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Conserved domains on  [gi|1868342385|ref|XP_035299804|]
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5-aminolevulinate synthase, nonspecific, mitochondrial isoform X2 [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) ...
 196-601 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 1868342385 196 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 275
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 276 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 355
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 356 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 435
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 436 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLM 515
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 516 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1868342385 596 VGLELK 601
Cdd:TIGR01821 397 LGLPLS 402
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-137 8.44e-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: 8.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385   2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAAHCQQIRE-TPPANEkkaakaavqqapdE 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGP-------------T 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1868342385  81 SQQTPdgtQLPAGHPSPTASQGSGSKCPFLAAQLSQTGSNVFRKASLELQEDVQEMH 137
Cdd:pfam09029  61 AKQAK---ALPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 196-601 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 1868342385 196 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 275
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 276 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 355
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 356 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 435
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 436 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLM 515
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 516 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1868342385 596 VGLELK 601
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 242-589 1.59e-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: 1.59e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 242 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 321
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 322 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 400
Cdd:cd06454    81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 401 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPML 480
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 481 LAGALESVRILKSaeGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 559
Cdd:cd06454   239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|
gi 1868342385 560 PTVPRGEELLRIAPTPHHTPQMMSFFLEKL 589
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 196-607 3.32e-168

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 486.28  E-value: 3.32e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 196 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 275
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 276 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 355
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 356 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 435
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 436 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQMLM 515
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 516 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                         410
                  ....*....|..
gi 1868342385 596 VGLELKPHSSAE 607
Cdd:PRK13392  398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 198-595 1.16e-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: 1.16e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 198 YDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 277
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 278 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 357
Cdd:COG0156    73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 358 NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDI 437
Cdd:COG0156   151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 438 ISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLMDA 517
Cdd:COG0156   231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868342385 518 GLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:COG0156   309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
247-589 2.53e-69

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 229.11  E-value: 2.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 247 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 318
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 319 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 391
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 392 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVG---GYIASTSLLVDTVRS 465
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 466 YAAGFIFTTSLPPMLLAGALESvrILKSAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDE 545
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1868342385 546 LMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMSFFLEKL 589
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-137 8.44e-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: 8.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385   2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAAHCQQIRE-TPPANEkkaakaavqqapdE 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGP-------------T 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1868342385  81 SQQTPdgtQLPAGHPSPTASQGSGSKCPFLAAQLSQTGSNVFRKASLELQEDVQEMH 137
Cdd:pfam09029  61 AKQAK---ALPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
 
Name Accession Description Interval E-value
5aminolev_synth TIGR01821
5-aminolevulinic acid synthase; This model represents 5-aminolevulinic acid synthase, an ...
 196-601 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 1868342385 196 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 275
Cdd:TIGR01821   1 MDYDQFFNKEIDKLHLEGRYRVFADLERQAGEFPFAQWHRPD--GAKDVTVWCSNDYLGMGQHPEVLQAMHETLDKYGAG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 276 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 355
Cdd:TIGR01821  79 AGGTRNISGTNIPHVELEAELADLHGKESALVFTSGYVANDATLATLAKIIPGCVIFSDELNHASMIEGIRHSGAEKFIF 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 356 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 435
Cdd:TIGR01821 159 RHNDVAHLEKLLQSVDPNRPKIIAFESVYSMDGDIAPIEEICDLADKYGALTYLDEVHAVGLYGPRGGGIAERDGLMHRI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 436 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLM 515
Cdd:TIGR01821 239 DIIEGTLAKAFGVVGGYIAASRKLIDAIRSYAPGFIFTTSLPPAIAAGATASIRHLKESQ--DLRRAHQENVKRLKNLLE 316

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 516 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:TIGR01821 317 ALGIPVIPNPSHIVPVIIGDAALCKKVSDLLLNKHGIYVQPINYPTVPRGTERLRITPTPAHTDKMIDDLVEALLLVWDR 396


