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Conserved domains on  [gi|354470902|ref|XP_003497683|]
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5-aminolevulinate synthase, nonspecific, mitochondrial isoform X1 [Cricetulus griseus]

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) ...
 197-602 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: 651.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  197 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 276
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  277 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 356
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  357 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 436
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  437 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLM 516
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  517 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 354470902  597 VGLELK 602
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-138 6.82e-52

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: 174.22  E-value: 6.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902    2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAAHCQQIRE-TPPANEkekaakaavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGP-------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 354470902   81 ESQQTPdgtQLPAGHPSPTASQGSGSKCPFLAAQLSQTGSNVFRKASLELQEDVQEMH 138
Cdd:pfam09029  60 TAKQAK---ALPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 197-602 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: 651.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  197 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 276
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  277 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 356
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  357 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 436
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  437 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLM 516
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  517 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 354470902  597 VGLELK 602
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 243-590 1.55e-177

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: 507.48  E-value: 1.55e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 243 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 323 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 401
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 402 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPML 481
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 482 LAGALESVRILKSaeGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 560
Cdd:cd06454  239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                        330       340       350
                 ....*....|....*....|....*....|
gi 354470902 561 PTVPRGEELLRIAPTPHHTPQMMSFFLEKL 590
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 197-608 3.21e-168

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 486.28  E-value: 3.21e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 197 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 276
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 277 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 356
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 357 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 436
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 437 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQMLM 516
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 517 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 354470902 597 VGLELKPHSSAE 608
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 199-596 1.03e-157

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: 458.36  E-value: 1.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 199 YDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 278
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 279 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 358
Cdd:COG0156   73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 359 NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDI 438
Cdd:COG0156  151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 439 ISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLMDA 518
Cdd:COG0156  231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354470902 519 GLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:COG0156  309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
248-590 2.56e-69

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 229.11  E-value: 2.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  248 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 319
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  320 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 392
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  393 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVG---GYIASTSLLVDTVRS 466
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  467 YAAGFIFTTSLPPMLLAGALESvrILKSAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDE 546
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 354470902  547 LMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMSFFLEKL 590
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-138 6.82e-52

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: 174.22  E-value: 6.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902    2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAAHCQQIRE-TPPANEkekaakaavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGP-------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 354470902   81 ESQQTPdgtQLPAGHPSPTASQGSGSKCPFLAAQLSQTGSNVFRKASLELQEDVQEMH 138
Cdd:pfam09029  60 TAKQAK---ALPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 197-602 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: 651.02  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  197 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 276
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  277 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 356
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  357 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 436
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  437 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLM 516
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  517 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 354470902  597 VGLELK 602
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 243-590 1.55e-177

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: 507.48  E-value: 1.55e-177
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 243 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:cd06454    1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 323 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 401
Cdd:cd06454   81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 402 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPML 481
Cdd:cd06454  159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 482 LAGALESVRILKSaeGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 560
Cdd:cd06454  239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                        330       340       350
                 ....*....|....*....|....*....|
gi 354470902 561 PTVPRGEELLRIAPTPHHTPQMMSFFLEKL 590
Cdd:cd06454  316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 197-608 3.21e-168

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 486.28  E-value: 3.21e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 197 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 276
Cdd:PRK13392   2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 277 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 356
Cdd:PRK13392  80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 357 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 436
Cdd:PRK13392 160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 437 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQMLM 516
Cdd:PRK13392 240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 517 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:PRK13392 318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                        410
                 ....*....|..
gi 354470902 597 VGLELKPHSSAE 608
Cdd:PRK13392 398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 199-596 1.03e-157

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: 458.36  E-value: 1.03e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 199 YDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 278
Cdd:COG0156    1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 279 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 358
Cdd:COG0156   73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 359 NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDI 438
Cdd:COG0156  151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 439 ISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLMDA 518
Cdd:COG0156  231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 354470902 519 GLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 596
Cdd:COG0156  309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 243-590 4.87e-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: 296.49  E-value: 4.87e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  243 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  323 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAH 402
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  403 EFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIIS-GTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPML 481
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  482 LAGALESVRILksAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYP 561
Cdd:TIGR00858 254 AAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ-QQGIFVGAIRPP 330

                         330       340
                  ....*....|....*....|....*....
gi 354470902  562 TVPRGEELLRIAPTPHHTPQMMSFFLEKL 590
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 203-590 6.01e-95

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 297.07  E-value: 6.01e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 203 FEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRN 282
Cdd:PRK05958   7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 283 ISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVN 362
Cdd:PRK05958  79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 363 HLRELLQRSDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIIS-G 441
Cdd:PRK05958 157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILvG 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 442 TLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGralRRQH-QRNVKLMRQMLMDAGL 520
Cdd:PRK05958 236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 521 PVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKL 590
Cdd:PRK05958 313 QLMDSQSAIQPLIVGDNERALALAAALQEQ-GFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 202-602 6.60e-90

