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Conserved domains on  [gi|41152048|ref|NP_958444|]
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5-aminolevulinate synthase, nonspecific, mitochondrial [Danio rerio]

Protein Classification

Preseq_ALAS and KBL_like domain-containing protein( domain architecture ID 11181659)

Preseq_ALAS and KBL_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
AAT_I super family cl18945
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 170-575 0e+00

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


The actual alignment was detected with superfamily member TIGR01821:

Pssm-ID: 450240 [Multi-domain]  Cd Length: 402  Bit Score: 668.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   170 FRYDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYTESlsFKRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSG 249
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   250 AGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKMMPGCEIYSDAGNHASMIQGIRNSGAKKFIF 329
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   330 RHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKM 409
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   410 DIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEgrTLRRKHQRNVTLLRQMLM 489
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   490 DSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRYNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 41152048   570 VGLPLK 575
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 1-120 2.64e-58

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: 190.78  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048     1 MDAIIRCPFLSRVPQTFLQQARKSLVAYAVKCPVMMdlasrplLRPLCSSSASFQKV-EDSSSAGHEASDAPAVPAGHPA 79
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEkEETPVAGPTAKQAKALPLGHPS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 41152048    80 PPAGHASASKCPFLAAEMSQKNSGVVRQASMALQEDVSEVR 120
Cdd:pfam09029  74 PQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 170-575 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: 668.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   170 FRYDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYTESlsFKRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSG 249
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   250 AGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKMMPGCEIYSDAGNHASMIQGIRNSGAKKFIF 329
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   330 RHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKM 409
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   410 DIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEgrTLRRKHQRNVTLLRQMLM 489
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   490 DSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRYNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 41152048   570 VGLPLK 575
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 216-567 8.20e-180

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: 512.49  E-value: 8.20e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 216 RNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFT 295
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 296 LakMMPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSD-PSTPKIVAFETVHSMDGAVCPLEQLCDVA 374
Cdd:cd06454  81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 375 HEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPML 454
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 455 LSGARQSVQILKSEEGRtlRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVAD-AEKNTEVCDIMMSRyNIYVQAINY 533
Cdd:cd06454 239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315

                       330       340       350
                ....*....|....*....|....*....|....
gi 41152048 534 PTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTW 567
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 170-581 2.94e-177

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 508.24  E-value: 2.94e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  170 FRYDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYteSLSFKRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSG 249
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDH--GPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  250 AGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKMMPGCEIYSDAGNHASMIQGIRNSGAKKFIF 329
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  330 RHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKM 409
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  410 DIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKseEGRTLRRKHQRNVTLLRQMLM 489
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  490 DSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRYNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 41152048  570 VGLPLKPHSSAE 581
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 172-569 1.53e-162

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: 469.92  E-value: 1.53e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 172 YDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDyteslsfkRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAG 251
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 252 GTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKmmPGCEIYSDAGNHASMIQGIRNSGAKKFIFRH 331
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 332 NDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDI 411
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 412 ISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEGRtlRRKHQRNVTLLRQMLMDS 491
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152048 492 GLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRyNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
221-563 1.02e-68

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 226.80  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   221 WCSNDYLGMSRhPRVVQTIMDTlgkhgsGAGGTRNISGTSKFHVDLEHELADLHG--------KDAALLFTSCFVANDST 292
Cdd:pfam00155   6 LGSNEYLGDTL-PAVAKAEKDA------LAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   293 LFTLAKMmPGCEIYSDAGNHASMIQGIRNSGAKKFIFR-------HNDAKHLRELLEKSdpstPKIVAFETVHSMDGAVC 365
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   366 PLEQLCDVA---HEFGAVTFVDEVHAVGLYGPrGGGIGDRDSVMHKMD-IISGTLGKAFGCVG---GYIASTHALVDTVR 438
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGS-PDAVATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   439 SYAAGFIFTTSLPPMLLSGArqSVQILKSEEGRTLRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVADAEKNTEVCD 518
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAAL--SDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 41152048   519 IMMSRYNIYVQAINYPTVargEELLRIAPTpHHTPQMMKYFVDKL 563
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGV---PGWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 1-120 2.64e-58

