQ 269
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 273-439 5.90e-12

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: 64.33  E-value: 5.90e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 273 LHELLEKEIASL--HNKEAALLFTSCYVANDSTLCTLGKhlPGVQLFSDAGNHASMIQGIINSRAPK-HIFNHND----P 345
Cdd:cd01494     1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAELAGAKpVPVPVDDagygG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 346 LHLEQLLRKADPGIPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVGLYGENGAGIGErdgvmHKMDLITG 425
Cdd:cd01494    79 LDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADVVTF 153

                         170
                  ....*....|....*
gi 1697440459 426 TLGKAF-GNIGGYVA 439
Cdd:cd01494   154 SLHKNLgGEGGGVVI 168
OAT_like cd00610
Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP) ...
 231-572 5.31e-09

Acetyl ornithine aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to ornithine aminotransferase, acetylornithine aminotransferase, alanine-glyoxylate aminotransferase, dialkylglycine decarboxylase, 4-aminobutyrate aminotransferase, beta-alanine-pyruvate aminotransferase, adenosylmethionine-8-amino-7-oxononanoate aminotransferase, and glutamate-1-semialdehyde 2,1-aminomutase. All the enzymes belonging to this family act on basic amino acids and their derivatives are involved in transamination or decarboxylation.


Pssm-ID: 99735 [Multi-domain]  Cd Length: 413  Bit Score: 58.35  E-value: 5.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 231 VWCSNdyVGMSwHPVVKKAVREALEK--HGAGAGGTRNisgnsPLHELLEKEIASLHNKEAALLFTSC-YVANDS----- 302
Cdd:cd00610    45 IGVLN--LGHN-HPEVVEALKEQLAKltHFSLGFFYNE-----PAVELAELLLALTPEGLDKVFFVNSgTEAVEAalkla 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 303 -------------------TLCTLGK--HLPGVQLFSDAGNHASMIQGiiNSRAPKHIFNHNDplhLEQLLRKADPGIPK 361
Cdd:cd00610   117 raytgrkkiisfegayhgrTLGALSLtgSKKYRGGFGPLLPGVLHVPY--PYRYRPPAELADD---LEALEEALEEHPEE 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 362 IVAF--ETVHSMSGAVCP----LEELCDIAHKYGALTFVDEVHA-VGLYGENGAgiGERDGVmhKMDLItgTLGKAFGN- 433
Cdd:cd00610   192 VAAVivEPIQGEGGVIVPppgyLKALRELCRKHGILLIADEVQTgFGRTGKMFA--FEHFGV--EPDIV--TLGKGLGGg 265

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 434 --IGGYVAStaQAIDMIRSYASGFIFTT-SLPPTILAGATAAIRILRnDEGRMLRSKHQSnvKYLRDRLLE--------- 501
Cdd:cd00610   266 lpLGAVLGR--EEIMDAFPAGPGLHGGTfGGNPLACAAALAVLEVLE-EEGLLENAAELG--EYLRERLRElaekhplvg 340

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1697440459 502 --------IGIPAVQCPSHIIPihigDPKMATTICNELMsKHNIYVQainyptvPQGEEKLRVAPTPHHSRDMMDNFVD 572
Cdd:cd00610   341 dvrgrglmIGIELVKDRATKPP----DKELAAKIIKAAL-ERGLLLR-------PSGGNVIRLLPPLIITEEEIDEGLD 407
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 341-512 1.89e-08

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 56.58  E-value: 1.89e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 341 NHNDPLHLEQLLRKADPGiPKIVAFETVHSMSGAVCP---LEELCDIAHKYGALTFVDEVHavGLYGENGAGIGERDGVM 417
Cdd:cd00609   115 EGGFLLDLELLEAAKTPK-TKLLYLNNPNNPTGAVLSeeeLEELAELAKKHGILIISDEAY--AELVYDGEPPPALALLD 191

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 418 HKMDLIT-GTLGKAFGNIG---GYVASTAQAIdmIRSYASGFIFTTSLPPTIlaGATAAIRILRNDEGRM--LRSKHQSN 491
Cdd:cd00609   192 AYERVIVlRSFSKTFGLPGlriGYLIAPPEEL--LERLKKLLPYTTSGPSTL--SQAAAAAALDDGEEHLeeLRERYRRR 267

                         170       180
                  ....*....|....*....|.
gi 1697440459 492 VKYLRDRLLEIGIPAVQCPSH 512
Cdd:cd00609   268 RDALLEALKELGPLVVVKPSG 288
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 268-395 3.91e-07

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: 52.59  E-value: 3.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 268 SGNsPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTL---GKHLpgvqLFSDAGNHASmiQGIINSRAPKHIFN--H 342
Cdd:cd00614    37 IGN-PTVDALEKKLAALEGGEAALAFSSGMAAISTVLLALlkaGDHV----VASDDLYGGT--YRLFERLLPKLGIEvtF 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1697440459 343 NDPLHLEQLLRKADPGiPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVD 395
Cdd:cd00614   110 VDPDDPEALEAAIKPE-TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
346-401 6.18e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.06  E-value: 6.18e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1697440459 346 LHLEQLLRKADPGiPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVG 401
Cdd:COG0520   142 LDLEALEALLTPR-TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
Aminotran_3 pfam00202
Aminotransferase class-III;
243-503 4.15e-06

Aminotransferase class-III;


