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Conserved domains on  [gi|1958806736|ref|XP_038955432|]
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5-aminolevulinate synthase, erythroid-specific, mitochondrial isoform X1 [Rattus norvegicus]

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 ...
 149-554 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: 737.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 149 FGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEAsmDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAG 228
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 229 AGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAVKFVF 308
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 309 RHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKL 388
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 389 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 468
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 469 DRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1958806736 549 VGLPLQ 554
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS super family cl07589
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 5-100 2.54e-13

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: 66.75  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736   5 AMLLRSCPVLSKGPTGLLGKVAKTyqFLFGIGRCPILATQGPTCSQIHLKATK-----------------AGADSPSW-- 65
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLQGEKeetpvagptakqakalpLGHPSPQAgq 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958806736  66 -TKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFK 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 ...
 149-554 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: 737.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 149 FGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEAsmDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAG 228
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 229 AGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAVKFVF 308
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 309 RHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKL 388
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 389 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 468
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 469 DRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1958806736 549 VGLPLQ 554
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 195-546 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: 522.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 195 KDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFT 274
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 275 LAklLPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSD-PKTPKIVAFETVHSMDGAICPLEELCDVA 353
Cdd:cd06454    81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 354 HQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMV 433
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 434 LSGALESVRLLKGeeGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVG-NAALNSKICDLLLaKHSIYVQAINY 512
Cdd:cd06454   239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958806736 513 PTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAW 546
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 149-552 0e+00

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 517.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 149 FGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAqhFSEASMDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAG 228
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRA--RDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 229 AGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAVKFVF 308
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 309 RHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKL 388
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 389 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKgeEGQALRRAHQRNVKHMRQLLM 468
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 469 DRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397


                  ....
gi 1958806736 549 VGLP 552
Cdd:PRK13392  398 LELP 401
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 151-548 3.18e-168

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: 483.40  E-value: 3.18e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 151 YDQFFRDKIMEKKQDHTYRVFKTVNRWANAypfaqhfsEASMDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAG 230
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGP--------RVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 231 GTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKllPGCEIYSDAGNHASMIQGIRNSGAVKFVFRH 310
Cdd:COG0156    73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 311 NDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDI 390
Cdd:COG0156   151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 391 ISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEgqALRRAHQRNVKHMRQLLMDR 470
Cdd:COG0156   231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806736 471 GFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHsIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:COG0156   309 GFDLGPSESPIVPVIVGDAERALALADALLERG-IYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
195-542 2.66e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 232.97  E-value: 2.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 195 KDVSVWCSNDYLGiSRHPRVLQAIEEtlknhgAGAGGTRNISGTSKFHVELEQELAELHH--------KDSALLFSSCFV 266
Cdd:pfam00155   1 TDKINLGSNEYLG-DTLPAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 267 ANDSTLFTLAkLLPGCEIYSDAGNHASMIQGIRNSGAVKFVFR-------HNDPGHLKKLLEKSdpktPKIVAFETVHSM 339
Cdd:pfam00155  74 ANIEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 340 DGAICPLEELCDVA---HQYGALTFVDEVHAVGLYGTRGAgIGERDGIMHKLD-IISGTLGKAFGCVG---GYIASTRDL 412
Cdd:pfam00155 149 TGTVATLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 413 VDMVRSYAAGFIFTTSLPPMVLSGALESvrLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALN 492
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958806736 493 SKICDLLLAKHSIYVQAINYPTVPrgeELLRLAPSpHHSPQMMENFVEKL 542
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 5-100 2.54e-13

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: 66.75  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736   5 AMLLRSCPVLSKGPTGLLGKVAKTyqFLFGIGRCPILATQGPTCSQIHLKATK-----------------AGADSPSW-- 65
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLQGEKeetpvagptakqakalpLGHPSPQAgq 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958806736  66 -TKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFK 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 ...
 149-554 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: 737.31  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 149 FGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEAsmDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAG 228
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 229 AGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAVKFVF 308
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 309 RHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKL 388
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 389 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEegQALRRAHQRNVKHMRQLLM 468
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKES--QDLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 469 DRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1958806736 549 VGLPLQ 554
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 195-546 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: 522.51  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 195 KDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFT 274
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 275 LAklLPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSD-PKTPKIVAFETVHSMDGAICPLEELCDVA 353
Cdd:cd06454    81 LA--GKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 354 HQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMV 433
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 434 LSGALESVRLLKGeeGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVG-NAALNSKICDLLLaKHSIYVQAINY 512
Cdd:cd06454   239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGdDPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1958806736 513 PTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAW 546
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 149-552 0e+00