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: 190.78  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048     1 MDAIIRCPFLSRVPQTFLQQARKSLVAYAVKCPVMMdlasrplLRPLCSSSASFQKV-EDSSSAGHEASDAPAVPAGHPA 79
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEkEETPVAGPTAKQAKALPLGHPS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 41152048    80 PPAGHASASKCPFLAAEMSQKNSGVVRQASMALQEDVSEVR 120
Cdd:pfam09029  74 PQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 170-575 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: 668.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   170 FRYDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYTESlsFKRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSG 249
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   250 AGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKMMPGCEIYSDAGNHASMIQGIRNSGAKKFIF 329
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   330 RHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKM 409
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   410 DIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEgrTLRRKHQRNVTLLRQMLM 489
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   490 DSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRYNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 41152048   570 VGLPLK 575
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 216-567 8.20e-180

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: 512.49  E-value: 8.20e-180
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 216 RNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFT 295
Cdd:cd06454   1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 296 LakMMPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSD-PSTPKIVAFETVHSMDGAVCPLEQLCDVA 374
Cdd:cd06454  81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 375 HEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPML 454
Cdd:cd06454 159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 455 LSGARQSVQILKSEEGRtlRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVAD-AEKNTEVCDIMMSRyNIYVQAINY 533
Cdd:cd06454 239 AAAALAALEVLQGGPER--RERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315

                       330       340       350
                ....*....|....*....|....*....|....
gi 41152048 534 PTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTW 567
Cdd:cd06454 316 PTVPRGTARLRISLSAAHTKEDIDRLLEALKEVG 349
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 170-581 2.94e-177

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 508.24  E-value: 2.94e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  170 FRYDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYteSLSFKRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSG 249
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDH--GPDGPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  250 AGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKMMPGCEIYSDAGNHASMIQGIRNSGAKKFIF 329
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  330 RHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKM 409
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  410 DIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKseEGRTLRRKHQRNVTLLRQMLM 489
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  490 DSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRYNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 41152048  570 VGLPLKPHSSAE 581
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 172-569 1.53e-162

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: 469.92  E-value: 1.53e-162
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 172 YDEFFEKKIEEKKSDHTYRVFKTVNRRATEFPMADDyteslsfkRNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAG 251
Cdd:COG0156   1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 252 GTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKmmPGCEIYSDAGNHASMIQGIRNSGAKKFIFRH 331
Cdd:COG0156  73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 332 NDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDI 411
Cdd:COG0156 151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 412 ISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEGRtlRRKHQRNVTLLRQMLMDS 491
Cdd:COG0156 231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                       330       340       350       360       370       380       390
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 41152048 492 GLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRyNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTWTE 569
Cdd:COG0156 309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 176-567 1.31e-97

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 303.23  E-value: 1.31e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  176 FEKKIEEKKSDHTYRVFKTVNRRATEFPMADDYTEsLSFkrnvsvwCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRN 255
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDGRRM-LNF-------ASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  256 ISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLakMMPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAK 335
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  336 HLRELLEKSDPStPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGG-------IGDRDsvmhk 408
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGlaaeaglAGEPD----- 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  409 mDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGARQSVQILKSEEGRtlRRKHQRNVTLLRQML 488
Cdd:PRK05958 231 -VILVGTLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPER--RERLAALIARLRAGL 307

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 41152048  489 MDSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRyNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQTW 567
Cdd:PRK05958 308 RALGFQLMDSQSAIQPLIVGDNERALALAAALQEQ-GFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEALAEAL 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 216-564 1.18e-95

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: 297.26  E-value: 1.18e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   216 RNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFT 295
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   296 LAKmmPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAH 375
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   376 EFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIIS-GTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTTSLPPML 454
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   455 LSGARQSVQILksEEGRTLRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVADAEKNTEVCDiMMSRYNIYVQAINYP 534
Cdd:TIGR00858 254 AAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAE-ELQQQGIFVGAIRPP 330

                         330       340       350
                  ....*....|....*....|....*....|
gi 41152048   535 TVARGEELLRIAPTPHHTPQMMKYFVDKLT 564
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEALK 360
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 222-572 2.16e-86

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 274.77  E-value: 2.16e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  222 CSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLakMMP 301
Cdd:PRK06939  48 CANNYLGLANHPELIAAAKAALDSHGFGMASVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGK 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  302 GCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSDPSTP--KIVAFETVHSMDGAVCPLEQLCDVAHEFGA 379
Cdd:PRK06939 126 EDAIISDALNHASIIDGVRLCKAKRYRYANNDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDA 205