                  ....*.
gi 1868342385 596 VGLELK 601
Cdd:TIGR01821 397 LGLPLS 402
KBL_like cd06454
KBL_like; this family belongs to the pyridoxal phosphate (PLP)-dependent aspartate ...
 242-589 1.59e-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: 1.59e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 242 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 321
Cdd:cd06454     1 KKVLNFCSNDYLGLANHPEVIEAAKEALDKYGVGAGGSRLISGTSDLHEELEEELAEFHGKEAALVFSSGYAANDGVLST 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 322 LakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSD-PSVPKIVAFETVHSMDGAVCPLEELCDVA 400
Cdd:cd06454    81 L--AGKGDLIISDSLNHASIIDGIRLSGAKKRIFKHNDMEDLEKLLREARrPYGKKLIVTEGVYSMDGDIAPLPELVDLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 401 HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPML 480
Cdd:cd06454   159 KKYGAILFVDEAHSVGVYGPHGRGVEEFGGLTDDVDIIMGTLGKAFGAVGGYIAGSKELIDYLRSYARGFIFSTSLPPAV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 481 LAGALESVRILKSaeGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVAD-AAKNTEICDELMtRHNIYVQAINY 559
Cdd:cd06454   239 AAAALAALEVLQG--GPERRERLQENVRYLRRGLKELGFPVGGSPSHIIPPLIGDdPAKAVAFSDALL-ERGIYVQAIRY 315

                         330       340       350
                  ....*....|....*....|....*....|
gi 1868342385 560 PTVPRGEELLRIAPTPHHTPQMMSFFLEKL 589
Cdd:cd06454   316 PTVPRGTARLRISLSAAHTKEDIDRLLEAL 345
PRK13392 PRK13392
5-aminolevulinate synthase; Provisional
 196-607 3.32e-168

5-aminolevulinate synthase; Provisional


Pssm-ID: 184023 [Multi-domain]  Cd Length: 410  Bit Score: 486.28  E-value: 3.32e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 196 FQYDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSliTKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAG 275
Cdd:PRK13392    2 MNYDSYFDAALAQLHQEGRYRVFADLEREAGRFPRARDHGPD--GPRRVTIWCSNDYLGMGQHPDVIGAMVDALDRYGAG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 276 AGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKMMPGCEIYSDSGNHASMIQGIRNSRVPKYIF 355
Cdd:PRK13392   80 AGGTRNISGTSHPHVLLERELADLHGKESALLFTSGYVSNDAALSTLGKLLPGCVILSDALNHASMIEGIRRSGAEKQVF 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 356 RHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 435
Cdd:PRK13392  160 RHNDLADLEEQLASVDPDRPKLIAFESVYSMDGDIAPIEAICDLADRYNALTYVDEVHAVGLYGARGGGIAERDGLMDRI 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 436 DIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQMLM 515
Cdd:PRK13392  240 DMIQGTLAKAFGCLGGYIAASADLIDFVRSFAPGFIFTTALPPAVAAGATAAIRHLK--TSQTERDAHQDRVAALKAKLN 317

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 516 DAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:PRK13392  318 ANGIPVMPSPSHIVPVMVGDPTLCKAISDRLMSEHGIYIQPINYPTVPRGTERLRITPTPLHDDEDIDALVAALVAIWDR 397

                         410
                  ....*....|..
gi 1868342385 596 VGLELKPHSSAE 607
Cdd:PRK13392  398 LELPRWREAAQA 409
BioF COG0156
7-keto-8-aminopelargonate synthetase or related enzyme [Coenzyme transport and metabolism]; ...
 198-595 1.16e-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: 1.16e-157
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 198 YDRFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 277
Cdd:COG0156     1 LLDRLEAELAALKAAGLYRYLRVLESPQGPRVTIDG--------REVLNFSSNDYLGLANHPRVIEAAAEALDRYGTGSG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 278 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 357
Cdd:COG0156    73 GSRLVSGTTPLHEELEEELAEFLGKEAALLFSSGYAANLGVISALAG--RGDLIFSDELNHASIIDGARLSGAKVVRFRH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 358 NDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDI 437
Cdd:COG0156   151 NDMDDLERLLKKARAARRKLIVTDGVFSMDGDIAPLPEIVELAEKYGALLYVDDAHGTGVLGETGRGLVEHFGLEDRVDI 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 438 ISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEgrALRRQHQRNVKLMRQMLMDA 517
Cdd:COG0156   231 IMGTLSKALGSSGGFVAGSKELIDYLRNRARPFIFSTALPPAVAAAALAALEILREEP--ELRERLWENIAYFREGLKEL 308