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 517.87  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 149 FGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAqhFSEASMDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAG 228
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRA--RDHGPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 229 AGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAVKFVF 308
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 309 RHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKL 388
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 389 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKgeEGQALRRAHQRNVKHMRQLLM 468
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 469 DRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397


                  ....
gi 1958806736 549 VGLP 552
Cdd:PRK13392  398 LELP 401
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 151-548 3.18e-168

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: 483.40  E-value: 3.18e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 151 YDQFFRDKIMEKKQDHTYRVFKTVNRWANAypfaqhfsEASMDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAG 230
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGP--------RVTIDGREVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 231 GTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKllPGCEIYSDAGNHASMIQGIRNSGAVKFVFRH 310
Cdd:COG0156    73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 311 NDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDI 390
Cdd:COG0156   151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 391 ISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEgqALRRAHQRNVKHMRQLLMDR 470
Cdd:COG0156   231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806736 471 GFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHsIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTE 548
Cdd:COG0156   309 GFDLGPSESPIVPVIVGDAERALALADALLERG-IYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 201-542 1.13e-103

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 318.26  E-value: 1.13e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 201 CSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKllP 280
Cdd:PRK05958   45 ASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRLVTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTALAG--K 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 281 GCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSDPKtPKIVAFETVHSMDGAICPLEELCDVAHQYGALT 360
Cdd:PRK05958  123 GDLIVSDKLNHASLIDGARLSRARVRRYPHNDVDALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWL 201

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 361 FVDEVHAVGLYGTRGAGIGERDG-IMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALE 439
Cdd:PRK05958  202 LVDEAHGTGVLGPQGRGLAAEAGlAGEPDVILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARA 281

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 440 SVRLLKGEEGqalRRAH-QRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAkHSIYVQAINYPTVPRG 518
Cdd:PRK05958  282 ALRILRREPE---RRERlAALIARLRAGLRALGFQLMDSQSAIQPLIVGDNERALALAAALQE-QGFWVGAIRPPTVPAG 357

                         330       340
                  ....*....|....*....|....
gi 1958806736 519 EELLRLAPSPHHSPQMMENFVEKL 542
Cdd:PRK05958  358 TSRLRITLTAAHTEADIDRLLEAL 381
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 193-550 1.27e-100

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 310.97  E-value: 1.27e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 193 DSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTL 272
Cdd:PRK06939   40 DGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLF 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 273 FTLakLLPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSDPKTP--KIVAFETVHSMDGAICPLEELC 350
Cdd:PRK06939  120 ETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEIC 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 351 DVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIISGTLGKAF-GCVGGYIASTRDLVDMVRSYAAGFIFTTSL 429
Cdd:PRK06939  198 DLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSL 277

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 430 PPMVLSGALESVRLLkgEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNSKICDLLLAKHsIYVQA 509
Cdd:PRK06939  278 APAIVAASIKVLELL--EESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEEG-VYVIG 354

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1958806736 510 INYPTVPRGEELLRLAPSPHHSPQMmenfVEKLLLAWTEVG 550
Cdd:PRK06939  355 FSFPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFEKVG 391
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 188-542 2.55e-100

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: 308.81  E-value: 2.55e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 188 SEASMDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVA 267
Cdd:TIGR00858   9 PEVVRDGRRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 268 NDSTLFTLAKllPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSDPKTPKIVAFETVHSMDGAICPLE 347
Cdd:TIGR00858  89 NVGVISALVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLP 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 348 ELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIIS-GTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 426
Cdd:TIGR00858 167 QLVALAERYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFS 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 427 TSLPPMVLSGALESVRLLkgEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALNskicdLLLAKH--- 503
Cdd:TIGR00858 247 TALPPAVAAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASA-----LALAEElqq 319

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1958806736 504 -SIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKL 542
Cdd:TIGR00858 320 qGIFVGAIRPPTVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
195-542 2.66e-71

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 232.97  E-value: 2.66e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 195 KDVSVWCSNDYLGiSRHPRVLQAIEEtlknhgAGAGGTRNISGTSKFHVELEQELAELHH--------KDSALLFSSCFV 266
Cdd:pfam00155   1 TDKINLGSNEYLG-DTLPAVAKAEKD------ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 267 ANDSTLFTLAkLLPGCEIYSDAGNHASMIQGIRNSGAVKFVFR-------HNDPGHLKKLLEKSdpktPKIVAFETVHSM 339
Cdd:pfam00155  74 ANIEALIFLL-ANPGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNP 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 340 DGAICPLEELCDVA---HQYGALTFVDEVHAVGLYGTRGAgIGERDGIMHKLD-IISGTLGKAFGCVG---GYIASTRDL 412
Cdd:pfam00155 149 TGTVATLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDA-VATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 413 VDMVRSYAAGFIFTTSLPPMVLSGALESvrLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPSHIIPIRVGNAALN 492
Cdd:pfam00155 228 ISQLRKLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETA 305