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  380 VTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIISGTLGKAF-GCVGGYIASTHALVDTVRSYAAGFIFTTSLPPMLLSGA 458
Cdd:PRK06939 206 LVMVDDSHAVGFVGENGRGTVEHFGVMDRVDIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAAS 285

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  459 RQSVQILksEEGRTLRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVADAEKNTEVCDIMMSRyNIYVQAINYPTVAR 538
Cdd:PRK06939 286 IKVLELL--EESDELRDRLWENARYFREGMTAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPK 362

                        330       340       350
                 ....*....|....*....|....*....|....
gi 41152048  539 GEELLRIAPTPHHTPQMMKYFVDKLTQTWTEVGL 572
Cdd:PRK06939 363 GQARIRTQMSAAHTKEQLDRAIDAFEKVGKELGV 396
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
221-563 1.02e-68

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 226.80  E-value: 1.02e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   221 WCSNDYLGMSRhPRVVQTIMDTlgkhgsGAGGTRNISGTSKFHVDLEHELADLHG--------KDAALLFTSCFVANDST 292
Cdd:pfam00155   6 LGSNEYLGDTL-PAVAKAEKDA------LAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   293 LFTLAKMmPGCEIYSDAGNHASMIQGIRNSGAKKFIFR-------HNDAKHLRELLEKSdpstPKIVAFETVHSMDGAVC 365
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   366 PLEQLCDVA---HEFGAVTFVDEVHAVGLYGPrGGGIGDRDSVMHKMD-IISGTLGKAFGCVG---GYIASTHALVDTVR 438
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGS-PDAVATRALLAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   439 SYAAGFIFTTSLPPMLLSGArqSVQILKSEEGRTLRRKHQRNVTLLRQMLMDSGLPVIHCPSHIIPVRVADAEKNTEVCD 518
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAAL--SDPLLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 41152048   519 IMMSRYNIYVQAINYPTVargEELLRIAPTpHHTPQMMKYFVDKL 563
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGV---PGWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 1-120 2.64e-58

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: 190.78  E-value: 2.64e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048     1 MDAIIRCPFLSRVPQTFLQQARKSLVAYAVKCPVMMdlasrplLRPLCSSSASFQKV-EDSSSAGHEASDAPAVPAGHPA 79
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEkEETPVAGPTAKQAKALPLGHPS 73

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 41152048    80 PPAGHASASKCPFLAAEMSQKNSGVVRQASMALQEDVSEVR 120
Cdd:pfam09029  74 PQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
223-576 5.71e-47

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 170.19  E-value: 5.71e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  223 SNDYLGMSRHPRVVQTIMDTLGKHGSGA--GGTRNISGTSKfhVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKmm 300
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEGDSLvmSAVFLHDDSPK--PQFEKKLAAFTGFESCLLCQSGWAANVGLLQTIAD-- 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  301 PGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSDPStpkIVAFETVHSMDGAVCPLEQLCDVAHEFGAV 380
Cdd:PRK07179 137 PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFGCV 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  381 TFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIISGTLGKAFGCVGGYIASTHALVDTVR--SYAAgfIFTTSLPPMLLSGA 458
Cdd:PRK07179 214 LVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIAGL 291

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  459 RQSVQILKSEEGRtlRRKHQRNVTLLRQMLMDSGLPvIHCPSHIIPVrVADAEKNTEVC-DIMMSRyNIYVQAINYPTVA 537
Cdd:PRK07179 292 EATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCAPATP 366

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 41152048  538 RGEELLRIAPTPHHTPQMMKYFVDKLTQTWTEVGLPLKP 576
Cdd:PRK07179 367 KNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN02483 PLN02483
serine palmitoyltransferase
 223-505 2.36e-46

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 170.71  E-value: 2.36e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  223 SNDYLGMSRH-----PRVvqtiMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLa 297
Cdd:PLN02483 107 SYNYLGFAAAdeyctPRV----IESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL- 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  298 kMMPGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKS----DPSTPK-----IVAFETVHSMDGAVCPLE 368
Cdd:PLN02483 182 -IGKGGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLREQiaegQPRTHRpwkkiIVIVEGIYSMEGELCKLP 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  369 QLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHK-MDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFT 447
Cdd:PLN02483 261 EIVAVCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYA 340

