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Conserved domains on  [gi|83977442|ref|NP_000023|]
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5-aminolevulinate synthase, erythroid-specific, mitochondrial isoform a precursor [Homo sapiens]

Protein Classification

PLP-dependent aminotransferase family protein; bifunctional SDR family oxidoreductase/aminotransferase class I/II-fold pyridoxal phosphate-dependent enzyme( domain architecture ID 10940224)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 143-548 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: 761.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   143 FSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASvaSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAG 222
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDG--AKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   223 AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF 302
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   303 RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI 382
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   383 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 462
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   463 DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA 542
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 83977442   543 VGLPLQ 548
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS super family cl07589
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 5-100 6.76e-14

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: 68.29  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442     5 AMLLQCCPVLARGPTSLLGKVVKThqFLFGIGRCPILATQGPNCSQIHL----KATKAGGDSPSWAK----GH------- 69
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLqgekEETPVAGPTAKQAKalplGHpspqagq 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 83977442    70 -----CPFMLSELQDGKSKIVQKAAPEVQEDVKAFK 100
Cdd:pfam09029  79 svaskCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 143-548 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: 761.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   143 FSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASvaSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAG 222
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDG--AKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   223 AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF 302
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   303 RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI 382
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   383 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 462
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   463 DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA 542
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 83977442   543 VGLPLQ 548
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 189-540 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: 530.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 189 KDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFT 268
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 269 LAkiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKS-NPKIPKIVAFETVHSMDGAICPLEELCDVS 347
Cdd:cd06454  81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 348 HQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMV 427
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 428 LSGALESVRLLKGeeGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVG-NAALNSKLCDLLLsKHGIYVQAINY 506
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRY 315

                       330       340       350
                ....*....|....*....|....*....|....
gi 83977442 507 PTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW 540
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 142-546 0e+00

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 522.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  142 VFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAqhFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGA 221
Cdd:PRK13392   1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRA--RDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  222 GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV 301
Cdd:PRK13392  79 GAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  302 FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK 381
Cdd:PRK13392 159 FRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  382 IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKgeEGQALRRAHQRNVKHMRQLL 461
Cdd:PRK13392 239 IDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  462 MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT 541
Cdd:PRK13392 317 NANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWD 396


                 ....*
gi 83977442  542 AVGLP 546
Cdd:PRK13392 397 RLELP 401
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 145-536 1.43e-171

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: 491.87  E-value: 1.43e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 145 YDQFFRDKIMEKKQDHTYRVFKTVNRWADAypfaqhfsEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAG 224
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGP--------RVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 225 GTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRH 304
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 305 NDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDI 384
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 385 ISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEgqALRRAHQRNVKHMRQLLMDR 464
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83977442 465 GLPVIPCPSHIIPIRVGNAALNSKLCDLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKL 536
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
189-536 5.72e-73

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 237.20  E-value: 5.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   189 KDVSVWCSNDYLGMSRhPQVLQATQEtlqrhgAGAGGTRNISGTSKFHVELEQELAELH--------QKDSALLFSSCFV 260
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   261 ANDSTLFTLAKiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFR-------HNDPDHLKKLLEKSnpkiPKIVAFETVHSM 333
Cdd:pfam00155  74 ANIEALIFLLA-NPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   334 DGAICPLEELC---DVSHQYGALTFVDEVHAVGLYGSRGAgIGERDGIMHKID-IISGTLGKAFGCVG---GYIASTRDL 406
Cdd:pfam00155 149 TGTVATLEELEkllDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   407 VDMVRSYAAGFIFTTSLPPMVLSGALESvrLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALN 486
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 83977442   487 SKLCDLLLSKHGIYVQAINYPTVPrgeELLRLAPSpHHSPQMMEDFVEKL 536
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 5-100 6.76e-14

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: 68.29  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442     5 AMLLQCCPVLARGPTSLLGKVVKThqFLFGIGRCPILATQGPNCSQIHL----KATKAGGDSPSWAK----GH------- 69
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLqgekEETPVAGPTAKQAKalplGHpspqagq 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 83977442    70 -----CPFMLSELQDGKSKIVQKAAPEVQEDVKAFK 100
Cdd:pfam09029  79 svaskCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 143-548 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: 761.58  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   143 FSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAQHFSEASvaSKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAG 222
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPDG--AKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   223 AGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFVF 302
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   303 RHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKI 382
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   383 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 462
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   463 DRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTA 542
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 83977442   543 VGLPLQ 548
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 189-540 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: 530.60  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 189 KDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFT 268
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 269 LAkiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKS-NPKIPKIVAFETVHSMDGAICPLEELCDVS 347
Cdd:cd06454  81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREArRPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 348 HQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMV 427
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 428 LSGALESVRLLKGeeGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVG-NAALNSKLCDLLLsKHGIYVQAINY 506
Cdd:cd06454 239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRY 315

