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Conserved domains on  [gi|767922625|ref|XP_011531779|]
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5-aminolevulinate synthase, non-specific, mitochondrial isoform X1 [Homo sapiens]

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) ...
 214-603 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: 635.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 453
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  454 DIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrVLRRQHQRNVKLMRQMLM 533
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  534 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYF 603
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDL 386
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 19-154 1.04e-54

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: 181.54  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625   19 ESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSTAAVHYQQIKE-TPPASEKDKTAKAkvqqtpd 97
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767922625   98 gsqqspdgtqLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEM 154
Cdd:pfam09029  67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEV 113
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 214-603 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: 635.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 453
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  454 DIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrVLRRQHQRNVKLMRQMLM 533
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  534 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYF 603
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDL 386
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 260-604 1.20e-175

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: 501.71  E-value: 1.20e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 340 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 418
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 419 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPML 498
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 499 LAGALESVRILKSaeGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVAD-AAKNTEVCDELMSRhNIYVQAINY 577
Cdd:cd06454  239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315

                        330       340
                 ....*....|....*....|....*..
gi 767922625 578 PTVPRGEELLRIAPTPHHTPQMMNYFL 604
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLL 342
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 214-596 1.28e-169

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 488.98  E-value: 1.28e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 453
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 454 DIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLM 533
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922625 534 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHT 596
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHD 380
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 216-604 1.99e-156

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: 454.12  E-value: 1.99e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 216 YDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDysdslitkKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAG 295
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 296 GTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 375
Cdd:COG0156   73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 376 NDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDI 455
Cdd:COG0156  151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 456 ISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDA 535
Cdd:COG0156  231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922625 536 GLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFL 604
Cdd:COG0156  309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLL 376
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
265-604 1.15e-67

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 224.11  E-value: 1.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  265 WCSNDYLGMsrhprVCGAVMDTLKQhgAGAGGTRNISGTSKFHVDLERELADLHG--------KDAALLFSSCFVANDST 336
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  337 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVSHLRELLQRSdpsvPKIVAFETVHSMDGAVC 409
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  410 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDgVMPKMD-IISGTLGKAFGCVG---GYIASTSSLIDTVR 482
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  483 SYAAGFIFTTSLPPMLLAGALESvrILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCD 562
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 767922625  563 ELMSRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNYFL 604
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELL 348
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 19-154 1.04e-54

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: 181.54  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625   19 ESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSTAAVHYQQIKE-TPPASEKDKTAKAkvqqtpd 97
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767922625   98 gsqqspdgtqLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEM 154
Cdd:pfam09029  67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEV 113
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 214-603 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: 635.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 453
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  454 DIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrVLRRQHQRNVKLMRQMLM 533
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  534 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYF 603
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDL 386
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 260-604 1.20e-175

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: 501.71  E-value: 1.20e-175
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 340 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 418
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 419 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPML 498
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 499 LAGALESVRILKSaeGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVAD-AAKNTEVCDELMSRhNIYVQAINY 577
Cdd:cd06454  239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALLER-GIYVQAIRY 315

                        330       340
                 ....*....|....*....|....*..
gi 767922625 578 PTVPRGEELLRIAPTPHHTPQMMNYFL 604
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLL 342
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 214-596 1.28e-169

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 488.98  E-value: 1.28e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 214 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAG 293
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 294 AGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 373
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 374 RHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 453
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 454 DIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLM 533
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLKTSQTE--RDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922625 534 DAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRHNIYVQAINYPTVPRGEELLRIAPTPHHT 596
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHD 380
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 216-604 1.99e-156

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: 454.12  E-value: 1.99e-156
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 216 YDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDysdslitkKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAG 295
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 296 GTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 375
Cdd:COG0156   73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 376 NDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDI 455
Cdd:COG0156  151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 456 ISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDA 535
Cdd:COG0156  231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEPEL--RERLWENIAYFREGLKEL 308

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922625 536 GLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMNYFL 604
Cdd:COG0156  309 GFDLGPSESPIVPVIVGDAERALALADALLER-GIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLL 376
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 220-600 3.81e-95

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 296.68  E-value: 3.81e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 220 FEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDysdslitkKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRN 299
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 300 ISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVS 379
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 380 HLRELLQRSDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGG-GIGDRDGVMPKMDIISG 458
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRgLAAEAGLAGEPDVILVG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 459 TLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGrvlRRQH-QRNVKLMRQMLMDAGL 537
Cdd:PRK05958 236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922625 538 PVVHCPSHIIPVRVADAAKNTEVCDELmSRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMM 600
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAAL-QEQGFWVGAIRPPTVPAGTSRLRITLTAAHTEADI 374
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 260-598 2.17e-94

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: 294.18  E-value: 2.17e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  340 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAH 419
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  420 EFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIIS-GTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPML 498
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  499 LAGALESVRILksAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYP 578
Cdd:TIGR00858 254 AAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQQQ-GIFVGAIRPP 330

                         330       340
                  ....*....|....*....|
gi 767922625  579 TVPRGEELLRIAPTPHHTPQ 598
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPG 350
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 219-601 1.95e-87