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 41152048  448 TSLPPMLLSGARQSVQILKSEEGRTL-RRKHQR---NVTLLRQMLMDSGLPVI-HCPSHIIPV 505
Cdd:PLN02483 341 TSMSPPAVQQVISAIKVILGEDGTNRgAQKLAQireNSNFFRSELQKMGFEVLgDNDSPVMPI 403
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 216-564 6.42e-46

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 169.08  E-value: 6.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  216 RNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFT 295
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  296 L--------AKMMP----GCEIYSDAGNHASMIQGIR----NSGAKKFIFRHNDAKHLRELLEkSDPSTPKIVAFETVHS 359
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLS-SCKMKRKVVVTDSLFS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  360 MDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSVMHKMDIISGTLGKAFGCVGGYIASTHALVDTVRS 439
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  440 YAAGFIFTTSLPPMLLSGARQSVQILKSEEGRtlRRKHQRNVTLLRQMlmdSGLPVihcPSHIIPVRVADAEKNTEVcdi 519
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKA--- 409

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 41152048  520 mmSRY----NIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLT 564
Cdd:PLN02955 410 --SRYllksGFHVMAIRPPTVPPNSCRLRVTLSAAHTTEDVKKLITALS 456
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 220-511 2.13e-33

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 131.95  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  220 VWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFTLAKM 299
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  300 mpGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEK----------SDPSTPKIVAFETVHSMDGAVCPLEQ 369
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLEQvraqdvalkrKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  370 LCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSV--MHKMDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFT 447
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLkpMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152048  448 TSLPPMLLSGARQSVQILKSEEgRTLRRKHQrNVTLLRQMLMDSGLPVIHCP-----------SHIIPVRVADAE 511
Cdd:PLN03227 240 ASAPPFLAKADATATAGELAGP-QLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQE 312
PLN02822 PLN02822
serine palmitoyltransferase
 216-490 7.10e-32

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 129.09  E-value: 7.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  216 RNVSVWCSNDYLGMSRHPRVVQTIMDTLGKHGSGAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFT 295
Cdd:PLN02822 109 KDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSVIPA 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  296 LAKMmpGCEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEK---SDPSTPKI---VAFETVHSMDGAVCPLEQ 369
Cdd:PLN02822 189 FCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEKltaENKRKKKLrryIVVEAIYQNSGQIAPLDE 266

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  370 LCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDRDSV-MHKMDIISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTT 448
Cdd:PLN02822 267 IVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGYVFSA 346

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 41152048  449 SLPPMLLSGARQSVQILksEEGRTLRRKHQRNVTLLRQMLMD 490
Cdd:PLN02822 347 SLPPYLASAAITAIDVL--EDNPSVLAKLKENIALLHKGLSD 386
PRK07505 PRK07505
hypothetical protein; Provisional
 222-565 1.43e-27

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 115.08  E-value: 1.43e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  222 CSNDYLGMSRHPRVVQTIMDTLGKHGsgaggTRNISgTSKFHV------DLEHELADLHGKDAaLLFTSCFVANDSTLFT 295
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALKRTG-----SLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  296 LAK--MMPGCEIYS--DAGNHASM--IQGIRNSGAKKFIFRHNDAKHLRELLEKSDpsTPKIVAfETVHSMdGAVCPLEQ 369
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTNK--TVAYVA-DGVYSM-GGIAPVKE 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  370 LCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGdRDSVMHKMD---IISGTLGKAFGCVGGYIA-STHALVDTVRSYAAGFI 445
Cdd:PRK07505 201 LLRLQEKYGLFLYIDDAHGLSIYGKNGEGYV-RSELDYRLNertIIAASLGKAFGASGGVIMlGDAEQIELILRYAGPLA 279

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  446 FTTSLPPMLLSGARQSVQILKSEEGRTLRRKHQRNVTLLRQMLMD--SGLPVihcpshiiPVRVA---DAEKNTEVCDIM 520
Cdd:PRK07505 280 FSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAIKAAKQL 351

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 41152048  521 MSRyNIYVQAINYPTVARGEELLRIAPTPHHTPQMMKYFVDKLTQ 565
Cdd:PRK07505 352 LDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTNDEIKRLCSLLKE 395
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 223-476 4.91e-23