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 284.40  E-value: 6.60e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 202 FFEKKIDEKKNDHTY---RVFKTVNRrAQIfpmaddytdSLITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 278
Cdd:PRK06939   8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 279 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 358
Cdd:PRK06939  78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 359 NDVNHLRELLQRSDPSVP--KIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 436
Cdd:PRK06939 156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRV 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 437 DIISGTLGKAF-GCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQML 515
Cdd:PRK06939 236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 516 MDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmsffLEKLLITWK 595
Cdd:PRK06939 314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFE 388


                 ....*..
gi 354470902 596 RVGLELK 602
Cdd:PRK06939 389 KVGKELG 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
248-590 2.56e-69

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 229.11  E-value: 2.56e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  248 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 319
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  320 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 392
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  393 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVG---GYIASTSLLVDTVRS 466
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902  467 YAAGFIFTTSLPPMLLAGALESvrILKSAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDE 546
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 354470902  547 LMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMSFFLEKL 590
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-138 6.82e-52

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: 174.22  E-value: 6.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902    2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAAHCQQIRE-TPPANEkekaakaavqqapd 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGP-------------- 59

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 354470902   81 ESQQTPdgtQLPAGHPSPTASQGSGSKCPFLAAQLSQTGSNVFRKASLELQEDVQEMH 138
Cdd:pfam09029  60 TAKQAK---ALPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PLN02483 PLN02483
serine palmitoyltransferase
 250-608 3.33e-45

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 167.63  E-value: 3.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 250 SNDYLGMSRHPRVCGA-VMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMP 328
Cdd:PLN02483 107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 329 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--------RSDPSVPKI-VAFETVHSMDGAVCPLEELCD 399
Cdd:PLN02483 185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLPEIVA 264

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 400 VAHEFGAITFVDEVHAVGLYGARGGGIGDRDGV-MSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLP 478
Cdd:PLN02483 265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 479 PMLLAGALESVRILKSAEG-----RALRRQHQrNVKLMRQMLMDAGLPVI-HCPSHIIPVRVADAAKNTEICDELMTRhN 552
Cdd:PLN02483 345 PPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-N 422

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 354470902 553 IYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKRVGLELKPHSSAE 608
Cdd:PLN02483 423 VAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKK 478
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 243-581 1.73e-44

8-amino-7-oxononanoate synthase


Pssm-ID: 178541 [Multi-domain]  Cd Length: 476  Bit Score: 165.62  E-value: 1.73e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 243 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:PLN02955 102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 323 L--------AKMMP----GCEIYSDSGNHASMIQGIR----NSRVPKYIFRHNDVNHLRELLQRSDPSvPKIVAFETVHS 386
Cdd:PLN02955 182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 387 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRS 466
Cdd:PLN02955 261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 467 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRalRRQHQRNVKLMRQMlmdAGLPVihcPSHIIPVRVADAAKNTEICDE 546
Cdd:PLN02955 341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412

                        330       340       350
                 ....*....|....*....|....*....|....*
gi 354470902 547 LMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 581
Cdd:PLN02955 413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
250-603 4.29e-43

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 159.79  E-value: 4.29e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 250 SNDYLGMSRHPRVCGAVMETVKQHGAG----AGGTRNISGTSKFhvelEQALADLHGKDAALLFSSCFVANDSTLFTLAK 325
Cdd:PRK07179  61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 326 mmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSvpkIVAFETVHSMDGAVCPLEELCDVAHEFG 405
Cdd:PRK07179 137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 406 AITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVR--SYAAgfIFTTSLPPMLLA 483
Cdd:PRK07179 212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 484 GALESVRILKSAEGRalRRQHQRNVKLMRQMLMDAGLPvIHCPSHIIPVrVADAAKNTEIC-DELMTRhNIYVQAINYPT 562
Cdd:PRK07179 290 GLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCAPA 364

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 354470902 563 VPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKRVGLELKP 603
Cdd:PRK07179 365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 247-553 1.25e-32

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 130.02  E-value: 1.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 247 VWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKM 326
Cdd:PLN03227   2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 327 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELL----------QRSDPSVPKIVAFETVHSMDGAVCPLEE 396
Cdd:PLN03227  82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 397 LCDVAHEFGAITFVDEVHAVGLYG--ARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFT 474
Cdd:PLN03227 160 LVALKEEFHYRLILDESFSFGTLGksGRGSLEHAGLKPMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 475 TSLPPMLLAGALESVRILKsAEGRALRRQHQrNVKLMRQMLMDAGLPVIHCP-----------SHIIPVRVADAAKnTEI 543
Cdd:PLN03227 240 ASAPPFLAKADATATAGEL-AGPQLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316

                        330
                 ....*....|
gi 354470902 544 CDELMTRHNI 553
Cdd:PLN03227 317 TDETLILDQI 326
PRK07505 PRK07505
hypothetical protein; Provisional
 249-581 3.05e-27