Pssm-ID: 395148 [Multi-domain]  Cd Length: 397  Bit Score: 49.25  E-value: 4.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 243 HPVVKKAVREALEKhgaGAGGTRNISGNSPLHELLEKeIASLHNKEAALLFTSCYVANDSTLCTLGKHLPGVQ------- 315
Cdd:pfam00202  45 HPALVAAVKTQADK---LSHVSFGAFTNEPALDLAEK-LLKLTPGDRVFLMNSGSEANETAVKLARKWYREKGatgrtki 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 316 -------------LFSDAGNHASMIQGIINSRAPKHIFNHNDPLH---------LEQLLRKADPGIPKIVaFETVHSMSG 373
Cdd:pfam00202 121 iafsgafhgrtmgALSVTGSKPKYKTGFGPFLPGFPRLPYPDPEFlkeqrcleeLEALIAVKDDEVAAVI-VEPIQGEGG 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 374 AVCP----LEELCDIAHKYGALTFVDEVhAVGLyGENGAGIG-ERDGVmhKMDLItgTLGKAFGniGGYVASTAQAIDMI 448
Cdd:pfam00202 200 VNPPspgfLAGLRAICKKHGVLLIADEV-QTGF-GRTGKLFAhEHWGV--PPDIM--TFAKALT--GGFPLAATLGRAEV 271

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1697440459 449 -RSYASGFIFTTSLP-PTILAGATAAIRILRNDegrMLRSKHQSNVKYLRDRLLEIG 503
Cdd:pfam00202 272 mQAFAPGSHGGTFGGnPLACAAALATLEIIEDE---DLLQNAARLGAYLKEGLEDLQ 325
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 7-83 1.31e-05

5-aminolevulinate synthase presequence; The N terminal presequence domain found in 5-aminolevulinate synthase exists as an amphipathic helix, with a positively charged surface provided by lysine residues and no stable helix at the N-terminus. The domain is essential for the import process by which ALAS is transported into the mitochondria: translocase of the outer membrane (Tom) and translocase of the inner membrane protein complexes appear responsible for recognition and import through the mitochondrial membrane. The protein Tom20 is anchored to the mitochondrial outer membrane, and its interaction with presequences is thought to be the recognition step which allows subsequent import.


Pssm-ID: 462658  Cd Length: 114  Bit Score: 44.41  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459   7 CPFLTKFSVSYIRQHAPQVLSNINHCP--YAGSISHYSSSLQQQLESVTVGAAQAETV---------------VASKCPF 69
Cdd:pfam09029   7 CPFLSRVPQAFLQKARKSLLSYAQRCPvmMTRALSTSSANLQGEKEETPVAGPTAKQAkalplghpspqagqsVASKCPF 86

                          90
                  ....*....|....*
gi 1697440459  70 GAKE-DPPSSPKVRE 83
Cdd:pfam09029  87 LAAEmGQKNSNVVRK 101
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 344-541 5.73e-05

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


Pssm-ID: 425567 [Multi-domain]  Cd Length: 368  Bit Score: 45.70  E-value: 5.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 344 DPLHLEQLLRKAdpgiPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVDEVHAVG--------------------LY 403
Cdd:pfam00266 128 DLDELEKLITPK----TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIGhrpidvqklgvdflafsghkLY 203

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 404 GENGAGI--GeRDGVMHKMD-LITGtlgkafgniGGYVASTaqAIDMIRSYASGFIFTTSLPPTILA-GATAAIRILRND 479
Cdd:pfam00266 204 GPTGIGVlyG-RRDLLEKMPpLLGG---------GGMIETV--SLQESTFADAPWKFEAGTPNIAGIiGLGAALEYLSEI 271

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1697440459 480 EGRMLRSKHQSNVKYLRDRLLEIG---IPAVQCPSHII--PIHIGDPKMATTICNElmskHNIYVQA 541
Cdd:pfam00266 272 GLEAIEKHEHELAQYLYERLLSLPgirLYGPERRASIIsfNFKGVHPHDVATLLDE----SGIAVRS 334
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 268-395 7.85e-05

Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; Cystathionine beta-lyase/cystathionine gamma-synthase is part of the Pathway/BioSystem: Methionine biosynthesis


Pssm-ID: 440391 [Multi-domain]  Cd Length: 389  Bit Score: 45.43  E-value: 7.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697440459 268 SGNsPLHELLEKEIASLHNKEAALLFTSCYVANDSTLCTL---GKHLpgvqLFSDA---GNHAsmiqgIINSRAPK---- 337
Cdd:COG0626    55 YGN-PTRRALEEALAALEGGEAALAFASGMAAISAVLLALlkaGDHV----VASDDlygGTRR-----LLDKVLARfgie 124

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1697440459 338 -HIFNHNDPLHLEQLLRKAdpgiPKIVAFETVHSMSGAVCPLEELCDIAHKYGALTFVD 395
Cdd:COG0626   125 vTFVDPTDLAAVEAAIRPN----TKLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 344-401 1.35e-04

Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.


Pssm-ID: 99746 [Multi-domain]  Cd Length: 373  Bit Score: 44.38  E-value: 1.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1697440459 344 DPLHLEQLLRKAdpgiPKIVAFetVHsMS---GAVCPLEELCDIAHKYGALTFVDEVHAVG 401
Cdd:cd06453   128 DLEALEKLLTER----TKLVAV--TH-VSnvlGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
 
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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