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1868342385 518 GLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKR 595
Cdd:COG0156   309 GFDLGPSESPIVPVIVGDAERALALADALL-ERGIYVSAIRPPTVPKGTARLRITLSAAHTEEDIDRLLEALAEVGKE 385
bioF TIGR00858
8-amino-7-oxononanoate synthase; 7-keto-8-aminopelargonic acid synthetase is an alternate name. ...
 242-589 6.68e-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: 296.10  E-value: 6.68e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 242 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 321
Cdd:TIGR00858  16 RRLLNFSSNDYLGLASHPEVIQAAQQGAEQYGAGSTASRLVSGNSPLHEELEEELAEWKGTEAALLFSSGYLANVGVISA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 322 LAKmmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSVPKIVAFETVHSMDGAVCPLEELCDVAH 401
Cdd:TIGR00858  96 LVG--KGDLILSDALNHASLIDGCRLSGARVRRYRHNDVEHLERLLEKNRGERRKLIVTDGVFSMDGDIAPLPQLVALAE 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 402 EFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIIS-GTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPML 480
Cdd:TIGR00858 174 RYGAWLMVDDAHGTGVLGEDGRGTLEHFGLKPEPVDIQvGTLSKALGSYGAYVAGSQALIDYLINRARTLIFSTALPPAV 253

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 481 LAGALESVRILksAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDELMtRHNIYVQAINYP 560
Cdd:TIGR00858 254 AAAALAALELI--QEEPWRREKLLALIARLRAGLEALGFTLMPSCTPIVPVIIGDNASALALAEELQ-QQGIFVGAIRPP 330

                         330       340
                  ....*....|....*....|....*....
gi 1868342385 561 TVPRGEELLRIAPTPHHTPQMMSFFLEKL 589
Cdd:TIGR00858 331 TVPAGTSRLRLTLSAAHTPGDIDRLAEAL 359
PRK05958 PRK05958
8-amino-7-oxononanoate synthase; Reviewed
 202-589 1.10e-94

8-amino-7-oxononanoate synthase; Reviewed


Pssm-ID: 235655 [Multi-domain]  Cd Length: 385  Bit Score: 296.68  E-value: 1.10e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 202 FEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDytdslitkKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRN 281
Cdd:PRK05958    7 LEAALAQRRAAGLYRSLRPREGGAGRWLVVDG--------RRMLNFASNDYLGLARHPRLIAAAQQAARRYGAGSGGSRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 282 ISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVN 361
Cdd:PRK05958   79 VTGNSPAHEALEEELAEWFGAERALLFSSGYAANLAVLTAL--AGKGDLIVSDKLNHASLIDGARLSRARVRRYPHNDVD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 362 HLRELLQRSDPSvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIIS-G 440
Cdd:PRK05958  157 ALEALLAKWRAG-RALIVTESVFSMDGDLAPLAELVALARRHGAWLLVDEAHGTGVLGPQGRGLAAEAGLAGEPDVILvG 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 441 TLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKSAEGralRRQH-QRNVKLMRQMLMDAGL 519
Cdd:PRK05958  236 TLGKALGSSGAAVLGSETLIDYLINRARPFIFTTALPPAQAAAARAALRILRREPE---RRERlAALIARLRAGLRALGF 312

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 520 PVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKL 589
Cdd:PRK05958  313 QLMDSQSAIQPLIVGDNERALALAAALQEQ-GFWVGAIRPPTVPAGTSRLRITLTAAHTEADIDRLLEAL 381
PRK06939 PRK06939
2-amino-3-ketobutyrate coenzyme A ligase; Provisional
 201-601 6.65e-90