                       330       340       350
                ....*....|....*....|....*....|....
gi 83977442 507 PTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAW 540
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 142-546 0e+00

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 522.11  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  142 VFSYDQFFRDKIMEKKQDHTYRVFKTVNRWADAYPFAqhFSEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGA 221
Cdd:PRK13392   1 MMNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRA--RDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  222 GAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKILPGCEIYSDAGNHASMIQGIRNSGAAKFV 301
Cdd:PRK13392  79 GAGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  302 FRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK 381
Cdd:PRK13392 159 FRHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDR 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  382 IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKgeEGQALRRAHQRNVKHMRQLL 461
Cdd:PRK13392 239 IDMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKL 316

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  462 MDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLSKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWT 541
Cdd:PRK13392 317 NANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWD 396


                 ....*
gi 83977442  542 AVGLP 546
Cdd:PRK13392 397 RLELP 401
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 145-536 1.43e-171

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: 491.87  E-value: 1.43e-171
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 145 YDQFFRDKIMEKKQDHTYRVFKTVNRWADAypfaqhfsEASVASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAG 224
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGP--------RVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 225 GTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRH 304
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 305 NDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDI 384
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 385 ISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEgqALRRAHQRNVKHMRQLLMDR 464
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 83977442 465 GLPVIPCPSHIIPIRVGNAALNSKLCDLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKL 536
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEAL 379
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 195-536 1.61e-107

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 327.89  E-value: 1.61e-107
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  195 CSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKilP 274
Cdd:PRK05958  45 ASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAG--K 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  275 GCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKiPKIVAFETVHSMDGAICPLEELCDVSHQYGALT 354
Cdd:PRK05958 123 GDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWL 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  355 FVDEVHAVGLYGSRGAGIGERDGIMHKIDIIS-GTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALE 433
Cdd:PRK05958 202 LVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILvGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARA 281

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  434 SVRLLKGEEGqalRRAH-QRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGN--AALN-SKLCDlllsKHGIYVQAINYPTV 509
Cdd:PRK05958 282 ALRILRREPE---RRERlAALIARLRAGLRALGFQLMDSQSAIQPLIVGDneRALAlAAALQ----EQGFWVGAIRPPTV 354

                        330       340
                 ....*....|....*....|....*..
gi 83977442  510 PRGEELLRLAPSPHHSPQMMEDFVEKL 536
Cdd:PRK05958 355 PAGTSRLRITLTAAHTEADIDRLLEAL 381
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 194-536 7.35e-102

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: 312.66  E-value: 7.35e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   194 WCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKil 273
Cdd:TIGR00858  21 FSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISALVG-- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   274 PGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGAL 353
Cdd:TIGR00858  99 KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAERYGAW 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   354 TFVDEVHAVGLYGSRGAGIGERDGIMHKIDIIS-GTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGAL 432
Cdd:TIGR00858 179 LMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAVAAAAL 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   433 ESVRLLkgEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNsklcdLLLSKH----GIYVQAINYPT 508
Cdd:TIGR00858 259 AALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASA-----LALAEElqqqGIFVGAIRPPT 331

                         330       340
                  ....*....|....*....|....*...
gi 83977442   509 VPRGEELLRLAPSPHHSPQMMEDFVEKL 536
Cdd:TIGR00858 332 VPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 144-544 3.02e-101

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 312.52  E-value: 3.02e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  144 SYDQFFRDKIMEKKQDHTY---RVFKTVNRwadaypfaqhfSEASVAS-KDVSVWCSNDYLGMSRHPQVLQATQETLQRH 219
Cdd:PRK06939   4 AFYAQLREELEEIKAEGLYkeeRVITSPQG-----------ADITVADgKEVINFCANNYLGLANHPELIAAAKAALDSH 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  220 GAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVAND---STLFTlakilPGCEIYSDAGNHASMIQGIRNSG 296
Cdd:PRK06939  73 GFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGglfETLLG-----KEDAIISDALNHASIIDGVRLCK 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  297 AAKFVFRHNDPDHLKKLLEKSNPKIP--KIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGE 374
Cdd:PRK06939 148 AKRYRYANNDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVE 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  375 RDGIMHKIDIISGTLGKAF-GCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLkgEEGQALRRAHQRN 453
Cdd:PRK06939 228 HFGVMDRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELL--EESDELRDRLWEN 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  454 VKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALNSKLCDLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMmedfV 533
Cdd:PRK06939 306 ARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLL-EEGVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----L 380