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 114.31  E-value: 3.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 249 CSNDYLGMSRHPRVCGAVMETVKqhgagAGGTRNISgTSKFHV------ELEQALADLHGKDAaLLFSSCFVANDSTLFT 322
Cdd:PRK07505  52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 323 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVNHLRELLQRSdpsvpKIVAF--ETVHSMdGAVCPL 394
Cdd:PRK07505 125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 395 EELCDVAHEFGAITFVDEVHAVGLYGargggIGDRDGVMSKMD-------IISGTLGKAFGCVGGYIA-STSLLVDTVRS 466
Cdd:PRK07505 199 KELLRLQEKYGLFLYIDDAHGLSIYG-----KNGEGYVRSELDyrlnertIIAASLGKAFGASGGVIMlGDAEQIELILR 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 467 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRALRRQHQRNVKLMRQMLMD--AGLPVihcpshiiPVRVA---DAAKNT 541
Cdd:PRK07505 274 YAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAI 345

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 354470902 542 EICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 581
Cdd:PRK07505 346 KAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
PLN02822 PLN02822
serine palmitoyltransferase
 240-517 3.77e-27

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 115.22  E-value: 3.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 240 ITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDST 319
Cdd:PLN02822 106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 320 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ-------RSDPSVPKIVAfETVHSMDGAVC 392
Cdd:PLN02822 186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVV-EAIYQNSGQIA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 393 PLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGV-MSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGF 471
Cdd:PLN02822 263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 354470902 472 IFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQMLMD 517
Cdd:PLN02822 343 VFSASLPPYLASAAITAIDVLE--DNPSVLAKLKENIALLHKGLSD 386
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 250-542 2.83e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 96.00  E-value: 2.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 250 SNDYLGMSRHPRVCGAVMETVKQH-------GAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 322
Cdd:PRK05937  11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 323 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDV 400
Cdd:PRK05937  91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscRQRSFGRIFIFVCSVYSFKGTLAPLEQIIAL 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 401 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISgTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPM 480
Cdd:PRK05937 169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 481 LLAGALESVRILkSAEGRALRRQ--------HQR-----------------NVKLMRQMLMDAGLPV-IHCPSHIIPVRV 534
Cdd:PRK05937 248 LLISIQVAYDFL-SQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326


                 ....*...
gi 354470902 535 ADAAKNTE 542
Cdd:PRK05937 327 NLHAFNTE 334
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 289-452 7.68e-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: 67.02  E-value: 7.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 289 FHVELEQALADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS--MIQGIRNSRVPKYIFRHNDVNHL 364
Cdd:cd01494    1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSryWVAAELAGAKPVPVPVDDAGYGG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 365 RELLQRSD---PSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDrdgvmSKMDIISG 441
Cdd:cd01494   79 LDVAILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADVVTF 153

                        170
                 ....*....|.
gi 354470902 442 TLGKAFGCVGG 452
Cdd:cd01494  154 SLHKNLGGEGG 164
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 290-411 2.69e-07

CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed step of methionine biosynthesis. This pathway is unique to microorganisms and plants, rendering the enzyme an attractive target for the development of antimicrobials and herbicides. This subgroup also includes cystathionine gamma-lyases (CGL), O-acetylhomoserine sulfhydrylases and O-acetylhomoserine thiol lyases. CGL's are very similar to CGS's. Members of this group are widely distributed among all three forms of life.


Pssm-ID: 99738 [Multi-domain]  Cd Length: 369  Bit Score: 52.97  E-value: 2.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 290 HVELEQALADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQ---GIRNSRVPKyifrhNDV 361
Cdd:cd00614   42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLpklGIEVTFVDP-----DDP 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 354470902 362 NHLRELLQRSdpsvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 411
Cdd:cd00614  116 EALEAAIKPE----TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 394-573 1.83e-06

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


Pssm-ID: 99734 [Multi-domain]  Cd Length: 350  Bit Score: 50.42  E-value: 1.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 394 LEELCDVAHEFGAITFVDEVHAvGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVG---GY-IASTSLLVDTVRSYAa 469
Cdd:cd00609  154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL- 231

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 354470902 470 gfIFTTSLPPMLLAGALESVRILKSAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPS---HI-IPVRVADAAkntEICD 545
Cdd:cd00609  232 --PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLE 306

                        170       180
                 ....*....|....*....|....*...
gi 354470902 546 ELMTRHNIYVQAINYPtVPRGEELLRIA 573
Cdd:cd00609  307 RLLLEAGVVVRPGSAF-GEGGEGFVRLS 333
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
360-417 7.40e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 48.60  E-value: 7.40e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 354470902 360 DVNHLRELLqrsDPSVpKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 417
Cdd:COG0520  143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 376-417 7.28e-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: 39.15  E-value: 7.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 354470902  376 PKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 417
Cdd:pfam00266 140 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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