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


Pssm-ID: 235893 [Multi-domain]  Cd Length: 397  Bit Score: 284.40  E-value: 6.65e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 201 FFEKKIDEKKNDHTY---RVFKTVNRrAQIfpmaddytdSLITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAG 277
Cdd:PRK06939    8 QLREELEEIKAEGLYkeeRVITSPQG-ADI---------TVADGKEVINFCANNYLGLANHPELIAAAKAALDSHGFGMA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 278 GTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMPGCEIYSDSGNHASMIQGIRNSRVPKYIFRH 357
Cdd:PRK06939   78 SVRFICGTQDLHKELEEKLAKFLGTEDAILYSSCFDANGGLFETL--LGKEDAIISDALNHASIIDGVRLCKAKRYRYAN 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 358 NDVNHLRELLQRSDPSVP--KIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKM 435
Cdd:PRK06939  156 NDMADLEAQLKEAKEAGArhKLIATDGVFSMDGDIAPLPEICDLADKYDALVMVDDSHAVGFVGENGRGTVEHFGVMDRV 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 436 DIISGTLGKAF-GCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQML 514
Cdd:PRK06939  236 DIITGTLGKALgGASGGYTAGRKEVIDWLRQRSRPYLFSNSLAPAIVAASIKVLELLE--ESDELRDRLWENARYFREGM 313

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 515 MDAGLPVIHCPSHIIPVRVADAAKNTEICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQMmsffLEKLLITWK 594
Cdd:PRK06939  314 TAAGFTLGPGEHPIIPVMLGDAKLAQEFADRLLEE-GVYVIGFSFPVVPKGQARIRTQMSAAHTKEQ----LDRAIDAFE 388


                  ....*..
gi 1868342385 595 RVGLELK 601
Cdd:PRK06939  389 KVGKELG 395
Aminotran_1_2 pfam00155
Aminotransferase class I and II;
247-589 2.53e-69

Aminotransferase class I and II;


Pssm-ID: 395103 [Multi-domain]  Cd Length: 351  Bit Score: 229.11  E-value: 2.53e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 247 WCSNDYLGMsrhprVCGAVMETVKQhgAGAGGTRNISGTSKFHVELEQALADLHG--------KDAALLFSSCFVANDST 318
Cdd:pfam00155   6 LGSNEYLGD-----TLPAVAKAEKD--ALAGGTRNLYGPTDGHPELREALAKFLGrspvlkldREAAVVFGSGAGANIEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 319 LFTLAKMmPGCEIYSDSGNHASMIQGIRNSRVPKYIFR-------HNDVNHLRELLQRSdpsvPKIVAFETVHSMDGAVC 391
Cdd:pfam00155  79 LIFLLAN-PGDAILVPAPTYASYIRIARLAGGEVVRYPlydsndfHLDFDALEAALKEK----PKVVLHTSPHNPTGTVA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 392 PLEELCDVA---HEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVG---GYIASTSLLVDTVRS 465
Cdd:pfam00155 154 TLEELEKLLdlaKEHNILLLVDEAYAGFVFGSPDAVATRALLAEGPNLLVVGSFSKAFGLAGwrvGYILGNAAVISQLRK 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 466 YAAGFIFTTSLPPMLLAGALESvrILKSAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPSHIIPVRVADAAKNTEICDE 545
Cdd:pfam00155 234 LARPFYSSTHLQAAAAAALSDP--LLVASELEEMRQRIKERRDYLRDGLQAAGLSVLPSQAGFFLLTGLDPETAKELAQV 311

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1868342385 546 LMTRHNIYVQAINYPTVPrgeELLRIAPTpHHTPQMMSFFLEKL 589
Cdd:pfam00155 312 LLEEVGVYVTPGSSPGVP---GWLRITVA-GGTEEELEELLEAI 351
Preseq_ALAS pfam09029
5-aminolevulinate synthase presequence; The N terminal presequence domain found in ...
 2-137 8.44e-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: 8.44e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385   2 ETVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMevgakpaPRTLSTSAAHCQQIRE-TPPANEkkaakaavqqapdE 80
Cdd:pfam09029   1 ASVLRRCPFLSRVPQAFLQKARKSLLSYAQRCPVMM-------TRALSTSSANLQGEKEeTPVAGP-------------T 60