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1958806736 493 SKICDLLLAKHSIYVQAINYPTVPrgeELLRLAPSpHHSPQMMENFVEKL 542
Cdd:pfam00155 306 KELAQVLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
PLN02483 PLN02483
serine palmitoyltransferase
 202-551 1.58e-56

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 198.06  E-value: 1.58e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 202 SNDYLGISRH-----PRVLqaieETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLA 276
Cdd:PLN02483  107 SYNYLGFAAAdeyctPRVI----ESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPALI 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 277 KllPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKS----DPKTPK-----IVAFETVHSMDGAICPLE 347
Cdd:PLN02483  183 G--KGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegQPRTHRpwkkiIVIVEGIYSMEGELCKLP 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 348 ELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHK-LDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 426
Cdd:PLN02483  261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYA 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 427 TSLPPMVLSGALESVRLLKGEEG-----QALRRAHQrNVKHMRQLLMDRGFPVI-PCPSHIIPIRVGNAAlnsKICDL-- 498
Cdd:PLN02483  341 TSMSPPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPA---KIPAFsr 416

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1958806736 499 LLAKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGL 551
Cdd:PLN02483  417 ECLKQNVAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGI 469
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 173-545 4.81e-54

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 191.04  E-value: 4.81e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 173 TVNRWANAYPFA--QHFSEASMD------SKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVE 244
Cdd:PLN02955   72 TFQKWLHDIPSNgeEIFSGDALAeerkgrFKKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 245 LEQELAELHHKDSALLFSSCFVANDSTLFTL---AKLLPGCE---------IYSDAGNHASMIQGIR---NSGAVK-FVF 308
Cdd:PLN02955  152 LESSLADLKKKEDCLVCPTGFAANMAAMVAIgsvASLLAASGkplknekvaIFSDALNHASIIDGVRlaeRQGNVEvFVY 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 309 RHNDPGHLKKLLEKSDPKTpKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKL 388
Cdd:PLN02955  232 RHCDMYHLNSLLSSCKMKR-KVVVTDSLFSMDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADV 310

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 389 DIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFTTSLPPMVLSGALESVRLLKGEEGQalRRAHQRNVKHMRQLlm 468
Cdd:PLN02955  311 DLCVGTLSKAAGCHGGFIACSKKWKQLIQSRGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL-- 386

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958806736 469 drgfPVIPCPSHIIPIRVGNAALNSKICDLLLaKHSIYVQAINYPTVPRGEELLRLAPSPHHSPQMmenfVEKLLLA 545
Cdd:PLN02955  387 ----SGVDISSPIISLVVGNQEKALKASRYLL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTED----VKKLITA 454
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
202-553 3.11e-45

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 165.18  E-value: 3.11e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 202 SNDYLGISRHPRVLQAIEETLKNHGAG----AGGTRNISGTSKFhvelEQELAELHHKDSALLFSSCFVANDSTLFTLAK 277
Cdd:PRK07179   61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 278 llPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEKSDPKtpkIVAFETVHSMDGAICPLEELCDVAHQYG 357
Cdd:PRK07179  137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 358 ALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIISGTLGKAFGCVGGYIASTRDLVDMVR--SYAAgfIFTTSLPPMVLS 435
Cdd:PRK07179  212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 436 GALESVRLLKGEEGqalRRAH-QRNVKHMRQLLMDRGFPvIPCPSHIIPIRVGNAAlNSKICDLLLAKHSIYVQAINYPT 514
Cdd:PRK07179  290 GLEATLEVIESADD---RRARlHANARFLREGLSELGYN-IRSESQIIALETGSER-NTEVLRDALEERNVFGAVFCAPA 364

                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1958806736 515 VPRGEELLRLAPSPHHSPQMMENFVEKLLLAWTEVGLPL 553
Cdd:PRK07179  365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWF 403
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 199-473 5.19e-35

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 136.19  E-value: 5.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 199 VWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSCFVANDSTLFTLAKl 278
Cdd:PLN03227    2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAK- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 279 lPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEK----------SDPKTPKIVAFETVHSMDGAICPLEE 348
Cdd:PLN03227   81 -RGDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 349 LCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGI--MHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSYAAGFIFT 426
Cdd:PLN03227  160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1958806736 427 TSLPPMVLSGALESVRLLKGEEgQALRRAHQrNVKHMRQLLMDRGFP 473
Cdd:PLN03227  240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHP 284
PRK07505 PRK07505
hypothetical protein; Provisional
 201-542 2.36e-34