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 101.01  E-value: 4.91e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  223 SNDYLGMSRHPRVVQTIMDTLGKHGS-------GAGGTRNISGTSKFHVDLEHELADLHGKDAALLFTSCFVANDSTLFT 295
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYCRqfphaqlGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  296 LAKMMPgcEIYSDAGNHASMIQGIRNSGAKKFIFRHNDAKHLRELLEKSDP-STPKIVAFE-TVHSMDGAVCPLEQLCDV 373
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLESCRQrSFGRIFIFVcSVYSFKGTLAPLEQIIAL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048  374 AHEFGAVTFVDEVHAVGLYGPRGGGIgdrdsvMHKMDI-----ISGTLGKAFGCVGGYIASTHALVDTVRSYAAGFIFTT 448
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGF------CHSLGYenfyaVLVTYSKALGSMGAALLSSSEVKQDLMLNSPPLRYST 242

                        250       260
                 ....*....|....*....|....*...
gi 41152048  449 SLPPMLLSGARQSVQILkSEEGRTLRRK 476
Cdd:PRK05937 243 GLPPHLLISIQVAYDFL-SQEGELARKQ 269
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 262-425 8.03e-13

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


Pssm-ID: 99742 [Multi-domain]  Cd Length: 170  Bit Score: 66.64  E-value: 8.03e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 262 FHVDLEHELADL--HGKDAALLFTSCFVANDSTLFTLAkmMPGCEIYSDAGNHASMIQGIRNS-GAKKFIFRHNDAKHLR 338
Cdd:cd01494   1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSRYWVAAELaGAKPVPVPVDDAGYGG 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 339 ----ELLEKSDPSTPKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVGLYGPRGGGIGDrdsvmHKMDIISG 414
Cdd:cd01494  79 ldvaILEELKAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADVVTF 153

                       170
                ....*....|.
gi 41152048 415 TLGKAFGCVGG 425
Cdd:cd01494 154 SLHKNLGGEGG 164
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
333-403 5.45e-07

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 52.06  E-value: 5.45e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 333 DAKHLRELLeksDPSTpKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVDEVHAVG--------------------LY 392
Cdd:COG0520 143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVPhlpvdvqalgcdfyafsghkLY 218

                        90
                ....*....|...
gi 41152048 393 GPRGGGI--GDRD 403
Cdd:COG0520 219 GPTGIGVlyGKRE 231
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 266-384 4.35e-06

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: 49.12  E-value: 4.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 266 LEHELADLHGKDAALLFTSCFVANDSTLFTLAK-----MMPGCeIYSDAGNHASMIqgIRNSGAK-KFIfrhnDAKHLRE 339
Cdd:cd00614  45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERL--LPKLGIEvTFV----DPDDPEA 117

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 41152048 340 LLEKSDPSTpKIVAFETVHSMDGAVCPLEQLCDVAHEFGAVTFVD 384
Cdd:cd00614 118 LEAAIKPET-KLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 301-399 1.02e-03

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: 41.85  E-value: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048   301 PGCEI-YSDAGNHASMI--QGIRN-SGAKKFIFRHNDAKHLR--ELLEKSDPSTpKIVAFETVHSMDGAVCPLEQLCDVA 374
Cdd:pfam00266  87 PGDEIvITEMEHHANLVpwQELAKrTGARVRVLPLDEDGLLDldELEKLITPKT-KLVAITHVSNVTGTIQPVPEIGKLA 165

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 41152048   375 HEFGAVTFVDEVHAVG--------------------LYGPRGGGI 399
Cdd:pfam00266 166 HQYGALVLVDAAQAIGhrpidvqklgvdflafsghkLYGPTGIGV 210
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 367-501 1.34e-03

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: 41.17  E-value: 1.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 41152048 367 LEQLCDVAHEFGAVTFVDEVHA----VGLYGPRGGGIGDRDSVmhkmdIISGTLGKAFGCVG---GY-IASTHALVDTVR 438
Cdd:cd00609 154 LEELAELAKKHGILIISDEAYAelvyDGEPPPALALLDAYERV-----IVLRSFSKTFGLPGlriGYlIAPPEELLERLK 228

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 41152048 439 SYAAGFIFTTSLPpmllsGARQSVQILKSEEG--RTLRRKHQRNVTLLRQMLMDSGLPVIHCPSH 501
Cdd:cd00609 229 KLLPYTTSGPSTL-----SQAAAAAALDDGEEhlEELRERYRRRRDALLEALKELGPLVVVKPSG 288
 
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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