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1868342385  81 SQQTPdgtQLPAGHPSPTASQGSGSKCPFLAAQLSQTGSNVFRKASLELQEDVQEMH 137
Cdd:pfam09029  61 AKQAK---ALPLGHPSPQAGQSVASKCPFLAAEMGQKNSNVVRKASPEVQEDVQEVK 114
PLN02483 PLN02483
serine palmitoyltransferase
 249-607 3.29e-45

serine palmitoyltransferase


Pssm-ID: 178101 [Multi-domain]  Cd Length: 489  Bit Score: 167.63  E-value: 3.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 249 SNDYLGMSRHPRVCGA-VMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLakMMP 327
Cdd:PLN02483  107 SYNYLGFAAADEYCTPrVIESLKKYSASTCSSRVDGGTTKLHRELEELVARFVGKPAAIVFGMGYATNSTIIPAL--IGK 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 328 GCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--------RSDPSVPKI-VAFETVHSMDGAVCPLEELCD 398
Cdd:PLN02483  185 GGLIISDSLNHNSIVNGARGSGATIRVFQHNTPSHLEEVLReqiaegqpRTHRPWKKIiVIVEGIYSMEGELCKLPEIVA 264

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 399 VAHEFGAITFVDEVHAVGLYGARGGGIGDRDGV-MSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLP 477
Cdd:PLN02483  265 VCKKYKAYVYLDEAHSIGAVGKTGRGVCELLGVdPADVDIMMGTFTKSFGSCGGYIAGSKELIQYLKRTCPAHLYATSMS 344

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 478 PMLLAGALESVRILKSAEG-----RALRRQHQrNVKLMRQMLMDAGLPVI-HCPSHIIPVRVADAAKNTEICDELMTRhN 551
Cdd:PLN02483  345 PPAVQQVISAIKVILGEDGtnrgaQKLAQIRE-NSNFFRSELQKMGFEVLgDNDSPVMPIMLYNPAKIPAFSRECLKQ-N 422

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1868342385 552 IYVQAINYPTVPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKRVGLELKPHSSAE 607
Cdd:PLN02483  423 VAVVVVGFPATPLLLARARICISASHSREDLIKALEVISEVGDLVGIKYFPAEPKK 478
PLN02955 PLN02955
8-amino-7-oxononanoate synthase
 242-580 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 1868342385 242 KQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 321
Cdd:PLN02955  102 KKLLLFSGNDYLGLSSHPTISNAAANAAKEYGMGPKGSALICGYTTYHRLLESSLADLKKKEDCLVCPTGFAANMAAMVA 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 322 L--------AKMMP----GCEIYSDSGNHASMIQGIR----NSRVPKYIFRHNDVNHLRELLQRSDPSvPKIVAFETVHS 385
Cdd:PLN02955  182 IgsvasllaASGKPlkneKVAIFSDALNHASIIDGVRlaerQGNVEVFVYRHCDMYHLNSLLSSCKMK-RKVVVTDSLFS 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 386 MDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRS 465
Cdd:PLN02955  261 MDGDFAPMEELSQLRKKYGFLLVIDDAHGTFVCGENGGGVAEEFNCEADVDLCVGTLSKAAGCHGGFIACSKKWKQLIQS 340

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 466 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRalRRQHQRNVKLMRQMlmdAGLPVihcPSHIIPVRVADAAKNTEICDE 545
Cdd:PLN02955  341 RGRSFIFSTAIPVPMAAAAYAAVVVARKEKWR--RKAIWERVKEFKAL---SGVDI---SSPIISLVVGNQEKALKASRY 412

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1868342385 546 LMtRHNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 580
Cdd:PLN02955  413 LL-KSGFHVMAIRPPTVPPNSCRLRVTLSAAHTTE 446
PRK07179 PRK07179
quorum-sensing autoinducer synthase;
249-602 4.69e-43

quorum-sensing autoinducer synthase;