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 134.72  E-value: 2.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 201 CSNDYLGISRHPRVLQAIEETLKNHGagaggTRNISgTSKFHV------ELEQELAELHHKDsALLFSSCFVANDSTLFT 274
Cdd:PRK07505   52 VSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELFGAS-VLTFTSCSAAHLGILPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 275 LAK--LLPGCEIYS--DAGNHASM--IQGI-RNSGAVKFVfRHNDPGHLKKLLEKSdpKTPKIVAfETVHSMDGAIcPLE 347
Cdd:PRK07505  125 LASghLTGGVPPHMvfDKNAHASLniLKGIcADETEVETI-DHNDLDALEDICKTN--KTVAYVA-DGVYSMGGIA-PVK 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 348 ELCDVAHQYGALTFVDEVHAVGLYGTRGAG--IGERDGIMHKLDIISGTLGKAFGCVGGYIA-STRDLVDMVRSYAAGFI 424
Cdd:PRK07505  200 ELLRLQEKYGLFLYIDDAHGLSIYGKNGEGyvRSELDYRLNERTIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLA 279

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 425 FTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMD--RGFPVipcpshiiPIR---VGNAALNSKICDLL 499
Cdd:PRK07505  280 FSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRliyIGDEDTAIKAAKQL 351

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1958806736 500 LAKhSIYVQAINYPTVPRGEELLRLAPSPHHSPQMMENFVEKL 542
Cdd:PRK07505  352 LDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLL 393
PLN02822 PLN02822
serine palmitoyltransferase
 192-446 2.00e-33

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 133.33  E-value: 2.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 192 MDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSScfvandsT 271
Cdd:PLN02822  106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSY-------G 178

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 272 LFTLAKLLPG-CE----IYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLE------KSDPKTPKIVAFETVHSMD 340
Cdd:PLN02822  179 LSTIFSVIPAfCKkgdiIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenKRKKKLRRYIVVEAIYQNS 258

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 341 GAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGI-MHKLDIISGTLGKAFGCVGGYIASTRDLVDMVRSY 419
Cdd:PLN02822  259 GQIAPLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLS 338

                         250       260
                  ....*....|....*....|....*..
gi 1958806736 420 AAGFIFTTSLPPMVLSGALESVRLLKG 446
Cdd:PLN02822  339 SSGYVFSASLPPYLASAAITAIDVLED 365
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 192-434 6.16e-25

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 106.79  E-value: 6.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 192 MDSKDVSVWCSNDYLGISRHPRVLQAIEETLKNH-------GAGAGGTRNISGTSKFHVELEQELAELHHKDSALLFSSC 264
Cdd:PRK05937    1 MKESLSIDFVTNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 265 FVANDSTLFTLAKLLPgcEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPGHLKKLLEksdpkTPKIVAFE-------TVH 337
Cdd:PRK05937   81 YMANLGLCAHLSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLE-----SCRQRSFGrififvcSVY 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 338 SMDGAICPLEELCDVAHQYGALTFVDEVHAVGLYGTRGAGIGERDGIMHKLDIISgTLGKAFGCVGGYIASTRDLVDMVR 417
Cdd:PRK05937  154 SFKGTLAPLEQIIALSKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLM 232

                         250
                  ....*....|....*..
gi 1958806736 418 SYAAGFIFTTSLPPMVL 434
Cdd:PRK05937  233 LNSPPLRYSTGLPPHLL 249
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 241-404 2.33e-15

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: 73.96  E-value: 2.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 241 FHVELEQELAELHHK--DSALLFSSCFVANDSTLFTLAKllPGCEIYSDAGNHASMIQGIRNSGAVKFVFRHNDPG---- 314
Cdd:cd01494     1 KLEELEEKLARLLQPgnDKAVFVPSGTGANEAALLALLG--PGDEVIVDANGHGSRYWVAAELAGAKPVPVPVDDAgygg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 315 -HLKKLLEKSDPKTPKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVGlyGTRGAGIGERDGimhKLDIISG 393
Cdd:cd01494    79 lDVAILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGG--ASPAPGVLIPEG---GADVVTF 153

                         170
                  ....*....|.
gi 1958806736 394 TLGKAFGCVGG 404
Cdd:cd01494   154 SLHKNLGGEGG 164
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 5-100 2.54e-13