                        410
                 ....*....|.
gi 83977442  534 EKLLLAWTAVG 544
Cdd:PRK06939 381 DRAIDAFEKVG 391
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
189-536 5.72e-73

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 237.20  E-value: 5.72e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   189 KDVSVWCSNDYLGMSRhPQVLQATQEtlqrhgAGAGGTRNISGTSKFHVELEQELAELH--------QKDSALLFSSCFV 260
Cdd:pfam00155   1 TDKINLGSNEYLGDTL-PAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLgrspvlklDREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   261 ANDSTLFTLAKiLPGCEIYSDAGNHASMIQGIRNSGAAKFVFR-------HNDPDHLKKLLEKSnpkiPKIVAFETVHSM 333
Cdd:pfam00155  74 ANIEALIFLLA-NPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   334 DGAICPLEELC---DVSHQYGALTFVDEVHAVGLYGSRGAgIGERDGIMHKID-IISGTLGKAFGCVG---GYIASTRDL 406
Cdd:pfam00155 149 TGTVATLEELEkllDLAKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   407 VDMVRSYAAGFIFTTSLPPMVLSGALESvrLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPSHIIPIRVGNAALN 486
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 83977442   487 SKLCDLLLSKHGIYVQAINYPTVPrgeELLRLAPSpHHSPQMMEDFVEKL 536
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 188-539 2.36e-56

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 197.20  E-value: 2.36e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  188 SKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLF 267
Cdd:PLN02955 101 FKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMV 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  268 TL---AKILPGCE---------IYSDAGNHASMIQGIR---NSGAAK-FVFRHNDPDHLKKLLekSNPKIP-KIVAFETV 330
Cdd:PLN02955 181 AIgsvASLLAASGkplknekvaIFSDALNHASIIDGVRlaeRQGNVEvFVYRHCDMYHLNSLL--SSCKMKrKVVVTDSL 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  331 HSMDGAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMV 410
Cdd:PLN02955 259 FSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLI 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  411 RSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQalRRAHQRNVKHMRQLlmdRGLPVipcPSHIIPIRVGNAALNSKLC 490
Cdd:PLN02955 339 QSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKAS 410

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 83977442  491 DLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSpqmMEDfVEKLLLA 539
Cdd:PLN02955 411 RYLL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHT---TED-VKKLITA 454
PLN02483 PLN02483
serine palmitoyltransferase
 196-530 5.03e-55

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 193.83  E-value: 5.03e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  196 SNDYLGMSRH-----PQVLqatqETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLa 270
Cdd:PLN02483 107 SYNYLGFAAAdeyctPRVI----ESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  271 kILPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKS----NPKIPK-----IVAFETVHSMDGAICPLE 341
Cdd:PLN02483 182 -IGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegQPRTHRpwkkiIVIVEGIYSMEGELCKLP 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  342 ELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHK-IDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 420
Cdd:PLN02483 261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYA 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  421 TSLPPMVLSGALESVRLLKGEEG-----QALRRAHQrNVKHMRQLLMDRGLPVI-PCPSHIIPIRVGNAALNSKLCDLLL 494
Cdd:PLN02483 341 TSMSPPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECL 419

                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 83977442  495 sKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMME 530
Cdd:PLN02483 420 -KQNVAVVVVGFPATPLLLARARICISASHSREDLI 454
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
196-547 1.10e-46

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 169.03  E-value: 1.10e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  196 SNDYLGMSRHPQVLQATQETLQRHGAG----AGGTRNISGTSKFhvelEQELAELHQKDSALLFSSCFVANDSTLFTLAK 271
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  272 ilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEKSNPKIpkiVAFETVHSMDGAICPLEELCDVSHQYG 351
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPGI---IVVDSVYSTTGTIAPLADIVDIAEEFG 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  352 ALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVGGYIASTRDLVDMVR--SYAAgfIFTTSLPPMVLS 429
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  430 GALESVRLLKGEEGqalRRAH-QRNVKHMRQLLMDRGLPvIPCPSHIIPIRVGNAALNSKLCDLLLSKhGIYVQAINYPT 508
Cdd:PRK07179 290 GLEATLEVIESADD---RRARlHANARFLREGLSELGYN-IRSESQIIALETGSERNTEVLRDALEER-NVFGAVFCAPA 364