Pssm-ID: 180866 [Multi-domain]  Cd Length: 407  Bit Score: 159.79  E-value: 4.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 249 SNDYLGMSRHPRVCGAVMETVKQHGAG----AGGTRNISGTSKFhvelEQALADLHGKDAALLFSSCFVANDSTLFTLAK 324
Cdd:PRK07179   61 SNDYLNLSGHPDIIKAQIAALQEEGDSlvmsAVFLHDDSPKPQF----EKKLAAFTGFESCLLCQSGWAANVGLLQTIAD 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 325 mmPGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQRSDPSvpkIVAFETVHSMDGAVCPLEELCDVAHEFG 404
Cdd:PRK07179  137 --PNTPVYIDFFAHMSLWEGVRAAGAQAHPFRHNDVDHLRRQIERHGPG---IIVVDSVYSTTGTIAPLADIVDIAEEFG 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 405 AITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVR--SYAAgfIFTTSLPPMLLA 482
Cdd:PRK07179  212 CVLVVDESHSLGTHGPQGAGLVAELGLTSRVHFITASLAKAFAGRAGIITCPRELAEYVPfvSYPA--IFSSTLLPHEIA 289

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 483 GALESVRILKSAEGRalRRQHQRNVKLMRQMLMDAGLPvIHCPSHIIPVrVADAAKNTEIC-DELMTRhNIYVQAINYPT 561
Cdd:PRK07179  290 GLEATLEVIESADDR--RARLHANARFLREGLSELGYN-IRSESQIIAL-ETGSERNTEVLrDALEER-NVFGAVFCAPA 364

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1868342385 562 VPRGEELLRIAPTPHHTPQMMSFFLEKLLITWKRVGLELKP 602
Cdd:PRK07179  365 TPKNRNLIRLSLNADLTASDLDRVLEVCREARDEVDLWFWK 405
PLN03227 PLN03227
serine palmitoyltransferase-like protein; Provisional
 246-552 1.26e-32

serine palmitoyltransferase-like protein; Provisional


Pssm-ID: 178766 [Multi-domain]  Cd Length: 392  Bit Score: 130.02  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 246 VWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFTLAKM 325
Cdd:PLN03227    2 NFATHDFLSTSSSPTLRQTALESLSHYGCGSCGPRGFYGTIDAHLELEQCMAEFLGTESAILYSDGASTTSSTVAAFAKR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 326 mpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELL----------QRSDPSVPKIVAFETVHSMDGAVCPLEE 395
Cdd:PLN03227   82 --GDLLVVDRGVNEALLVGVSLSRANVRWFRHNDMKDLRRVLeqvraqdvalKRKPTDQRRFLVVEGLYKNTGTLAPLKE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 396 LCDVAHEFGAITFVDEVHAVGLYG--ARGGGIGDRDGVMSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFT 473
Cdd:PLN03227  160 LVALKEEFHYRLILDESFSFGTLGksGRGSLEHAGLKPMVHAEIVTFSLENAFGSVGGMTVGSEEVVDHQRLSGSGYCFS 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 474 TSLPPMLLAGALESVRILKsAEGRALRRQHQrNVKLMRQMLMDAGLPVIHCP-----------SHIIPVRVADAAKnTEI 542
Cdd:PLN03227  240 ASAPPFLAKADATATAGEL-AGPQLLNRLHD-SIANLYSTLTNSSHPYALKLrnrlvitsdpiSPIIYLRLSDQEA-TRR 316

                         330
                  ....*....|
gi 1868342385 543 CDELMTRHNI 552
Cdd:PLN03227  317 TDETLILDQI 326
PRK07505 PRK07505
hypothetical protein; Provisional
 248-580 3.44e-27

hypothetical protein; Provisional


Pssm-ID: 181006 [Multi-domain]  Cd Length: 402  Bit Score: 114.31  E-value: 3.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 248 CSNDYLGMSRHPRVCGAVMETVKqhgagAGGTRNISgTSKFHV------ELEQALADLHGKDAaLLFSSCFVANDSTLFT 321
Cdd:PRK07505   52 VSCSYLGLDTHPAIIEGAVDALK-----RTGSLHLS-SSRTRVrsqilkDLEEALSELFGASV-LTFTSCSAAHLGILPL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 322 LAK--MMPGCEIYS--DSGNHASM--IQGIRNSRVPKYIFRHNDVNHLRELLQRSdpsvpKIVAF--ETVHSMdGAVCPL 393
Cdd:PRK07505  125 LASghLTGGVPPHMvfDKNAHASLniLKGICADETEVETIDHNDLDALEDICKTN-----KTVAYvaDGVYSM-GGIAPV 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 394 EELCDVAHEFGAITFVDEVHAVGLYGargggIGDRDGVMSKMD-------IISGTLGKAFGCVGGYIA-STSLLVDTVRS 465
Cdd:PRK07505  199 KELLRLQEKYGLFLYIDDAHGLSIYG-----KNGEGYVRSELDyrlnertIIAASLGKAFGASGGVIMlGDAEQIELILR 273