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 277.46  E-value: 1.95e-87
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 219 FFEKKIDEKKNDHTY---RVFKTVNRrAHIfpmaddysdSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAG 295
Cdd:PRK06939   8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 296 GTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 375
Cdd:PRK06939  78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 376 NDVSHLRELLQRSDPSVP--KIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKM 453
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 454 DIISGTLGKAF-GCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRVLRRQHQRNVKLMRQML 532
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922625 533 MDAGLPVVHCPSHIIPVRVADAAKNTEVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMN 601
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQLD 381
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
265-604 1.15e-67

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 224.11  E-value: 1.15e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  265 WCSNDYLGMsrhprVCGAVMDTLKQhgAGAGGTRNISGTSKFHVDLERELADLHG--------KDAALLFSSCFVANDST 336
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  337 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVSHLRELLQRSdpsvPKIVAFETVHSMDGAVC 409
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  410 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDgVMPKMD-IISGTLGKAFGCVG---GYIASTSSLIDTVR 482
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRAL-LAEGPNlLVVGSFSKAFGLAGwrvGYILGNAAVISQLR 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625  483 SYAAGFIFTTSLPPMLLAGALESvrILKSAEGRVLRRQHQRNVKLMRQMLMDAGLPVVHCPSHIIPVRVADAAKNTEVCD 562
Cdd:pfam00155 233 KLARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQ 310

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 767922625  563 ELMSRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMNYFL 604
Cdd:pfam00155 311 VLLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELL 348
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 19-154 1.04e-54

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: 181.54  E-value: 1.04e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625   19 ESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRALSTAAVHYQQIKE-TPPASEKDKTAKAkvqqtpd 97
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGPTAKQAKA------- 66

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767922625   98 gsqqspdgtqLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEM 154
Cdd:pfam09029  67 ----------LPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEV 113
PLN02483 PLN02483
serine palmitoyltransferase
 267-581 1.05e-45

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 168.79  E-value: 1.05e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 267 SNDYLGMSRHPRVCGA-VMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLakMMP 345
Cdd:PLN02483 107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 346 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQ--------RSDPSVPKI-VAFETVHSMDGAVCPLEELCD 416
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLPEIVA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 417 VAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPK-MDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLP 495
Cdd:PLN02483 265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVDPAdVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 496 PMLLAGALESVRILKSAEG-----RVLRRQHQrNVKLMRQMLMDAGLPVV-HCPSHIIPVRVADAAKNTEVCDELMSRhN 569
Cdd:PLN02483 345 PPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-N 422

                        330
                 ....*....|..
gi 767922625 570 IYVQAINYPTVP 581
Cdd:PLN02483 423 VAVVVVGFPATP 434
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
267-604 1.77e-45

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 165.95  E-value: 1.77e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 267 SNDYLGMSRHPRVCGAVMDTLKQHGagaggtRNISGTSKFHVD------LERELADLHGKDAALLFSSCFVANDSTLFTL 340
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEG------DSLVMSAVFLHDdspkpqFEKKLAAFTGFESCLLCQSGWAANVGLLQTI 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 341 AKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQRSDPSvpkIVAFETVHSMDGAVCPLEELCDVAHE 420
Cdd:PRK07179 135 AD--PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEE 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 421 FGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVR--SYAAgfIFTTSLPPML 498
Cdd:PRK07179 210 FGCVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHE 287

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 499 LAGALESVRILKSAEGRvlRRQHQRNVKLMRQMLMDAGLPvVHCPSHIIPVrVADAAKNTEVC-DELMSRhNIYVQAINY 577
Cdd:PRK07179 288 IAGLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCA 362

                        330       340
                 ....*....|....*....|....*..
gi 767922625 578 PTVPRGEELLRIAPTPHHTPQMMNYFL 604
Cdd:PRK07179 363 PATPKNRNLIRLSLNADLTASDLDRVL 389
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 260-598 1.47e-43

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 162.54  E-value: 1.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 260 KQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 340 L--------AKMMP----GCEIYSDSGNHASMIQGIR----NSRVPKYIFRHNDVSHLRELLQRSDPSvPKIVAFETVHS 403
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 404 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVGGYIASTSSLIDTVRS 483
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 484 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRvlRRQHQRNVKLMRQMlmdAGLPVvhcPSHIIPVRVADAAKNTEVCDE 563
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 767922625 564 LMsRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 598
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 264-570 1.66e-31

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 126.56  E-value: 1.66e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 264 VWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFTLAKM 343
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 344 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELL----------QRSDPSVPKIVAFETVHSMDGAVCPLEE 413
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 414 LCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP--KMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFT 491
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGKSGRGSLEHAGLKPmvHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 492 TSLPPMLLAGALESVRILKsAEGRVLRRQHQrNVKLMRQMLMDAGLPVVHCP-----------SHIIPVRVADAAKnTEV 560
Cdd:PLN03227 240 ASAPPFLAKADATATAGEL-AGPQLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316