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 83977442  509 VPRGEELLRLAPSPHHSPQMMEDFVEKLLLAWTAVGLPL 547
Cdd:PRK07179 365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 193-467 1.02e-37

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 143.89  E-value: 1.02e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  193 VWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKi 272
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  273 lPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLEK----------SNPKIPKIVAFETVHSMDGAICPLEE 342
Cdd:PLN03227  81 -RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  343 LCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGI--MHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 420
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 83977442  421 TSLPPMVLSGALESVRLLKGEEgQALRRAHQrNVKHMRQLLMDRGLP 467
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHP 284
PLN02822 PLN02822
serine palmitoyltransferase
 186-511 2.91e-36

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 141.42  E-value: 2.91e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  186 VASKDVSVWCSNDYLGMSRHPQVLQATQETLQRHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSScfvandsT 265
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSY-------G 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  266 LFTLAKILPG-CE----IYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLE------KSNPKIPKIVAFETVHSMD 334
Cdd:PLN02822 179 LSTIFSVIPAfCKkgdiIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenKRKKKLRRYIVVEAIYQNS 258

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  335 GAICPLEELCDVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGI-MHKIDIISGTLGKAFGCVGGYIASTRDLVDMVRSY 413
Cdd:PLN02822 259 GQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLS 338

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  414 AAGFIFTTSLPPMVLSGALESVRLLKgEEGQALRRAHQrNVKHMRQLLMD-RGLPVIPCP-SHIIPIRV----GNAALNS 487
Cdd:PLN02822 339 SSGYVFSASLPPYLASAAITAIDVLE-DNPSVLAKLKE-NIALLHKGLSDiPGLSIGSNTlSPIVFLHLekstGSAKEDL 416

                        330       340
                 ....*....|....*....|....*...
gi 83977442  488 KL----CDLLLSKHGIYVQAINYPTVPR 511
Cdd:PLN02822 417 SLlehiADRMLKEDSVLVVVSKRSTLDK 444
PRK07505 PRK07505
hypothetical protein; Provisional
 195-536 3.46e-35

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 137.03  E-value: 3.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  195 CSNDYLGMSRHPQVLQATQETLQRHGagaggTRNISgTSKFHV------ELEQELAELHQKDsALLFSSCFVANDSTLFT 268
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELFGAS-VLTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  269 LAK-ILPGCE---IYSDAGNHASM--IQGIrnsgAAKF--VFR--HNDPDHLKKLleKSNPKIPKIVAfETVHSMDGAIc 338
Cdd:PRK07505 125 LASgHLTGGVpphMVFDKNAHASLniLKGI----CADEteVETidHNDLDALEDI--CKTNKTVAYVA-DGVYSMGGIA- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  339 PLEELCDVSHQYGALTFVDEVHAVGLYGSRGAG--IGERDGIMHKIDIISGTLGKAFGCVGGYIA-STRDLVDMVRSYAA 415
Cdd:PRK07505 197 PVKELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAG 276

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  416 GFIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMD--RGLPVipcpshiiPIR---VGNAALNSKLC 490
Cdd:PRK07505 277 PLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRliyIGDEDTAIKAA 348

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*.
gi 83977442  491 DLLLsKHGIYVQAINYPTVPRGEELLRLAPSPHHSPQMMEDFVEKL 536
Cdd:PRK07505 349 KQLL-DRGFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 196-428 4.84e-27

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 112.95  E-value: 4.84e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  196 SNDYLGMSRHPQVLQATQETLQRH-------GAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFT 268
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  269 LAKILPgcEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPDHLKKLLE----KSNPKIPKIVAfeTVHSMDGAICPLEELC 344
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscrqRSFGRIFIFVC--SVYSFKGTLAPLEQII 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442  345 DVSHQYGALTFVDEVHAVGLYGSRGAGIGERDGIMHKIDIISgTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLP 424
Cdd:PRK05937 167 ALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLP 245


                 ....
gi 83977442  425 PMVL 428
Cdd:PRK05937 246 PHLL 249
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 235-398 4.24e-17