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 466 YAAGFIFTTSLPPMLLAGALESVRILKSAEGRALRRQHQRNVKLMRQMLMD--AGLPVihcpshiiPVRVA---DAAKNT 540
Cdd:PRK07505  274 YAGPLAFSQSLNVAALGAILASAEIHLSEELDQLQQKLQNNIALFDSLIPTeqSGSFL--------PIRLIyigDEDTAI 345

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1868342385 541 EICDELMTRhNIYVQAINYPTVPRGEELLRIAPTPHHTPQ 580
Cdd:PRK07505  346 KAAKQLLDR-GFYTSPVFFPVVAKGRAGLRIMFRASHTND 384
PLN02822 PLN02822
serine palmitoyltransferase
 239-516 3.75e-27

serine palmitoyltransferase


Pssm-ID: 178417 [Multi-domain]  Cd Length: 481  Bit Score: 115.22  E-value: 3.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 239 ITKKQVSVWCSNDYLGMSRHPRVCGAVMETVKQHGAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDST 318
Cdd:PLN02822  106 INGKDVVNFASANYLGLIGNEKIKESCTSALEKYGVGSCGPRGFYGTIDVHLDCETKIAKFLGTPDSILYSYGLSTIFSV 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 319 LFTLAKMmpGCEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ-------RSDPSVPKIVAfETVHSMDGAVC 391
Cdd:PLN02822  186 IPAFCKK--GDIIVADEGVHWGIQNGLYLSRSTIVYFKHNDMESLRNTLEkltaenkRKKKLRRYIVV-EAIYQNSGQIA 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 392 PLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDRDGV-MSKMDIISGTLGKAFGCVGGYIASTSLLVDTVRSYAAGF 470
Cdd:PLN02822  263 PLDEIVRLKEKYRFRVLLDESNSFGVLGKSGRGLSEHFGVpIEKIDIITAAMGHALATEGGFCTGSARVVDHQRLSSSGY 342

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1868342385 471 IFTTSLPPMLLAGALESVRILKsaEGRALRRQHQRNVKLMRQMLMD 516
Cdd:PLN02822  343 VFSASLPPYLASAAITAIDVLE--DNPSVLAKLKENIALLHKGLSD 386
PRK05937 PRK05937
8-amino-7-oxononanoate synthase; Provisional
 249-541 3.27e-21

8-amino-7-oxononanoate synthase; Provisional


Pssm-ID: 102071 [Multi-domain]  Cd Length: 370  Bit Score: 96.00  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 249 SNDYLGMSRHPRVCGAVMETVKQH-------GAGAGGTRNISGTSKFHVELEQALADLHGKDAALLFSSCFVANDSTLFT 321
Cdd:PRK05937   11 TNDFLGFSRSDTLVHEVEKRYRLYcrqfphaQLGYGGSRAILGPSSLLDDLEHKIAHFHGAPEAFIVPSGYMANLGLCAH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 322 LAKMMPgcEIYSDSGNHASMIQGIRNSRVPKYIFRHNDVNHLRELLQ--RSDPSVPKIVAFETVHSMDGAVCPLEELCDV 399
Cdd:PRK05937   91 LSSVTD--YVLWDEQVHISVVYSLSVISGWHQSFRHNDLDHLESLLEscRQRSFGRIFIFVCSVYSFKGTLAPLEQIIAL 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 400 AHEFGAITFVDEVHAVGLYGARGGGIGDRDGVMSKMDIISgTLGKAFGCVGGYIASTSLLVDTVRSYAAGFIFTTSLPPM 479
Cdd:PRK05937  169 SKKYHAHLIVDEAHAMGIFGDDGKGFCHSLGYENFYAVLV-TYSKALGSMGAALLSSSEVKQDLMLNSPPLRYSTGLPPH 247