                        330
                 ....*....|
gi 767922625 561 CDELMSRHNI 570
Cdd:PLN03227 317 TDETLILDQI 326
PLN02822 PLN02822
serine palmitoyltransferase
 257-534 1.19e-28

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 119.46  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 257 ITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDST 336
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 337 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQ-------RSDPSVPKIVAfETVHSMDGAVC 409
Cdd:PLN02822 186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVV-EAIYQNSGQIA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 410 PLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMP-KMDIISGTLGKAFGCVGGYIASTSSLIDTVRSYAAGF 488
Cdd:PLN02822 263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVPIeKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767922625 489 IFTTSLPPMLLAGALESVRILKSaEGRVLRRQHQrNVKLMRQMLMD 534
Cdd:PLN02822 343 VFSASLPPYLASAAITAIDVLED-NPSVLAKLKE-NIALLHKGLSD 386
PRK07505 PRK07505
hypothetical protein; Provisional
 266-598 1.23e-26

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 112.38  E-value: 1.23e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 266 CSNDYLGMSRHPRVCGAVMDTLKqhgagAGGTRNISgTSKFHV------DLERELADLHGKDAaLLFSSCFVANDSTLFT 339
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 340 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVSHLRELLQRSdpsvpKIVAF--ETVHSMdGAVCPL 411
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 412 EELCDVAHEFGAITFVDEVHAVGLYGargggIGDRDGVMPKMD-------IISGTLGKAFGCVGGYIA-STSSLIDTVRS 483
Cdd:PRK07505 199 KELLRLQEKYGLFLYIDDAHGLSIYG-----KNGEGYVRSELDyrlnertIIAASLGKAFGASGGVIMlGDAEQIELILR 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 484 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRVLRRQHQRNVKLMRQMLMD--AGLPVvhcpshiiPVRVA---DAAKNT 558
Cdd:PRK07505 274 YAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAI 345

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 767922625 559 EVCDELMSRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 598
Cdd:PRK07505 346 KAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 267-559 4.12e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 95.62  E-value: 4.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 267 SNDYLGMSRHPRVCGAVMDTLKQH-------GAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTLFT 339
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 340 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVSHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDV 417
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscRQRSFGRIFIFVCSVYSFKGTLAPLEQIIAL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 418 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMPKMDIISgTLGKAFGCVGGYIASTSSLIDTVRSYAAGFIFTTSLPPM 497
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 498 LLAGALESVRILkSAEGRVLRRQ--------HQR-----------------NVKLMRQMLMDAGLPV-VHCPSHIIPVRV 551
Cdd:PRK05937 248 LLISIQVAYDFL-SQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326


                 ....*...
gi 767922625 552 ADAAKNTE 559
Cdd:PRK05937 327 NLHAFNTE 334
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 306-469 1.43e-11

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: 63.17  E-value: 1.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 306 FHVDLERELADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS--MIQGIRNSRVPKYIFRHNDVSHL 381
Cdd:cd01494    1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSryWVAAELAGAKPVPVPVDDAGYGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 382 RELLQRSD---PSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRdgvmpKMDIISG 458
Cdd:cd01494   79 LDVAILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPEG-----GADVVTF 153

                        170
                 ....*....|.
gi 767922625 459 TLGKAFGCVGG 469
Cdd:cd01494  154 SLHKNLGGEGG 164
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 411-590 8.71e-07

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: 51.19  E-value: 8.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 411 LEELCDVAHEFGAITFVDEVHAvGLYGARGGGIGDRDGVMPKMDIISGTLGKAFGCVG---GYIASTSSLIdtVRSYAAG 487
Cdd:cd00609  154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYLIAPPEEL--LERLKKL 230

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 488 FIFTTSLPPMLLAGALEsvRILKSAEGRV--LRRQHQRNVKLMRQMLMDAGLPVVHCPS---HI-IPVRVADAAkntEVC 561
Cdd:cd00609  231 LPYTTSGPSTLSQAAAA--AALDDGEEHLeeLRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFL 305

                        170       180
                 ....*....|....*....|....*....
gi 767922625 562 DELMSRHNIYVQAINYPtVPRGEELLRIA 590
Cdd:cd00609  306 ERLLLEAGVVVRPGSAF-GEGGEGFVRLS 333
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 310-428 2.16e-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: 50.28  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922625 310 LERELADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQ---GIRNSRVPKyifrhNDVSHL 381
Cdd:cd00614   45 LEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLpklGIEVTFVDP-----DDPEAL 118

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 767922625 382 RELLQRSdpsvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 428
Cdd:cd00614  119 EAAIKPE----TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
377-434 4.97e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 48.98  E-value: 4.97e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767922625 377 DVSHLRELLqrsDPSVpKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 434
Cdd:COG0520  143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 377-434 3.96e-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: 39.92  E-value: 3.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767922625  377 DVSHLRELLqrsDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 434
Cdd:pfam00266 128 DLDELEKLI---TPK-TKLVAITHVSNVTGTIQPVPEIGKLAHQYGALVLVDAAQAIG 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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