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: 78.96  E-value: 4.24e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 235 FHVELEQELAELHQK--DSALLFSSCFVANDSTLFTLAKilPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPD---- 308
Cdd:cd01494   1 KLEELEEKLARLLQPgnDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAgygg 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 309 -HLKKLLEKSNPKIPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVGlyGSRGAGIGERDGimhKIDIISG 387
Cdd:cd01494  79 lDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG--ASPAPGVLIPEG---GADVVTF 153

                       170
                ....*....|.
gi 83977442 388 TLGKAFGCVGG 398
Cdd:cd01494 154 SLHKNLGGEGG 164
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 5-100 6.76e-14

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: 68.29  E-value: 6.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442     5 AMLLQCCPVLARGPTSLLGKVVKThqFLFGIGRCPILATQGPNCSQIHL----KATKAGGDSPSWAK----GH------- 69
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLqgekEETPVAGPTAKQAKalplGHpspqagq 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 83977442    70 -----CPFMLSELQDGKSKIVQKAAPEVQEDVKAFK 100
Cdd:pfam09029  79 svaskCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 206-363 9.83e-08

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: 54.18  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   206 PQVLQATQETLqRHGAGAGGtrniSGTSKFHVELEQELAELHQKDSALLFSScfvANDSTLFT--------------LAK 271
Cdd:pfam00266  13 QEVLDAIQEYY-TDYNGNVH----RGVHTLGKEATQAYEEAREKVAEFINAP---SNDEIIFTsgtteainlvalslGRS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442   272 ILPGCEI-YSDAGNHASMI--QGIRNSGAAKFVF------RHNDPDHLKKLLeksNPKiPKIVAFETVHSMDGAICPLEE 342
Cdd:pfam00266  85 LKPGDEIvITEMEHHANLVpwQELAKRTGARVRVlpldedGLLDLDELEKLI---TPK-TKLVAITHVSNVTGTIQPVPE 160

                         170       180
                  ....*....|....*....|.
gi 83977442   343 LCDVSHQYGALTFVDEVHAVG 363
Cdd:pfam00266 161 IGKLAHQYGALVLVDAAQAIG 181
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 236-357 2.33e-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: 52.97  E-value: 2.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 236 HVELEQELAELHQKDSALLFSSCFVANDSTLFTLAK----ILPGCEIYSDAGNHASMIqgIRNSG-AAKFVfrhnDPDHL 310
Cdd:cd00614  42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLYGGTYRLFERL--LPKLGiEVTFV----DPDDP 115

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 83977442 311 KKLLEKSNPKiPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVD 357
Cdd:cd00614 116 EALEAAIKPE-TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
306-372 5.63e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.06  E-value: 5.63e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 306 DPDHLKKLLeksNPKiPKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVG--------------------LY 365
Cdd:COG0520 143 DLEALEALL---TPR-TKLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPhlpvdvqalgcdfyafsghkLY 218


                ....*..
gi 83977442 366 GSRGAGI 372
Cdd:COG0520 219 GPTGIGV 225
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 206-501 2.25e-05

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: 46.95  E-value: 2.25e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 206 PQVLQATQETLQRHGAGAGGTrnisgtSKFHVELEQELAELHQKDSALLF--SSCFVANDST--LFTLAKIL--PGCEIY 279
Cdd:cd00609  14 PEVLEALAAAALRAGLLGYYP------DPGLPELREAIAEWLGRRGGVDVppEEIVVTNGAQeaLSLLLRALlnPGDEVL 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 280 SDAGNHASMIQGIRNSGAaKFVF-----RHNDPDHLKKLLEKSNPKiPKIVAFETVHSMDGAICP---LEELCDVSHQYG 351
Cdd:cd00609  88 VPDPTYPGYEAAARLAGA-EVVPvpldeEGGFLLDLELLEAAKTPK-TKLLYLNNPNNPTGAVLSeeeLEELAELAKKHG 165

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 83977442 352 ALTFVDEVHAvGLYGSRGAGIGERDGIMHKIDIISGTLGKAFGCVG---GY-IASTRDLVDMVRSYAagfIFTTSLPPMV 427
Cdd:cd00609 166 ILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL---PYTTSGPSTL 241

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 83977442 428 LSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGLPVIPCPS---HI-IPIRVGNAAlnsKLCDLLLSKHGIYV 501
Cdd:cd00609 242 SQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLERLLLEAGVVV 316
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 306-363 7.50e-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: 42.07  E-value: 7.50e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 83977442 306 DPDHLKKLLeksNPKIpKIVAFETVHSMDGAICPLEELCDVSHQYGALTFVDEVHAVG 363
Cdd:cd06453 128 DLEALEKLL---TERT-KLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 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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