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 480 LLAGALESVRILkSAEGRALRRQ--------HQR-----------------NVKLMRQMLMDAGLPV-IHCPSHIIPVRV 533
Cdd:PRK05937  248 LLISIQVAYDFL-SQEGELARKQlfrlkeyfAQKfssaapgcvqpiflpgiSEQELYSKLVETGIRVgVVCFPTGPFLRV 326


                  ....*...
gi 1868342385 534 ADAAKNTE 541
Cdd:PRK05937  327 NLHAFNTE 334
AAT_I cd01494
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ...
 288-451 7.81e-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: 7.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 288 FHVELEQALADL--HGKDAALLFSSCFVANDSTLFTLAkmMPGCEIYSDSGNHAS--MIQGIRNSRVPKYIFRHNDVNHL 363
Cdd:cd01494     1 KLEELEEKLARLlqPGNDKAVFVPSGTGANEAALLALL--GPGDEVIVDANGHGSryWVAAELAGAKPVPVPVDDAGYGG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 364 RELLQRSD---PSVPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVGLYGARGGGIGDrdgvmSKMDIISG 440
Cdd:cd01494    79 LDVAILEElkaKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGVLIPE-----GGADVVTF 153

                         170
                  ....*....|.
gi 1868342385 441 TLGKAFGCVGG 451
Cdd:cd01494   154 SLHKNLGGEGG 164
CGS_like cd00614
CGS_like: Cystathionine gamma-synthase is a PLP dependent enzyme and catalyzes the committed ...
 289-410 2.71e-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: 2.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 289 HVELEQALADLHGKDAALLFSSCFVANDSTLFTLAK-----MMPGCeIYSDSGNHASMIQ---GIRNSRVPKyifrhNDV 360
Cdd:cd00614    42 VDALEKKLAALEGGEAALAFSSGMAAISTVLLALLKagdhvVASDD-LYGGTYRLFERLLpklGIEVTFVDP-----DDP 115

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1868342385 361 NHLRELLQRSdpsvPKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVD 410
Cdd:cd00614   116 EALEAAIKPE----TKLVYVESPTNPTLKVVDIEAIAELAHEHGALLVVD 161
AAT_like cd00609
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ...
 393-572 1.85e-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: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 393 LEELCDVAHEFGAITFVDEVHAvGLYGARGGGIGDRDGVMSKMDIISGTLGKAFGCVG---GY-IASTSLLVDTVRSYAa 468
Cdd:cd00609   154 LEELAELAKKHGILIISDEAYA-ELVYDGEPPPALALLDAYERVIVLRSFSKTFGLPGlriGYlIAPPEELLERLKKLL- 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1868342385 469 gfIFTTSLPPMLLAGALESVRILKSAEGRALRRQHQRNVKLMRQMLMDAGLPVIHCPS---HI-IPVRVADAAkntEICD 544
Cdd:cd00609   232 --PYTTSGPSTLSQAAAAAALDDGEEHLEELRERYRRRRDALLEALKELGPLVVVKPSggfFLwLDLPEGDDE---EFLE 306

                         170       180
                  ....*....|....*....|....*...
gi 1868342385 545 ELMTRHNIYVQAINYPtVPRGEELLRIA 572
Cdd:cd00609   307 RLLLEAGVVVRPGSAF-GEGGEGFVRLS 333
CsdA COG0520
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
359-416 7.38e-06

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


Pssm-ID: 440286 [Multi-domain]  Cd Length: 396  Bit Score: 48.60  E-value: 7.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1868342385 359 DVNHLRELLqrsDPSVpKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 416
Cdd:COG0520   143 DLEALEALL---TPRT-KLVAVTHVSNVTGTVNPVKEIAALAHAHGALVLVDGAQSVP 196
Aminotran_5 pfam00266
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ...
 375-416 7.27e-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: 7.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1868342385 375 PKIVAFETVHSMDGAVCPLEELCDVAHEFGAITFVDEVHAVG 416
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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