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: 66.75  E-value: 2.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736   5 AMLLRSCPVLSKGPTGLLGKVAKTyqFLFGIGRCPILATQGPTCSQIHLKATK-----------------AGADSPSW-- 65
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKS--LLSYAQRCPVMMTRALSTSSANLQGEKeetpvagptakqakalpLGHPSPQAgq 78

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1958806736  66 -TKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFK 100
Cdd:pfam09029  79 sVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 242-363 2.59e-09

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: 59.14  E-value: 2.59e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 242 HVELEQELAELHHKDSALLFSSCFVANDSTLFTLAK----LLPGCEIYSDAGNHASMIqgIRNSG-AVKFVfrhnDPGHL 316
Cdd:cd00614    42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhVVASDDLYGGTYRLFERL--LPKLGiEVTFV----DPDDP 115

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1958806736 317 KKLLEKSDPKTpKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVD 363
Cdd:cd00614   116 EALEAAIKPET-KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
274-378 1.40e-08

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 57.07  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 274 TLAKLLPGCEI-YSDA---GNHASMIQGIRNSGA-VKFV----FRHNDPGHLKKLLeksDPKTpKIVAFETVHSMDGAIC 344
Cdd:COG0520    96 GLGRLKPGDEIlITEMehhSNIVPWQELAERTGAeVRVIpldeDGELDLEALEALL---TPRT-KLVAVTHVSNVTGTVN 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1958806736 345 PLEELCDVAHQYGALTFVDEVHAVG--------------------LYGTRGAGI 378
Cdd:COG0520   172 PVKEIAALAHAHGALVLVDGAQSVPhlpvdvqalgcdfyafsghkLYGPTGIGV 225
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 212-369 2.86e-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: 56.10  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 212 PRVLQAIEETLKNHGAGAGgtrniSGTSKFHVELEQELAELHHKDSALLFSScfvANDSTLFT--------------LAK 277
Cdd:pfam00266  13 QEVLDAIQEYYTDYNGNVH-----RGVHTLGKEATQAYEEAREKVAEFINAP---SNDEIIFTsgtteainlvalslGRS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 278 LLPGCEI-YSDAGNHASMI--QGIRN-SGAVKFVFRHNDPGH--LKKLLEKSDPKTpKIVAFETVHSMDGAICPLEELCD 351
Cdd:pfam00266  85 LKPGDEIvITEMEHHANLVpwQELAKrTGARVRVLPLDEDGLldLDELEKLITPKT-KLVAITHVSNVTGTIQPVPEIGK 163

                         170
                  ....*....|....*...
gi 1958806736 352 VAHQYGALTFVDEVHAVG 369
Cdd:pfam00266 164 LAHQYGALVLVDAAQAIG 181
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 346-507 7.73e-06

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: 48.49  E-value: 7.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 346 LEELCDVAHQYGALTFVDEVHAvGLYGTRGAGIGERDGIMHKLDIISGTLGKAFGCVG---GY-IASTRDLVDMVRSYAa 421
Cdd:cd00609   154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 422 gfIFTTSLPPMVLSGALESVRLLKGEEGQALRRAHQRNVKHMRQLLMDRGFPVIPCPS---HI-IPIRVGNAAlnsKICD 497
Cdd:cd00609   232 --PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLE 306

                         170
                  ....*....|
gi 1958806736 498 LLLAKHSIYV 507
Cdd:cd00609   307 RLLLEAGVVV 316
SufS_like cd06453
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ...
 312-369 1.18e-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: 44.76  E-value: 1.18e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958806736 312 DPGHLKKLLeksDPKTpKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVDEVHAVG 369
Cdd:cd06453   128 DLEALEKLL---TERT-KLVAVTHVSNVLGTINPVKEIGEIAHEAGVPVLVDGAQSAG 181
MetC COG0626
Cystathionine beta-lyase/cystathionine gamma-synthase [Amino acid transport and metabolism]; ...
 244-363 5.36e-04

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: 42.73  E-value: 5.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958806736 244 ELEQELAELHHKDSALLFSSCFVANDSTLFTLAKllPGCEI-YSDA---GNHAsMIQGIRNSGAVKFVFRhnDPGHLKKL 319
Cdd:COG0626    62 ALEEALAALEGGEAALAFASGMAAISAVLLALLK--AGDHVvASDDlygGTRR-LLDKVLARFGIEVTFV--DPTDLAAV 136

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1958806736 320 LEKSDPKTpKIVAFETVHSMDGAICPLEELCDVAHQYGALTFVD 363
Cdd:COG0626   137 EAAIRPNT-KLVFLETPSNPTLEVVDIAAIAAIAHAAGALLVVD 179
 
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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